CNRS Nantes University UFIP UFIP
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***  OXIDOREDUCTASE 24-JUN-08 3DK8  ***

elNémo ID: 22011404191129999

Job options:

ID        	=	 22011404191129999
JOBID     	=	 OXIDOREDUCTASE 24-JUN-08 3DK8
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    OXIDOREDUCTASE                          24-JUN-08   3DK8              
TITLE     CATALYTIC CYCLE OF HUMAN GLUTATHIONE REDUCTASE NEAR 1 A RESOLUTION    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE REDUCTASE;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 45 TO 522;                                    
COMPND   5 SYNONYM: GRASE, GR;                                                  
COMPND   6 EC: 1.8.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GSR, GLUR, GRD1;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    FLAVOENZYME, GLUTATHIONE, NICOTINAMIDE, ALTERNATIVE INITIATION, FAD,  
KEYWDS   2 FLAVOPROTEIN, MITOCHONDRION, NADP, OXIDOREDUCTASE, PHOSPHOPROTEIN,   
KEYWDS   3 REDOX-ACTIVE CENTER, TRANSIT PEPTIDE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.S.BERKHOLZ,H.R.FABER,S.N.SAVVIDES,P.A.KARPLUS                       
REVDAT   6   25-OCT-17 3DK8    1       REMARK                                   
REVDAT   5   25-DEC-13 3DK8    1       AUTHOR                                   
REVDAT   4   13-JUL-11 3DK8    1       VERSN                                    
REVDAT   3   24-FEB-09 3DK8    1       VERSN                                    
REVDAT   2   16-SEP-08 3DK8    1       JRNL                                     
REVDAT   1   05-AUG-08 3DK8    0                                                
JRNL        AUTH   D.S.BERKHOLZ,H.R.FABER,S.N.SAVVIDES,P.A.KARPLUS              
JRNL        TITL   CATALYTIC CYCLE OF HUMAN GLUTATHIONE REDUCTASE NEAR 1 A      
JRNL        TITL 2 RESOLUTION.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 382   371 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18638483                                                     
JRNL        DOI    10.1016/J.JMB.2008.06.083                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELX                                                
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.1                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
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) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.124                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.157                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.900                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 7671                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 155146                 
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)) : 0.120                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.153                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 4.900                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 6891                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 139319                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 3496                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 117                                           
REMARK   3   SOLVENT ATOMS      : 839                                           
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                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.016                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.033                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.088                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.103                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.035                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.053                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.099                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3DK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000048141.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 250008                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 30.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 3DK9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% AMMONIUM SULFATE, 0.1 M POTASSIUM     
REMARK 280  PHOSPHATE AND 0.1% BETA-OCTYL GLUCOSIDE, PH 7.0, VAPOR DIFFUSION,   
REMARK 280  HANGING DROP, TEMPERATURE 298K, PH 7.00                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       60.01550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.14050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       60.01550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.14050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       75.65275            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       71.29664            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CE   MET A  79  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     ALA A     1                                                      
REMARK 465     CYS A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  93    CG   CD   CE   NZ                                   
REMARK 470     LYS A 296    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O2   GOL A   604     O    HOH A  1051              0.47            
REMARK 500   O1   GOL A   604     O    HOH A  1035              0.87            
REMARK 500   C2   GOL A   604     O    HOH A  1051              0.98            
REMARK 500   C1   GOL A   604     O    HOH A  1035              2.05            
REMARK 500   C1   GOL A   604     O    HOH A  1051              2.07            
REMARK 500   C3   GOL A   604     O    HOH A  1051              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  22   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A  37   CD  -  NE  -  CZ  ANGL. DEV. =  23.9 DEGREES          
REMARK 500    ARG A  37   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    HIS A  75   CE1 -  NE2 -  CD2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    GLU A  77   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    HIS A  82   CA  -  CB  -  CG  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG A 103   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG A 189   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 218   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 224   CD  -  NE  -  CZ  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG A 224   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 224   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    GLU A 239   OE1 -  CD  -  OE2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG A 272   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ARG A 272   CD  -  NE  -  CZ  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG A 272   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    MET A 276   CA  -  CB  -  CG  ANGL. DEV. =  12.4 DEGREES          
REMARK 500    MET A 406   CG  -  SD  -  CE  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    CYS A 417   N   -  CA  -  CB  ANGL. DEV. =  19.2 DEGREES          
REMARK 500    CYS A 417   CA  -  CB  -  SG  ANGL. DEV. = -16.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  52     -121.83   -128.07                                   
REMARK 500    VAL A  61       26.81   -142.42                                   
REMARK 500    CYS A  90       52.09    -98.65                                   
REMARK 500    GLU A  91       70.53    -55.39                                   
REMARK 500    GLU A  91       73.18    166.39                                   
REMARK 500    HIS A 219     -147.63   -125.67                                   
REMARK 500    ALA A 336       72.32     56.71                                   
REMARK 500    ASN A 425     -178.72     64.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GSH A  482                                                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     GOL A   602                                                      
REMARK 615     GOL A   604                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 582                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 605                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DJG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DJJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DK4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3DK9   RELATED DB: PDB                                   
DBREF  3DK8 A   18   478  UNP    P00390   GSHR_HUMAN      45    522             
SEQRES   1 A  478  ALA CYS ARG GLN GLU PRO GLN PRO GLN GLY PRO PRO PRO          
SEQRES   2 A  478  ALA ALA GLY ALA VAL ALA SER TYR ASP TYR LEU VAL ILE          
SEQRES   3 A  478  GLY GLY GLY SER GLY GLY LEU ALA SER ALA ARG ARG ALA          
SEQRES   4 A  478  ALA GLU LEU GLY ALA ARG ALA ALA VAL VAL GLU SER HIS          
SEQRES   5 A  478  LYS LEU GLY GLY THR CYS VAL ASN VAL GLY CYS VAL PRO          
SEQRES   6 A  478  LYS LYS VAL MET TRP ASN THR ALA VAL HIS SER GLU PHE          
SEQRES   7 A  478  MET HIS ASP HIS ALA ASP TYR GLY PHE PRO SER CYS GLU          
SEQRES   8 A  478  GLY LYS PHE ASN TRP ARG VAL ILE LYS GLU LYS ARG ASP          
SEQRES   9 A  478  ALA TYR VAL SER ARG LEU ASN ALA ILE TYR GLN ASN ASN          
SEQRES  10 A  478  LEU THR LYS SER HIS ILE GLU ILE ILE ARG GLY HIS ALA          
SEQRES  11 A  478  ALA PHE THR SER ASP PRO LYS PRO THR ILE GLU VAL SER          
SEQRES  12 A  478  GLY LYS LYS TYR THR ALA PRO HIS ILE LEU ILE ALA THR          
SEQRES  13 A  478  GLY GLY MET PRO SER THR PRO HIS GLU SER GLN ILE PRO          
SEQRES  14 A  478  GLY ALA SER LEU GLY ILE THR SER ASP GLY PHE PHE GLN          
SEQRES  15 A  478  LEU GLU GLU LEU PRO GLY ARG SER VAL ILE VAL GLY ALA          
SEQRES  16 A  478  GLY TYR ILE ALA VAL GLU MET ALA GLY ILE LEU SER ALA          
SEQRES  17 A  478  LEU GLY SER LYS THR SER LEU MET ILE ARG HIS ASP LYS          
SEQRES  18 A  478  VAL LEU ARG SER PHE ASP SER MET ILE SER THR ASN CYS          
SEQRES  19 A  478  THR GLU GLU LEU GLU ASN ALA GLY VAL GLU VAL LEU LYS          
SEQRES  20 A  478  PHE SER GLN VAL LYS GLU VAL LYS LYS THR LEU SER GLY          
SEQRES  21 A  478  LEU GLU VAL SER MET VAL THR ALA VAL PRO GLY ARG LEU          
SEQRES  22 A  478  PRO VAL MET THR MET ILE PRO ASP VAL ASP CYS LEU LEU          
SEQRES  23 A  478  TRP ALA ILE GLY ARG VAL PRO ASN THR LYS ASP LEU SER          
SEQRES  24 A  478  LEU ASN LYS LEU GLY ILE GLN THR ASP ASP LYS GLY HIS          
SEQRES  25 A  478  ILE ILE VAL ASP GLU PHE GLN ASN THR ASN VAL LYS GLY          
SEQRES  26 A  478  ILE TYR ALA VAL GLY ASP VAL CYS GLY LYS ALA LEU LEU          
SEQRES  27 A  478  THR PRO VAL ALA ILE ALA ALA GLY ARG LYS LEU ALA HIS          
SEQRES  28 A  478  ARG LEU PHE GLU TYR LYS GLU ASP SER LYS LEU ASP TYR          
SEQRES  29 A  478  ASN ASN ILE PRO THR VAL VAL PHE SER HIS PRO PRO ILE          
SEQRES  30 A  478  GLY THR VAL GLY LEU THR GLU ASP GLU ALA ILE HIS LYS          
SEQRES  31 A  478  TYR GLY ILE GLU ASN VAL LYS THR TYR SER THR SER PHE          
SEQRES  32 A  478  THR PRO MET TYR HIS ALA VAL THR LYS ARG LYS THR LYS          
SEQRES  33 A  478  CYS VAL MET LYS MET VAL CYS ALA ASN LYS GLU GLU LYS          
SEQRES  34 A  478  VAL VAL GLY ILE HIS MET GLN GLY LEU GLY CYS ASP GLU          
SEQRES  35 A  478  MET LEU GLN GLY PHE ALA VAL ALA VAL LYS MET GLY ALA          
SEQRES  36 A  478  THR LYS ALA ASP PHE ASP ASN THR VAL ALA ILE HIS PRO          
SEQRES  37 A  478  THR SER SER GLU GLU LEU VAL THR LEU ARG                      
HET    SO4  A 580       5                                                       
HET    SO4  A 582       5                                                       
HET    FAD  A 479      53                                                       
HET    GSH  A 481      22                                                       
HET    GSH  A 482      10                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    GOL  A 604       6                                                       
HET    GOL  A 605       6                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     GSH GLUTATHIONE                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  FAD    C27 H33 N9 O15 P2                                            
FORMUL   5  GSH    2(C10 H17 N3 O6 S)                                           
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL  11  HOH   *839(H2 O)                                                    
HELIX    1   1 GLY A   29  LEU A   42  1                                  14    
HELIX    2   2 GLY A   55  VAL A   61  1                                   7    
HELIX    3   3 GLY A   62  HIS A   80  1                                  19    
HELIX    4   4 ASN A   95  SER A  121  1                                  27    
HELIX    5   5 GLY A  170  GLY A  174  5                                   5    
HELIX    6   6 THR A  176  PHE A  181  1                                   6    
HELIX    7   7 GLY A  196  LEU A  209  1                                  14    
HELIX    8   8 ASP A  227  ALA A  241  1                                  15    
HELIX    9   9 SER A  299  LEU A  303  5                                   5    
HELIX   10  10 GLY A  330  GLY A  334  5                                   5    
HELIX   11  11 LEU A  338  GLU A  355  1                                  18    
HELIX   12  12 THR A  383  GLY A  392  1                                  10    
HELIX   13  13 PRO A  405  THR A  411  5                                   7    
HELIX   14  14 GLY A  439  MET A  453  1                                  15    
HELIX   15  15 THR A  456  ASN A  462  1                                   7    
HELIX   16  16 SER A  470  THR A  476  5                                   7    
SHEET    1   A 4 VAL A  18  SER A  20  0                                        
SHEET    2   A 4 LYS A 145  THR A 148  1  O  THR A 148   N  ALA A  19           
SHEET    3   A 4 THR A 139  VAL A 142 -1  N  ILE A 140   O  TYR A 147           
SHEET    4   A 4 ALA A 130  PHE A 132 -1  N  ALA A 131   O  GLU A 141           
SHEET    1   B 5 GLU A 124  ARG A 127  0                                        
SHEET    2   B 5 ALA A  46  GLU A  50  1  N  VAL A  48   O  ILE A 126           
SHEET    3   B 5 TYR A  23  ILE A  26  1  N  VAL A  25   O  VAL A  49           
SHEET    4   B 5 ILE A 152  ILE A 154  1  O  LEU A 153   N  ILE A  26           
SHEET    5   B 5 ILE A 326  ALA A 328  1  O  TYR A 327   N  ILE A 154           
SHEET    1   C 2 GLY A 158  PRO A 160  0                                        
SHEET    2   C 2 ARG A 291  PRO A 293 -1  O  VAL A 292   N  MET A 159           
SHEET    1   D 4 GLU A 244  LEU A 246  0                                        
SHEET    2   D 4 LYS A 212  MET A 216  1  N  LEU A 215   O  LEU A 246           
SHEET    3   D 4 ARG A 189  VAL A 193  1  N  ILE A 192   O  MET A 216           
SHEET    4   D 4 CYS A 284  TRP A 287  1  O  LEU A 286   N  VAL A 193           
SHEET    1   E 3 SER A 249  LYS A 256  0                                        
SHEET    2   E 3 LEU A 261  THR A 267 -1  O  SER A 264   N  LYS A 252           
SHEET    3   E 3 VAL A 275  VAL A 282 -1  O  ILE A 279   N  VAL A 263           
SHEET    1   F 5 THR A 369  VAL A 371  0                                        
SHEET    2   F 5 ILE A 377  GLY A 381 -1  O  ILE A 377   N  VAL A 371           
SHEET    3   F 5 LYS A 429  GLN A 436 -1  O  MET A 435   N  GLY A 378           
SHEET    4   F 5 CYS A 417  ALA A 424 -1  N  VAL A 422   O  GLY A 432           
SHEET    5   F 5 VAL A 396  PHE A 403 -1  N  TYR A 399   O  MET A 421           
LINK         SG  CYS A  58                 SG2BGSH A 481     1555   1555  2.03  
CISPEP   1 HIS A  374    PRO A  375          0         0.86                     
CISPEP   2 HIS A  467    PRO A  468          0       -10.54                     
SITE     1 AC1  9 ALA A 195  ARG A 218  HIS A 219  ARG A 224                    
SITE     2 AC1  9 HOH A1023  HOH A1113  HOH A1296  HOH A2125                    
SITE     3 AC1  9 HOH A3004                                                     
SITE     1 AC2  9 ARG A 218  HIS A 219  THR A 257  LEU A 258                    
SITE     2 AC2  9 HOH A1321  HOH A1360  HOH A1407  HOH A1640                    
SITE     3 AC2  9 HOH A3004                                                     
SITE     1 AC3 40 GLY A  27  GLY A  29  SER A  30  GLY A  31                    
SITE     2 AC3 40 GLU A  50  SER A  51  GLY A  56  THR A  57                    
SITE     3 AC3 40 CYS A  58  GLY A  62  CYS A  63  LYS A  66                    
SITE     4 AC3 40 GLY A 128  HIS A 129  ALA A 130  ALA A 155                    
SITE     5 AC3 40 THR A 156  GLY A 157  TYR A 197  ARG A 291                    
SITE     6 AC3 40 ASN A 294  LEU A 298  GLY A 330  ASP A 331                    
SITE     7 AC3 40 LEU A 337  LEU A 338  THR A 339  PRO A 340                    
SITE     8 AC3 40 HIS A 467  PRO A 468  HOH A1001  HOH A1002                    
SITE     9 AC3 40 HOH A1007  HOH A1024  HOH A1063  HOH A1080                    
SITE    10 AC3 40 HOH A1084  HOH A1243  HOH A1269  HOH A1425                    
SITE     1 AC4 21 SER A  30  ARG A  37  CYS A  58  VAL A  59                    
SITE     2 AC4 21 VAL A  64  TYR A 114  THR A 339  ILE A 343                    
SITE     3 AC4 21 ARG A 347  HIS A 467  THR A 476  HOH A1058                    
SITE     4 AC4 21 HOH A1149  HOH A1191  HOH A1192  HOH A1655                    
SITE     5 AC4 21 HOH A1744  HOH A2795  HOH A2800  HOH A3101                    
SITE     6 AC4 21 HOH A3301                                                     
SITE     1 AC5 11 PRO A 405  MET A 406  THR A 469  GLU A 472                    
SITE     2 AC5 11 GLU A 473  HOH A1019  HOH A1061  HOH A1199                    
SITE     3 AC5 11 HOH A1655  HOH A2800  HOH A3305                               
SITE     1 AC6  8 ASN A 320  LYS A 324  GLY A 325  TYR A 327                    
SITE     2 AC6  8 ARG A 352  HOH A1069  HOH A1285  HOH A1445                    
SITE     1 AC7  8 GLU A 101  LYS A 102  ALA A 105  HIS A 122                    
SITE     2 AC7  8 HOH A1068  HOH A1152  HOH A1639  HOH A1798                    
CRYST1  120.031   62.281   83.980  90.00 121.90  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008331  0.000000  0.005186        0.00000                         
SCALE2      0.000000  0.016056  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014026        0.00000                         
ATOM      1  N   ALA A  17     -13.673  26.736  18.805  1.00 58.09           N  
ANISOU    1  N   ALA A  17     3864   9877   8331  -1674  -2871   1773       N  
ATOM      2  CA  ALA A  17     -13.227  27.367  20.042  1.00 50.73           C  
ANISOU    2  CA  ALA A  17     2587   8860   7828  -1334  -1417   1482       C  
ATOM      3  C   ALA A  17     -11.696  27.351  20.108  1.00 39.84           C  
ANISOU    3  C   ALA A  17     2414   7366   5360  -1053   -244     -2       C  
ATOM      4  O   ALA A  17     -11.086  26.459  19.538  1.00 53.51           O  
ANISOU    4  O   ALA A  17     4214   7805   8312  -1097   -238  -2023       O  
ATOM      5  CB  ALA A  17     -13.798  26.665  21.261  1.00 57.24           C  
ANISOU    5  CB  ALA A  17     2613  10546   8589  -2466     40    929       C  
ATOM      6  N   VAL A  18     -11.107  28.323  20.772  1.00 35.54           N  
ANISOU    6  N   VAL A  18     1867   7726   3912    268   -644   -509       N  
ATOM      7  CA  VAL A  18      -9.677  28.416  20.833  1.00 27.43           C  
ANISOU    7  CA  VAL A  18     1839   5830   2754    287    -85   -509       C  
ATOM      8  C   VAL A  18      -9.241  28.715  22.283  1.00 22.27           C  
ANISOU    8  C   VAL A  18     1273   4591   2598   -282    344   -199       C  
ATOM      9  O   VAL A  18      -9.683  29.658  22.898  1.00 29.15           O  
ANISOU    9  O   VAL A  18     2325   6058   2693   1274    157   -574       O  
ATOM     10  CB AVAL A  18      -9.062  29.486  19.913  0.57 26.63           C  
ANISOU   10  CB AVAL A  18     2634   5296   2188   1272    346   -539       C  
ATOM     11  CB BVAL A  18      -9.061  29.465  19.884  0.43 28.54           C  
ANISOU   11  CB BVAL A  18     2557   5876   2410   1091    -26    -51       C  
ATOM     12  CG1AVAL A  18      -7.544  29.448  20.015  0.57 18.90           C  
ANISOU   12  CG1AVAL A  18     2615   2949   1617    543    282   -666       C  
ATOM     13  CG1BVAL A  18      -9.087  30.873  20.458  0.43 28.93           C  
ANISOU   13  CG1BVAL A  18     3420   5538   2033   1428    360    509       C  
ATOM     14  CG2AVAL A  18      -9.544  29.261  18.491  0.57 27.67           C  
ANISOU   14  CG2AVAL A  18     3293   4404   2815   2276   -860   -389       C  
ATOM     15  CG2BVAL A  18      -7.616  29.098  19.533  0.43 24.29           C  
ANISOU   15  CG2BVAL A  18     2014   5364   1853   -262   -238  -1534       C  
ATOM     16  N   ALA A  19      -8.382  27.843  22.770  1.00 20.07           N  
ANISOU   16  N   ALA A  19     1801   3575   2251   -663    168   -358       N  
ATOM     17  CA  ALA A  19      -7.867  28.095  24.122  1.00 17.09           C  
ANISOU   17  CA  ALA A  19     1452   2992   2049   -453    512   -393       C  
ATOM     18  C   ALA A  19      -6.668  29.046  24.100  1.00 14.57           C  
ANISOU   18  C   ALA A  19     1326   2392   1817   -152    362   -133       C  
ATOM     19  O   ALA A  19      -5.774  28.807  23.257  1.00 18.01           O  
ANISOU   19  O   ALA A  19     1863   2974   2005   -666    847   -723       O  
ATOM     20  CB  ALA A  19      -7.476  26.755  24.693  1.00 19.22           C  
ANISOU   20  CB  ALA A  19     1984   2820   2500   -895    429    -62       C  
ATOM     21  N   SER A  20      -6.644  30.014  24.983  1.00 14.07           N  
ANISOU   21  N   SER A  20     1207   2494   1646    -26    226   -145       N  
ATOM     22  CA  SER A  20      -5.566  31.029  25.016  1.00 13.98           C  
ANISOU   22  CA  SER A  20     1235   2485   1592    -15    280   -263       C  
ATOM     23  C   SER A  20      -4.690  30.813  26.219  1.00 15.20           C  
ANISOU   23  C   SER A  20     1230   2946   1599   -156    248   -147       C  
ATOM     24  O   SER A  20      -5.159  30.535  27.320  1.00 16.06           O  
ANISOU   24  O   SER A  20     1044   3380   1681    -15    398    -58       O  
ATOM     25  CB ASER A  20      -6.269  32.360  25.031  0.61 16.15           C  
ANISOU   25  CB ASER A  20     1909   2407   1821    128    148   -329       C  
ATOM     26  CB BSER A  20      -6.067  32.457  24.981  0.39 14.97           C  
ANISOU   26  CB BSER A  20     1163   2492   2033     54    774    -96       C  
ATOM     27  OG ASER A  20      -7.023  32.693  23.871  0.61 18.17           O  
ANISOU   27  OG ASER A  20     2598   2530   1776    281     13    -20       O  
ATOM     28  OG BSER A  20      -4.961  33.364  24.864  0.39 22.78           O  
ANISOU   28  OG BSER A  20     2500   2908   3248   -921   1254   -682       O  
ATOM     29  N   TYR A  21      -3.379  31.013  26.003  1.00 14.97           N  
ANISOU   29  N   TYR A  21     1151   3026   1512     -9    404   -369       N  
ATOM     30  CA  TYR A  21      -2.311  30.931  26.944  1.00 15.03           C  
ANISOU   30  CA  TYR A  21     1164   2813   1734    206    357   -505       C  
ATOM     31  C   TYR A  21      -1.430  32.172  26.847  1.00 14.60           C  
ANISOU   31  C   TYR A  21      876   2563   2108    446     74   -418       C  
ATOM     32  O   TYR A  21      -1.497  32.883  25.838  1.00 16.13           O  
ANISOU   32  O   TYR A  21     1213   2633   2283    194     27   -360       O  
ATOM     33  CB  TYR A  21      -1.428  29.653  26.709  1.00 15.30           C  
ANISOU   33  CB  TYR A  21     1247   2631   1937    105    459   -663       C  
ATOM     34  CG  TYR A  21      -2.236  28.393  26.889  1.00 16.82           C  
ANISOU   34  CG  TYR A  21     1386   2782   2224   -118    790   -896       C  
ATOM     35  CD1 TYR A  21      -3.089  27.928  25.895  1.00 21.63           C  
ANISOU   35  CD1 TYR A  21     2260   3513   2445   -636    696  -1325       C  
ATOM     36  CD2 TYR A  21      -2.190  27.700  28.101  1.00 16.66           C  
ANISOU   36  CD2 TYR A  21     1204   2355   2770     84    664   -679       C  
ATOM     37  CE1 TYR A  21      -3.835  26.794  26.070  1.00 26.54           C  
ANISOU   37  CE1 TYR A  21     3038   3179   3866   -762    176  -1366       C  
ATOM     38  CE2 TYR A  21      -2.950  26.538  28.296  1.00 19.86           C  
ANISOU   38  CE2 TYR A  21     1635   2320   3592    108   1023   -586       C  
ATOM     39  CZ  TYR A  21      -3.762  26.108  27.261  1.00 22.73           C  
ANISOU   39  CZ  TYR A  21     1762   2543   4330   -292    798  -1161       C  
ATOM     40  OH  TYR A  21      -4.550  24.994  27.388  1.00 30.19           O  
ANISOU   40  OH  TYR A  21     1991   2927   6550   -528    789   -717       O  
ATOM     41  N   ASP A  22      -0.606  32.427  27.853  1.00 14.75           N  
ANISOU   41  N   ASP A  22      961   2543   2100    463    207   -614       N  
ATOM     42  CA  ASP A  22       0.436  33.422  27.676  1.00 15.74           C  
ANISOU   42  CA  ASP A  22     1243   2066   2673    454   -144   -388       C  
ATOM     43  C   ASP A  22       1.586  32.967  26.802  1.00 15.29           C  
ANISOU   43  C   ASP A  22     1150   1761   2899    304    187   -107       C  
ATOM     44  O   ASP A  22       2.228  33.749  26.135  1.00 16.42           O  
ANISOU   44  O   ASP A  22     1333   1665   3240    244     25     81       O  
ATOM     45  CB AASP A  22       1.146  33.850  28.954  0.29 12.62           C  
ANISOU   45  CB AASP A  22      717   1748   2329    468      1    322       C  
ATOM     46  CB BASP A  22       0.929  33.820  29.071  0.71 20.34           C  
ANISOU   46  CB BASP A  22     2725   2004   2998    573   -698   -917       C  
ATOM     47  CG AASP A  22       0.308  34.756  29.801  0.29 10.62           C  
ANISOU   47  CG AASP A  22      872   1242   1919   -107    487    537       C  
ATOM     48  CG BASP A  22      -0.112  34.333  30.039  0.71 23.43           C  
ANISOU   48  CG BASP A  22     2958   2995   2950   1458  -1185  -1368       C  
ATOM     49  OD1AASP A  22       0.247  34.477  31.010  0.29 10.88           O  
ANISOU   49  OD1AASP A  22      593   1445   2098     26    363    908       O  
ATOM     50  OD1BASP A  22      -0.110  33.971  31.230  0.71 22.74           O  
ANISOU   50  OD1BASP A  22     3051   2640   2950   1172   -813  -1535       O  
ATOM     51  OD2AASP A  22      -0.325  35.727  29.368  0.29 11.60           O  
ANISOU   51  OD2AASP A  22     1805   1470   1131    533    648    272       O  
ATOM     52  OD2BASP A  22      -0.994  35.097  29.574  0.71 29.85           O  
ANISOU   52  OD2BASP A  22     3820   3099   4421   1998  -1472  -1150       O  
ATOM     53  N   TYR A  23       1.857  31.638  26.865  1.00 13.16           N  
ANISOU   53  N   TYR A  23     1002   1664   2335    170    251    -78       N  
ATOM     54  CA  TYR A  23       3.039  31.088  26.216  1.00 12.13           C  
ANISOU   54  CA  TYR A  23      950   1614   2043    185    234     11       C  
ATOM     55  C   TYR A  23       2.696  29.675  25.724  1.00 11.11           C  
ANISOU   55  C   TYR A  23      871   1588   1760    184    168     84       C  
ATOM     56  O   TYR A  23       2.320  28.841  26.543  1.00 12.46           O  
ANISOU   56  O   TYR A  23     1386   1687   1663     89    292     73       O  
ATOM     57  CB  TYR A  23       4.229  31.002  27.138  1.00 11.18           C  
ANISOU   57  CB  TYR A  23     1031   1534   1683    215    254    -89       C  
ATOM     58  CG  TYR A  23       5.623  30.913  26.588  1.00 10.43           C  
ANISOU   58  CG  TYR A  23     1046   1407   1509    213    233    -80       C  
ATOM     59  CD1 TYR A  23       5.966  31.484  25.382  1.00 11.59           C  
ANISOU   59  CD1 TYR A  23     1070   1669   1665    278    183    168       C  
ATOM     60  CD2 TYR A  23       6.641  30.300  27.321  1.00 10.49           C  
ANISOU   60  CD2 TYR A  23     1070   1576   1339    177    298    -70       C  
ATOM     61  CE1 TYR A  23       7.271  31.414  24.898  1.00 10.96           C  
ANISOU   61  CE1 TYR A  23     1054   1716   1397    253    183    -10       C  
ATOM     62  CE2 TYR A  23       7.951  30.271  26.865  1.00 10.36           C  
ANISOU   62  CE2 TYR A  23     1072   1544   1320    213    152    -93       C  
ATOM     63  CZ  TYR A  23       8.256  30.827  25.653  1.00 10.36           C  
ANISOU   63  CZ  TYR A  23     1031   1446   1457    176    325     -5       C  
ATOM     64  OH  TYR A  23       9.550  30.868  25.137  1.00 11.51           O  
ANISOU   64  OH  TYR A  23      979   1786   1607    171    279    -10       O  
ATOM     65  N   LEU A  24       2.870  29.421  24.442  1.00 11.39           N  
ANISOU   65  N   LEU A  24      972   1613   1744    186    313    129       N  
ATOM     66  CA  LEU A  24       2.708  28.104  23.858  1.00 11.97           C  
ANISOU   66  CA  LEU A  24      922   1650   1976     77    176    -41       C  
ATOM     67  C   LEU A  24       4.057  27.662  23.343  1.00 10.27           C  
ANISOU   67  C   LEU A  24     1065   1558   1278     49    138      0       C  
ATOM     68  O   LEU A  24       4.644  28.390  22.540  1.00 12.21           O  
ANISOU   68  O   LEU A  24     1367   1685   1588    178    434    238       O  
ATOM     69  CB  LEU A  24       1.701  28.115  22.695  1.00 15.51           C  
ANISOU   69  CB  LEU A  24     1314   2515   2063    -29   -154    487       C  
ATOM     70  CG  LEU A  24       0.239  28.127  22.985  1.00 17.56           C  
ANISOU   70  CG  LEU A  24     1404   3099   2170    360    -17    -95       C  
ATOM     71  CD1 LEU A  24      -0.427  28.206  21.592  1.00 22.81           C  
ANISOU   71  CD1 LEU A  24     1564   4595   2509   -846   -491   1048       C  
ATOM     72  CD2 LEU A  24      -0.158  26.839  23.675  1.00 32.95           C  
ANISOU   72  CD2 LEU A  24     3358   6657   2504  -2905   -705   1952       C  
ATOM     73  N   VAL A  25       4.513  26.507  23.784  1.00 10.86           N  
ANISOU   73  N   VAL A  25      957   1645   1524    125    188    111       N  
ATOM     74  CA  VAL A  25       5.817  25.953  23.400  1.00 10.36           C  
ANISOU   74  CA  VAL A  25     1037   1487   1412     54    252    -27       C  
ATOM     75  C   VAL A  25       5.606  24.686  22.612  1.00 10.22           C  
ANISOU   75  C   VAL A  25      968   1495   1421     58    207     12       C  
ATOM     76  O   VAL A  25       4.980  23.737  23.092  1.00 11.79           O  
ANISOU   76  O   VAL A  25     1424   1533   1524      1    359    -41       O  
ATOM     77  CB  VAL A  25       6.636  25.727  24.670  1.00 10.63           C  
ANISOU   77  CB  VAL A  25     1009   1564   1468     46    154     78       C  
ATOM     78  CG1 VAL A  25       7.941  25.001  24.322  1.00 11.96           C  
ANISOU   78  CG1 VAL A  25     1051   1749   1744    170    117    -25       C  
ATOM     79  CG2 VAL A  25       6.902  27.013  25.399  1.00 11.33           C  
ANISOU   79  CG2 VAL A  25     1346   1659   1299     33    239     27       C  
ATOM     80  N   ILE A  26       6.140  24.640  21.386  1.00 10.72           N  
ANISOU   80  N   ILE A  26     1003   1582   1489    -15    252    -75       N  
ATOM     81  CA  ILE A  26       6.018  23.480  20.509  1.00 10.47           C  
ANISOU   81  CA  ILE A  26     1064   1486   1426    -53    206    -46       C  
ATOM     82  C   ILE A  26       7.317  22.691  20.608  1.00 10.18           C  
ANISOU   82  C   ILE A  26     1100   1466   1303    -51    183   -105       C  
ATOM     83  O   ILE A  26       8.347  23.100  20.094  1.00 11.35           O  
ANISOU   83  O   ILE A  26     1066   1596   1651    -41    296     31       O  
ATOM     84  CB  ILE A  26       5.736  23.863  19.055  1.00 11.92           C  
ANISOU   84  CB  ILE A  26     1221   1794   1513     58    165     42       C  
ATOM     85  CG1 ILE A  26       4.587  24.842  18.897  1.00 13.81           C  
ANISOU   85  CG1 ILE A  26     1229   2132   1887    200    160    157       C  
ATOM     86  CG2 ILE A  26       5.477  22.599  18.249  1.00 12.97           C  
ANISOU   86  CG2 ILE A  26     1167   2272   1488    -25    269   -316       C  
ATOM     87  CD1 ILE A  26       4.482  25.459  17.523  1.00 19.18           C  
ANISOU   87  CD1 ILE A  26     1857   3392   2040    742     26    499       C  
ATOM     88  N   GLY A  27       7.237  21.560  21.313  1.00 10.57           N  
ANISOU   88  N   GLY A  27     1068   1484   1464     64    272    -23       N  
ATOM     89  CA  GLY A  27       8.370  20.682  21.531  1.00 11.29           C  
ANISOU   89  CA  GLY A  27     1157   1528   1605    101    165     43       C  
ATOM     90  C   GLY A  27       8.717  20.632  22.996  1.00 10.64           C  
ANISOU   90  C   GLY A  27     1042   1512   1489    -51    186    -58       C  
ATOM     91  O   GLY A  27       8.977  21.665  23.635  1.00 12.58           O  
ANISOU   91  O   GLY A  27     1514   1592   1672    -26    243    -47       O  
ATOM     92  N   GLY A  28       8.823  19.441  23.561  1.00 11.36           N  
ANISOU   92  N   GLY A  28     1263   1565   1488     44    226    -20       N  
ATOM     93  CA  GLY A  28       9.146  19.182  24.942  1.00 11.40           C  
ANISOU   93  CA  GLY A  28     1083   1714   1533    -69    246     99       C  
ATOM     94  C   GLY A  28      10.520  18.549  25.142  1.00 10.18           C  
ANISOU   94  C   GLY A  28     1073   1386   1408    -77    258    -17       C  
ATOM     95  O   GLY A  28      10.694  17.648  25.960  1.00 11.34           O  
ANISOU   95  O   GLY A  28     1317   1588   1406    -37    273     93       O  
ATOM     96  N   GLY A  29      11.515  19.041  24.399  1.00 11.39           N  
ANISOU   96  N   GLY A  29     1070   1663   1595     30    174    239       N  
ATOM     97  CA  GLY A  29      12.902  18.749  24.576  1.00 10.63           C  
ANISOU   97  CA  GLY A  29     1001   1605   1431    121    226     -8       C  
ATOM     98  C   GLY A  29      13.589  19.812  25.378  1.00  9.83           C  
ANISOU   98  C   GLY A  29     1107   1370   1258    158    239     21       C  
ATOM     99  O   GLY A  29      12.970  20.598  26.130  1.00 11.01           O  
ANISOU   99  O   GLY A  29     1087   1666   1430     97    346    -46       O  
ATOM    100  N   SER A  30      14.916  19.862  25.321  1.00 10.64           N  
ANISOU  100  N   SER A  30     1010   1629   1403     52    254   -111       N  
ATOM    101  CA  SER A  30      15.680  20.723  26.197  1.00 11.86           C  
ANISOU  101  CA  SER A  30     1382   1448   1677     76     82   -159       C  
ATOM    102  C   SER A  30      15.258  22.164  26.158  1.00 10.24           C  
ANISOU  102  C   SER A  30      952   1507   1434     54    225   -137       C  
ATOM    103  O   SER A  30      15.062  22.818  27.208  1.00 11.46           O  
ANISOU  103  O   SER A  30     1210   1714   1431     57    196   -235       O  
ATOM    104  CB  SER A  30      17.201  20.612  25.763  1.00 16.24           C  
ANISOU  104  CB  SER A  30     1062   1730   3377    402   -667   -810       C  
ATOM    105  OG  SER A  30      17.679  19.291  25.972  1.00 18.11           O  
ANISOU  105  OG  SER A  30     1600   2107   3174    438    -15    202       O  
ATOM    106  N   GLY A  31      15.183  22.723  24.957  1.00 10.79           N  
ANISOU  106  N   GLY A  31     1097   1588   1416    139    353   -101       N  
ATOM    107  CA  GLY A  31      14.864  24.117  24.803  1.00 11.16           C  
ANISOU  107  CA  GLY A  31     1255   1589   1396     -3    453    -24       C  
ATOM    108  C   GLY A  31      13.435  24.474  25.220  1.00  9.82           C  
ANISOU  108  C   GLY A  31     1118   1398   1214     88    239     63       C  
ATOM    109  O   GLY A  31      13.214  25.458  25.949  1.00 10.79           O  
ANISOU  109  O   GLY A  31     1147   1551   1402     -3    349   -159       O  
ATOM    110  N   GLY A  32      12.486  23.652  24.814  1.00  9.92           N  
ANISOU  110  N   GLY A  32     1069   1384   1318    189    306   -137       N  
ATOM    111  CA  GLY A  32      11.082  23.924  25.146  1.00 10.32           C  
ANISOU  111  CA  GLY A  32     1017   1546   1359    199    246   -114       C  
ATOM    112  C   GLY A  32      10.779  23.762  26.599  1.00 10.15           C  
ANISOU  112  C   GLY A  32      974   1565   1317    -42    252   -104       C  
ATOM    113  O   GLY A  32      10.110  24.598  27.235  1.00 10.73           O  
ANISOU  113  O   GLY A  32     1016   1673   1387    147    199   -253       O  
ATOM    114  N   LEU A  33      11.288  22.675  27.204  1.00 10.01           N  
ANISOU  114  N   LEU A  33      980   1598   1227    120    355   -163       N  
ATOM    115  CA  LEU A  33      11.112  22.456  28.635  1.00 10.05           C  
ANISOU  115  CA  LEU A  33      923   1679   1217    -30    272   -130       C  
ATOM    116  C   LEU A  33      11.677  23.602  29.424  1.00  9.74           C  
ANISOU  116  C   LEU A  33      961   1520   1218     85    119    -41       C  
ATOM    117  O   LEU A  33      11.060  24.155  30.362  1.00 10.54           O  
ANISOU  117  O   LEU A  33     1129   1593   1281     88    372    -89       O  
ATOM    118  CB  LEU A  33      11.719  21.132  29.103  1.00 11.49           C  
ANISOU  118  CB  LEU A  33     1381   1630   1356    -65    333    -64       C  
ATOM    119  CG  LEU A  33      11.138  19.828  28.575  1.00 12.32           C  
ANISOU  119  CG  LEU A  33     1544   1664   1474   -184    570     17       C  
ATOM    120  CD1 LEU A  33      12.019  18.658  28.969  1.00 13.26           C  
ANISOU  120  CD1 LEU A  33     1862   1631   1545   -182    310     43       C  
ATOM    121  CD2 LEU A  33       9.723  19.650  29.091  1.00 18.26           C  
ANISOU  121  CD2 LEU A  33     1582   2408   2947   -491    850   -508       C  
ATOM    122  N   ALA A  34      12.921  23.984  29.128  1.00  9.72           N  
ANISOU  122  N   ALA A  34      940   1493   1259     87    350    -85       N  
ATOM    123  CA  ALA A  34      13.578  24.998  29.929  1.00  9.81           C  
ANISOU  123  CA  ALA A  34     1011   1431   1285    143    158    -27       C  
ATOM    124  C   ALA A  34      12.858  26.334  29.759  1.00  9.34           C  
ANISOU  124  C   ALA A  34      858   1448   1243     82    286     52       C  
ATOM    125  O   ALA A  34      12.688  27.096  30.752  1.00  9.68           O  
ANISOU  125  O   ALA A  34      970   1496   1212    101    219    -64       O  
ATOM    126  CB  ALA A  34      15.037  25.143  29.544  1.00 12.36           C  
ANISOU  126  CB  ALA A  34      956   1720   2022    194    236   -409       C  
ATOM    127  N   SER A  35      12.467  26.703  28.557  1.00  9.33           N  
ANISOU  127  N   SER A  35      944   1430   1172    112    289    130       N  
ATOM    128  CA  SER A  35      11.838  27.990  28.354  1.00  9.43           C  
ANISOU  128  CA  SER A  35      844   1462   1277     61    224     -5       C  
ATOM    129  C   SER A  35      10.446  28.026  29.064  1.00  9.33           C  
ANISOU  129  C   SER A  35      915   1401   1228     77    238    -81       C  
ATOM    130  O   SER A  35      10.112  28.999  29.743  1.00  9.68           O  
ANISOU  130  O   SER A  35      992   1414   1272     69    350    -21       O  
ATOM    131  CB  SER A  35      11.675  28.295  26.885  1.00 10.37           C  
ANISOU  131  CB  SER A  35     1120   1600   1219    213    332    174       C  
ATOM    132  OG  SER A  35      11.437  29.678  26.677  1.00 10.39           O  
ANISOU  132  OG  SER A  35     1038   1499   1410    134    306     62       O  
ATOM    133  N   ALA A  36       9.682  26.953  28.911  1.00  9.40           N  
ANISOU  133  N   ALA A  36      831   1503   1238     86    341   -200       N  
ATOM    134  CA  ALA A  36       8.342  26.903  29.562  1.00  9.47           C  
ANISOU  134  CA  ALA A  36      968   1456   1173     31    346    -54       C  
ATOM    135  C   ALA A  36       8.472  26.980  31.075  1.00  9.60           C  
ANISOU  135  C   ALA A  36      948   1416   1284    -62    388    -59       C  
ATOM    136  O   ALA A  36       7.695  27.685  31.742  1.00 10.01           O  
ANISOU  136  O   ALA A  36     1013   1483   1308     18    465    -40       O  
ATOM    137  CB  ALA A  36       7.634  25.629  29.150  1.00 10.57           C  
ANISOU  137  CB  ALA A  36      948   1719   1350   -125    354   -123       C  
ATOM    138  N   ARG A  37       9.424  26.245  31.646  1.00  9.48           N  
ANISOU  138  N   ARG A  37      905   1498   1197    -42    344    -16       N  
ATOM    139  CA  ARG A  37       9.575  26.233  33.112  1.00  9.80           C  
ANISOU  139  CA  ARG A  37      975   1486   1262    -49    385     -5       C  
ATOM    140  C   ARG A  37       9.971  27.611  33.629  1.00 10.00           C  
ANISOU  140  C   ARG A  37     1031   1540   1228     89    281   -117       C  
ATOM    141  O   ARG A  37       9.453  28.065  34.653  1.00 10.32           O  
ANISOU  141  O   ARG A  37     1111   1523   1285     59    377    -87       O  
ATOM    142  CB AARG A  37      10.586  25.166  33.492  0.45 12.25           C  
ANISOU  142  CB AARG A  37     1459   1518   1677     75   -196   -111       C  
ATOM    143  CB BARG A  37      10.539  25.158  33.580  0.55  9.81           C  
ANISOU  143  CB BARG A  37      971   1569   1187    -46    494    152       C  
ATOM    144  CG AARG A  37       9.883  23.809  33.399  0.45 13.72           C  
ANISOU  144  CG AARG A  37     1504   1516   2192     86    115   -159       C  
ATOM    145  CG BARG A  37      10.025  23.764  33.250  0.55 12.06           C  
ANISOU  145  CG BARG A  37     1115   1541   1925    -78    503    201       C  
ATOM    146  CD AARG A  37       9.395  23.426  34.799  0.45 19.74           C  
ANISOU  146  CD AARG A  37     2911   2048   2540   -114    336    454       C  
ATOM    147  CD BARG A  37      10.997  22.639  33.574  0.55 12.27           C  
ANISOU  147  CD BARG A  37      998   1592   2074    -83    121    -32       C  
ATOM    148  NE AARG A  37      10.390  22.780  35.558  0.45 20.83           N  
ANISOU  148  NE AARG A  37     3379   2036   2497    308    330    364       N  
ATOM    149  NE BARG A  37      11.297  22.576  34.984  0.55 12.58           N  
ANISOU  149  NE BARG A  37     1565   1417   1796    148    715    137       N  
ATOM    150  CZ AARG A  37      10.776  22.350  36.725  0.45 16.73           C  
ANISOU  150  CZ AARG A  37     1832   2199   2326    -64    695    314       C  
ATOM    151  CZ BARG A  37      12.291  21.842  35.503  0.55 12.40           C  
ANISOU  151  CZ BARG A  37     1252   1630   1828    -41    594    260       C  
ATOM    152  NH1AARG A  37       9.964  22.571  37.744  0.45 24.02           N  
ANISOU  152  NH1AARG A  37     2722   3760   2645   1027    937   -284       N  
ATOM    153  NH1BARG A  37      13.083  21.118  34.721  0.55 17.62           N  
ANISOU  153  NH1BARG A  37     1637   1810   3247    389   1551    640       N  
ATOM    154  NH2AARG A  37      11.956  21.710  36.844  0.45 15.72           N  
ANISOU  154  NH2AARG A  37     1126   2251   2595   -661    573    -41       N  
ATOM    155  NH2BARG A  37      12.509  21.813  36.808  0.55 19.69           N  
ANISOU  155  NH2BARG A  37     2073   3434   1975   -851    250    770       N  
ATOM    156  N   ARG A  38      10.868  28.316  32.917  1.00  9.47           N  
ANISOU  156  N   ARG A  38      894   1446   1259     91    371    -94       N  
ATOM    157  CA  ARG A  38      11.249  29.645  33.389  1.00 10.01           C  
ANISOU  157  CA  ARG A  38     1045   1492   1266     74    312    -57       C  
ATOM    158  C   ARG A  38      10.106  30.633  33.209  1.00  9.88           C  
ANISOU  158  C   ARG A  38     1011   1419   1325     65    295    -70       C  
ATOM    159  O   ARG A  38       9.867  31.457  34.111  1.00 10.73           O  
ANISOU  159  O   ARG A  38     1151   1534   1392     89    325   -162       O  
ATOM    160  CB  ARG A  38      12.538  30.125  32.689  1.00 10.28           C  
ANISOU  160  CB  ARG A  38     1015   1503   1386     76    321    -82       C  
ATOM    161  CG  ARG A  38      13.090  31.396  33.216  1.00 11.28           C  
ANISOU  161  CG  ARG A  38      972   1640   1672    -15    260   -135       C  
ATOM    162  CD  ARG A  38      13.376  31.406  34.741  1.00 12.03           C  
ANISOU  162  CD  ARG A  38     1265   1754   1552    -22    316   -376       C  
ATOM    163  NE  ARG A  38      14.266  30.346  35.090  1.00 12.36           N  
ANISOU  163  NE  ARG A  38     1369   1800   1528   -130    188    -28       N  
ATOM    164  CZ  ARG A  38      15.572  30.311  34.945  1.00 12.47           C  
ANISOU  164  CZ  ARG A  38     1419   1595   1725     -7    127   -198       C  
ATOM    165  NH1 ARG A  38      16.270  29.231  35.254  1.00 14.37           N  
ANISOU  165  NH1 ARG A  38     1787   1839   1835    281     28   -111       N  
ATOM    166  NH2 ARG A  38      16.210  31.371  34.501  1.00 14.19           N  
ANISOU  166  NH2 ARG A  38     1181   1871   2341     54    144    248       N  
ATOM    167  N   ALA A  39       9.362  30.556  32.103  1.00  9.89           N  
ANISOU  167  N   ALA A  39      914   1501   1342    -29    347    -17       N  
ATOM    168  CA  ALA A  39       8.227  31.440  31.904  1.00  9.90           C  
ANISOU  168  CA  ALA A  39     1038   1388   1334    128    385    -19       C  
ATOM    169  C   ALA A  39       7.197  31.234  33.024  1.00 10.57           C  
ANISOU  169  C   ALA A  39     1053   1486   1477    107    410    -24       C  
ATOM    170  O   ALA A  39       6.650  32.201  33.571  1.00 10.32           O  
ANISOU  170  O   ALA A  39     1119   1464   1339    162    404    -84       O  
ATOM    171  CB  ALA A  39       7.573  31.119  30.562  1.00 10.89           C  
ANISOU  171  CB  ALA A  39     1205   1542   1391    181    223    -22       C  
ATOM    172  N   ALA A  40       6.921  29.982  33.397  1.00 10.30           N  
ANISOU  172  N   ALA A  40     1129   1507   1277    123    499    -13       N  
ATOM    173  CA  ALA A  40       5.953  29.693  34.468  1.00 10.97           C  
ANISOU  173  CA  ALA A  40     1015   1556   1596     79    480    -61       C  
ATOM    174  C   ALA A  40       6.431  30.264  35.788  1.00 10.70           C  
ANISOU  174  C   ALA A  40     1165   1426   1475     86    525     10       C  
ATOM    175  O   ALA A  40       5.597  30.753  36.590  1.00 11.54           O  
ANISOU  175  O   ALA A  40     1209   1661   1516     37    574    -50       O  
ATOM    176  CB  ALA A  40       5.722  28.196  34.533  1.00 11.92           C  
ANISOU  176  CB  ALA A  40     1468   1569   1493    -95    635    -26       C  
ATOM    177  N   GLU A  41       7.723  30.190  36.091  1.00 11.32           N  
ANISOU  177  N   GLU A  41     1218   1795   1289    260    458    147       N  
ATOM    178  CA  GLU A  41       8.229  30.843  37.291  1.00 12.33           C  
ANISOU  178  CA  GLU A  41     1432   2042   1212    182    396    160       C  
ATOM    179  C   GLU A  41       7.910  32.311  37.323  1.00 11.88           C  
ANISOU  179  C   GLU A  41     1282   1998   1235    -79    275     90       C  
ATOM    180  O   GLU A  41       7.708  32.862  38.445  1.00 14.61           O  
ANISOU  180  O   GLU A  41     2107   2175   1269    146    426    -12       O  
ATOM    181  CB AGLU A  41       9.759  30.788  37.441  0.48 13.82           C  
ANISOU  181  CB AGLU A  41     1435   2464   1352    197    265    286       C  
ATOM    182  CB BGLU A  41       9.731  30.504  37.444  0.52 14.54           C  
ANISOU  182  CB BGLU A  41     1387   2329   1809     93    181     63       C  
ATOM    183  CG AGLU A  41      10.320  29.439  37.747  0.48 12.33           C  
ANISOU  183  CG AGLU A  41     1156   2398   1129    249    411     76       C  
ATOM    184  CG BGLU A  41      10.438  31.062  38.654  0.52 17.53           C  
ANISOU  184  CG BGLU A  41     1585   3097   1979    132    132   -320       C  
ATOM    185  CD AGLU A  41      11.791  29.486  38.117  0.48 17.83           C  
ANISOU  185  CD AGLU A  41     1082   3035   2658    418    319   -119       C  
ATOM    186  CD BGLU A  41      11.950  30.899  38.563  0.52 23.74           C  
ANISOU  186  CD BGLU A  41     1628   3417   3977    765   -806   -512       C  
ATOM    187  OE1AGLU A  41      12.470  30.521  37.934  0.48 21.41           O  
ANISOU  187  OE1AGLU A  41     1094   3365   3674    207    -76    223       O  
ATOM    188  OE1BGLU A  41      12.358  29.776  38.215  0.52 27.64           O  
ANISOU  188  OE1BGLU A  41     2716   3646   4138   1493   -617   -144       O  
ATOM    189  OE2AGLU A  41      12.260  28.420  38.597  0.48 18.54           O  
ANISOU  189  OE2AGLU A  41     1083   3413   2548    449     96    161       O  
ATOM    190  OE2BGLU A  41      12.690  31.876  38.768  0.52 32.00           O  
ANISOU  190  OE2BGLU A  41     1560   4790   5808     31   -430  -1552       O  
ATOM    191  N   LEU A  42       7.886  32.994  36.228  1.00 11.22           N  
ANISOU  191  N   LEU A  42     1267   1733   1265   -143    301     54       N  
ATOM    192  CA  LEU A  42       7.572  34.393  36.090  1.00 11.67           C  
ANISOU  192  CA  LEU A  42     1488   1591   1356   -207    286    -83       C  
ATOM    193  C   LEU A  42       6.078  34.677  36.001  1.00 12.02           C  
ANISOU  193  C   LEU A  42     1513   1647   1408     50    582   -142       C  
ATOM    194  O   LEU A  42       5.653  35.828  35.884  1.00 14.73           O  
ANISOU  194  O   LEU A  42     1954   1574   2067     35    798     -3       O  
ATOM    195  CB  LEU A  42       8.327  34.937  34.894  1.00 12.74           C  
ANISOU  195  CB  LEU A  42     1385   2047   1409   -394    224    207       C  
ATOM    196  CG  LEU A  42       9.838  34.867  34.993  1.00 14.25           C  
ANISOU  196  CG  LEU A  42     1420   2395   1598   -327    129    276       C  
ATOM    197  CD1 LEU A  42      10.553  35.048  33.669  1.00 13.97           C  
ANISOU  197  CD1 LEU A  42     1471   2008   1829   -270    365     43       C  
ATOM    198  CD2 LEU A  42      10.320  35.925  35.999  1.00 24.04           C  
ANISOU  198  CD2 LEU A  42     2482   4784   1866  -1952    422   -562       C  
ATOM    199  N   GLY A  43       5.248  33.642  36.116  1.00 11.62           N  
ANISOU  199  N   GLY A  43     1203   1617   1595     73    362   -162       N  
ATOM    200  CA  GLY A  43       3.790  33.781  36.161  1.00 11.96           C  
ANISOU  200  CA  GLY A  43     1271   1715   1559    144    320   -133       C  
ATOM    201  C   GLY A  43       3.063  33.444  34.917  1.00 11.00           C  
ANISOU  201  C   GLY A  43     1183   1519   1475    133    421    -39       C  
ATOM    202  O   GLY A  43       1.835  33.492  34.893  1.00 12.20           O  
ANISOU  202  O   GLY A  43     1059   1765   1811     41    460   -246       O  
ATOM    203  N   ALA A  44       3.778  33.165  33.824  1.00 11.19           N  
ANISOU  203  N   ALA A  44     1045   1722   1484    146    391   -106       N  
ATOM    204  CA  ALA A  44       3.091  32.858  32.556  1.00 11.77           C  
ANISOU  204  CA  ALA A  44      994   1729   1750    130    209   -397       C  
ATOM    205  C   ALA A  44       2.208  31.632  32.699  1.00 12.42           C  
ANISOU  205  C   ALA A  44      869   1850   2000    254    365   -414       C  
ATOM    206  O   ALA A  44       2.666  30.632  33.274  1.00 13.35           O  
ANISOU  206  O   ALA A  44     1262   1873   1939    214    479   -220       O  
ATOM    207  CB  ALA A  44       4.118  32.642  31.461  1.00 12.14           C  
ANISOU  207  CB  ALA A  44     1312   1857   1445    173    272    -86       C  
ATOM    208  N   ARG A  45       1.063  31.664  32.093  1.00 13.49           N  
ANISOU  208  N   ARG A  45     1000   2084   2040     -6    281   -573       N  
ATOM    209  CA  ARG A  45       0.159  30.580  31.794  1.00 14.32           C  
ANISOU  209  CA  ARG A  45     1079   2063   2297   -128    465   -650       C  
ATOM    210  C   ARG A  45       0.628  29.875  30.513  1.00 12.80           C  
ANISOU  210  C   ARG A  45     1132   1826   1906      6    163   -413       C  
ATOM    211  O   ARG A  45       0.503  30.398  29.431  1.00 15.49           O  
ANISOU  211  O   ARG A  45     1463   2269   2152    521    -47   -298       O  
ATOM    212  CB  ARG A  45      -1.236  31.165  31.571  1.00 16.20           C  
ANISOU  212  CB  ARG A  45     1056   2547   2553     -4    313   -753       C  
ATOM    213  CG  ARG A  45      -1.814  31.910  32.770  1.00 15.59           C  
ANISOU  213  CG  ARG A  45     1461   2439   2023    291    418   -156       C  
ATOM    214  CD  ARG A  45      -2.973  32.925  32.511  1.00 16.37           C  
ANISOU  214  CD  ARG A  45     1607   2443   2170    314    493   -340       C  
ATOM    215  NE  ARG A  45      -2.491  34.124  31.842  1.00 18.72           N  
ANISOU  215  NE  ARG A  45     2117   2359   2636    622    426    -94       N  
ATOM    216  CZ  ARG A  45      -3.253  35.185  31.533  1.00 20.06           C  
ANISOU  216  CZ  ARG A  45     2166   2983   2472   1020    698    228       C  
ATOM    217  NH1 ARG A  45      -4.525  35.223  31.857  1.00 21.76           N  
ANISOU  217  NH1 ARG A  45     2048   3408   2813    912    454    -49       N  
ATOM    218  NH2 ARG A  45      -2.755  36.273  30.900  1.00 21.82           N  
ANISOU  218  NH2 ARG A  45     2161   3095   3035    637   -264    701       N  
ATOM    219  N   ALA A  46       1.326  28.729  30.748  1.00 13.69           N  
ANISOU  219  N   ALA A  46     1359   1866   1976    146    455   -267       N  
ATOM    220  CA  ALA A  46       2.058  28.094  29.665  1.00 12.42           C  
ANISOU  220  CA  ALA A  46     1374   1686   1660    152    269   -218       C  
ATOM    221  C   ALA A  46       1.542  26.691  29.374  1.00 11.07           C  
ANISOU  221  C   ALA A  46     1078   1619   1507    316    295    -20       C  
ATOM    222  O   ALA A  46       1.017  25.989  30.226  1.00 12.15           O  
ANISOU  222  O   ALA A  46     1346   1777   1494    142    489      4       O  
ATOM    223  CB  ALA A  46       3.557  27.975  30.001  1.00 14.73           C  
ANISOU  223  CB  ALA A  46     1224   1968   2405    -15    529   -280       C  
ATOM    224  N   ALA A  47       1.803  26.258  28.139  1.00 11.42           N  
ANISOU  224  N   ALA A  47     1297   1575   1467    121    455    -14       N  
ATOM    225  CA  ALA A  47       1.539  24.895  27.705  1.00 11.75           C  
ANISOU  225  CA  ALA A  47     1109   1705   1651     -2    358   -133       C  
ATOM    226  C   ALA A  47       2.704  24.431  26.826  1.00 11.26           C  
ANISOU  226  C   ALA A  47     1172   1556   1549     26    291    -37       C  
ATOM    227  O   ALA A  47       3.225  25.251  26.049  1.00 12.10           O  
ANISOU  227  O   ALA A  47     1429   1593   1576     30    560     -3       O  
ATOM    228  CB  ALA A  47       0.216  24.774  26.976  1.00 13.29           C  
ANISOU  228  CB  ALA A  47     1107   1983   1960    175    311   -142       C  
ATOM    229  N   VAL A  48       3.036  23.157  26.915  1.00 10.79           N  
ANISOU  229  N   VAL A  48     1128   1632   1338     33    439     -7       N  
ATOM    230  CA  VAL A  48       4.024  22.475  26.075  1.00 10.64           C  
ANISOU  230  CA  VAL A  48     1162   1445   1437    -19    382    -74       C  
ATOM    231  C   VAL A  48       3.329  21.418  25.222  1.00 10.83           C  
ANISOU  231  C   VAL A  48      947   1662   1507    -82    436    -93       C  
ATOM    232  O   VAL A  48       2.617  20.578  25.792  1.00 12.17           O  
ANISOU  232  O   VAL A  48     1220   1827   1577   -260    402   -193       O  
ATOM    233  CB  VAL A  48       5.121  21.832  26.930  1.00 11.14           C  
ANISOU  233  CB  VAL A  48     1185   1554   1494     59    358    -96       C  
ATOM    234  CG1 VAL A  48       6.027  20.928  26.099  1.00 12.62           C  
ANISOU  234  CG1 VAL A  48     1342   1738   1715    187    443   -109       C  
ATOM    235  CG2 VAL A  48       5.942  22.869  27.658  1.00 12.13           C  
ANISOU  235  CG2 VAL A  48     1280   1750   1580   -112    253    -52       C  
ATOM    236  N   VAL A  49       3.545  21.467  23.933  1.00 11.10           N  
ANISOU  236  N   VAL A  49     1159   1531   1526    -80    289    -48       N  
ATOM    237  CA  VAL A  49       3.047  20.438  22.999  1.00 11.09           C  
ANISOU  237  CA  VAL A  49     1126   1553   1534    -93    305    -89       C  
ATOM    238  C   VAL A  49       4.157  19.458  22.749  1.00 11.48           C  
ANISOU  238  C   VAL A  49     1009   1720   1633    -95    300   -237       C  
ATOM    239  O   VAL A  49       5.291  19.852  22.409  1.00 12.35           O  
ANISOU  239  O   VAL A  49     1181   1712   1800    -81    361   -267       O  
ATOM    240  CB  VAL A  49       2.546  21.058  21.689  1.00 12.44           C  
ANISOU  240  CB  VAL A  49     1309   1836   1583    -59    197   -127       C  
ATOM    241  CG1 VAL A  49       1.804  20.017  20.908  1.00 13.69           C  
ANISOU  241  CG1 VAL A  49     1224   2152   1825    -89    -34   -239       C  
ATOM    242  CG2 VAL A  49       1.677  22.286  21.879  1.00 15.12           C  
ANISOU  242  CG2 VAL A  49     1738   2006   2002    246     79    -97       C  
ATOM    243  N   GLU A  50       3.867  18.168  22.844  1.00 11.63           N  
ANISOU  243  N   GLU A  50     1041   1653   1724    -97    258   -295       N  
ATOM    244  CA  GLU A  50       4.884  17.126  22.625  1.00 11.90           C  
ANISOU  244  CA  GLU A  50     1243   1605   1675    -39    281   -180       C  
ATOM    245  C   GLU A  50       4.208  15.936  21.918  1.00 11.74           C  
ANISOU  245  C   GLU A  50     1145   1624   1693      8    200   -209       C  
ATOM    246  O   GLU A  50       3.249  15.367  22.435  1.00 13.13           O  
ANISOU  246  O   GLU A  50     1300   1907   1782   -155    262   -137       O  
ATOM    247  CB  GLU A  50       5.566  16.687  23.873  1.00 12.82           C  
ANISOU  247  CB  GLU A  50     1150   1914   1808    -92    207    -87       C  
ATOM    248  CG  GLU A  50       6.556  15.514  23.769  1.00 13.09           C  
ANISOU  248  CG  GLU A  50     1252   1821   1899   -112    134   -127       C  
ATOM    249  CD  GLU A  50       7.586  15.741  22.684  1.00 12.99           C  
ANISOU  249  CD  GLU A  50     1303   1806   1827   -229    293   -247       C  
ATOM    250  OE1 GLU A  50       8.377  16.731  22.831  1.00 13.42           O  
ANISOU  250  OE1 GLU A  50     1314   1700   2086   -117    163   -235       O  
ATOM    251  OE2 GLU A  50       7.706  14.902  21.757  1.00 13.74           O  
ANISOU  251  OE2 GLU A  50     1338   1689   2195   -180    304   -319       O  
ATOM    252  N   SER A  51       4.762  15.547  20.758  1.00 12.06           N  
ANISOU  252  N   SER A  51     1185   1788   1611    -28     85   -280       N  
ATOM    253  CA  SER A  51       4.193  14.443  20.000  1.00 13.16           C  
ANISOU  253  CA  SER A  51     1264   1929   1806     50     64   -408       C  
ATOM    254  C   SER A  51       4.718  13.081  20.389  1.00 13.02           C  
ANISOU  254  C   SER A  51     1126   1778   2044   -118     47   -386       C  
ATOM    255  O   SER A  51       4.082  12.068  20.064  1.00 15.26           O  
ANISOU  255  O   SER A  51     1497   1997   2304   -135   -140   -478       O  
ATOM    256  CB  SER A  51       4.500  14.687  18.522  1.00 14.75           C  
ANISOU  256  CB  SER A  51     1738   2056   1810    -57     97   -476       C  
ATOM    257  OG  SER A  51       5.899  14.803  18.314  1.00 16.13           O  
ANISOU  257  OG  SER A  51     1780   2287   2061     55    425   -281       O  
ATOM    258  N   HIS A  52       5.869  13.028  21.042  1.00 13.05           N  
ANISOU  258  N   HIS A  52     1236   1675   2049    -98     60   -307       N  
ATOM    259  CA  HIS A  52       6.550  11.795  21.414  1.00 13.69           C  
ANISOU  259  CA  HIS A  52     1267   1659   2276   -237    -46   -164       C  
ATOM    260  C   HIS A  52       6.878  11.821  22.891  1.00 14.57           C  
ANISOU  260  C   HIS A  52     1473   1918   2144    -44     72   -142       C  
ATOM    261  O   HIS A  52       5.963  11.876  23.710  1.00 17.97           O  
ANISOU  261  O   HIS A  52     1430   2997   2402    163     73    261       O  
ATOM    262  CB  HIS A  52       7.748  11.584  20.479  1.00 15.77           C  
ANISOU  262  CB  HIS A  52     1736   1980   2277    264    234   -251       C  
ATOM    263  CG  HIS A  52       7.322  11.291  19.063  1.00 20.14           C  
ANISOU  263  CG  HIS A  52     2449   2781   2421    257    100   -472       C  
ATOM    264  ND1 HIS A  52       6.910  12.283  18.164  1.00 21.65           N  
ANISOU  264  ND1 HIS A  52     2910   2958   2357    695    -53   -532       N  
ATOM    265  CD2 HIS A  52       7.230  10.118  18.394  1.00 30.14           C  
ANISOU  265  CD2 HIS A  52     5466   3074   2911   1551   -758  -1098       C  
ATOM    266  CE1 HIS A  52       6.601  11.716  17.005  1.00 21.24           C  
ANISOU  266  CE1 HIS A  52     2618   3045   2407    200    145   -580       C  
ATOM    267  NE2 HIS A  52       6.780  10.386  17.102  1.00 32.02           N  
ANISOU  267  NE2 HIS A  52     5678   3220   3268   1279  -1372  -1027       N  
ATOM    268  N   LYS A  53       8.129  11.700  23.282  1.00 15.59           N  
ANISOU  268  N   LYS A  53     1315   2518   2091   -260     55   -373       N  
ATOM    269  CA  LYS A  53       8.487  11.571  24.683  1.00 14.84           C  
ANISOU  269  CA  LYS A  53     1474   2044   2119    -99    122   -300       C  
ATOM    270  C   LYS A  53       9.153  12.824  25.209  1.00 13.78           C  
ANISOU  270  C   LYS A  53     1435   1990   1811   -145    146   -120       C  
ATOM    271  O   LYS A  53      10.067  13.443  24.633  1.00 13.92           O  
ANISOU  271  O   LYS A  53     1306   1902   2082    -62    211    -35       O  
ATOM    272  CB  LYS A  53       9.467  10.401  24.887  1.00 17.35           C  
ANISOU  272  CB  LYS A  53     1814   2130   2650    123   -213   -549       C  
ATOM    273  CG  LYS A  53       8.726   9.045  24.668  1.00 20.63           C  
ANISOU  273  CG  LYS A  53     2256   2133   3451     46   -784   -350       C  
ATOM    274  CD  LYS A  53       9.616   7.897  25.127  1.00 24.10           C  
ANISOU  274  CD  LYS A  53     2197   2324   4635     47   -538      1       C  
ATOM    275  CE  LYS A  53       8.916   6.544  24.882  1.00 26.82           C  
ANISOU  275  CE  LYS A  53     3498   2140   4552    -21   -791   -178       C  
ATOM    276  NZ  LYS A  53       9.897   5.410  24.913  1.00 29.11           N  
ANISOU  276  NZ  LYS A  53     4269   2625   4168    600   -368   -345       N  
ATOM    277  N   LEU A  54       8.651  13.267  26.366  1.00 14.44           N  
ANISOU  277  N   LEU A  54     1475   2141   1869   -130    265   -154       N  
ATOM    278  CA  LEU A  54       9.256  14.405  27.032  1.00 12.70           C  
ANISOU  278  CA  LEU A  54     1473   1745   1608     95    240    147       C  
ATOM    279  C   LEU A  54      10.721  14.126  27.302  1.00 12.75           C  
ANISOU  279  C   LEU A  54     1427   1637   1780     95    189    236       C  
ATOM    280  O   LEU A  54      11.158  13.014  27.576  1.00 14.40           O  
ANISOU  280  O   LEU A  54     1683   1534   2253     36    127    261       O  
ATOM    281  CB  LEU A  54       8.506  14.717  28.347  1.00 14.34           C  
ANISOU  281  CB  LEU A  54     1661   2069   1718     -6    433     -3       C  
ATOM    282  CG  LEU A  54       7.102  15.275  28.155  1.00 14.62           C  
ANISOU  282  CG  LEU A  54     1739   2084   1731     42    510     67       C  
ATOM    283  CD1 LEU A  54       6.367  15.330  29.492  1.00 18.69           C  
ANISOU  283  CD1 LEU A  54     2086   2892   2125    548    903    299       C  
ATOM    284  CD2 LEU A  54       7.102  16.627  27.484  1.00 14.85           C  
ANISOU  284  CD2 LEU A  54     1591   2002   2047    -39    333    -53       C  
ATOM    285  N   GLY A  55      11.493  15.228  27.207  1.00 12.31           N  
ANISOU  285  N   GLY A  55     1313   1475   1889    171    272    -11       N  
ATOM    286  CA  GLY A  55      12.928  15.147  27.256  1.00 12.17           C  
ANISOU  286  CA  GLY A  55     1311   1612   1700    217    156     10       C  
ATOM    287  C   GLY A  55      13.608  15.191  25.918  1.00 11.67           C  
ANISOU  287  C   GLY A  55     1101   1584   1750    100    133     43       C  
ATOM    288  O   GLY A  55      14.841  15.423  25.821  1.00 12.98           O  
ANISOU  288  O   GLY A  55     1375   1671   1886   -156    153     12       O  
ATOM    289  N   GLY A  56      12.873  14.960  24.863  1.00 11.86           N  
ANISOU  289  N   GLY A  56     1125   1640   1742     70    205     -8       N  
ATOM    290  CA  GLY A  56      13.363  15.115  23.527  1.00 12.15           C  
ANISOU  290  CA  GLY A  56     1161   1688   1766    105    162    170       C  
ATOM    291  C   GLY A  56      14.602  14.305  23.236  1.00 10.56           C  
ANISOU  291  C   GLY A  56     1190   1374   1447     69    109     83       C  
ATOM    292  O   GLY A  56      14.786  13.204  23.716  1.00 11.69           O  
ANISOU  292  O   GLY A  56     1227   1445   1769     43    205    161       O  
ATOM    293  N   THR A  57      15.461  14.894  22.410  1.00 11.69           N  
ANISOU  293  N   THR A  57     1225   1473   1745    146    250    297       N  
ATOM    294  CA  THR A  57      16.662  14.192  21.965  1.00 11.79           C  
ANISOU  294  CA  THR A  57     1193   1451   1833     -3    327    201       C  
ATOM    295  C   THR A  57      17.600  13.937  23.130  1.00 11.97           C  
ANISOU  295  C   THR A  57     1237   1581   1729    172    453    334       C  
ATOM    296  O   THR A  57      18.134  12.824  23.210  1.00 12.82           O  
ANISOU  296  O   THR A  57     1304   1683   1885    313    507    374       O  
ATOM    297  CB  THR A  57      17.289  15.000  20.800  1.00 13.36           C  
ANISOU  297  CB  THR A  57     1612   1843   1621     96    418    222       C  
ATOM    298  OG1 THR A  57      16.301  15.015  19.755  1.00 14.85           O  
ANISOU  298  OG1 THR A  57     1845   2058   1738     13    219    136       O  
ATOM    299  CG2 THR A  57      18.589  14.375  20.329  1.00 14.76           C  
ANISOU  299  CG2 THR A  57     1535   2151   1920    -70    575     47       C  
ATOM    300  N   CYS A  58      17.777  14.917  24.005  1.00 12.60           N  
ANISOU  300  N   CYS A  58     1201   1566   2023     65     89    372       N  
ATOM    301  CA  CYS A  58      18.702  14.838  25.119  1.00 13.59           C  
ANISOU  301  CA  CYS A  58     1371   1743   2051    -76     13    488       C  
ATOM    302  C   CYS A  58      18.444  13.557  25.933  1.00 11.25           C  
ANISOU  302  C   CYS A  58     1021   1633   1622   -125    -11    248       C  
ATOM    303  O   CYS A  58      19.355  12.763  26.213  1.00 13.92           O  
ANISOU  303  O   CYS A  58     1054   1868   2366    -19    155    492       O  
ATOM    304  CB  CYS A  58      18.586  16.089  26.025  1.00 16.77           C  
ANISOU  304  CB  CYS A  58     1297   1557   3518   -234   -470    -42       C  
ATOM    305  SG  CYS A  58      19.650  16.191  27.449  1.00 15.40           S  
ANISOU  305  SG  CYS A  58     1356   2266   2230     50    242     50       S  
ATOM    306  N   VAL A  59      17.210  13.382  26.344  1.00 10.94           N  
ANISOU  306  N   VAL A  59      979   1447   1729     -8     23    120       N  
ATOM    307  CA  VAL A  59      16.904  12.261  27.256  1.00 10.15           C  
ANISOU  307  CA  VAL A  59     1051   1460   1344     61     16     64       C  
ATOM    308  C   VAL A  59      16.830  10.974  26.479  1.00  9.70           C  
ANISOU  308  C   VAL A  59      866   1496   1323    -18    171      6       C  
ATOM    309  O   VAL A  59      17.255   9.920  26.982  1.00 10.75           O  
ANISOU  309  O   VAL A  59     1033   1544   1509     49    225     69       O  
ATOM    310  CB  VAL A  59      15.551  12.541  27.955  1.00 11.76           C  
ANISOU  310  CB  VAL A  59     1082   1862   1525     56    148   -235       C  
ATOM    311  CG1 VAL A  59      15.008  11.285  28.623  1.00 13.17           C  
ANISOU  311  CG1 VAL A  59     1574   1997   1433    348    534     90       C  
ATOM    312  CG2 VAL A  59      15.690  13.728  28.922  1.00 13.84           C  
ANISOU  312  CG2 VAL A  59     1578   2090   1592    373    -32   -402       C  
ATOM    313  N   ASN A  60      16.204  10.960  25.288  1.00 10.09           N  
ANISOU  313  N   ASN A  60     1091   1470   1271     53    174    -15       N  
ATOM    314  CA  ASN A  60      15.761   9.715  24.692  1.00 10.18           C  
ANISOU  314  CA  ASN A  60     1024   1431   1412    -64    242      1       C  
ATOM    315  C   ASN A  60      16.770   9.136  23.689  1.00 10.88           C  
ANISOU  315  C   ASN A  60     1114   1420   1598      3    318    -28       C  
ATOM    316  O   ASN A  60      16.897   7.902  23.646  1.00 12.24           O  
ANISOU  316  O   ASN A  60     1284   1545   1820     -4    346    -64       O  
ATOM    317  CB  ASN A  60      14.399   9.932  24.002  1.00 10.02           C  
ANISOU  317  CB  ASN A  60     1055   1437   1316    -53    279     16       C  
ATOM    318  CG  ASN A  60      13.339  10.272  25.019  1.00 10.73           C  
ANISOU  318  CG  ASN A  60     1064   1631   1382    109    271     99       C  
ATOM    319  OD1 ASN A  60      12.873   9.387  25.756  1.00 11.41           O  
ANISOU  319  OD1 ASN A  60     1196   1618   1521     56    381     96       O  
ATOM    320  ND2 ASN A  60      12.975  11.521  25.134  1.00 12.01           N  
ANISOU  320  ND2 ASN A  60     1051   1658   1855     92    362    102       N  
ATOM    321  N   VAL A  61      17.429   9.925  22.872  1.00 10.82           N  
ANISOU  321  N   VAL A  61     1214   1578   1319    -69    366   -129       N  
ATOM    322  CA  VAL A  61      18.255   9.403  21.762  1.00 11.24           C  
ANISOU  322  CA  VAL A  61     1255   1643   1373    -58    259   -313       C  
ATOM    323  C   VAL A  61      19.525  10.236  21.582  1.00 11.12           C  
ANISOU  323  C   VAL A  61     1171   1532   1521     53    309   -188       C  
ATOM    324  O   VAL A  61      20.097  10.258  20.478  1.00 13.75           O  
ANISOU  324  O   VAL A  61     1260   2367   1598   -183    390   -355       O  
ATOM    325  CB  VAL A  61      17.442   9.318  20.439  1.00 12.75           C  
ANISOU  325  CB  VAL A  61     1471   1874   1498   -193    228   -317       C  
ATOM    326  CG1 VAL A  61      16.369   8.252  20.544  1.00 14.54           C  
ANISOU  326  CG1 VAL A  61     1486   2234   1803   -521    148   -239       C  
ATOM    327  CG2 VAL A  61      16.903  10.660  20.023  1.00 13.25           C  
ANISOU  327  CG2 VAL A  61     1545   2102   1387    128    280    -41       C  
ATOM    328  N   GLY A  62      20.024  10.880  22.616  1.00 10.64           N  
ANISOU  328  N   GLY A  62     1098   1480   1466    -81    317    -57       N  
ATOM    329  CA  GLY A  62      21.101  11.808  22.534  1.00 11.34           C  
ANISOU  329  CA  GLY A  62     1037   1638   1635      3    157     21       C  
ATOM    330  C   GLY A  62      22.014  11.728  23.734  1.00 10.50           C  
ANISOU  330  C   GLY A  62      978   1667   1345     68    283      3       C  
ATOM    331  O   GLY A  62      22.495  10.674  24.095  1.00 11.64           O  
ANISOU  331  O   GLY A  62     1108   1629   1686    168    224    105       O  
ATOM    332  N   CYS A  63      22.239  12.891  24.340  1.00 11.08           N  
ANISOU  332  N   CYS A  63     1021   1658   1529     11    202     49       N  
ATOM    333  CA  CYS A  63      23.169  13.127  25.436  1.00 11.46           C  
ANISOU  333  CA  CYS A  63     1111   1772   1471   -114    259     46       C  
ATOM    334  C   CYS A  63      23.179  11.986  26.450  1.00  9.98           C  
ANISOU  334  C   CYS A  63     1001   1540   1249     17    189   -182       C  
ATOM    335  O   CYS A  63      24.230  11.440  26.757  1.00 10.98           O  
ANISOU  335  O   CYS A  63      992   1610   1568    165    194   -166       O  
ATOM    336  CB  CYS A  63      22.806  14.429  26.187  1.00 14.47           C  
ANISOU  336  CB  CYS A  63     1757   1527   2214    -50    249   -168       C  
ATOM    337  SG  CYS A  63      22.536  15.849  25.127  1.00 13.71           S  
ANISOU  337  SG  CYS A  63     1503   1810   1896     90    337     27       S  
ATOM    338  N   VAL A  64      22.023  11.671  27.057  1.00 10.67           N  
ANISOU  338  N   VAL A  64      993   1560   1500    168    290     47       N  
ATOM    339  CA  VAL A  64      21.974  10.786  28.195  1.00 11.40           C  
ANISOU  339  CA  VAL A  64     1183   1738   1411    232    345     57       C  
ATOM    340  C   VAL A  64      22.308   9.350  27.787  1.00 10.22           C  
ANISOU  340  C   VAL A  64      958   1563   1363    136    450    164       C  
ATOM    341  O   VAL A  64      23.251   8.752  28.346  1.00 10.79           O  
ANISOU  341  O   VAL A  64      994   1707   1398    199    362     27       O  
ATOM    342  CB  VAL A  64      20.605  10.886  28.900  1.00 14.19           C  
ANISOU  342  CB  VAL A  64     1437   2155   1797    589    658    300       C  
ATOM    343  CG1 VAL A  64      20.515   9.784  29.940  1.00 19.00           C  
ANISOU  343  CG1 VAL A  64     2156   3174   1888   1094   1256    905       C  
ATOM    344  CG2 VAL A  64      20.456  12.251  29.542  1.00 16.85           C  
ANISOU  344  CG2 VAL A  64     1801   2740   1861    842    553   -208       C  
ATOM    345  N   PRO A  65      21.601   8.710  26.842  1.00 10.75           N  
ANISOU  345  N   PRO A  65      925   1546   1614     87    284    154       N  
ATOM    346  CA  PRO A  65      21.966   7.333  26.518  1.00 11.24           C  
ANISOU  346  CA  PRO A  65      895   1581   1793     33    298    116       C  
ATOM    347  C   PRO A  65      23.364   7.249  25.904  1.00  9.97           C  
ANISOU  347  C   PRO A  65      986   1489   1313     59    185     40       C  
ATOM    348  O   PRO A  65      24.046   6.229  26.113  1.00 10.40           O  
ANISOU  348  O   PRO A  65      959   1491   1501      4    228     54       O  
ATOM    349  CB  PRO A  65      20.835   6.842  25.609  1.00 12.39           C  
ANISOU  349  CB  PRO A  65     1090   1695   1924    -85    208    145       C  
ATOM    350  CG  PRO A  65      20.301   8.104  25.010  1.00 12.23           C  
ANISOU  350  CG  PRO A  65     1100   1820   1726    -80     83    269       C  
ATOM    351  CD  PRO A  65      20.377   9.147  26.108  1.00 11.79           C  
ANISOU  351  CD  PRO A  65      913   1876   1691    132    294    204       C  
ATOM    352  N   LYS A  66      23.779   8.259  25.179  1.00 10.10           N  
ANISOU  352  N   LYS A  66      962   1447   1430      3    220    110       N  
ATOM    353  CA  LYS A  66      25.181   8.266  24.672  1.00 10.08           C  
ANISOU  353  CA  LYS A  66      997   1613   1218    200    293    -72       C  
ATOM    354  C   LYS A  66      26.127   8.194  25.844  1.00  9.61           C  
ANISOU  354  C   LYS A  66      942   1354   1356     -2    233     92       C  
ATOM    355  O   LYS A  66      27.116   7.416  25.817  1.00  9.98           O  
ANISOU  355  O   LYS A  66      960   1517   1316     94    292     29       O  
ATOM    356  CB  LYS A  66      25.393   9.504  23.822  1.00 10.97           C  
ANISOU  356  CB  LYS A  66      968   1614   1587    112    221    131       C  
ATOM    357  CG  LYS A  66      26.818   9.671  23.280  1.00 12.99           C  
ANISOU  357  CG  LYS A  66     1327   1927   1682    140    504    239       C  
ATOM    358  CD  LYS A  66      27.860  10.324  24.162  1.00 14.52           C  
ANISOU  358  CD  LYS A  66     1070   2341   2108     41    372    311       C  
ATOM    359  CE  LYS A  66      27.603  11.694  24.751  1.00 16.29           C  
ANISOU  359  CE  LYS A  66     1433   2448   2308   -288    454    -52       C  
ATOM    360  NZ  LYS A  66      27.480  12.681  23.620  1.00 15.93           N  
ANISOU  360  NZ  LYS A  66     1490   2109   2455    360    354   -198       N  
ATOM    361  N   LYS A  67      25.944   9.019  26.868  1.00  9.87           N  
ANISOU  361  N   LYS A  67      850   1552   1348     71    174     40       N  
ATOM    362  CA  LYS A  67      26.864   9.037  27.973  1.00 10.16           C  
ANISOU  362  CA  LYS A  67      858   1613   1389    123    199     18       C  
ATOM    363  C   LYS A  67      26.916   7.752  28.763  1.00  9.55           C  
ANISOU  363  C   LYS A  67      904   1577   1149     38    220   -123       C  
ATOM    364  O   LYS A  67      27.977   7.283  29.195  1.00 10.08           O  
ANISOU  364  O   LYS A  67      905   1572   1355    110    235    -40       O  
ATOM    365  CB  LYS A  67      26.583  10.229  28.901  1.00 10.70           C  
ANISOU  365  CB  LYS A  67      992   1652   1420    -36    347    -88       C  
ATOM    366  CG  LYS A  67      27.617  10.416  30.008  1.00 10.72           C  
ANISOU  366  CG  LYS A  67      939   1526   1607    -67    274    -49       C  
ATOM    367  CD  LYS A  67      28.942  10.948  29.523  1.00 11.56           C  
ANISOU  367  CD  LYS A  67     1072   1828   1491   -284    331   -106       C  
ATOM    368  CE  LYS A  67      29.949  11.182  30.626  1.00 11.49           C  
ANISOU  368  CE  LYS A  67      989   1811   1565   -131    216   -185       C  
ATOM    369  NZ  LYS A  67      29.606  12.267  31.574  1.00 12.78           N  
ANISOU  369  NZ  LYS A  67     1272   1898   1687    -41    231   -236       N  
ATOM    370  N   VAL A  68      25.736   7.092  28.896  1.00  9.80           N  
ANISOU  370  N   VAL A  68      942   1539   1242     85    213    -31       N  
ATOM    371  CA  VAL A  68      25.723   5.786  29.539  1.00  9.98           C  
ANISOU  371  CA  VAL A  68      969   1519   1305     32    279    -50       C  
ATOM    372  C   VAL A  68      26.607   4.823  28.739  1.00  9.54           C  
ANISOU  372  C   VAL A  68      940   1384   1300    -97    273     10       C  
ATOM    373  O   VAL A  68      27.409   4.033  29.282  1.00 10.11           O  
ANISOU  373  O   VAL A  68     1038   1444   1361     58    252     68       O  
ATOM    374  CB  VAL A  68      24.290   5.215  29.689  1.00 10.52           C  
ANISOU  374  CB  VAL A  68     1016   1719   1263    -38    229    -11       C  
ATOM    375  CG1 VAL A  68      24.331   3.790  30.226  1.00 12.11           C  
ANISOU  375  CG1 VAL A  68     1080   1855   1666   -158    304    170       C  
ATOM    376  CG2 VAL A  68      23.499   6.112  30.634  1.00 12.15           C  
ANISOU  376  CG2 VAL A  68     1102   2110   1403     71    507     88       C  
ATOM    377  N   MET A  69      26.466   4.843  27.408  1.00  9.87           N  
ANISOU  377  N   MET A  69      926   1493   1331      8    290    -36       N  
ATOM    378  CA  MET A  69      27.263   3.956  26.559  1.00 10.43           C  
ANISOU  378  CA  MET A  69     1125   1385   1451    -15    361   -151       C  
ATOM    379  C   MET A  69      28.728   4.334  26.568  1.00  9.86           C  
ANISOU  379  C   MET A  69      986   1478   1281     96    342     72       C  
ATOM    380  O   MET A  69      29.612   3.440  26.537  1.00 10.05           O  
ANISOU  380  O   MET A  69     1075   1376   1368    112    305     44       O  
ATOM    381  CB  MET A  69      26.724   3.938  25.151  1.00 10.96           C  
ANISOU  381  CB  MET A  69     1093   1574   1496    118    279    -17       C  
ATOM    382  CG  MET A  69      25.331   3.346  25.025  1.00 11.81           C  
ANISOU  382  CG  MET A  69     1129   1700   1656      1    193    -35       C  
ATOM    383  SD  MET A  69      25.106   1.724  25.773  1.00 13.61           S  
ANISOU  383  SD  MET A  69     1257   1682   2232   -115    262    -44       S  
ATOM    384  CE  MET A  69      26.046   0.720  24.620  1.00 20.69           C  
ANISOU  384  CE  MET A  69     1965   1729   4166   -104    869   -648       C  
ATOM    385  N   TRP A  70      29.065   5.616  26.706  1.00 10.21           N  
ANISOU  385  N   TRP A  70      941   1451   1489    106    257    -58       N  
ATOM    386  CA  TRP A  70      30.461   6.048  26.832  1.00 10.12           C  
ANISOU  386  CA  TRP A  70      975   1542   1327     62    299    138       C  
ATOM    387  C   TRP A  70      31.048   5.508  28.126  1.00 10.16           C  
ANISOU  387  C   TRP A  70     1007   1494   1360      3    313    112       C  
ATOM    388  O   TRP A  70      32.175   4.990  28.154  1.00 10.73           O  
ANISOU  388  O   TRP A  70      969   1607   1500    122    290    140       O  
ATOM    389  CB  TRP A  70      30.563   7.558  26.715  1.00 10.41           C  
ANISOU  389  CB  TRP A  70      960   1521   1474    101    217     -3       C  
ATOM    390  CG  TRP A  70      31.973   8.070  26.751  1.00 11.27           C  
ANISOU  390  CG  TRP A  70     1059   1609   1615    -85    410     25       C  
ATOM    391  CD1 TRP A  70      32.861   8.070  25.704  1.00 11.73           C  
ANISOU  391  CD1 TRP A  70     1091   1745   1623    -26    439    131       C  
ATOM    392  CD2 TRP A  70      32.654   8.648  27.891  1.00 11.73           C  
ANISOU  392  CD2 TRP A  70      943   1864   1650   -149    406      5       C  
ATOM    393  NE1 TRP A  70      34.046   8.622  26.127  1.00 12.12           N  
ANISOU  393  NE1 TRP A  70      899   2148   1558     -3    395    182       N  
ATOM    394  CE2 TRP A  70      33.946   8.982  27.423  1.00 11.89           C  
ANISOU  394  CE2 TRP A  70     1024   1826   1669   -147    412    114       C  
ATOM    395  CE3 TRP A  70      32.342   8.925  29.191  1.00 13.32           C  
ANISOU  395  CE3 TRP A  70     1029   2283   1749   -215    467   -322       C  
ATOM    396  CZ2 TRP A  70      34.902   9.586  28.255  1.00 15.77           C  
ANISOU  396  CZ2 TRP A  70     1104   2848   2041   -358    315   -245       C  
ATOM    397  CZ3 TRP A  70      33.268   9.519  30.010  1.00 17.48           C  
ANISOU  397  CZ3 TRP A  70     1385   3371   1883   -614    393   -547       C  
ATOM    398  CH2 TRP A  70      34.521   9.837  29.564  1.00 16.94           C  
ANISOU  398  CH2 TRP A  70     1225   3196   2015   -470    234   -365       C  
ATOM    399  N   ASN A  71      30.317   5.645  29.236  1.00 10.10           N  
ANISOU  399  N   ASN A  71     1038   1531   1270     32    261    -24       N  
ATOM    400  CA  ASN A  71      30.767   5.095  30.500  1.00 10.51           C  
ANISOU  400  CA  ASN A  71     1047   1649   1299    -37    373     49       C  
ATOM    401  C   ASN A  71      31.043   3.606  30.427  1.00 10.18           C  
ANISOU  401  C   ASN A  71      973   1626   1268     63    387    150       C  
ATOM    402  O   ASN A  71      32.003   3.072  30.997  1.00 12.14           O  
ANISOU  402  O   ASN A  71     1163   2074   1377    242    325     49       O  
ATOM    403  CB  ASN A  71      29.791   5.414  31.625  1.00 10.33           C  
ANISOU  403  CB  ASN A  71     1101   1647   1176    -70    244    -15       C  
ATOM    404  CG  ASN A  71      29.812   6.843  32.064  1.00 11.44           C  
ANISOU  404  CG  ASN A  71     1243   1706   1398   -339    350   -253       C  
ATOM    405  OD1 ASN A  71      30.811   7.514  31.979  1.00 16.11           O  
ANISOU  405  OD1 ASN A  71     1524   2476   2120   -758    793   -749       O  
ATOM    406  ND2 ASN A  71      28.665   7.320  32.572  1.00 11.62           N  
ANISOU  406  ND2 ASN A  71     1334   1630   1452    -72    414    -20       N  
ATOM    407  N   THR A  72      30.205   2.902  29.665  1.00 10.47           N  
ANISOU  407  N   THR A  72     1102   1446   1431     65    318    139       N  
ATOM    408  CA  THR A  72      30.374   1.458  29.460  1.00 10.80           C  
ANISOU  408  CA  THR A  72     1192   1506   1407    112    386     89       C  
ATOM    409  C   THR A  72      31.669   1.177  28.686  1.00 11.25           C  
ANISOU  409  C   THR A  72     1199   1604   1473    167    273    179       C  
ATOM    410  O   THR A  72      32.458   0.306  29.021  1.00 12.20           O  
ANISOU  410  O   THR A  72     1321   1785   1531    367    394    398       O  
ATOM    411  CB  THR A  72      29.164   0.892  28.718  1.00 11.00           C  
ANISOU  411  CB  THR A  72     1246   1521   1413     37    423     50       C  
ATOM    412  OG1 THR A  72      27.945   1.233  29.409  1.00 11.75           O  
ANISOU  412  OG1 THR A  72     1180   1695   1589    -54    403     47       O  
ATOM    413  CG2 THR A  72      29.168  -0.624  28.598  1.00 12.63           C  
ANISOU  413  CG2 THR A  72     1522   1573   1705     20    336     32       C  
ATOM    414  N   ALA A  73      31.882   1.950  27.614  1.00 10.71           N  
ANISOU  414  N   ALA A  73     1138   1492   1441    183    338    214       N  
ATOM    415  CA  ALA A  73      33.103   1.840  26.799  1.00 11.78           C  
ANISOU  415  CA  ALA A  73     1294   1631   1551     54    438    124       C  
ATOM    416  C   ALA A  73      34.330   2.166  27.606  1.00 12.27           C  
ANISOU  416  C   ALA A  73     1154   1813   1695    216    361    122       C  
ATOM    417  O   ALA A  73      35.388   1.488  27.492  1.00 13.66           O  
ANISOU  417  O   ALA A  73     1313   2230   1648    520    559    324       O  
ATOM    418  CB  ALA A  73      32.964   2.768  25.614  1.00 11.56           C  
ANISOU  418  CB  ALA A  73     1222   1780   1391    139    480     88       C  
ATOM    419  N  AVAL A  74      34.336   3.244  28.383  0.52 12.43           N  
ANISOU  419  N  AVAL A  74      954   2320   1450    267    357    -70       N  
ATOM    420  N  BVAL A  74      34.227   3.045  28.588  0.47 11.95           N  
ANISOU  420  N  BVAL A  74      918   1935   1687    139    231     95       N  
ATOM    421  CA AVAL A  74      35.425   3.728  29.223  0.52 12.73           C  
ANISOU  421  CA AVAL A  74     1320   2165   1352     -6    291    128       C  
ATOM    422  CA BVAL A  74      35.383   3.166  29.493  0.47 12.18           C  
ANISOU  422  CA BVAL A  74      839   2186   1601     79    309    307       C  
ATOM    423  C  AVAL A  74      35.852   2.666  30.237  0.52 11.66           C  
ANISOU  423  C  AVAL A  74      929   2049   1453    147    363     32       C  
ATOM    424  C  BVAL A  74      35.616   1.904  30.322  0.47 13.25           C  
ANISOU  424  C  BVAL A  74      966   2347   1721    -89    227    449       C  
ATOM    425  O  AVAL A  74      37.023   2.390  30.460  0.52 12.04           O  
ANISOU  425  O  AVAL A  74      847   1903   1824    -13    295   -125       O  
ATOM    426  O  BVAL A  74      36.785   1.581  30.560  0.47 13.13           O  
ANISOU  426  O  BVAL A  74      958   1887   2146     37    332    448       O  
ATOM    427  CB AVAL A  74      35.084   5.025  30.002  0.52 13.92           C  
ANISOU  427  CB AVAL A  74     1208   2304   1776    602   -325    -25       C  
ATOM    428  CB BVAL A  74      35.263   4.427  30.348  0.47 13.90           C  
ANISOU  428  CB BVAL A  74     1049   2433   1797     -4     96     15       C  
ATOM    429  CG1AVAL A  74      36.069   5.288  31.141  0.52 15.42           C  
ANISOU  429  CG1AVAL A  74      788   3322   1748    193    183   -610       C  
ATOM    430  CG1BVAL A  74      36.535   4.752  31.133  0.47 26.26           C  
ANISOU  430  CG1BVAL A  74     2370   3078   4529   1156  -2015  -1119       C  
ATOM    431  CG2AVAL A  74      35.029   6.217  29.053  0.52 14.95           C  
ANISOU  431  CG2AVAL A  74     1409   2123   2147   -257    202     71       C  
ATOM    432  CG2BVAL A  74      35.020   5.625  29.449  0.47 14.79           C  
ANISOU  432  CG2BVAL A  74      650   2208   2763    215     92    147       C  
ATOM    433  N  AHIS A  75      34.854   2.064  30.858  0.52 12.27           N  
ANISOU  433  N  AHIS A  75     1010   2134   1520    -14    345    105       N  
ATOM    434  N  BHIS A  75      34.587   1.174  30.727  0.47 12.56           N  
ANISOU  434  N  BHIS A  75      945   1875   1953     70    258    319       N  
ATOM    435  CA AHIS A  75      35.058   0.973  31.785  0.52 13.89           C  
ANISOU  435  CA AHIS A  75     1127   2106   2046   -225     70    246       C  
ATOM    436  CA BHIS A  75      34.787  -0.071  31.447  0.47 12.58           C  
ANISOU  436  CA BHIS A  75     1259   1720   1801    200    353    157       C  
ATOM    437  C  AHIS A  75      35.799  -0.142  31.072  0.52 13.69           C  
ANISOU  437  C  AHIS A  75     1167   2167   1865    -13    203    605       C  
ATOM    438  C  BHIS A  75      35.546  -1.094  30.595  0.47 13.97           C  
ANISOU  438  C  BHIS A  75     1196   2215   1897    445    209    -44       C  
ATOM    439  O  AHIS A  75      36.795  -0.704  31.558  0.52 14.86           O  
ANISOU  439  O  AHIS A  75     1150   2314   2181    -25     38    616       O  
ATOM    440  O  BHIS A  75      36.301  -1.875  31.176  0.47 13.86           O  
ANISOU  440  O  BHIS A  75     1092   2116   2059    405    278     56       O  
ATOM    441  CB AHIS A  75      33.689   0.577  32.357  0.52 14.14           C  
ANISOU  441  CB AHIS A  75     1475   2246   1652   -269    373    170       C  
ATOM    442  CB BHIS A  75      33.468  -0.677  31.938  0.47 11.34           C  
ANISOU  442  CB BHIS A  75     1256   1565   1487    161    227    198       C  
ATOM    443  CG AHIS A  75      33.860  -0.597  33.241  0.52 14.77           C  
ANISOU  443  CG AHIS A  75     1446   2180   1987   -266    181    198       C  
ATOM    444  CG BHIS A  75      33.131  -0.354  33.339  0.47 10.24           C  
ANISOU  444  CG BHIS A  75      940   1477   1475     45     32     66       C  
ATOM    445  ND1AHIS A  75      34.254  -0.480  34.569  0.52 14.50           N  
ANISOU  445  ND1AHIS A  75     1321   2165   2024    -66     18    307       N  
ATOM    446  ND1BHIS A  75      33.537  -1.207  34.340  0.47 10.93           N  
ANISOU  446  ND1BHIS A  75     1139   1619   1394     33    402    197       N  
ATOM    447  CD2AHIS A  75      33.752  -1.898  32.944  0.52 17.20           C  
ANISOU  447  CD2AHIS A  75     2198   2215   2123   -709     60    333       C  
ATOM    448  CD2BHIS A  75      32.476   0.722  33.889  0.47 11.27           C  
ANISOU  448  CD2BHIS A  75      879   1620   1782    -85    346    -48       C  
ATOM    449  CE1AHIS A  75      34.361  -1.704  35.086  0.52 15.04           C  
ANISOU  449  CE1AHIS A  75     1831   1945   1940     27    502    121       C  
ATOM    450  CE1BHIS A  75      33.154  -0.668  35.480  0.47 11.76           C  
ANISOU  450  CE1BHIS A  75     1304   1709   1456   -309    388    -74       C  
ATOM    451  NE2AHIS A  75      34.038  -2.521  34.118  0.52 16.63           N  
ANISOU  451  NE2AHIS A  75     1964   2275   2077   -382    114    270       N  
ATOM    452  NE2BHIS A  75      32.495   0.489  35.233  0.47 13.03           N  
ANISOU  452  NE2BHIS A  75     1574   1707   1670   -128    282   -245       N  
ATOM    453  N  ASER A  76      35.330  -0.491  29.865  0.52 13.48           N  
ANISOU  453  N  ASER A  76     1249   1776   2095    102     81    402       N  
ATOM    454  N  BSER A  76      35.368  -1.113  29.274  0.47 14.58           N  
ANISOU  454  N  BSER A  76     1958   1707   1876    235    131   -129       N  
ATOM    455  CA ASER A  76      35.984  -1.599  29.144  0.52 15.15           C  
ANISOU  455  CA ASER A  76     1664   1562   2529    143    167    415       C  
ATOM    456  CA BSER A  76      36.249  -1.968  28.471  0.47 16.99           C  
ANISOU  456  CA BSER A  76     2385   1946   2124    200    527   -245       C  
ATOM    457  C  ASER A  76      37.436  -1.306  28.852  0.52 15.22           C  
ANISOU  457  C  ASER A  76     1582   1538   2662    416    199     47       C  
ATOM    458  C  BSER A  76      37.698  -1.564  28.606  0.47 18.20           C  
ANISOU  458  C  BSER A  76     2263   2247   2404    480    590    -54       C  
ATOM    459  O  ASER A  76      38.367  -2.100  29.084  0.52 16.14           O  
ANISOU  459  O  ASER A  76     1798   2123   2211    823    171   -147       O  
ATOM    460  O  BSER A  76      38.586  -2.420  28.493  0.47 20.44           O  
ANISOU  460  O  BSER A  76     2687   3057   2023   1014    844   -481       O  
ATOM    461  CB ASER A  76      35.222  -1.821  27.843  0.52 16.58           C  
ANISOU  461  CB ASER A  76     1701   1789   2811    361     53   -136       C  
ATOM    462  CB BSER A  76      35.772  -1.879  27.020  0.47 19.99           C  
ANISOU  462  CB BSER A  76     3445   2017   2134    -12    210   -581       C  
ATOM    463  OG ASER A  76      35.557  -2.899  27.018  0.52 23.15           O  
ANISOU  463  OG ASER A  76     3380   1977   3439   -302    909   -554       O  
ATOM    464  OG BSER A  76      36.256  -0.684  26.415  0.47 22.39           O  
ANISOU  464  OG BSER A  76     3058   2876   2575    306    625    384       O  
ATOM    465  N  AGLU A  77      37.686  -0.102  28.318  0.52 13.32           N  
ANISOU  465  N  AGLU A  77     1350   1901   1812    237    319    111       N  
ATOM    466  N  BGLU A  77      38.058  -0.304  28.859  0.47 16.46           N  
ANISOU  466  N  BGLU A  77     1658   2363   2234    202    370    385       N  
ATOM    467  CA AGLU A  77      39.059   0.313  28.008  0.52 16.14           C  
ANISOU  467  CA AGLU A  77     1378   2614   2139    131    400     92       C  
ATOM    468  CA BGLU A  77      39.495  -0.070  29.030  0.47 18.55           C  
ANISOU  468  CA BGLU A  77     1427   3120   2503    510    648    353       C  
ATOM    469  C  AGLU A  77      39.933   0.251  29.239  0.52 14.14           C  
ANISOU  469  C  AGLU A  77     1017   2054   2299    224    459    266       C  
ATOM    470  C  BGLU A  77      40.029  -0.342  30.415  0.47 18.30           C  
ANISOU  470  C  BGLU A  77     1573   2870   2510    -27    326     96       C  
ATOM    471  O  AGLU A  77      41.051  -0.300  29.215  0.52 16.58           O  
ANISOU  471  O  AGLU A  77     1296   2173   2829    578    485    284       O  
ATOM    472  O  BGLU A  77      41.178  -0.720  30.579  0.47 17.99           O  
ANISOU  472  O  BGLU A  77     1649   2359   2826     64    206    -13       O  
ATOM    473  CB AGLU A  77      38.978   1.707  27.366  0.52 16.81           C  
ANISOU  473  CB AGLU A  77     1039   3253   2094     39    633    805       C  
ATOM    474  CB BGLU A  77      39.783   1.397  28.698  0.47 22.41           C  
ANISOU  474  CB BGLU A  77     2095   3665   2756   -687     58    654       C  
ATOM    475  CG AGLU A  77      38.366   1.543  25.994  0.52 22.76           C  
ANISOU  475  CG AGLU A  77     2147   4614   1886    172    622    656       C  
ATOM    476  CG BGLU A  77      39.984   1.418  27.166  0.47 30.05           C  
ANISOU  476  CG BGLU A  77     3800   5004   2615   -968   -373   1227       C  
ATOM    477  CD AGLU A  77      39.128   0.659  25.027  0.52 31.60           C  
ANISOU  477  CD AGLU A  77     3115   6397   2497    811    770   -229       C  
ATOM    478  CD BGLU A  77      39.964   2.852  26.812  0.47 28.39           C  
ANISOU  478  CD BGLU A  77     3282   4858   2646  -1424   -317    971       C  
ATOM    479  OE1AGLU A  77      38.879  -0.557  24.886  0.52 36.19           O  
ANISOU  479  OE1AGLU A  77     3677   6706   3369    511   1681  -1381       O  
ATOM    480  OE1BGLU A  77      39.757   3.364  25.697  0.47 73.71           O  
ANISOU  480  OE1BGLU A  77    15311   7538   5158  -3381  -2999   4050       O  
ATOM    481  OE2AGLU A  77      40.035   1.175  24.344  0.52 40.27           O  
ANISOU  481  OE2AGLU A  77     4451   6412   4439   1427   2665    116       O  
ATOM    482  OE2BGLU A  77      40.242   3.668  27.747  0.47 45.96           O  
ANISOU  482  OE2BGLU A  77     5710   6452   5300   -900   1274  -2081       O  
ATOM    483  N  APHE A  78      39.466   0.773  30.358  0.52 13.90           N  
ANISOU  483  N  APHE A  78     1090   2117   2074    351    335    475       N  
ATOM    484  N  BPHE A  78      39.177  -0.129  31.416  0.47 19.49           N  
ANISOU  484  N  BPHE A  78     2156   2868   2381    906    294    233       N  
ATOM    485  CA APHE A  78      40.317   0.753  31.559  0.52 15.84           C  
ANISOU  485  CA APHE A  78     1408   2329   2280    355     27    465       C  
ATOM    486  CA BPHE A  78      39.506  -0.590  32.764  0.47 19.36           C  
ANISOU  486  CA BPHE A  78     2165   2947   2244   1026    232   -117       C  
ATOM    487  C  APHE A  78      40.575  -0.664  32.019  0.52 13.53           C  
ANISOU  487  C  APHE A  78     1072   2378   1689    399    452    358       C  
ATOM    488  C  BPHE A  78      39.900  -2.047  32.677  0.47 19.14           C  
ANISOU  488  C  BPHE A  78     2553   2979   1741   1157    -65   -126       C  
ATOM    489  O  APHE A  78      41.620  -0.920  32.612  0.52 13.65           O  
ANISOU  489  O  APHE A  78     1109   2014   2065    402    269    222       O  
ATOM    490  O  BPHE A  78      40.903  -2.464  33.244  0.47 18.98           O  
ANISOU  490  O  BPHE A  78     2079   3120   2014    960     92   -101       O  
ATOM    491  CB APHE A  78      39.640   1.538  32.670  0.52 17.71           C  
ANISOU  491  CB APHE A  78     2338   2091   2299    385    -28    246       C  
ATOM    492  CB BPHE A  78      38.333  -0.403  33.741  0.47 22.68           C  
ANISOU  492  CB BPHE A  78     2684   3261   2674   1168    815    267       C  
ATOM    493  CG APHE A  78      39.936   3.038  32.753  0.52 20.06           C  
ANISOU  493  CG APHE A  78     1659   2085   3878    349   -542    211       C  
ATOM    494  CG BPHE A  78      37.852   1.022  33.917  0.47 25.23           C  
ANISOU  494  CG BPHE A  78     2341   3402   3841    883    721   -905       C  
ATOM    495  CD1APHE A  78      38.856   3.897  32.902  0.52 19.18           C  
ANISOU  495  CD1APHE A  78     1523   2245   3519    148    -10   -462       C  
ATOM    496  CD1BPHE A  78      36.531   1.382  34.091  0.47 31.03           C  
ANISOU  496  CD1BPHE A  78     2570   4706   4515   1487    297  -1964       C  
ATOM    497  CD2APHE A  78      41.219   3.580  32.689  0.52 21.88           C  
ANISOU  497  CD2APHE A  78     1653   2606   4055    334    528   1115       C  
ATOM    498  CD2BPHE A  78      38.807   2.036  33.891  0.47 26.33           C  
ANISOU  498  CD2BPHE A  78     3605   3689   2710    164   1121   -616       C  
ATOM    499  CE1APHE A  78      39.024   5.261  32.994  0.52 22.33           C  
ANISOU  499  CE1APHE A  78     1780   2342   4363    297   -308  -1248       C  
ATOM    500  CE1BPHE A  78      36.190   2.723  34.162  0.47 31.71           C  
ANISOU  500  CE1BPHE A  78     2072   4746   5229   1437    152  -1959       C  
ATOM    501  CE2APHE A  78      41.379   4.966  32.781  0.52 25.68           C  
ANISOU  501  CE2APHE A  78     1628   2867   5263   -168   -254    412       C  
ATOM    502  CE2BPHE A  78      38.466   3.355  33.995  0.47 27.85           C  
ANISOU  502  CE2BPHE A  78     2839   3702   4040    228   -299   -537       C  
ATOM    503  CZ APHE A  78      40.293   5.810  32.931  0.52 23.56           C  
ANISOU  503  CZ APHE A  78     2247   2259   4448   -133     34     93       C  
ATOM    504  CZ BPHE A  78      37.136   3.706  34.165  0.47 35.91           C  
ANISOU  504  CZ BPHE A  78     3095   5036   5513    773   -373  -1284       C  
ATOM    505  N  AMET A  79      39.643  -1.583  31.847  0.52 15.34           N  
ANISOU  505  N  AMET A  79     1129   2252   2448    424     44    569       N  
ATOM    506  N  BMET A  79      39.115  -2.826  31.943  0.47 16.77           N  
ANISOU  506  N  BMET A  79     1751   2778   1845    865    427    165       N  
ATOM    507  CA AMET A  79      39.836  -2.946  32.383  0.52 16.99           C  
ANISOU  507  CA AMET A  79     1604   2329   2521    426     38    627       C  
ATOM    508  CA BMET A  79      39.341  -4.254  31.780  0.47 18.17           C  
ANISOU  508  CA BMET A  79     1979   2751   2174    939    348    163       C  
ATOM    509  C  AMET A  79      40.927  -3.669  31.613  0.52 16.97           C  
ANISOU  509  C  AMET A  79     1852   2057   2537    350    -91     91       C  
ATOM    510  C  BMET A  79      40.738  -4.469  31.204  0.47 17.90           C  
ANISOU  510  C  BMET A  79     2169   2675   1956    934    550    -43       C  
ATOM    511  O  AMET A  79      41.538  -4.627  32.146  0.52 17.02           O  
ANISOU  511  O  AMET A  79     1574   1906   2987    182   -184    126       O  
ATOM    512  O  BMET A  79      41.443  -5.351  31.729  0.47 14.58           O  
ANISOU  512  O  BMET A  79     1335   2527   1678    204    255     98       O  
ATOM    513  CB AMET A  79      38.547  -3.751  32.470  0.52 20.10           C  
ANISOU  513  CB AMET A  79     2036   2570   3031     91    240    931       C  
ATOM    514  CB BMET A  79      38.229  -4.921  30.980  0.47 24.31           C  
ANISOU  514  CB BMET A  79     2313   3076   3849    769    -25   -527       C  
ATOM    515  CG AMET A  79      37.593  -3.207  33.536  0.52 23.51           C  
ANISOU  515  CG AMET A  79     1929   3616   3388    514    523   1255       C  
ATOM    516  CG BMET A  79      38.399  -6.435  30.742  0.47 27.21           C  
ANISOU  516  CG BMET A  79     2524   2960   4853    712   -301   -299       C  
ATOM    517  SD AMET A  79      38.211  -3.235  35.243  0.52 24.73           S  
ANISOU  517  SD AMET A  79     2404   3784   3209    198    605    515       S  
ATOM    518  SD BMET A  79      37.156  -7.073  29.608  0.47 58.58           S  
ANISOU  518  SD BMET A  79     4494   3343  14422     53  -4685  -1700       S  
ATOM    519  CE AMET A  79      37.828  -4.945  35.649  0.52 85.07           C  
ANISOU  519  CE AMET A  79    27909   2082   2332      0   -856      0       C  
ATOM    520  CE BMET A  79      36.534  -5.548  28.901  0.47 50.27           C  
ANISOU  520  CE BMET A  79     2164   9752   7184   -353    189   5512       C  
ATOM    521  N  AHIS A  80      41.305  -3.125  30.447  0.52 17.63           N  
ANISOU  521  N  AHIS A  80     2220   2498   1979    519   -210   -274       N  
ATOM    522  N  BHIS A  80      41.161  -3.687  30.211  0.47 16.96           N  
ANISOU  522  N  BHIS A  80     1665   2698   2081    906     97    199       N  
ATOM    523  CA AHIS A  80      42.419  -3.594  29.632  0.52 18.25           C  
ANISOU  523  CA AHIS A  80     2282   2382   2269    574    -62    -43       C  
ATOM    524  CA BHIS A  80      42.492  -3.926  29.629  0.47 16.50           C  
ANISOU  524  CA BHIS A  80     1694   2502   2075    516    200    -15       C  
ATOM    525  C  AHIS A  80      43.738  -3.405  30.380  0.52 17.61           C  
ANISOU  525  C  AHIS A  80     2212   2427   2053    627    116   -401       C  
ATOM    526  C  BHIS A  80      43.658  -3.588  30.541  0.47 13.31           C  
ANISOU  526  C  BHIS A  80     1523   1595   1938    411    421    102       C  
ATOM    527  O  AHIS A  80      44.775  -3.951  30.036  0.52 17.20           O  
ANISOU  527  O  AHIS A  80     2239   2472   1825    621     79   -580       O  
ATOM    528  O  BHIS A  80      44.685  -4.277  30.413  0.47 15.11           O  
ANISOU  528  O  BHIS A  80     2011   1974   1757   1007      7    113       O  
ATOM    529  CB AHIS A  80      42.559  -2.884  28.287  0.52 22.36           C  
ANISOU  529  CB AHIS A  80     2949   3398   2149   1014    131    113       C  
ATOM    530  CB BHIS A  80      42.698  -3.194  28.286  0.47 21.04           C  
ANISOU  530  CB BHIS A  80     2998   3371   1625   1163    488   -124       C  
ATOM    531  CG AHIS A  80      41.778  -3.374  27.130  0.52 29.14           C  
ANISOU  531  CG AHIS A  80     4058   4810   2203   1380   -186   -538       C  
ATOM    532  CG BHIS A  80      41.599  -3.442  27.318  0.47 25.71           C  
ANISOU  532  CG BHIS A  80     3348   4706   1714   1205    272   -476       C  
ATOM    533  ND1AHIS A  80      42.025  -4.568  26.495  0.52 31.28           N  
ANISOU  533  ND1AHIS A  80     4021   5535   2328   1426     92  -1154       N  
ATOM    534  ND1BHIS A  80      40.959  -4.647  27.169  0.47 28.03           N  
ANISOU  534  ND1BHIS A  80     2931   5334   2384    741    218   -559       N  
ATOM    535  CD2AHIS A  80      40.739  -2.792  26.477  0.52 29.46           C  
ANISOU  535  CD2AHIS A  80     4038   5311   1845   1276   -248   -488       C  
ATOM    536  CD2BHIS A  80      41.032  -2.592  26.428  0.47 28.48           C  
ANISOU  536  CD2BHIS A  80     3459   5420   1943   1502    -26   -408       C  
ATOM    537  CE1AHIS A  80      41.151  -4.694  25.505  0.52 34.36           C  
ANISOU  537  CE1AHIS A  80     4481   5868   2705   1401   -321  -1240       C  
ATOM    538  CE1BHIS A  80      40.034  -4.531  26.231  0.47 33.26           C  
ANISOU  538  CE1BHIS A  80     4153   5865   2620   1056   -527   -995       C  
ATOM    539  NE2AHIS A  80      40.361  -3.633  25.465  0.52 31.54           N  
ANISOU  539  NE2AHIS A  80     3692   6058   2234   1255     79  -1137       N  
ATOM    540  NE2BHIS A  80      40.061  -3.293  25.760  0.47 28.99           N  
ANISOU  540  NE2BHIS A  80     2595   5826   2595   1903    212  -1008       N  
ATOM    541  N   ASP A  81      43.651  -2.609  31.442  1.00 15.37           N  
ANISOU  541  N   ASP A  81     2074   1984   1784    654    406    -13       N  
ATOM    542  CA  ASP A  81      44.747  -2.244  32.299  1.00 15.50           C  
ANISOU  542  CA  ASP A  81     2327   1843   1719    543    298   -114       C  
ATOM    543  C   ASP A  81      44.747  -2.978  33.648  1.00 15.74           C  
ANISOU  543  C   ASP A  81     2002   2066   1914    860    401    116       C  
ATOM    544  O   ASP A  81      45.633  -2.728  34.483  1.00 16.63           O  
ANISOU  544  O   ASP A  81     2302   2243   1772    777    369     39       O  
ATOM    545  CB  ASP A  81      44.671  -0.727  32.564  1.00 18.30           C  
ANISOU  545  CB  ASP A  81     3266   1790   1897    488    619    -36       C  
ATOM    546  CG  ASP A  81      44.700   0.128  31.329  1.00 14.32           C  
ANISOU  546  CG  ASP A  81     1801   1925   1715    445    248    -91       C  
ATOM    547  OD1 ASP A  81      44.205   1.294  31.448  1.00 14.96           O  
ANISOU  547  OD1 ASP A  81     1947   1811   1928    283    435    -55       O  
ATOM    548  OD2 ASP A  81      45.161  -0.310  30.253  1.00 15.21           O  
ANISOU  548  OD2 ASP A  81     1819   2186   1773    499    274   -156       O  
ATOM    549  N   HIS A  82      43.808  -3.869  33.863  1.00 16.59           N  
ANISOU  549  N   HIS A  82     1797   2615   1892    789    602    254       N  
ATOM    550  CA  HIS A  82      43.594  -4.460  35.185  1.00 17.28           C  
ANISOU  550  CA  HIS A  82     1641   3112   1811    677    439    336       C  
ATOM    551  C   HIS A  82      44.797  -5.291  35.642  1.00 16.69           C  
ANISOU  551  C   HIS A  82     1935   2378   2027    623    231     73       C  
ATOM    552  O   HIS A  82      45.258  -5.126  36.777  1.00 17.33           O  
ANISOU  552  O   HIS A  82     2162   2477   1945    801    240    245       O  
ATOM    553  CB AHIS A  82      42.371  -5.408  35.100  0.52 19.50           C  
ANISOU  553  CB AHIS A  82     1797   3293   2319    533    419    624       C  
ATOM    554  CB BHIS A  82      42.215  -5.086  35.249  0.47 17.64           C  
ANISOU  554  CB BHIS A  82     1902   2887   1915    399    332    349       C  
ATOM    555  CG AHIS A  82      41.690  -6.053  36.272  0.52 18.12           C  
ANISOU  555  CG AHIS A  82     2186   2352   2346    479    477    357       C  
ATOM    556  CG BHIS A  82      41.633  -5.010  36.634  0.47 14.55           C  
ANISOU  556  CG BHIS A  82     1632   1632   2263    350    430    172       C  
ATOM    557  ND1AHIS A  82      41.372  -7.385  36.512  0.52 21.61           N  
ANISOU  557  ND1AHIS A  82     3292   2366   2554     -8     69     -5       N  
ATOM    558  ND1BHIS A  82      41.366  -3.959  37.456  0.47 14.37           N  
ANISOU  558  ND1BHIS A  82     1068   1975   2418     68    516    -25       N  
ATOM    559  CD2AHIS A  82      41.222  -5.430  37.389  0.52 16.37           C  
ANISOU  559  CD2AHIS A  82     1529   2304   2387   -180    402     84       C  
ATOM    560  CD2BHIS A  82      41.194  -6.105  37.302  0.47 17.04           C  
ANISOU  560  CD2BHIS A  82     2340   1982   2153   -426    369     35       C  
ATOM    561  CE1AHIS A  82      40.780  -7.495  37.679  0.52 20.81           C  
ANISOU  561  CE1AHIS A  82     2891   2231   2786    -81      8    605       C  
ATOM    562  CE1BHIS A  82      40.802  -4.397  38.586  0.47 15.05           C  
ANISOU  562  CE1BHIS A  82     1243   2073   2403   -194    550    -59       C  
ATOM    563  NE2AHIS A  82      40.648  -6.307  38.263  0.52 20.10           N  
ANISOU  563  NE2AHIS A  82     2364   2732   2542   -288    654    227       N  
ATOM    564  NE2BHIS A  82      40.708  -5.703  38.525  0.47 15.35           N  
ANISOU  564  NE2BHIS A  82     1373   2068   2393    -25    429    103       N  
ATOM    565  N   ALA A  83      45.373  -6.096  34.768  1.00 17.28           N  
ANISOU  565  N   ALA A  83     2060   2292   2215    667    145     32       N  
ATOM    566  CA  ALA A  83      46.556  -6.877  35.117  1.00 16.69           C  
ANISOU  566  CA  ALA A  83     2062   1731   2548    491     78    -17       C  
ATOM    567  C   ALA A  83      47.737  -5.931  35.389  1.00 15.15           C  
ANISOU  567  C   ALA A  83     1990   1904   1864    481    362     70       C  
ATOM    568  O   ALA A  83      48.544  -6.219  36.269  1.00 15.77           O  
ANISOU  568  O   ALA A  83     2014   1852   2124    558    198      1       O  
ATOM    569  CB  ALA A  83      46.842  -7.904  34.012  1.00 21.24           C  
ANISOU  569  CB  ALA A  83     2827   1969   3275    620     76   -530       C  
ATOM    570  N   ASP A  84      47.859  -4.859  34.599  1.00 15.28           N  
ANISOU  570  N   ASP A  84     1838   1939   2029    562    508    120       N  
ATOM    571  CA  ASP A  84      49.000  -3.953  34.834  1.00 14.52           C  
ANISOU  571  CA  ASP A  84     1600   2112   1803    643    512    210       C  
ATOM    572  C   ASP A  84      48.947  -3.327  36.226  1.00 15.80           C  
ANISOU  572  C   ASP A  84     2341   1869   1795    529    493    199       C  
ATOM    573  O   ASP A  84      49.961  -3.017  36.820  1.00 18.19           O  
ANISOU  573  O   ASP A  84     2714   2337   1860     -3    532      4       O  
ATOM    574  CB  ASP A  84      49.048  -2.864  33.801  1.00 16.09           C  
ANISOU  574  CB  ASP A  84     2138   2106   1869    416    484    253       C  
ATOM    575  CG  ASP A  84      49.536  -3.309  32.433  1.00 18.63           C  
ANISOU  575  CG  ASP A  84     2310   2794   1975    774    646    248       C  
ATOM    576  OD1 ASP A  84      49.254  -2.636  31.445  1.00 19.09           O  
ANISOU  576  OD1 ASP A  84     2396   2913   1944    538    664    308       O  
ATOM    577  OD2 ASP A  84      50.226  -4.369  32.365  1.00 27.84           O  
ANISOU  577  OD2 ASP A  84     4181   3967   2431   2301   1355    588       O  
ATOM    578  N   TYR A  85      47.737  -3.108  36.739  1.00 15.50           N  
ANISOU  578  N   TYR A  85     2600   1605   1684    472    696     83       N  
ATOM    579  CA  TYR A  85      47.525  -2.554  38.070  1.00 15.97           C  
ANISOU  579  CA  TYR A  85     2897   1448   1724    332    716      6       C  
ATOM    580  C   TYR A  85      47.497  -3.590  39.194  1.00 16.56           C  
ANISOU  580  C   TYR A  85     2819   1621   1852    332    813    142       C  
ATOM    581  O   TYR A  85      47.212  -3.240  40.312  1.00 21.84           O  
ANISOU  581  O   TYR A  85     4810   1805   1682    774    595    161       O  
ATOM    582  CB  TYR A  85      46.280  -1.643  38.043  1.00 16.50           C  
ANISOU  582  CB  TYR A  85     2998   1582   1689    410    844     89       C  
ATOM    583  CG  TYR A  85      46.606  -0.199  37.769  1.00 14.88           C  
ANISOU  583  CG  TYR A  85     2492   1550   1613    375    686     18       C  
ATOM    584  CD1 TYR A  85      46.451   0.372  36.511  1.00 16.67           C  
ANISOU  584  CD1 TYR A  85     3383   1419   1534    240    567   -113       C  
ATOM    585  CD2 TYR A  85      47.072   0.655  38.768  1.00 14.04           C  
ANISOU  585  CD2 TYR A  85     2277   1554   1504    527    569    154       C  
ATOM    586  CE1 TYR A  85      46.737   1.696  36.208  1.00 14.79           C  
ANISOU  586  CE1 TYR A  85     2609   1371   1638    323    185     -4       C  
ATOM    587  CE2 TYR A  85      47.378   1.951  38.518  1.00 14.51           C  
ANISOU  587  CE2 TYR A  85     2670   1413   1431    613    439     38       C  
ATOM    588  CZ  TYR A  85      47.203   2.489  37.238  1.00 14.26           C  
ANISOU  588  CZ  TYR A  85     2709   1306   1402    626    401    -62       C  
ATOM    589  OH  TYR A  85      47.538   3.808  37.048  1.00 13.40           O  
ANISOU  589  OH  TYR A  85     2122   1482   1486    331    193    -26       O  
ATOM    590  N   GLY A  86      47.853  -4.838  38.897  1.00 14.14           N  
ANISOU  590  N   GLY A  86     2067   1531   1776    242    465    239       N  
ATOM    591  CA  GLY A  86      48.077  -5.812  39.931  1.00 14.85           C  
ANISOU  591  CA  GLY A  86     2022   1576   2043    119    187    265       C  
ATOM    592  C   GLY A  86      46.925  -6.785  40.128  1.00 15.20           C  
ANISOU  592  C   GLY A  86     1955   1651   2170    129    417    332       C  
ATOM    593  O   GLY A  86      47.009  -7.552  41.100  1.00 17.03           O  
ANISOU  593  O   GLY A  86     2556   1901   2014     62    337    365       O  
ATOM    594  N   PHE A  87      45.927  -6.807  39.325  1.00 17.25           N  
ANISOU  594  N   PHE A  87     1753   2330   2469    -30    420    581       N  
ATOM    595  CA  PHE A  87      44.790  -7.697  39.545  1.00 21.41           C  
ANISOU  595  CA  PHE A  87     2337   3384   2413   -812    649    443       C  
ATOM    596  C   PHE A  87      44.812  -8.813  38.534  1.00 24.88           C  
ANISOU  596  C   PHE A  87     3083   3245   3126   -856    255    178       C  
ATOM    597  O   PHE A  87      45.389  -8.651  37.439  1.00 29.07           O  
ANISOU  597  O   PHE A  87     5020   3085   2942  -1570    609   -395       O  
ATOM    598  CB  PHE A  87      43.511  -6.860  39.416  1.00 25.11           C  
ANISOU  598  CB  PHE A  87     1816   4895   2830   -635     96   -708       C  
ATOM    599  CG  PHE A  87      43.384  -5.672  40.371  1.00 25.80           C  
ANISOU  599  CG  PHE A  87     1315   5506   2983   -204    109  -1075       C  
ATOM    600  CD1 PHE A  87      42.663  -5.876  41.552  1.00 29.69           C  
ANISOU  600  CD1 PHE A  87     1475   6674   3131    224    289   -948       C  
ATOM    601  CD2 PHE A  87      43.973  -4.452  40.112  1.00 24.63           C  
ANISOU  601  CD2 PHE A  87     1753   4513   3091    775   -321   -866       C  
ATOM    602  CE1 PHE A  87      42.522  -4.835  42.449  1.00 32.14           C  
ANISOU  602  CE1 PHE A  87     1696   7291   3224    336    532  -1239       C  
ATOM    603  CE2 PHE A  87      43.844  -3.402  41.021  1.00 25.88           C  
ANISOU  603  CE2 PHE A  87     1557   5016   3261    949   -265  -1102       C  
ATOM    604  CZ  PHE A  87      43.168  -3.616  42.207  1.00 32.19           C  
ANISOU  604  CZ  PHE A  87     1965   6786   3481    570    145  -1537       C  
ATOM    605  N  APRO A  88      44.316  -9.999  38.846  0.50 26.40           N  
ANISOU  605  N  APRO A  88     3484   3338   3210   -900    -67    473       N  
ATOM    606  N  BPRO A  88      44.070  -9.879  38.786  0.50 28.36           N  
ANISOU  606  N  BPRO A  88     4206   3422   3148  -1297   -305    718       N  
ATOM    607  CA APRO A  88      44.125 -10.997  37.785  0.50 27.98           C  
ANISOU  607  CA APRO A  88     3830   3080   3720   -658   -337    293       C  
ATOM    608  CA BPRO A  88      43.854 -10.948  37.804  0.50 31.19           C  
ANISOU  608  CA BPRO A  88     4771   3375   3705  -1413   -609    548       C  
ATOM    609  C  APRO A  88      43.182 -10.437  36.719  0.50 27.91           C  
ANISOU  609  C  APRO A  88     4350   2969   3285   -164   -256   -117       C  
ATOM    610  C  BPRO A  88      43.510 -10.434  36.407  0.50 31.56           C  
ANISOU  610  C  BPRO A  88     5209   3240   3542   -510   -715     76       C  
ATOM    611  O  APRO A  88      42.138  -9.893  37.044  0.50 26.88           O  
ANISOU  611  O  APRO A  88     2948   4103   3163  -1133    -13    792       O  
ATOM    612  O  BPRO A  88      42.691  -9.521  36.365  0.50 30.74           O  
ANISOU  612  O  BPRO A  88     3118   4840   3723   -553   -545     90       O  
ATOM    613  CB APRO A  88      43.472 -12.189  38.488  0.50 32.14           C  
ANISOU  613  CB APRO A  88     4066   3584   4561  -1321  -1202    870       C  
ATOM    614  CB BPRO A  88      42.597 -11.652  38.337  0.50 36.42           C  
ANISOU  614  CB BPRO A  88     4581   4766   4492  -2091  -1183    800       C  
ATOM    615  CG APRO A  88      43.850 -12.036  39.924  0.50 26.13           C  
ANISOU  615  CG APRO A  88     1878   3647   4402   -986   -858   1173       C  
ATOM    616  CG BPRO A  88      42.679 -11.474  39.812  0.50 34.53           C  
ANISOU  616  CG BPRO A  88     4252   4558   4308  -2082   -663   1235       C  
ATOM    617  CD APRO A  88      43.939 -10.550  40.155  0.50 29.82           C  
ANISOU  617  CD APRO A  88     4238   3663   3430   -763   -273   1012       C  
ATOM    618  CD BPRO A  88      43.333 -10.146  40.037  0.50 31.60           C  
ANISOU  618  CD BPRO A  88     4181   4222   3604  -1695    -23    877       C  
ATOM    619  N  ASER A  89      43.588 -10.615  35.467  0.50 32.27           N  
ANISOU  619  N  ASER A  89     5005   3920   3335   -101     20   -101       N  
ATOM    620  N  BSER A  89      44.141 -11.032  35.397  0.50 36.73           N  
ANISOU  620  N  BSER A  89     7495   2835   3624    511  -1208   -532       N  
ATOM    621  CA ASER A  89      42.853 -10.132  34.319  0.50 37.33           C  
ANISOU  621  CA ASER A  89     5425   5533   3227    655   -432   -750       C  
ATOM    622  CA BSER A  89      43.991 -10.650  33.995  0.50 39.85           C  
ANISOU  622  CA BSER A  89     6469   5132   3540     -1   -800   -202       C  
ATOM    623  C  ASER A  89      41.409 -10.609  34.381  0.50 37.87           C  
ANISOU  623  C  ASER A  89     4722   6340   3325   1646    349  -1235       C  
ATOM    624  C  BSER A  89      42.568 -10.922  33.499  0.50 43.23           C  
ANISOU  624  C  BSER A  89     6227   6348   3852    403   -800   -280       C  
ATOM    625  O  ASER A  89      41.092 -11.634  34.951  0.50 36.09           O  
ANISOU  625  O  ASER A  89     3065   6651   3997   1663    -15   -797       O  
ATOM    626  O  BSER A  89      41.954 -11.913  33.895  0.50 46.75           O  
ANISOU  626  O  BSER A  89     6945   5778   5039   -398  -2989   -334       O  
ATOM    627  CB ASER A  89      43.425 -10.615  32.980  0.50 37.34           C  
ANISOU  627  CB ASER A  89     4721   6186   3282    238    345     -3       C  
ATOM    628  CB BSER A  89      44.985 -11.389  33.099  0.50 43.35           C  
ANISOU  628  CB BSER A  89     6295   5712   4463   -285    318    353       C  
ATOM    629  OG ASER A  89      44.655  -9.967  32.734  0.50 43.66           O  
ANISOU  629  OG ASER A  89     6931   5354   4302  -1444    490   1277       O  
ATOM    630  OG BSER A  89      46.156 -10.648  32.823  0.50 50.45           O  
ANISOU  630  OG BSER A  89     6025   5993   7152   -567   -225     46       O  
ATOM    631  N  ACYS A  90      40.618  -9.780  33.735  0.50 44.37           N  
ANISOU  631  N  ACYS A  90     5469   6925   4467   1521   -214   -353       N  
ATOM    632  N  BCYS A  90      42.090 -10.029  32.639  0.50 43.05           N  
ANISOU  632  N  BCYS A  90     5551   6899   3905   1020    112     64       N  
ATOM    633  CA ACYS A  90      39.195  -9.925  33.635  0.50 51.21           C  
ANISOU  633  CA ACYS A  90     5400   8046   6012   2160   -798  -1169       C  
ATOM    634  CA BCYS A  90      40.707 -10.082  32.161  0.50 52.21           C  
ANISOU  634  CA BCYS A  90     6032   8201   5606   1704   -906   -690       C  
ATOM    635  C  ACYS A  90      38.683 -10.552  32.348  0.50 53.01           C  
ANISOU  635  C  ACYS A  90     5333   8472   6337   1843   -665  -1585       C  
ATOM    636  C  BCYS A  90      40.570  -9.648  30.704  0.50 56.61           C  
ANISOU  636  C  BCYS A  90     6232  10091   5184   1565  -1283  -1266       C  
ATOM    637  O  ACYS A  90      37.805  -9.925  31.751  0.50 57.58           O  
ANISOU  637  O  ACYS A  90     5187  11080   5610   4119   -460  -3773       O  
ATOM    638  O  BCYS A  90      41.432  -8.937  30.175  0.50 56.61           O  
ANISOU  638  O  BCYS A  90     5567  13061   2882   1260   -755  -2001       O  
ATOM    639  CB ACYS A  90      38.575  -8.504  33.739  0.50 54.76           C  
ANISOU  639  CB ACYS A  90     6110   8131   6564   2420  -1360  -1404       C  
ATOM    640  CB BCYS A  90      39.847  -9.196  33.073  0.50 49.25           C  
ANISOU  640  CB BCYS A  90     5028   8082   5601    717   -217   -431       C  
ATOM    641  SG ACYS A  90      37.465  -8.546  35.156  0.50 48.22           S  
ANISOU  641  SG ACYS A  90     6967   5357   5995   2862  -1372  -1057       S  
ATOM    642  SG BCYS A  90      38.294  -9.903  33.661  0.50 62.23           S  
ANISOU  642  SG BCYS A  90     4391   9964   9289   -665   -901  -1674       S  
ATOM    643  N  AGLU A  91      39.205 -11.705  31.968  0.50 46.87           N  
ANISOU  643  N  AGLU A  91     4172   7629   6008   1098   -652   -965       N  
ATOM    644  N  BGLU A  91      39.505 -10.063  30.033  0.50 60.69           N  
ANISOU  644  N  BGLU A  91     6229  10655   6178   1428  -1465  -1659       N  
ATOM    645  CA AGLU A  91      38.887 -12.318  30.683  0.50 49.91           C  
ANISOU  645  CA AGLU A  91     4429   8315   6221   2621  -1290  -1389       C  
ATOM    646  CA BGLU A  91      39.102  -9.633  28.701  0.50 58.14           C  
ANISOU  646  CA BGLU A  91     4373  11166   6552    207  -1526   -964       C  
ATOM    647  C  AGLU A  91      37.393 -12.532  30.442  0.50 50.93           C  
ANISOU  647  C  AGLU A  91     4612   8749   5992   1910  -1255  -1446       C  
ATOM    648  C  BGLU A  91      38.027 -10.557  28.116  0.50 56.23           C  
ANISOU  648  C  BGLU A  91     4018  10558   6787    577   -778  -1724       C  
ATOM    649  O  AGLU A  91      36.923 -13.670  30.398  0.50 60.04           O  
ANISOU  649  O  AGLU A  91     7055   9560   6199    273  -2268    220       O  
ATOM    650  O  BGLU A  91      38.331 -11.334  27.208  0.50 61.87           O  
ANISOU  650  O  BGLU A  91     4938  12611   5960   -888    806  -2065       O  
ATOM    651  CB AGLU A  91      39.659 -13.634  30.485  0.50 55.91           C  
ANISOU  651  CB AGLU A  91     5683   8071   7489   2824  -2451  -1791       C  
ATOM    652  CB BGLU A  91      40.269  -9.574  27.710  0.50 62.06           C  
ANISOU  652  CB BGLU A  91     4516  11940   7126   -300  -1248   -633       C  
ATOM    653  CG AGLU A  91      39.785 -14.640  31.599  0.50 49.12           C  
ANISOU  653  CG AGLU A  91     3255   8788   6622   3401  -2267  -2037       C  
ATOM    654  CG BGLU A  91      39.864  -9.137  26.310  0.50 65.43           C  
ANISOU  654  CG BGLU A  91     5689  12201   6971  -1166  -1221   -426       C  
ATOM    655  CD AGLU A  91      38.519 -15.428  31.864  0.50 54.94           C  
ANISOU  655  CD AGLU A  91     5172   8816   6887   1709  -2373  -2587       C  
ATOM    656  CD BGLU A  91      40.555  -9.914  25.205  0.50 64.95           C  
ANISOU  656  CD BGLU A  91     5068  12504   7104  -1638   -988   -541       C  
ATOM    657  OE1AGLU A  91      38.494 -16.650  31.630  0.50 62.42           O  
ANISOU  657  OE1AGLU A  91     9106   9122   5489   1231  -2948  -3219       O  
ATOM    658  OE1BGLU A  91      41.676 -10.422  25.413  0.50 59.90           O  
ANISOU  658  OE1BGLU A  91     3643  11864   7251  -3215   -655   -631       O  
ATOM    659  OE2AGLU A  91      37.516 -14.816  32.295  0.50 53.93           O  
ANISOU  659  OE2AGLU A  91     4309   9528   6653    505  -1262  -2265       O  
ATOM    660  OE2BGLU A  91      39.949 -10.012  24.111  0.50 70.50           O  
ANISOU  660  OE2BGLU A  91     5738  13833   7215   -348  -1314  -1001       O  
ATOM    661  N  AGLY A  92      36.589 -11.482  30.226  0.50 51.16           N  
ANISOU  661  N  AGLY A  92     3804  10052   5583   2761   -239  -1890       N  
ATOM    662  N  BGLY A  92      36.809 -10.434  28.649  0.50 53.88           N  
ANISOU  662  N  BGLY A  92     3895   9576   7000   1125  -1033  -1950       N  
ATOM    663  CA AGLY A  92      35.163 -11.570  30.044  0.50 52.28           C  
ANISOU  663  CA AGLY A  92     4035   9986   5843   1684   -664  -1142       C  
ATOM    664  CA BGLY A  92      35.664 -11.272  28.363  0.50 49.97           C  
ANISOU  664  CA BGLY A  92     3658   9016   6312   1384   -927  -1612       C  
ATOM    665  C  AGLY A  92      34.387 -10.885  28.969  0.50 50.44           C  
ANISOU  665  C  AGLY A  92     4258   8914   5995   1491  -1252  -1786       C  
ATOM    666  C  BGLY A  92      34.535 -10.607  27.608  0.50 48.23           C  
ANISOU  666  C  BGLY A  92     3985   8198   6141   1548  -1001  -2073       C  
ATOM    667  O  AGLY A  92      34.465  -9.664  28.748  0.50 55.29           O  
ANISOU  667  O  AGLY A  92     5851   8725   6434   1259  -2891  -2269       O  
ATOM    668  O  BGLY A  92      34.546  -9.397  27.361  0.50 43.13           O  
ANISOU  668  O  BGLY A  92     3394   7848   5144   2047    532  -2980       O  
ATOM    669  N  ALYS A  93      33.530 -11.598  28.209  0.50 43.38           N  
ANISOU  669  N  ALYS A  93     3310   7759   5414   2450    -88  -2730       N  
ATOM    670  N  BLYS A  93      33.548 -11.439  27.242  0.50 43.19           N  
ANISOU  670  N  BLYS A  93     3275   7597   5536   2396   -397  -3144       N  
ATOM    671  CA ALYS A  93      32.825 -10.911  27.124  0.50 38.66           C  
ANISOU  671  CA ALYS A  93     2912   6687   5088   1711   -130  -3038       C  
ATOM    672  CA BLYS A  93      32.460 -10.994  26.399  0.50 40.63           C  
ANISOU  672  CA BLYS A  93     3409   6532   5494   2343   -338  -3030       C  
ATOM    673  C  ALYS A  93      31.689  -9.990  27.559  0.50 33.27           C  
ANISOU  673  C  ALYS A  93     2593   5163   4885    979      0  -2776       C  
ATOM    674  C  BLYS A  93      31.463 -10.153  27.204  0.50 32.64           C  
ANISOU  674  C  BLYS A  93     2693   4997   4712   1135    -38  -2521       C  
ATOM    675  O  ALYS A  93      30.923 -10.202  28.487  0.50 30.66           O  
ANISOU  675  O  ALYS A  93     3319   4963   3369   1864   -496  -2403       O  
ATOM    676  O  BLYS A  93      30.720 -10.606  28.061  0.50 32.53           O  
ANISOU  676  O  BLYS A  93     4085   4638   3636   1217   -418  -1935       O  
ATOM    677  CB ALYS A  93      32.244 -11.921  26.118  0.50 42.79           C  
ANISOU  677  CB ALYS A  93     5374   5553   5331   2182   -498  -3048       C  
ATOM    678  CB BLYS A  93      31.692 -12.124  25.713  0.50 39.97           C  
ANISOU  678  CB BLYS A  93     4440   6427   4319   2700   -625  -3185       C  
ATOM    679  N   PHE A  94      31.549  -8.900  26.816  1.00 31.21           N  
ANISOU  679  N   PHE A  94     2210   4972   4678    140    621  -2808       N  
ATOM    680  CA  PHE A  94      30.507  -7.930  27.144  1.00 25.00           C  
ANISOU  680  CA  PHE A  94     2108   3715   3676   -442   1195  -1726       C  
ATOM    681  C   PHE A  94      29.158  -8.472  26.740  1.00 22.60           C  
ANISOU  681  C   PHE A  94     2218   2854   3514   -248    680  -1369       C  
ATOM    682  O   PHE A  94      29.079  -9.146  25.734  1.00 24.11           O  
ANISOU  682  O   PHE A  94     2915   3215   3029   -577   1028  -1186       O  
ATOM    683  CB  PHE A  94      30.825  -6.694  26.337  1.00 29.20           C  
ANISOU  683  CB  PHE A  94     3161   4346   3586  -1295   2080  -1747       C  
ATOM    684  CG  PHE A  94      29.853  -5.589  26.442  1.00 23.96           C  
ANISOU  684  CG  PHE A  94     3030   3392   2680  -1717   1179   -940       C  
ATOM    685  CD1 PHE A  94      29.583  -4.997  27.692  1.00 18.67           C  
ANISOU  685  CD1 PHE A  94     2705   2074   2313   -847    540   -379       C  
ATOM    686  CD2 PHE A  94      29.193  -5.169  25.338  1.00 28.90           C  
ANISOU  686  CD2 PHE A  94     4904   4001   2075  -2332   1063   -512       C  
ATOM    687  CE1 PHE A  94      28.650  -4.010  27.735  1.00 17.31           C  
ANISOU  687  CE1 PHE A  94     2411   2135   2032   -895     62    171       C  
ATOM    688  CE2 PHE A  94      28.277  -4.149  25.391  1.00 26.29           C  
ANISOU  688  CE2 PHE A  94     3948   4009   2032  -2690   -106     91       C  
ATOM    689  CZ  PHE A  94      28.022  -3.563  26.611  1.00 23.57           C  
ANISOU  689  CZ  PHE A  94     4012   2640   2303  -1306   -685    233       C  
ATOM    690  N   ASN A  95      28.144  -8.127  27.529  1.00 16.33           N  
ANISOU  690  N   ASN A  95     1948   1961   2296    -81    384   -201       N  
ATOM    691  CA  ASN A  95      26.772  -8.469  27.183  1.00 16.12           C  
ANISOU  691  CA  ASN A  95     2039   1769   2317      0     95     18       C  
ATOM    692  C   ASN A  95      25.966  -7.191  26.945  1.00 15.02           C  
ANISOU  692  C   ASN A  95     1921   1704   2081    -96    456    -73       C  
ATOM    693  O   ASN A  95      25.504  -6.568  27.933  1.00 15.67           O  
ANISOU  693  O   ASN A  95     2110   1864   1980   -139    593   -115       O  
ATOM    694  CB  ASN A  95      26.181  -9.314  28.288  1.00 18.33           C  
ANISOU  694  CB  ASN A  95     1947   2008   3009    147    431    424       C  
ATOM    695  CG  ASN A  95      24.846  -9.897  27.890  1.00 24.01           C  
ANISOU  695  CG  ASN A  95     2124   2400   4599   -140    266    593       C  
ATOM    696  OD1 ASN A  95      24.166  -9.364  27.019  1.00 34.86           O  
ANISOU  696  OD1 ASN A  95     2977   2549   7719   -720  -1898   1249       O  
ATOM    697  ND2 ASN A  95      24.459 -10.995  28.511  1.00 30.52           N  
ANISOU  697  ND2 ASN A  95     3019   2352   6225   -511    331    832       N  
ATOM    698  N   TRP A  96      25.813  -6.798  25.716  1.00 15.18           N  
ANISOU  698  N   TRP A  96     2223   1581   1962    105    486   -104       N  
ATOM    699  CA  TRP A  96      25.094  -5.589  25.332  1.00 15.25           C  
ANISOU  699  CA  TRP A  96     1979   1785   2031    200    555   -147       C  
ATOM    700  C   TRP A  96      23.709  -5.510  25.923  1.00 15.16           C  
ANISOU  700  C   TRP A  96     2116   1650   1994     -3    680   -121       C  
ATOM    701  O   TRP A  96      23.250  -4.443  26.317  1.00 15.39           O  
ANISOU  701  O   TRP A  96     2028   1690   2128     18    761   -268       O  
ATOM    702  CB  TRP A  96      25.032  -5.564  23.775  1.00 16.53           C  
ANISOU  702  CB  TRP A  96     2220   2084   1979    375    666      5       C  
ATOM    703  CG  TRP A  96      24.374  -4.406  23.140  1.00 15.75           C  
ANISOU  703  CG  TRP A  96     1962   2054   1970    400    428   -178       C  
ATOM    704  CD1 TRP A  96      23.031  -4.175  23.020  1.00 17.08           C  
ANISOU  704  CD1 TRP A  96     2072   1962   2456    102    147   -142       C  
ATOM    705  CD2 TRP A  96      25.033  -3.289  22.506  1.00 16.19           C  
ANISOU  705  CD2 TRP A  96     1919   2102   2132    439    288    -64       C  
ATOM    706  NE1 TRP A  96      22.825  -3.003  22.378  1.00 17.37           N  
ANISOU  706  NE1 TRP A  96     1906   2170   2525    126     34    121       N  
ATOM    707  CE2 TRP A  96      24.048  -2.412  22.033  1.00 16.22           C  
ANISOU  707  CE2 TRP A  96     1842   2154   2167    165    -10     13       C  
ATOM    708  CE3 TRP A  96      26.367  -2.969  22.316  1.00 18.89           C  
ANISOU  708  CE3 TRP A  96     1939   2882   2355    415    603    432       C  
ATOM    709  CZ2 TRP A  96      24.372  -1.235  21.372  1.00 17.87           C  
ANISOU  709  CZ2 TRP A  96     2000   2273   2518    250    303    183       C  
ATOM    710  CZ3 TRP A  96      26.686  -1.805  21.658  1.00 18.68           C  
ANISOU  710  CZ3 TRP A  96     2122   2772   2205    323    359    361       C  
ATOM    711  CH2 TRP A  96      25.694  -0.916  21.174  1.00 18.29           C  
ANISOU  711  CH2 TRP A  96     2048   2577   2325     79    190    223       C  
ATOM    712  N   ARG A  97      22.967  -6.644  25.956  1.00 16.61           N  
ANISOU  712  N   ARG A  97     1880   1715   2717     87    433   -363       N  
ATOM    713  CA  ARG A  97      21.585  -6.609  26.474  1.00 18.12           C  
ANISOU  713  CA  ARG A  97     2007   1826   3050   -282    603   -707       C  
ATOM    714  C   ARG A  97      21.521  -6.116  27.916  1.00 15.79           C  
ANISOU  714  C   ARG A  97     1800   1411   2790    -41    652    -81       C  
ATOM    715  O   ARG A  97      20.553  -5.438  28.280  1.00 17.20           O  
ANISOU  715  O   ARG A  97     1708   1863   2964    -49    799   -372       O  
ATOM    716  CB  ARG A  97      20.995  -8.027  26.387  1.00 23.62           C  
ANISOU  716  CB  ARG A  97     2737   2255   3985   -836   1171   -973       C  
ATOM    717  CG  ARG A  97      19.585  -8.113  25.840  1.00 42.77           C  
ANISOU  717  CG  ARG A  97     4492   4384   7376  -2841  -1397    937       C  
ATOM    718  CD  ARG A  97      19.188  -9.515  25.345  1.00 59.16           C  
ANISOU  718  CD  ARG A  97     8575   5483   8420  -5059  -2627    869       C  
ATOM    719  NE  ARG A  97      17.983  -9.401  24.505  1.00 71.59           N  
ANISOU  719  NE  ARG A  97    10565   6970   9665  -5343  -4527    911       N  
ATOM    720  CZ  ARG A  97      17.948  -9.162  23.206  1.00 75.28           C  
ANISOU  720  CZ  ARG A  97     9774   8883   9945  -6308  -4277   1885       C  
ATOM    721  NH1 ARG A  97      19.074  -9.006  22.515  1.00 83.57           N  
ANISOU  721  NH1 ARG A  97     8692  12862  10197    698  -3246   1316       N  
ATOM    722  NH2 ARG A  97      16.818  -9.062  22.525  1.00 76.44           N  
ANISOU  722  NH2 ARG A  97     9179  10136   9728  -6786  -3609   3957       N  
ATOM    723  N   VAL A  98      22.520  -6.434  28.740  1.00 16.21           N  
ANISOU  723  N   VAL A  98     1906   1591   2662    196    814   -104       N  
ATOM    724  CA  VAL A  98      22.492  -6.027  30.152  1.00 16.90           C  
ANISOU  724  CA  VAL A  98     2172   1757   2494    224    839    121       C  
ATOM    725  C   VAL A  98      22.441  -4.495  30.255  1.00 16.00           C  
ANISOU  725  C   VAL A  98     2027   1757   2296     99    859    -43       C  
ATOM    726  O   VAL A  98      21.597  -3.935  30.964  1.00 16.05           O  
ANISOU  726  O   VAL A  98     1731   2034   2335   -248    822   -511       O  
ATOM    727  CB  VAL A  98      23.705  -6.615  30.885  1.00 19.20           C  
ANISOU  727  CB  VAL A  98     2566   2198   2531    465    779    295       C  
ATOM    728  CG1 VAL A  98      23.888  -6.005  32.266  1.00 20.35           C  
ANISOU  728  CG1 VAL A  98     2333   2639   2759    259    464    111       C  
ATOM    729  CG2 VAL A  98      23.610  -8.148  31.046  1.00 24.33           C  
ANISOU  729  CG2 VAL A  98     3669   2133   3445    824    292    256       C  
ATOM    730  N   ILE A  99      23.341  -3.834  29.555  1.00 14.56           N  
ANISOU  730  N   ILE A  99     1593   1669   2269    209    666    -13       N  
ATOM    731  CA  ILE A  99      23.369  -2.398  29.675  1.00 14.96           C  
ANISOU  731  CA  ILE A  99     1271   1702   2710    109    498   -186       C  
ATOM    732  C   ILE A  99      22.250  -1.762  28.880  1.00 12.93           C  
ANISOU  732  C   ILE A  99     1428   1335   2149   -126    612   -121       C  
ATOM    733  O   ILE A  99      21.728  -0.722  29.315  1.00 14.00           O  
ANISOU  733  O   ILE A  99     1312   1544   2465    -33    452   -283       O  
ATOM    734  CB AILE A  99      24.768  -1.882  29.268  0.47 16.09           C  
ANISOU  734  CB AILE A  99     1452   1997   2663   -109    558   -267       C  
ATOM    735  CB BILE A  99      24.750  -1.855  29.230  0.53 15.65           C  
ANISOU  735  CB BILE A  99     1493   1734   2718    243    658    674       C  
ATOM    736  CG1AILE A  99      25.638  -1.880  30.534  0.47 18.85           C  
ANISOU  736  CG1AILE A  99     1079   2920   3163    187    319    947       C  
ATOM    737  CG1BILE A  99      24.840  -0.368  29.638  0.53 17.68           C  
ANISOU  737  CG1BILE A  99     1399   2383   2936   -338    850   -486       C  
ATOM    738  CG2AILE A  99      24.677  -0.528  28.591  0.47 13.75           C  
ANISOU  738  CG2AILE A  99     1178   2576   1470    -27    545    -15       C  
ATOM    739  CG2BILE A  99      25.063  -2.075  27.775  0.53 22.02           C  
ANISOU  739  CG2BILE A  99     1731   3277   3360   -221   1171  -1034       C  
ATOM    740  CD1AILE A  99      25.269  -0.747  31.488  0.47 19.02           C  
ANISOU  740  CD1AILE A  99     1750   3832   1645   -364   -262    619       C  
ATOM    741  CD1BILE A  99      24.718  -0.149  31.136  0.53 18.89           C  
ANISOU  741  CD1BILE A  99     2198   2631   2348   -259  -1027    476       C  
ATOM    742  N   LYS A 100      21.807  -2.325  27.774  1.00 13.85           N  
ANISOU  742  N   LYS A 100     1544   1435   2284      7    633   -188       N  
ATOM    743  CA  LYS A 100      20.677  -1.771  27.030  1.00 14.16           C  
ANISOU  743  CA  LYS A 100     1760   1501   2121    115    531    -62       C  
ATOM    744  C   LYS A 100      19.453  -1.666  27.946  1.00 13.28           C  
ANISOU  744  C   LYS A 100     1550   1586   1911    150    284   -100       C  
ATOM    745  O   LYS A 100      18.760  -0.636  27.948  1.00 13.93           O  
ANISOU  745  O   LYS A 100     1703   1679   1909    288    396    -25       O  
ATOM    746  CB  LYS A 100      20.302  -2.583  25.799  1.00 18.64           C  
ANISOU  746  CB  LYS A 100     2407   2375   2301    154    417   -494       C  
ATOM    747  CG  LYS A 100      18.955  -2.217  25.174  1.00 26.39           C  
ANISOU  747  CG  LYS A 100     2218   4811   2997     35     38   -527       C  
ATOM    748  CD  LYS A 100      18.848  -2.274  23.713  1.00 35.11           C  
ANISOU  748  CD  LYS A 100     2728   7427   3185   1210   -172   -186       C  
ATOM    749  CE  LYS A 100      17.728  -1.375  23.202  1.00 23.44           C  
ANISOU  749  CE  LYS A 100     1943   4515   2447     49    555   -413       C  
ATOM    750  NZ  LYS A 100      16.359  -1.679  23.733  1.00 18.91           N  
ANISOU  750  NZ  LYS A 100     2280   2555   2350   -148    800   -623       N  
ATOM    751  N   GLU A 101      19.181  -2.735  28.694  1.00 13.13           N  
ANISOU  751  N   GLU A 101     1347   1538   2103     94    337   -176       N  
ATOM    752  CA  GLU A 101      17.982  -2.721  29.536  1.00 13.72           C  
ANISOU  752  CA  GLU A 101     1515   1604   2095    -94    293   -179       C  
ATOM    753  C   GLU A 101      18.116  -1.638  30.615  1.00 11.81           C  
ANISOU  753  C   GLU A 101     1232   1506   1750   -110    337     21       C  
ATOM    754  O   GLU A 101      17.143  -0.952  30.930  1.00 12.62           O  
ANISOU  754  O   GLU A 101     1204   1551   2038    -82    368     46       O  
ATOM    755  CB AGLU A 101      17.713  -4.074  30.158  0.57 16.55           C  
ANISOU  755  CB AGLU A 101     1787   1649   2852   -425    314    -90       C  
ATOM    756  CB BGLU A 101      17.845  -4.110  30.135  0.43 15.95           C  
ANISOU  756  CB BGLU A 101     1749   1549   2760   -100    688   -196       C  
ATOM    757  CG AGLU A 101      17.488  -5.220  29.246  0.57 18.70           C  
ANISOU  757  CG AGLU A 101     1603   1833   3668   -272    583   -621       C  
ATOM    758  CG BGLU A 101      16.840  -4.142  31.234  0.43 21.21           C  
ANISOU  758  CG BGLU A 101     1380   3073   3604   -411    966    481       C  
ATOM    759  CD AGLU A 101      17.669  -6.621  29.787  0.57 26.82           C  
ANISOU  759  CD AGLU A 101     3687   1775   4729    -31    236   -589       C  
ATOM    760  CD BGLU A 101      17.103  -3.907  32.692  0.43 30.02           C  
ANISOU  760  CD BGLU A 101     5425   3200   2782   -737   1775   1539       C  
ATOM    761  OE1AGLU A 101      18.020  -6.806  30.968  0.57 25.33           O  
ANISOU  761  OE1AGLU A 101     2918   1889   4817   -221    520     62       O  
ATOM    762  OE1BGLU A 101      16.331  -3.086  33.265  0.43 38.50           O  
ANISOU  762  OE1BGLU A 101     8426   2715   3487    -99   2112    925       O  
ATOM    763  OE2AGLU A 101      17.442  -7.540  28.960  0.57 35.26           O  
ANISOU  763  OE2AGLU A 101     5956   1799   5640   -874   -103   -729       O  
ATOM    764  OE2BGLU A 101      18.047  -4.477  33.248  0.43 32.03           O  
ANISOU  764  OE2BGLU A 101     3130   5879   3161  -2087    246   -450       O  
ATOM    765  N   LYS A 102      19.289  -1.531  31.219  1.00 12.02           N  
ANISOU  765  N   LYS A 102     1276   1404   1885    -30    308     77       N  
ATOM    766  CA  LYS A 102      19.498  -0.549  32.294  1.00 11.32           C  
ANISOU  766  CA  LYS A 102     1198   1526   1578    117    365    113       C  
ATOM    767  C   LYS A 102      19.417   0.880  31.757  1.00 10.67           C  
ANISOU  767  C   LYS A 102     1097   1489   1470    -33    283     86       C  
ATOM    768  O   LYS A 102      18.904   1.779  32.419  1.00 11.51           O  
ANISOU  768  O   LYS A 102     1254   1609   1512    -12    377    -27       O  
ATOM    769  CB  LYS A 102      20.804  -0.792  33.014  1.00 11.92           C  
ANISOU  769  CB  LYS A 102     1176   1694   1660     73    360    100       C  
ATOM    770  CG  LYS A 102      20.839  -2.123  33.766  1.00 13.83           C  
ANISOU  770  CG  LYS A 102     1724   1723   1810     -4     27    155       C  
ATOM    771  CD  LYS A 102      22.152  -2.378  34.459  1.00 14.47           C  
ANISOU  771  CD  LYS A 102     1459   2253   1787     35    153    112       C  
ATOM    772  CE  LYS A 102      22.214  -3.806  35.031  1.00 18.59           C  
ANISOU  772  CE  LYS A 102     2281   2316   2465    700     84    262       C  
ATOM    773  NZ  LYS A 102      23.406  -3.933  35.889  1.00 26.83           N  
ANISOU  773  NZ  LYS A 102     2420   4869   2906   1120     52   1012       N  
ATOM    774  N   ARG A 103      19.959   1.091  30.574  1.00 10.85           N  
ANISOU  774  N   ARG A 103     1131   1428   1565     36    403    134       N  
ATOM    775  CA  ARG A 103      19.915   2.382  29.898  1.00 10.67           C  
ANISOU  775  CA  ARG A 103     1196   1516   1343     65    282     85       C  
ATOM    776  C   ARG A 103      18.488   2.782  29.617  1.00 10.07           C  
ANISOU  776  C   ARG A 103     1121   1358   1347    -36    293    128       C  
ATOM    777  O   ARG A 103      18.063   3.900  29.879  1.00 10.92           O  
ANISOU  777  O   ARG A 103     1213   1376   1559     42    447     18       O  
ATOM    778  CB  ARG A 103      20.772   2.304  28.623  1.00 11.57           C  
ANISOU  778  CB  ARG A 103     1032   1542   1822     32    490    153       C  
ATOM    779  CG  ARG A 103      21.070   3.621  27.953  1.00 11.27           C  
ANISOU  779  CG  ARG A 103     1185   1462   1635    -79    419     83       C  
ATOM    780  CD  ARG A 103      21.759   3.425  26.621  1.00 11.42           C  
ANISOU  780  CD  ARG A 103     1200   1442   1696    -84    417    -56       C  
ATOM    781  NE  ARG A 103      20.744   3.008  25.644  1.00 12.81           N  
ANISOU  781  NE  ARG A 103     1284   1873   1710   -135    311    -10       N  
ATOM    782  CZ  ARG A 103      20.887   2.134  24.643  1.00 13.44           C  
ANISOU  782  CZ  ARG A 103     1397   1966   1746   -303    417    -71       C  
ATOM    783  NH1 ARG A 103      19.859   1.905  23.867  1.00 14.68           N  
ANISOU  783  NH1 ARG A 103     1476   2400   1703   -195    365   -215       N  
ATOM    784  NH2 ARG A 103      22.002   1.492  24.374  1.00 15.14           N  
ANISOU  784  NH2 ARG A 103     1261   2560   1931   -360    404   -520       N  
ATOM    785  N   ASP A 104      17.713   1.838  29.073  1.00 10.75           N  
ANISOU  785  N   ASP A 104     1214   1361   1508    -66    323    -10       N  
ATOM    786  CA  ASP A 104      16.309   2.111  28.781  1.00 11.04           C  
ANISOU  786  CA  ASP A 104     1217   1564   1413    -53    336     52       C  
ATOM    787  C   ASP A 104      15.541   2.432  30.053  1.00 10.32           C  
ANISOU  787  C   ASP A 104     1130   1359   1433   -148    232    -64       C  
ATOM    788  O   ASP A 104      14.657   3.329  30.011  1.00 11.25           O  
ANISOU  788  O   ASP A 104     1117   1486   1673    -60    312    -15       O  
ATOM    789  CB  ASP A 104      15.665   0.909  28.108  1.00 11.71           C  
ANISOU  789  CB  ASP A 104     1262   1559   1629     61    316   -197       C  
ATOM    790  CG  ASP A 104      16.007   0.637  26.645  1.00 13.29           C  
ANISOU  790  CG  ASP A 104     1419   2023   1608   -176    376   -111       C  
ATOM    791  OD1 ASP A 104      16.576   1.525  25.996  1.00 15.56           O  
ANISOU  791  OD1 ASP A 104     1888   2198   1827   -237    608     58       O  
ATOM    792  OD2 ASP A 104      15.642  -0.475  26.165  1.00 15.90           O  
ANISOU  792  OD2 ASP A 104     1903   2252   1885   -355    598   -443       O  
ATOM    793  N   ALA A 105      15.827   1.755  31.142  1.00 11.14           N  
ANISOU  793  N   ALA A 105     1338   1456   1439     -8    454     58       N  
ATOM    794  CA  ALA A 105      15.132   2.046  32.421  1.00 10.57           C  
ANISOU  794  CA  ALA A 105     1143   1461   1411    -51    399    -50       C  
ATOM    795  C   ALA A 105      15.454   3.447  32.870  1.00 10.72           C  
ANISOU  795  C   ALA A 105     1170   1407   1497    -80    313    -18       C  
ATOM    796  O   ALA A 105      14.560   4.188  33.359  1.00 11.06           O  
ANISOU  796  O   ALA A 105     1133   1439   1630     11    520    194       O  
ATOM    797  CB  ALA A 105      15.515   0.998  33.448  1.00 11.84           C  
ANISOU  797  CB  ALA A 105     1516   1468   1515    -85    527    153       C  
ATOM    798  N   TYR A 106      16.705   3.881  32.761  1.00 10.02           N  
ANISOU  798  N   TYR A 106     1078   1445   1285    -41    343    -88       N  
ATOM    799  CA  TYR A 106      17.099   5.246  33.140  1.00  9.97           C  
ANISOU  799  CA  TYR A 106     1018   1395   1375      1    320   -111       C  
ATOM    800  C   TYR A 106      16.357   6.293  32.312  1.00 10.22           C  
ANISOU  800  C   TYR A 106      983   1395   1506   -129    288    -68       C  
ATOM    801  O   TYR A 106      15.818   7.241  32.844  1.00 10.43           O  
ANISOU  801  O   TYR A 106     1055   1398   1510    -28    446     31       O  
ATOM    802  CB  TYR A 106      18.621   5.403  33.061  1.00 10.73           C  
ANISOU  802  CB  TYR A 106     1032   1690   1355    -25    311    -19       C  
ATOM    803  CG  TYR A 106      19.174   6.707  33.477  1.00 10.73           C  
ANISOU  803  CG  TYR A 106      951   1669   1458    -21    250     57       C  
ATOM    804  CD1 TYR A 106      18.670   7.473  34.534  1.00 11.80           C  
ANISOU  804  CD1 TYR A 106     1207   1692   1586   -136    351   -120       C  
ATOM    805  CD2 TYR A 106      20.258   7.260  32.832  1.00 12.16           C  
ANISOU  805  CD2 TYR A 106     1090   1883   1646    -85    370    125       C  
ATOM    806  CE1 TYR A 106      19.233   8.684  34.906  1.00 13.72           C  
ANISOU  806  CE1 TYR A 106     1263   1805   2145   -197    221   -294       C  
ATOM    807  CE2 TYR A 106      20.833   8.422  33.206  1.00 14.10           C  
ANISOU  807  CE2 TYR A 106     1203   2268   1886   -376    188    200       C  
ATOM    808  CZ  TYR A 106      20.313   9.153  34.223  1.00 13.74           C  
ANISOU  808  CZ  TYR A 106     1329   1818   2072   -312    -30     30       C  
ATOM    809  OH  TYR A 106      20.924  10.354  34.574  1.00 17.28           O  
ANISOU  809  OH  TYR A 106     1944   2020   2602   -757   -256    169       O  
ATOM    810  N   VAL A 107      16.272   6.051  31.007  1.00 10.28           N  
ANISOU  810  N   VAL A 107     1103   1331   1473     -8    330    -12       N  
ATOM    811  CA  VAL A 107      15.528   6.951  30.136  1.00 10.12           C  
ANISOU  811  CA  VAL A 107     1055   1362   1427     -1    362    -39       C  
ATOM    812  C   VAL A 107      14.085   7.075  30.613  1.00 10.54           C  
ANISOU  812  C   VAL A 107     1057   1509   1437      4    250   -114       C  
ATOM    813  O   VAL A 107      13.518   8.159  30.668  1.00 10.69           O  
ANISOU  813  O   VAL A 107     1180   1469   1412    106    412     74       O  
ATOM    814  CB  VAL A 107      15.663   6.510  28.689  1.00 11.29           C  
ANISOU  814  CB  VAL A 107     1441   1382   1468    107    515     63       C  
ATOM    815  CG1 VAL A 107      14.719   7.300  27.782  1.00 11.88           C  
ANISOU  815  CG1 VAL A 107     1459   1665   1390     98    402     13       C  
ATOM    816  CG2 VAL A 107      17.101   6.677  28.188  1.00 12.42           C  
ANISOU  816  CG2 VAL A 107     1467   1569   1684    119    643    279       C  
ATOM    817  N   SER A 108      13.466   5.920  30.937  1.00 10.61           N  
ANISOU  817  N   SER A 108     1092   1494   1446    -27    370     88       N  
ATOM    818  CA  SER A 108      12.091   5.945  31.450  1.00 10.76           C  
ANISOU  818  CA  SER A 108     1038   1526   1524     95    327     68       C  
ATOM    819  C   SER A 108      11.956   6.730  32.745  1.00 10.27           C  
ANISOU  819  C   SER A 108     1066   1279   1555    -20    376    122       C  
ATOM    820  O   SER A 108      10.974   7.460  32.914  1.00 10.88           O  
ANISOU  820  O   SER A 108      925   1451   1759    -43    399     12       O  
ATOM    821  CB  SER A 108      11.588   4.510  31.646  1.00 12.57           C  
ANISOU  821  CB  SER A 108     1158   1627   1992   -231    323   -286       C  
ATOM    822  OG  SER A 108      11.442   3.824  30.466  1.00 16.02           O  
ANISOU  822  OG  SER A 108     1756   2110   2222   -459    528   -491       O  
ATOM    823  N   ARG A 109      12.917   6.589  33.665  1.00 10.31           N  
ANISOU  823  N   ARG A 109     1031   1359   1527     19    383     74       N  
ATOM    824  CA  ARG A 109      12.898   7.379  34.884  1.00 10.36           C  
ANISOU  824  CA  ARG A 109      948   1448   1538     86    465     78       C  
ATOM    825  C   ARG A 109      12.935   8.860  34.581  1.00 10.78           C  
ANISOU  825  C   ARG A 109     1130   1416   1550    -48    434     86       C  
ATOM    826  O   ARG A 109      12.231   9.677  35.207  1.00 11.00           O  
ANISOU  826  O   ARG A 109     1217   1503   1460    -24    581     37       O  
ATOM    827  CB  ARG A 109      14.035   7.003  35.811  1.00 10.45           C  
ANISOU  827  CB  ARG A 109     1141   1460   1371     26    479     39       C  
ATOM    828  CG  ARG A 109      13.929   5.602  36.374  1.00 10.93           C  
ANISOU  828  CG  ARG A 109     1165   1543   1446     81    439    205       C  
ATOM    829  CD  ARG A 109      14.889   5.300  37.509  1.00 11.58           C  
ANISOU  829  CD  ARG A 109     1325   1629   1443    141    390     96       C  
ATOM    830  NE  ARG A 109      16.294   5.368  37.225  1.00 12.19           N  
ANISOU  830  NE  ARG A 109     1228   1784   1618    -97    313    -23       N  
ATOM    831  CZ  ARG A 109      17.029   4.420  36.706  1.00 11.43           C  
ANISOU  831  CZ  ARG A 109     1111   1770   1460    -70    260     73       C  
ATOM    832  NH1 ARG A 109      18.346   4.585  36.531  1.00 13.88           N  
ANISOU  832  NH1 ARG A 109     1044   2179   2051    -68    250    159       N  
ATOM    833  NH2 ARG A 109      16.513   3.303  36.267  1.00 11.51           N  
ANISOU  833  NH2 ARG A 109     1103   1815   1456    -21    346     73       N  
ATOM    834  N   LEU A 110      13.774   9.258  33.597  1.00 10.63           N  
ANISOU  834  N   LEU A 110     1109   1342   1589     30    560     20       N  
ATOM    835  CA  LEU A 110      13.861  10.656  33.202  1.00 10.41           C  
ANISOU  835  CA  LEU A 110     1139   1409   1409    -97    403     61       C  
ATOM    836  C   LEU A 110      12.594  11.165  32.542  1.00 10.14           C  
ANISOU  836  C   LEU A 110     1152   1416   1284    -14    473     68       C  
ATOM    837  O   LEU A 110      12.169  12.304  32.766  1.00 11.21           O  
ANISOU  837  O   LEU A 110     1216   1402   1641    -22    494     63       O  
ATOM    838  CB  LEU A 110      15.108  10.870  32.365  1.00 10.72           C  
ANISOU  838  CB  LEU A 110     1089   1469   1516    -82    462     62       C  
ATOM    839  CG  LEU A 110      16.459  10.668  33.058  1.00 11.30           C  
ANISOU  839  CG  LEU A 110     1149   1639   1505     15    460     86       C  
ATOM    840  CD1 LEU A 110      17.567  10.849  32.023  1.00 14.61           C  
ANISOU  840  CD1 LEU A 110     1183   2633   1734    -35    452     30       C  
ATOM    841  CD2 LEU A 110      16.640  11.605  34.214  1.00 14.64           C  
ANISOU  841  CD2 LEU A 110     1234   2386   1942     -7    253   -411       C  
ATOM    842  N   ASN A 111      11.960  10.337  31.720  1.00 10.61           N  
ANISOU  842  N   ASN A 111     1117   1401   1513     92    347     44       N  
ATOM    843  CA  ASN A 111      10.686  10.751  31.137  1.00 10.78           C  
ANISOU  843  CA  ASN A 111     1121   1486   1488     76    338      9       C  
ATOM    844  C   ASN A 111       9.692  11.098  32.242  1.00 10.86           C  
ANISOU  844  C   ASN A 111     1091   1471   1563      2    396     65       C  
ATOM    845  O   ASN A 111       8.956  12.084  32.134  1.00 11.82           O  
ANISOU  845  O   ASN A 111     1200   1641   1649    177    365     15       O  
ATOM    846  CB  ASN A 111      10.100   9.649  30.260  1.00 11.54           C  
ANISOU  846  CB  ASN A 111     1227   1652   1504     11    310      5       C  
ATOM    847  CG  ASN A 111      10.827   9.215  29.044  1.00 11.43           C  
ANISOU  847  CG  ASN A 111     1183   1709   1452     92    305    -35       C  
ATOM    848  OD1 ASN A 111      10.798   8.012  28.718  1.00 13.86           O  
ANISOU  848  OD1 ASN A 111     1416   1882   1968    -54    400   -242       O  
ATOM    849  ND2 ASN A 111      11.471  10.075  28.308  1.00 13.02           N  
ANISOU  849  ND2 ASN A 111     1283   2046   1617   -148    572   -208       N  
ATOM    850  N   ALA A 112       9.647  10.280  33.282  1.00 10.77           N  
ANISOU  850  N   ALA A 112     1131   1392   1569     16    403    -24       N  
ATOM    851  CA  ALA A 112       8.722  10.508  34.400  1.00 10.60           C  
ANISOU  851  CA  ALA A 112     1156   1485   1387    -15    373     -5       C  
ATOM    852  C   ALA A 112       9.083  11.778  35.168  1.00 10.11           C  
ANISOU  852  C   ALA A 112     1009   1474   1358     53    368     36       C  
ATOM    853  O   ALA A 112       8.178  12.527  35.568  1.00 11.27           O  
ANISOU  853  O   ALA A 112     1112   1515   1654     39    510    -23       O  
ATOM    854  CB  ALA A 112       8.675   9.309  35.314  1.00 11.59           C  
ANISOU  854  CB  ALA A 112     1216   1561   1625    -50    398    100       C  
ATOM    855  N   ILE A 113      10.356  12.040  35.379  1.00 10.15           N  
ANISOU  855  N   ILE A 113      954   1391   1512     60    347    -68       N  
ATOM    856  CA  ILE A 113      10.805  13.231  36.065  1.00 10.78           C  
ANISOU  856  CA  ILE A 113     1294   1506   1294     46    328    -53       C  
ATOM    857  C   ILE A 113      10.410  14.466  35.277  1.00 10.76           C  
ANISOU  857  C   ILE A 113     1288   1424   1378    -76    332     72       C  
ATOM    858  O   ILE A 113       9.897  15.439  35.881  1.00 11.71           O  
ANISOU  858  O   ILE A 113     1416   1519   1516     46    430     14       O  
ATOM    859  CB  ILE A 113      12.313  13.174  36.367  1.00 11.58           C  
ANISOU  859  CB  ILE A 113     1284   1532   1583   -112    101      7       C  
ATOM    860  CG1 ILE A 113      12.620  12.168  37.502  1.00 12.19           C  
ANISOU  860  CG1 ILE A 113     1317   1757   1556     27    250     61       C  
ATOM    861  CG2 ILE A 113      12.930  14.540  36.644  1.00 13.84           C  
ANISOU  861  CG2 ILE A 113     1477   1679   2103   -220     51     76       C  
ATOM    862  CD1 ILE A 113      14.019  11.673  37.573  1.00 15.23           C  
ANISOU  862  CD1 ILE A 113     1305   2257   2223     17      6    477       C  
ATOM    863  N   TYR A 114      10.646  14.515  33.975  1.00 11.56           N  
ANISOU  863  N   TYR A 114     1401   1520   1471    136    489    151       N  
ATOM    864  CA  TYR A 114      10.303  15.728  33.251  1.00 12.39           C  
ANISOU  864  CA  TYR A 114     1595   1662   1450    -33    330    306       C  
ATOM    865  C   TYR A 114       8.816  15.962  33.133  1.00 11.95           C  
ANISOU  865  C   TYR A 114     1577   1467   1498    136    358    162       C  
ATOM    866  O   TYR A 114       8.372  17.109  33.132  1.00 13.20           O  
ANISOU  866  O   TYR A 114     1807   1460   1750    113    482    246       O  
ATOM    867  CB  TYR A 114      11.057  15.752  31.853  1.00 13.07           C  
ANISOU  867  CB  TYR A 114     1828   1630   1508    -37    515     68       C  
ATOM    868  CG  TYR A 114      12.508  16.085  32.115  1.00 13.73           C  
ANISOU  868  CG  TYR A 114     1859   1682   1677   -139    552    201       C  
ATOM    869  CD1 TYR A 114      13.507  15.134  32.049  1.00 17.06           C  
ANISOU  869  CD1 TYR A 114     1807   1845   2830   -112    801    220       C  
ATOM    870  CD2 TYR A 114      12.931  17.371  32.540  1.00 15.62           C  
ANISOU  870  CD2 TYR A 114     1895   1912   2127   -241    613   -116       C  
ATOM    871  CE1 TYR A 114      14.821  15.416  32.304  1.00 18.69           C  
ANISOU  871  CE1 TYR A 114     1806   2393   2901    -50    886    290       C  
ATOM    872  CE2 TYR A 114      14.255  17.665  32.839  1.00 17.55           C  
ANISOU  872  CE2 TYR A 114     1890   2434   2345   -491    770   -336       C  
ATOM    873  CZ  TYR A 114      15.216  16.683  32.721  1.00 19.62           C  
ANISOU  873  CZ  TYR A 114     1739   2790   2924   -332    485     90       C  
ATOM    874  OH  TYR A 114      16.570  16.924  33.018  1.00 24.11           O  
ANISOU  874  OH  TYR A 114     1795   3826   3538   -457    233    660       O  
ATOM    875  N   GLN A 115       8.028  14.892  33.031  1.00 12.05           N  
ANISOU  875  N   GLN A 115     1525   1354   1701    243    177     92       N  
ATOM    876  CA  GLN A 115       6.571  15.057  33.113  1.00 12.95           C  
ANISOU  876  CA  GLN A 115     1518   1580   1821    236     15     66       C  
ATOM    877  C   GLN A 115       6.173  15.719  34.429  1.00 12.24           C  
ANISOU  877  C   GLN A 115     1381   1329   1941    135    217     86       C  
ATOM    878  O   GLN A 115       5.403  16.670  34.453  1.00 13.46           O  
ANISOU  878  O   GLN A 115     1366   1496   2250    205    258     60       O  
ATOM    879  CB  GLN A 115       5.861  13.703  32.908  1.00 13.38           C  
ANISOU  879  CB  GLN A 115     1701   1786   1597    -36     16     11       C  
ATOM    880  CG  GLN A 115       4.356  13.806  32.968  1.00 18.37           C  
ANISOU  880  CG  GLN A 115     1622   2413   2943     -6      0    -90       C  
ATOM    881  CD  GLN A 115       3.767  12.434  32.637  1.00 24.14           C  
ANISOU  881  CD  GLN A 115     2729   3141   3301  -1206   -627    197       C  
ATOM    882  OE1 GLN A 115       3.337  12.194  31.523  1.00 30.98           O  
ANISOU  882  OE1 GLN A 115     4731   3333   3708  -1117  -1427    162       O  
ATOM    883  NE2 GLN A 115       3.834  11.505  33.592  1.00 25.64           N  
ANISOU  883  NE2 GLN A 115     3662   2904   3177  -1051   -355     -3       N  
ATOM    884  N   ASN A 116       6.745  15.220  35.527  1.00 11.38           N  
ANISOU  884  N   ASN A 116     1276   1326   1722    203    407     47       N  
ATOM    885  CA  ASN A 116       6.440  15.787  36.827  1.00 11.99           C  
ANISOU  885  CA  ASN A 116     1340   1455   1759    -27    578     47       C  
ATOM    886  C   ASN A 116       6.917  17.224  36.949  1.00 11.43           C  
ANISOU  886  C   ASN A 116     1470   1454   1421    123    449     21       C  
ATOM    887  O   ASN A 116       6.252  18.042  37.582  1.00 12.46           O  
ANISOU  887  O   ASN A 116     1623   1513   1600    132    601    -58       O  
ATOM    888  CB  ASN A 116       7.043  14.916  37.893  1.00 14.19           C  
ANISOU  888  CB  ASN A 116     2217   1454   1722     76    654    175       C  
ATOM    889  CG  ASN A 116       6.678  15.384  39.288  1.00 15.78           C  
ANISOU  889  CG  ASN A 116     2874   1352   1769    -20    917    225       C  
ATOM    890  OD1 ASN A 116       7.550  15.655  40.133  1.00 22.56           O  
ANISOU  890  OD1 ASN A 116     4315   2295   1961   -626    352      1       O  
ATOM    891  ND2 ASN A 116       5.387  15.487  39.558  1.00 18.70           N  
ANISOU  891  ND2 ASN A 116     3358   1790   1956    586   1425    477       N  
ATOM    892  N   ASN A 117       8.063  17.552  36.368  1.00 11.60           N  
ANISOU  892  N   ASN A 117     1317   1380   1711     65    410      7       N  
ATOM    893  CA  ASN A 117       8.525  18.953  36.423  1.00 12.35           C  
ANISOU  893  CA  ASN A 117     1480   1543   1671    -39    280     39       C  
ATOM    894  C   ASN A 117       7.557  19.896  35.798  1.00 12.56           C  
ANISOU  894  C   ASN A 117     1500   1415   1856     91    325     20       C  
ATOM    895  O   ASN A 117       7.323  20.991  36.327  1.00 14.86           O  
ANISOU  895  O   ASN A 117     2303   1428   1914     51     74   -138       O  
ATOM    896  CB  ASN A 117       9.925  19.035  35.783  1.00 12.15           C  
ANISOU  896  CB  ASN A 117     1353   1401   1861    -80    233     34       C  
ATOM    897  CG  ASN A 117      11.090  18.389  36.494  1.00 13.94           C  
ANISOU  897  CG  ASN A 117     1576   1743   1976      2    133    207       C  
ATOM    898  OD1 ASN A 117      12.202  18.189  35.933  1.00 17.89           O  
ANISOU  898  OD1 ASN A 117     1621   2253   2922     58    526    147       O  
ATOM    899  ND2 ASN A 117      10.898  18.080  37.734  1.00 13.87           N  
ANISOU  899  ND2 ASN A 117     1298   1973   2000     55     -8    113       N  
ATOM    900  N   LEU A 118       6.943  19.478  34.682  1.00 11.86           N  
ANISOU  900  N   LEU A 118     1573   1246   1687    210    325     63       N  
ATOM    901  CA  LEU A 118       5.914  20.332  34.076  1.00 12.36           C  
ANISOU  901  CA  LEU A 118     1814   1406   1476    387    421    178       C  
ATOM    902  C   LEU A 118       4.664  20.399  34.941  1.00 12.51           C  
ANISOU  902  C   LEU A 118     1751   1542   1462    376    335     58       C  
ATOM    903  O   LEU A 118       4.142  21.486  35.174  1.00 14.15           O  
ANISOU  903  O   LEU A 118     1923   1649   1805    460    455     97       O  
ATOM    904  CB  LEU A 118       5.560  19.808  32.687  1.00 11.83           C  
ANISOU  904  CB  LEU A 118     1450   1412   1634    192    418     89       C  
ATOM    905  CG  LEU A 118       6.698  19.975  31.622  1.00 12.26           C  
ANISOU  905  CG  LEU A 118     1547   1634   1477    131    461     11       C  
ATOM    906  CD1 LEU A 118       6.140  19.500  30.290  1.00 14.01           C  
ANISOU  906  CD1 LEU A 118     1489   2191   1643   -273    493   -175       C  
ATOM    907  CD2 LEU A 118       7.286  21.360  31.559  1.00 13.71           C  
ANISOU  907  CD2 LEU A 118     1518   1618   2073     23    515     -6       C  
ATOM    908  N   THR A 119       4.147  19.253  35.409  1.00 14.51           N  
ANISOU  908  N   THR A 119     1841   1668   2002    508    817    270       N  
ATOM    909  CA  THR A 119       2.938  19.201  36.219  1.00 18.40           C  
ANISOU  909  CA  THR A 119     1964   2561   2468    505   1211     61       C  
ATOM    910  C   THR A 119       3.099  20.031  37.466  1.00 17.89           C  
ANISOU  910  C   THR A 119     2690   2327   1779   1040   1159    698       C  
ATOM    911  O   THR A 119       2.174  20.767  37.858  1.00 20.71           O  
ANISOU  911  O   THR A 119     3185   2512   2171   1369   1419    512       O  
ATOM    912  CB  THR A 119       2.615  17.683  36.521  1.00 23.18           C  
ANISOU  912  CB  THR A 119     2301   3065   3443   -447   1508    193       C  
ATOM    913  OG1 THR A 119       2.352  17.151  35.228  1.00 26.72           O  
ANISOU  913  OG1 THR A 119     2449   3395   4309   -775   1337   -536       O  
ATOM    914  CG2 THR A 119       1.417  17.690  37.414  1.00 26.99           C  
ANISOU  914  CG2 THR A 119     2537   3052   4668    243   2011    311       C  
ATOM    915  N   LYS A 120       4.212  19.932  38.164  1.00 20.29           N  
ANISOU  915  N   LYS A 120     3324   2741   1643   1357    723    590       N  
ATOM    916  CA  LYS A 120       4.456  20.645  39.418  1.00 24.91           C  
ANISOU  916  CA  LYS A 120     4300   3413   1752   1915    587    220       C  
ATOM    917  C   LYS A 120       4.530  22.138  39.203  1.00 24.50           C  
ANISOU  917  C   LYS A 120     4139   3215   1956   2359    287   -234       C  
ATOM    918  O   LYS A 120       4.267  22.890  40.127  1.00 29.70           O  
ANISOU  918  O   LYS A 120     5174   4192   1919   2687   -164   -855       O  
ATOM    919  CB  LYS A 120       5.764  20.112  40.054  1.00 34.50           C  
ANISOU  919  CB  LYS A 120     6838   3332   2940   3033  -1634   -735       C  
ATOM    920  CG  LYS A 120       5.468  19.086  41.154  1.00 54.11           C  
ANISOU  920  CG  LYS A 120    10119   5346   5093   2309  -2813   1596       C  
ATOM    921  CD  LYS A 120       6.436  19.450  42.290  1.00 62.10           C  
ANISOU  921  CD  LYS A 120    12875   5350   5368   1512  -4105   2117       C  
ATOM    922  CE  LYS A 120       7.863  19.058  41.903  1.00 68.49           C  
ANISOU  922  CE  LYS A 120    11806   3307  10908   2102  -6432   1010       C  
ATOM    923  NZ  LYS A 120       8.648  18.413  43.001  1.00109.88           N  
ANISOU  923  NZ  LYS A 120    19890   6409  15451   5551 -12129   -135       N  
ATOM    924  N   SER A 121       4.908  22.527  37.984  1.00 21.66           N  
ANISOU  924  N   SER A 121     3940   2569   1720   1630   -219   -290       N  
ATOM    925  CA  SER A 121       4.974  23.935  37.587  1.00 21.52           C  
ANISOU  925  CA  SER A 121     3689   2477   2012   1425   -762   -636       C  
ATOM    926  C   SER A 121       3.633  24.378  37.044  1.00 17.68           C  
ANISOU  926  C   SER A 121     2936   2179   1604   1144     81   -274       C  
ATOM    927  O   SER A 121       3.493  25.518  36.595  1.00 18.65           O  
ANISOU  927  O   SER A 121     2691   2226   2170   1018    234   -103       O  
ATOM    928  CB  SER A 121       6.105  24.163  36.610  1.00 23.32           C  
ANISOU  928  CB  SER A 121     2428   2134   4300    405   -797   -505       C  
ATOM    929  OG  SER A 121       7.458  24.009  36.959  1.00 33.32           O  
ANISOU  929  OG  SER A 121     2977   3640   6043   1153  -1736  -1679       O  
ATOM    930  N   HIS A 122       2.612  23.561  36.975  1.00 17.73           N  
ANISOU  930  N   HIS A 122     2910   2202   1623   1164    555     33       N  
ATOM    931  CA  HIS A 122       1.312  23.910  36.435  1.00 16.66           C  
ANISOU  931  CA  HIS A 122     2487   2007   1837    823    762    280       C  
ATOM    932  C   HIS A 122       1.385  24.300  34.983  1.00 14.72           C  
ANISOU  932  C   HIS A 122     1758   1930   1903    631    679    333       C  
ATOM    933  O   HIS A 122       0.637  25.148  34.514  1.00 17.05           O  
ANISOU  933  O   HIS A 122     1920   2529   2030   1027    564    236       O  
ATOM    934  CB  HIS A 122       0.621  25.045  37.292  1.00 23.69           C  
ANISOU  934  CB  HIS A 122     3112   3614   2276   1727   1069    -48       C  
ATOM    935  CG  HIS A 122       0.795  24.720  38.755  1.00 31.20           C  
ANISOU  935  CG  HIS A 122     4679   4963   2211   2666   1633    -36       C  
ATOM    936  ND1 HIS A 122       1.447  25.490  39.680  1.00 35.68           N  
ANISOU  936  ND1 HIS A 122     5054   6501   2001   2596    990    -97       N  
ATOM    937  CD2 HIS A 122       0.403  23.603  39.401  1.00 38.80           C  
ANISOU  937  CD2 HIS A 122     5951   6392   2400   2017   2030    885       C  
ATOM    938  CE1 HIS A 122       1.442  24.878  40.849  1.00 37.99           C  
ANISOU  938  CE1 HIS A 122     4958   7246   2229   3441   1541    249       C  
ATOM    939  NE2 HIS A 122       0.802  23.724  40.709  1.00 48.44           N  
ANISOU  939  NE2 HIS A 122     7867   7941   2596   1852   1392   1050       N  
ATOM    940  N   ILE A 123       2.241  23.616  34.245  1.00 12.28           N  
ANISOU  940  N   ILE A 123     1305   1616   1746    242    418     57       N  
ATOM    941  CA  ILE A 123       2.369  23.769  32.794  1.00 11.78           C  
ANISOU  941  CA  ILE A 123     1122   1680   1673     36    251    194       C  
ATOM    942  C   ILE A 123       1.535  22.684  32.167  1.00 12.06           C  
ANISOU  942  C   ILE A 123     1190   1761   1630    -18    479    105       C  
ATOM    943  O   ILE A 123       1.777  21.524  32.432  1.00 14.67           O  
ANISOU  943  O   ILE A 123     1556   1791   2228   -103    173    223       O  
ATOM    944  CB  ILE A 123       3.827  23.730  32.350  1.00 11.12           C  
ANISOU  944  CB  ILE A 123     1122   1522   1582    111    347     81       C  
ATOM    945  CG1 ILE A 123       4.621  24.877  33.018  1.00 12.26           C  
ANISOU  945  CG1 ILE A 123     1212   1583   1864     75    315    102       C  
ATOM    946  CG2 ILE A 123       3.935  23.735  30.844  1.00 12.77           C  
ANISOU  946  CG2 ILE A 123     1266   1940   1646    197    260    226       C  
ATOM    947  CD1 ILE A 123       6.133  24.690  32.965  1.00 15.31           C  
ANISOU  947  CD1 ILE A 123     1220   1787   2811    -92    189   -254       C  
ATOM    948  N   GLU A 124       0.582  23.059  31.309  1.00 12.83           N  
ANISOU  948  N   GLU A 124     1095   1863   1918     90    376   -120       N  
ATOM    949  CA  GLU A 124      -0.227  22.053  30.630  1.00 13.05           C  
ANISOU  949  CA  GLU A 124     1224   2005   1730    -96    544   -154       C  
ATOM    950  C   GLU A 124       0.583  21.269  29.634  1.00 12.90           C  
ANISOU  950  C   GLU A 124     1119   1846   1935    -18    512    -82       C  
ATOM    951  O   GLU A 124       1.357  21.893  28.906  1.00 13.68           O  
ANISOU  951  O   GLU A 124     1508   1878   1812    -80    649    -17       O  
ATOM    952  CB  GLU A 124      -1.405  22.777  29.941  1.00 15.37           C  
ANISOU  952  CB  GLU A 124     1096   2482   2263    197    412   -433       C  
ATOM    953  CG  GLU A 124      -2.367  21.848  29.237  1.00 21.78           C  
ANISOU  953  CG  GLU A 124     1820   3584   2871   -552      5   -356       C  
ATOM    954  CD  GLU A 124      -3.662  22.464  28.774  1.00 27.43           C  
ANISOU  954  CD  GLU A 124     1441   5030   3950     18    -58  -1279       C  
ATOM    955  OE1 GLU A 124      -4.378  21.735  28.026  1.00 34.15           O  
ANISOU  955  OE1 GLU A 124     2037   6066   4873    384   -508  -2271       O  
ATOM    956  OE2 GLU A 124      -3.943  23.619  29.185  1.00 33.21           O  
ANISOU  956  OE2 GLU A 124     1757   5017   5846    135    -50  -1693       O  
ATOM    957  N   ILE A 125       0.377  19.969  29.551  1.00 12.91           N  
ANISOU  957  N   ILE A 125     1304   1883   1718   -296    488   -119       N  
ATOM    958  CA  ILE A 125       0.998  19.155  28.541  1.00 13.11           C  
ANISOU  958  CA  ILE A 125     1142   1916   1925   -240    350   -275       C  
ATOM    959  C   ILE A 125      -0.069  18.794  27.504  1.00 13.65           C  
ANISOU  959  C   ILE A 125      943   2272   1970   -177    379   -331       C  
ATOM    960  O   ILE A 125      -1.073  18.169  27.825  1.00 16.12           O  
ANISOU  960  O   ILE A 125     1344   2614   2167   -650    378   -183       O  
ATOM    961  CB  ILE A 125       1.587  17.877  29.149  1.00 14.22           C  
ANISOU  961  CB  ILE A 125     1323   1856   2223   -332    322   -147       C  
ATOM    962  CG1 ILE A 125       2.555  18.167  30.281  1.00 15.66           C  
ANISOU  962  CG1 ILE A 125     1647   1968   2335   -158     93      0       C  
ATOM    963  CG2 ILE A 125       2.209  16.968  28.071  1.00 17.43           C  
ANISOU  963  CG2 ILE A 125     1976   2238   2410    324    155   -294       C  
ATOM    964  CD1 ILE A 125       3.054  16.994  31.118  1.00 17.75           C  
ANISOU  964  CD1 ILE A 125     1761   2053   2929    298     78     89       C  
ATOM    965  N   ILE A 126       0.187  19.178  26.264  1.00 13.49           N  
ANISOU  965  N   ILE A 126     1087   2169   1870   -296    412   -460       N  
ATOM    966  CA  ILE A 126      -0.684  18.875  25.140  1.00 14.10           C  
ANISOU  966  CA  ILE A 126     1148   2232   1976   -233    291   -332       C  
ATOM    967  C   ILE A 126      -0.021  17.782  24.319  1.00 13.78           C  
ANISOU  967  C   ILE A 126     1328   2119   1790   -426    261   -364       C  
ATOM    968  O   ILE A 126       1.046  17.998  23.757  1.00 14.49           O  
ANISOU  968  O   ILE A 126     1299   2100   2108   -354    511   -180       O  
ATOM    969  CB  ILE A 126      -0.975  20.137  24.311  1.00 14.34           C  
ANISOU  969  CB  ILE A 126     1124   2333   1990   -110    353   -333       C  
ATOM    970  CG1 ILE A 126      -1.548  21.278  25.136  1.00 16.10           C  
ANISOU  970  CG1 ILE A 126     1319   2422   2375    190    282   -278       C  
ATOM    971  CG2 ILE A 126      -1.872  19.795  23.120  1.00 17.03           C  
ANISOU  971  CG2 ILE A 126     1491   2568   2411   -268    -81   -118       C  
ATOM    972  CD1 ILE A 126      -1.581  22.651  24.473  1.00 19.58           C  
ANISOU  972  CD1 ILE A 126     1655   2394   3392    270   -244   -200       C  
ATOM    973  N   ARG A 127      -0.598  16.595  24.280  1.00 14.83           N  
ANISOU  973  N   ARG A 127     1391   2098   2147   -463    498   -293       N  
ATOM    974  CA  ARG A 127       0.000  15.457  23.619  1.00 15.68           C  
ANISOU  974  CA  ARG A 127     1626   2097   2235   -571    540   -499       C  
ATOM    975  C   ARG A 127      -0.446  15.398  22.183  1.00 16.58           C  
ANISOU  975  C   ARG A 127     1420   2531   2351   -567    426   -602       C  
ATOM    976  O   ARG A 127      -1.649  15.258  21.883  1.00 23.25           O  
ANISOU  976  O   ARG A 127     1412   4672   2751   -723    378   -756       O  
ATOM    977  CB  ARG A 127      -0.406  14.183  24.355  1.00 22.25           C  
ANISOU  977  CB  ARG A 127     3612   2018   2824   -617    869   -359       C  
ATOM    978  CG  ARG A 127      -0.012  14.250  25.826  1.00 27.70           C  
ANISOU  978  CG  ARG A 127     4969   2363   3193    240     21    397       C  
ATOM    979  CD  ARG A 127       1.258  13.518  26.047  1.00 31.88           C  
ANISOU  979  CD  ARG A 127     3403   5256   3456    373    -51  -2438       C  
ATOM    980  NE  ARG A 127       1.854  13.387  27.338  1.00 28.78           N  
ANISOU  980  NE  ARG A 127     3565   4097   3273    879    637   -687       N  
ATOM    981  CZ  ARG A 127       3.156  13.078  27.561  1.00 22.62           C  
ANISOU  981  CZ  ARG A 127     3329   2700   2565    107    772   -156       C  
ATOM    982  NH1 ARG A 127       4.002  12.880  26.595  1.00 23.37           N  
ANISOU  982  NH1 ARG A 127     3148   3128   2604    -17    886    490       N  
ATOM    983  NH2 ARG A 127       3.642  12.986  28.806  1.00 26.74           N  
ANISOU  983  NH2 ARG A 127     4337   3298   2526   -762    452    476       N  
ATOM    984  N   GLY A 128       0.428  15.473  21.217  1.00 14.40           N  
ANISOU  984  N   GLY A 128     1248   2162   2062   -285    128   -257       N  
ATOM    985  CA  GLY A 128       0.104  15.348  19.832  1.00 15.35           C  
ANISOU  985  CA  GLY A 128     1292   2380   2160   -308     62   -286       C  
ATOM    986  C   GLY A 128       1.062  16.219  19.018  1.00 13.81           C  
ANISOU  986  C   GLY A 128     1351   1925   1970    -62      4   -266       C  
ATOM    987  O   GLY A 128       1.994  16.839  19.535  1.00 14.24           O  
ANISOU  987  O   GLY A 128     1356   2002   2052   -141    210   -248       O  
ATOM    988  N   HIS A 129       0.828  16.214  17.692  1.00 15.33           N  
ANISOU  988  N   HIS A 129     1456   2320   2050    -65    -48   -220       N  
ATOM    989  CA  HIS A 129       1.604  16.970  16.727  1.00 15.31           C  
ANISOU  989  CA  HIS A 129     1617   2279   1919     14     64   -353       C  
ATOM    990  C   HIS A 129       0.982  18.309  16.418  1.00 14.19           C  
ANISOU  990  C   HIS A 129     1274   2369   1747     23    -70   -237       C  
ATOM    991  O   HIS A 129      -0.167  18.405  15.968  1.00 16.14           O  
ANISOU  991  O   HIS A 129     1303   2693   2136    -19    -95   -349       O  
ATOM    992  CB  HIS A 129       1.743  16.127  15.439  1.00 16.97           C  
ANISOU  992  CB  HIS A 129     1688   2678   2083     89     35   -612       C  
ATOM    993  CG  HIS A 129       2.513  16.865  14.391  1.00 17.74           C  
ANISOU  993  CG  HIS A 129     2054   2587   2101    243    260   -607       C  
ATOM    994  ND1 HIS A 129       1.969  17.696  13.461  1.00 21.25           N  
ANISOU  994  ND1 HIS A 129     2925   2909   2240    595    397   -463       N  
ATOM    995  CD2 HIS A 129       3.860  16.883  14.162  1.00 20.03           C  
ANISOU  995  CD2 HIS A 129     2160   3644   1805   -285    312   -606       C  
ATOM    996  CE1 HIS A 129       2.898  18.231  12.651  1.00 22.12           C  
ANISOU  996  CE1 HIS A 129     3537   3077   1791     71    417   -662       C  
ATOM    997  NE2 HIS A 129       4.069  17.735  13.079  1.00 23.24           N  
ANISOU  997  NE2 HIS A 129     3066   3814   1951   -312    551   -515       N  
ATOM    998  N   ALA A 130       1.699  19.392  16.683  1.00 13.13           N  
ANISOU  998  N   ALA A 130     1076   2365   1547    157     68   -134       N  
ATOM    999  CA  ALA A 130       1.262  20.757  16.389  1.00 13.55           C  
ANISOU  999  CA  ALA A 130     1277   2280   1592    160    142   -243       C  
ATOM   1000  C   ALA A 130       1.584  21.177  14.964  1.00 13.10           C  
ANISOU 1000  C   ALA A 130     1108   2298   1569     49    -21   -204       C  
ATOM   1001  O   ALA A 130       2.694  20.854  14.474  1.00 15.00           O  
ANISOU 1001  O   ALA A 130     1211   2683   1806    179    233     71       O  
ATOM   1002  CB  ALA A 130       1.884  21.793  17.317  1.00 13.64           C  
ANISOU 1002  CB  ALA A 130     1292   2461   1429     36    136   -151       C  
ATOM   1003  N   ALA A 131       0.702  21.910  14.346  1.00 14.61           N  
ANISOU 1003  N   ALA A 131     1233   2760   1557    190      3   -115       N  
ATOM   1004  CA  ALA A 131       0.948  22.683  13.143  1.00 15.27           C  
ANISOU 1004  CA  ALA A 131     1428   2853   1520    325     27    -35       C  
ATOM   1005  C   ALA A 131       0.268  24.022  13.212  1.00 14.84           C  
ANISOU 1005  C   ALA A 131     1296   2778   1563    224    128   -133       C  
ATOM   1006  O   ALA A 131      -0.788  24.145  13.834  1.00 16.86           O  
ANISOU 1006  O   ALA A 131     1539   3066   1800    455    312    119       O  
ATOM   1007  CB  ALA A 131       0.511  21.930  11.873  1.00 17.07           C  
ANISOU 1007  CB  ALA A 131     2312   2628   1547    285     66    -76       C  
ATOM   1008  N   PHE A 132       0.837  25.033  12.568  1.00 14.71           N  
ANISOU 1008  N   PHE A 132     1313   2841   1438    469    178      4       N  
ATOM   1009  CA  PHE A 132       0.177  26.320  12.504  1.00 15.92           C  
ANISOU 1009  CA  PHE A 132     1373   2862   1812    475    123     48       C  
ATOM   1010  C   PHE A 132      -1.048  26.296  11.605  1.00 17.03           C  
ANISOU 1010  C   PHE A 132     1625   3199   1648    606    -33    152       C  
ATOM   1011  O   PHE A 132      -1.122  25.515  10.659  1.00 19.19           O  
ANISOU 1011  O   PHE A 132     1846   3659   1785    429   -124    -35       O  
ATOM   1012  CB  PHE A 132       1.175  27.397  11.977  1.00 16.88           C  
ANISOU 1012  CB  PHE A 132     1809   2793   1813    366    174     14       C  
ATOM   1013  CG  PHE A 132       2.272  27.694  13.005  1.00 14.44           C  
ANISOU 1013  CG  PHE A 132     1729   2237   1521    294    241    226       C  
ATOM   1014  CD1 PHE A 132       3.533  27.142  12.938  1.00 14.96           C  
ANISOU 1014  CD1 PHE A 132     1699   2352   1635    172    177    -89       C  
ATOM   1015  CD2 PHE A 132       1.996  28.578  14.072  1.00 15.48           C  
ANISOU 1015  CD2 PHE A 132     2003   2302   1577    511    243    292       C  
ATOM   1016  CE1 PHE A 132       4.478  27.434  13.883  1.00 15.79           C  
ANISOU 1016  CE1 PHE A 132     1862   2397   1740    318    -43   -195       C  
ATOM   1017  CE2 PHE A 132       2.962  28.829  15.045  1.00 16.86           C  
ANISOU 1017  CE2 PHE A 132     2225   2535   1646    569    140    -14       C  
ATOM   1018  CZ  PHE A 132       4.208  28.268  14.958  1.00 16.02           C  
ANISOU 1018  CZ  PHE A 132     2145   2508   1433    612     38    -32       C  
ATOM   1019  N   THR A 133      -1.974  27.168  11.921  1.00 19.45           N  
ANISOU 1019  N   THR A 133     1692   3755   1941    960     61    323       N  
ATOM   1020  CA  THR A 133      -3.126  27.406  11.036  1.00 22.64           C  
ANISOU 1020  CA  THR A 133     1864   4549   2188   1062    -70    777       C  
ATOM   1021  C   THR A 133      -2.979  28.710  10.284  1.00 24.65           C  
ANISOU 1021  C   THR A 133     2310   4889   2167   1307    206   1028       C  
ATOM   1022  O   THR A 133      -2.046  29.466  10.569  1.00 26.39           O  
ANISOU 1022  O   THR A 133     2690   4500   2836   1079    726    751       O  
ATOM   1023  CB  THR A 133      -4.448  27.463  11.838  1.00 22.81           C  
ANISOU 1023  CB  THR A 133     1774   4290   2603    625     28    246       C  
ATOM   1024  OG1 THR A 133      -4.492  28.737  12.474  1.00 24.56           O  
ANISOU 1024  OG1 THR A 133     2219   4405   2707    680     50    101       O  
ATOM   1025  CG2 THR A 133      -4.564  26.378  12.892  1.00 24.84           C  
ANISOU 1025  CG2 THR A 133     1866   4541   3030    203    174    495       C  
ATOM   1026  N   SER A 134      -3.947  28.938   9.391  1.00 30.10           N  
ANISOU 1026  N   SER A 134     2856   5948   2631   2011    -70   1312       N  
ATOM   1027  CA  SER A 134      -3.888  30.174   8.620  1.00 35.87           C  
ANISOU 1027  CA  SER A 134     5076   5886   2666   2508   -282   1244       C  
ATOM   1028  C   SER A 134      -4.521  31.402   9.285  1.00 39.61           C  
ANISOU 1028  C   SER A 134     5273   6279   3497   3066   -160   1200       C  
ATOM   1029  O   SER A 134      -4.604  32.480   8.648  1.00 41.71           O  
ANISOU 1029  O   SER A 134     6190   6060   3598   2968   -123   1075       O  
ATOM   1030  CB ASER A 134      -4.583  30.015   7.245  0.73 45.69           C  
ANISOU 1030  CB ASER A 134     7286   7488   2587   2523   -830   1493       C  
ATOM   1031  CB BSER A 134      -4.514  29.944   7.229  0.27 41.30           C  
ANISOU 1031  CB BSER A 134     5982   7212   2500   1940   -362   1568       C  
ATOM   1032  OG ASER A 134      -5.889  29.489   7.421  0.73 57.81           O  
ANISOU 1032  OG ASER A 134     6571  10254   5140   2213  -2792   1905       O  
ATOM   1033  OG BSER A 134      -3.702  29.034   6.491  0.27 30.79           O  
ANISOU 1033  OG BSER A 134     2556   6840   2302   -783    304   1149       O  
ATOM   1034  N   ASP A 135      -4.958  31.267  10.514  1.00 33.04           N  
ANISOU 1034  N   ASP A 135     2949   5691   3915   2281      9    937       N  
ATOM   1035  CA  ASP A 135      -5.510  32.381  11.275  1.00 35.46           C  
ANISOU 1035  CA  ASP A 135     3243   5864   4366   2344   -386    408       C  
ATOM   1036  C   ASP A 135      -4.476  33.498  11.350  1.00 43.69           C  
ANISOU 1036  C   ASP A 135     5487   5543   5571   1523  -2140   1591       C  
ATOM   1037  O   ASP A 135      -3.302  33.266  11.698  1.00 40.06           O  
ANISOU 1037  O   ASP A 135     4242   4843   6134    759   -361   2609       O  
ATOM   1038  CB  ASP A 135      -5.983  31.905  12.659  1.00 40.10           C  
ANISOU 1038  CB  ASP A 135     3772   6869   4596   3113    438    444       C  
ATOM   1039  CG  ASP A 135      -6.966  30.745  12.469  1.00 48.93           C  
ANISOU 1039  CG  ASP A 135     3127   8449   7015   2099   -515   2811       C  
ATOM   1040  OD1 ASP A 135      -6.854  29.665  13.084  1.00 43.93           O  
ANISOU 1040  OD1 ASP A 135     5123   7598   3971   2302    284   1235       O  
ATOM   1041  OD2 ASP A 135      -7.907  30.932  11.642  1.00 70.44           O  
ANISOU 1041  OD2 ASP A 135     6798   7776  12189   2799  -4906   1632       O  
ATOM   1042  N   PRO A 136      -4.858  34.714  10.967  1.00 51.95           N  
ANISOU 1042  N   PRO A 136     7333   5683   6723   2046  -3164   1372       N  
ATOM   1043  CA  PRO A 136      -3.864  35.808  10.993  1.00 48.38           C  
ANISOU 1043  CA  PRO A 136     7594   5694   5093   1808  -1058   2637       C  
ATOM   1044  C   PRO A 136      -3.232  35.978  12.362  1.00 39.02           C  
ANISOU 1044  C   PRO A 136     3242   5864   5720   1557   -532   2074       C  
ATOM   1045  O   PRO A 136      -2.026  36.211  12.452  1.00 53.31           O  
ANISOU 1045  O   PRO A 136     3446   5965  10845    874   -443   2488       O  
ATOM   1046  CB  PRO A 136      -4.698  37.044  10.620  1.00 63.12           C  
ANISOU 1046  CB  PRO A 136    10231   6059   7694   2218  -3742   2822       C  
ATOM   1047  CG  PRO A 136      -5.727  36.456   9.699  1.00 67.03           C  
ANISOU 1047  CG  PRO A 136    10260   6561   8646   2260  -4108   2514       C  
ATOM   1048  CD  PRO A 136      -6.142  35.213  10.453  1.00 58.85           C  
ANISOU 1048  CD  PRO A 136     7837   6614   7909   2833  -3106   2099       C  
ATOM   1049  N   LYS A 137      -4.049  35.811  13.394  1.00 37.43           N  
ANISOU 1049  N   LYS A 137     4051   4934   5236   2511    -23    411       N  
ATOM   1050  CA  LYS A 137      -3.482  35.680  14.726  1.00 31.22           C  
ANISOU 1050  CA  LYS A 137     2859   3567   5438   1408    -86    394       C  
ATOM   1051  C   LYS A 137      -2.842  34.298  14.956  1.00 24.34           C  
ANISOU 1051  C   LYS A 137     1765   3266   4215    867    619    174       C  
ATOM   1052  O   LYS A 137      -3.602  33.305  14.837  1.00 27.76           O  
ANISOU 1052  O   LYS A 137     2340   3674   4532    380   -546   1179       O  
ATOM   1053  CB  LYS A 137      -4.557  35.821  15.786  1.00 37.81           C  
ANISOU 1053  CB  LYS A 137     4373   4680   5312   2696    276  -1015       C  
ATOM   1054  CG  LYS A 137      -4.035  35.695  17.211  1.00 51.49           C  
ANISOU 1054  CG  LYS A 137     8890   5577   5097   2444   -354   -928       C  
ATOM   1055  CD  LYS A 137      -5.109  36.076  18.228  1.00 58.32           C  
ANISOU 1055  CD  LYS A 137     9335   8051   4774   2496     83   -306       C  
ATOM   1056  CE  LYS A 137      -5.315  34.989  19.275  1.00 71.80           C  
ANISOU 1056  CE  LYS A 137    12863   9872   4547   1649   -226    454       C  
ATOM   1057  NZ  LYS A 137      -6.459  35.281  20.193  1.00 87.19           N  
ANISOU 1057  NZ  LYS A 137    15626  14624   2879    755   1064   -553       N  
ATOM   1058  N   PRO A 138      -1.553  34.250  15.232  1.00 22.96           N  
ANISOU 1058  N   PRO A 138     2094   3084   3545    705    -94    239       N  
ATOM   1059  CA  PRO A 138      -0.902  32.939  15.293  1.00 19.77           C  
ANISOU 1059  CA  PRO A 138     1810   2971   2732    603    330    -55       C  
ATOM   1060  C   PRO A 138      -1.574  31.951  16.241  1.00 19.25           C  
ANISOU 1060  C   PRO A 138     1620   3117   2580    577    268     41       C  
ATOM   1061  O   PRO A 138      -1.808  32.241  17.412  1.00 19.54           O  
ANISOU 1061  O   PRO A 138     1725   3009   2691    555    276   -160       O  
ATOM   1062  CB  PRO A 138       0.514  33.278  15.746  1.00 20.65           C  
ANISOU 1062  CB  PRO A 138     1844   3025   2975    414    230    214       C  
ATOM   1063  CG  PRO A 138       0.750  34.657  15.214  1.00 23.65           C  
ANISOU 1063  CG  PRO A 138     2191   3092   3702    393    209    469       C  
ATOM   1064  CD  PRO A 138      -0.576  35.350  15.410  1.00 25.06           C  
ANISOU 1064  CD  PRO A 138     2371   2952   4198    530    181    329       C  
ATOM   1065  N   THR A 139      -1.874  30.800  15.680  1.00 18.20           N  
ANISOU 1065  N   THR A 139     1781   2984   2149    725    457    265       N  
ATOM   1066  CA  THR A 139      -2.698  29.748  16.298  1.00 18.01           C  
ANISOU 1066  CA  THR A 139     1712   2987   2146    631    521    136       C  
ATOM   1067  C   THR A 139      -2.146  28.431  15.795  1.00 16.68           C  
ANISOU 1067  C   THR A 139     1866   3002   1469    731    222     56       C  
ATOM   1068  O   THR A 139      -1.692  28.308  14.635  1.00 19.96           O  
ANISOU 1068  O   THR A 139     2382   3552   1648    801    631    187       O  
ATOM   1069  CB  THR A 139      -4.166  29.921  15.842  1.00 21.66           C  
ANISOU 1069  CB  THR A 139     1782   3423   3024    836    181    248       C  
ATOM   1070  OG1 THR A 139      -4.599  31.223  16.223  1.00 23.99           O  
ANISOU 1070  OG1 THR A 139     1905   3524   3688    873    -44   -107       O  
ATOM   1071  CG2 THR A 139      -5.161  28.929  16.393  1.00 21.86           C  
ANISOU 1071  CG2 THR A 139     1788   3733   2783    320   -229   -181       C  
ATOM   1072  N   ILE A 140      -2.171  27.433  16.634  1.00 14.78           N  
ANISOU 1072  N   ILE A 140     1346   2827   1441    457    177   -114       N  
ATOM   1073  CA  ILE A 140      -1.775  26.083  16.283  1.00 15.05           C  
ANISOU 1073  CA  ILE A 140     1324   2778   1618    338    218   -229       C  
ATOM   1074  C   ILE A 140      -2.994  25.148  16.468  1.00 15.64           C  
ANISOU 1074  C   ILE A 140     1330   2855   1757    394    244   -208       C  
ATOM   1075  O   ILE A 140      -3.908  25.476  17.201  1.00 17.55           O  
ANISOU 1075  O   ILE A 140     1483   3163   2023    290    445   -500       O  
ATOM   1076  CB  ILE A 140      -0.588  25.557  17.112  1.00 15.94           C  
ANISOU 1076  CB  ILE A 140     1298   2735   2024    333    221    110       C  
ATOM   1077  CG1 ILE A 140      -0.912  25.486  18.577  1.00 18.30           C  
ANISOU 1077  CG1 ILE A 140     1461   3486   2006    550    177    435       C  
ATOM   1078  CG2 ILE A 140       0.636  26.419  16.833  1.00 17.63           C  
ANISOU 1078  CG2 ILE A 140     1382   2944   2373    175     39    371       C  
ATOM   1079  CD1 ILE A 140       0.149  24.792  19.459  1.00 22.28           C  
ANISOU 1079  CD1 ILE A 140     2598   3589   2280   1515    -47    174       C  
ATOM   1080  N   GLU A 141      -2.920  24.026  15.771  1.00 16.14           N  
ANISOU 1080  N   GLU A 141     1587   2770   1776    337    306   -258       N  
ATOM   1081  CA  GLU A 141      -3.903  22.947  15.910  1.00 16.33           C  
ANISOU 1081  CA  GLU A 141     1475   3032   1698    282    185   -322       C  
ATOM   1082  C   GLU A 141      -3.157  21.674  16.307  1.00 14.98           C  
ANISOU 1082  C   GLU A 141     1419   2598   1673     69     86   -637       C  
ATOM   1083  O   GLU A 141      -2.081  21.369  15.750  1.00 16.14           O  
ANISOU 1083  O   GLU A 141     1436   2873   1824    264    210   -422       O  
ATOM   1084  CB  GLU A 141      -4.740  22.797  14.631  1.00 21.53           C  
ANISOU 1084  CB  GLU A 141     1895   3920   2366    182   -453   -134       C  
ATOM   1085  CG  GLU A 141      -5.818  21.754  14.768  1.00 30.56           C  
ANISOU 1085  CG  GLU A 141     1948   6515   3149  -1099   -265   -454       C  
ATOM   1086  CD  GLU A 141      -6.667  21.635  13.524  1.00 43.87           C  
ANISOU 1086  CD  GLU A 141     2972   9604   4091  -1835  -1219   -669       C  
ATOM   1087  OE1 GLU A 141      -6.237  21.738  12.352  1.00 58.12           O  
ANISOU 1087  OE1 GLU A 141     4526  13943   3613  -1054  -1552   -149       O  
ATOM   1088  OE2 GLU A 141      -7.863  21.425  13.786  1.00 64.21           O  
ANISOU 1088  OE2 GLU A 141     3028  15144   6226  -3146  -1516   -914       O  
ATOM   1089  N   VAL A 142      -3.700  20.940  17.264  1.00 16.08           N  
ANISOU 1089  N   VAL A 142     1290   2736   2085     34    212   -475       N  
ATOM   1090  CA  VAL A 142      -3.191  19.683  17.753  1.00 16.37           C  
ANISOU 1090  CA  VAL A 142     1572   2413   2236   -111    282   -559       C  
ATOM   1091  C   VAL A 142      -4.406  18.746  17.859  1.00 20.49           C  
ANISOU 1091  C   VAL A 142     1537   2664   3585   -186    496   -811       C  
ATOM   1092  O   VAL A 142      -5.334  19.080  18.629  1.00 20.47           O  
ANISOU 1092  O   VAL A 142     1504   3027   3248   -121    459   -528       O  
ATOM   1093  CB  VAL A 142      -2.488  19.788  19.101  1.00 16.33           C  
ANISOU 1093  CB  VAL A 142     1550   2562   2092    132    426   -358       C  
ATOM   1094  CG1 VAL A 142      -1.854  18.428  19.450  1.00 18.75           C  
ANISOU 1094  CG1 VAL A 142     1962   2876   2287    519    542   -335       C  
ATOM   1095  CG2 VAL A 142      -1.478  20.903  19.115  1.00 15.96           C  
ANISOU 1095  CG2 VAL A 142     1217   3002   1843     -4    170   -132       C  
ATOM   1096  N   SER A 143      -4.436  17.656  17.117  1.00 22.05           N  
ANISOU 1096  N   SER A 143     1637   2595   4144   -184    244   -949       N  
ATOM   1097  CA  SER A 143      -5.546  16.701  17.206  1.00 24.69           C  
ANISOU 1097  CA  SER A 143     1771   3229   4379   -554    364  -1154       C  
ATOM   1098  C   SER A 143      -6.907  17.416  17.038  1.00 25.92           C  
ANISOU 1098  C   SER A 143     1651   3289   4908   -540    446  -1595       C  
ATOM   1099  O   SER A 143      -7.854  17.076  17.718  1.00 30.88           O  
ANISOU 1099  O   SER A 143     2018   3732   5983   -724   1104  -1927       O  
ATOM   1100  CB  SER A 143      -5.464  15.877  18.484  1.00 31.92           C  
ANISOU 1100  CB  SER A 143     3300   3293   5534   -198   1171   -152       C  
ATOM   1101  OG  SER A 143      -4.192  15.255  18.623  1.00 44.76           O  
ANISOU 1101  OG  SER A 143     3388   4269   9348   -376    349   2291       O  
ATOM   1102  N   GLY A 144      -6.995  18.379  16.116  1.00 26.41           N  
ANISOU 1102  N   GLY A 144     1686   3640   4708   -184   -187  -1656       N  
ATOM   1103  CA  GLY A 144      -8.233  19.018  15.781  1.00 28.53           C  
ANISOU 1103  CA  GLY A 144     1734   4616   4490    109   -346  -2218       C  
ATOM   1104  C   GLY A 144      -8.655  20.094  16.768  1.00 27.25           C  
ANISOU 1104  C   GLY A 144     1674   4514   4164    225   -373  -1959       C  
ATOM   1105  O   GLY A 144      -9.765  20.648  16.646  1.00 41.28           O  
ANISOU 1105  O   GLY A 144     1979   7466   6242   1352  -1135  -4113       O  
ATOM   1106  N   LYS A 145      -7.856  20.411  17.784  1.00 22.47           N  
ANISOU 1106  N   LYS A 145     1300   3762   3475   -339    204  -1307       N  
ATOM   1107  CA  LYS A 145      -8.170  21.420  18.765  1.00 20.67           C  
ANISOU 1107  CA  LYS A 145     1141   3508   3205   -124    101   -970       C  
ATOM   1108  C   LYS A 145      -7.208  22.587  18.541  1.00 18.79           C  
ANISOU 1108  C   LYS A 145     1205   3254   2681     37    150   -732       C  
ATOM   1109  O   LYS A 145      -6.014  22.362  18.275  1.00 18.03           O  
ANISOU 1109  O   LYS A 145     1217   3119   2515    -73    215   -748       O  
ATOM   1110  CB ALYS A 145      -8.072  20.965  20.220  0.57 22.32           C  
ANISOU 1110  CB ALYS A 145     1668   3541   3271   -419    518   -720       C  
ATOM   1111  CB BLYS A 145      -8.118  20.908  20.202  0.43 20.74           C  
ANISOU 1111  CB BLYS A 145     1272   3278   3329   -622    332   -812       C  
ATOM   1112  CG ALYS A 145      -8.864  19.754  20.645  0.57 26.08           C  
ANISOU 1112  CG ALYS A 145     2289   3105   4515   -362   -548    -82       C  
ATOM   1113  CG BLYS A 145      -8.372  22.032  21.198  0.43 27.10           C  
ANISOU 1113  CG BLYS A 145     3759   3450   3089   -343   -460   -975       C  
ATOM   1114  CD ALYS A 145      -8.163  18.996  21.762  0.57 48.12           C  
ANISOU 1114  CD ALYS A 145     7441   5369   5472  -1324  -2759   1408       C  
ATOM   1115  CD BLYS A 145      -8.757  21.438  22.543  0.43 29.80           C  
ANISOU 1115  CD BLYS A 145     3792   4229   3300   -540    396  -1156       C  
ATOM   1116  CE ALYS A 145      -8.671  19.456  23.122  0.57 54.91           C  
ANISOU 1116  CE ALYS A 145     9755   5967   5142   -140  -3445   1090       C  
ATOM   1117  CE BLYS A 145      -8.598  22.457  23.668  0.43 38.03           C  
ANISOU 1117  CE BLYS A 145     6543   4844   3061  -1112   -378  -1108       C  
ATOM   1118  NZ ALYS A 145      -8.321  18.514  24.230  0.57 67.39           N  
ANISOU 1118  NZ ALYS A 145    13194   7311   5099  -1981  -5514   1601       N  
ATOM   1119  NZ BLYS A 145      -9.818  22.484  24.525  0.43 50.38           N  
ANISOU 1119  NZ BLYS A 145     7429   6534   5177   2250    777  -2663       N  
ATOM   1120  N   LYS A 146      -7.688  23.829  18.693  1.00 20.06           N  
ANISOU 1120  N   LYS A 146     1000   3489   3132    -14    116  -1198       N  
ATOM   1121  CA  LYS A 146      -6.870  25.003  18.418  1.00 18.29           C  
ANISOU 1121  CA  LYS A 146     1238   3092   2620    210    -23  -1021       C  
ATOM   1122  C   LYS A 146      -6.444  25.718  19.690  1.00 16.25           C  
ANISOU 1122  C   LYS A 146     1078   2863   2234    217    300   -746       C  
ATOM   1123  O   LYS A 146      -7.153  25.787  20.700  1.00 17.48           O  
ANISOU 1123  O   LYS A 146     1091   3286   2264    -88    287   -597       O  
ATOM   1124  CB  LYS A 146      -7.613  26.007  17.539  1.00 21.93           C  
ANISOU 1124  CB  LYS A 146     1564   3959   2810    324   -456   -826       C  
ATOM   1125  CG  LYS A 146      -7.940  25.485  16.139  1.00 26.93           C  
ANISOU 1125  CG  LYS A 146     2098   5008   3125    111   -973  -1165       C  
ATOM   1126  CD  LYS A 146      -8.541  26.603  15.268  1.00 40.46           C  
ANISOU 1126  CD  LYS A 146     3646   7440   4288    813  -2304    -66       C  
ATOM   1127  CE  LYS A 146      -8.586  26.026  13.845  1.00 53.33           C  
ANISOU 1127  CE  LYS A 146     6979   9034   4251    124  -3268   -238       C  
ATOM   1128  NZ  LYS A 146      -8.688  27.100  12.810  1.00 70.70           N  
ANISOU 1128  NZ  LYS A 146    10224  11827   4812   1981  -3348   1284       N  
ATOM   1129  N   TYR A 147      -5.209  26.273  19.672  1.00 14.33           N  
ANISOU 1129  N   TYR A 147     1052   2596   1797    203    133   -460       N  
ATOM   1130  CA  TYR A 147      -4.598  26.925  20.786  1.00 13.58           C  
ANISOU 1130  CA  TYR A 147     1164   2493   1503    173    378   -408       C  
ATOM   1131  C   TYR A 147      -3.908  28.198  20.323  1.00 13.87           C  
ANISOU 1131  C   TYR A 147     1020   2678   1571     23    292   -321       C  
ATOM   1132  O   TYR A 147      -3.334  28.170  19.219  1.00 14.95           O  
ANISOU 1132  O   TYR A 147     1387   2655   1639     55    371   -237       O  
ATOM   1133  CB  TYR A 147      -3.559  26.020  21.432  1.00 14.97           C  
ANISOU 1133  CB  TYR A 147     1086   2679   1922     -6     89   -259       C  
ATOM   1134  CG  TYR A 147      -4.050  24.669  21.877  1.00 14.71           C  
ANISOU 1134  CG  TYR A 147     1053   2536   2002    138    248   -221       C  
ATOM   1135  CD1 TYR A 147      -4.492  24.429  23.169  1.00 16.38           C  
ANISOU 1135  CD1 TYR A 147     1320   2874   2031   -128    378   -362       C  
ATOM   1136  CD2 TYR A 147      -4.101  23.603  20.981  1.00 15.60           C  
ANISOU 1136  CD2 TYR A 147     1123   2737   2069   -104    310   -339       C  
ATOM   1137  CE1 TYR A 147      -4.958  23.167  23.551  1.00 17.31           C  
ANISOU 1137  CE1 TYR A 147     1605   3010   1964   -172    467   -241       C  
ATOM   1138  CE2 TYR A 147      -4.584  22.349  21.381  1.00 15.69           C  
ANISOU 1138  CE2 TYR A 147     1244   2574   2143     86    371   -440       C  
ATOM   1139  CZ  TYR A 147      -4.998  22.126  22.660  1.00 16.56           C  
ANISOU 1139  CZ  TYR A 147     1266   2769   2256   -230    248   -171       C  
ATOM   1140  OH  TYR A 147      -5.462  20.902  23.086  1.00 19.77           O  
ANISOU 1140  OH  TYR A 147     1784   2745   2983    -99    426    125       O  
ATOM   1141  N   THR A 148      -3.923  29.268  21.087  1.00 15.48           N  
ANISOU 1141  N   THR A 148     1289   2889   1703   -370    415   -499       N  
ATOM   1142  CA  THR A 148      -3.280  30.506  20.698  1.00 16.46           C  
ANISOU 1142  CA  THR A 148     1772   2763   1717   -269    539   -522       C  
ATOM   1143  C   THR A 148      -2.585  31.125  21.904  1.00 15.00           C  
ANISOU 1143  C   THR A 148     1479   2506   1715   -247    542   -355       C  
ATOM   1144  O   THR A 148      -2.894  30.782  23.067  1.00 16.53           O  
ANISOU 1144  O   THR A 148     1540   3039   1700   -420    564   -345       O  
ATOM   1145  CB  THR A 148      -4.274  31.480  20.056  1.00 18.46           C  
ANISOU 1145  CB  THR A 148     1970   3118   1925   -295    280   -221       C  
ATOM   1146  OG1 THR A 148      -3.532  32.556  19.493  1.00 21.00           O  
ANISOU 1146  OG1 THR A 148     2740   3124   2115   -496    405   -131       O  
ATOM   1147  CG2 THR A 148      -5.183  32.051  21.125  1.00 19.09           C  
ANISOU 1147  CG2 THR A 148     1912   3293   2046    130    209   -135       C  
ATOM   1148  N   ALA A 149      -1.646  32.013  21.619  1.00 14.34           N  
ANISOU 1148  N   ALA A 149     1267   2345   1838     -9    486   -195       N  
ATOM   1149  CA  ALA A 149      -0.950  32.799  22.622  1.00 13.58           C  
ANISOU 1149  CA  ALA A 149     1064   2104   1992    273    356   -230       C  
ATOM   1150  C   ALA A 149      -0.315  33.995  21.927  1.00 12.96           C  
ANISOU 1150  C   ALA A 149      870   2097   1959    400    128    -37       C  
ATOM   1151  O   ALA A 149       0.027  33.887  20.731  1.00 14.65           O  
ANISOU 1151  O   ALA A 149     1273   2270   2023    285    342    -93       O  
ATOM   1152  CB  ALA A 149       0.147  32.009  23.329  1.00 13.88           C  
ANISOU 1152  CB  ALA A 149     1194   1946   2135    324    434    -18       C  
ATOM   1153  N   PRO A 150      -0.029  35.064  22.684  1.00 13.98           N  
ANISOU 1153  N   PRO A 150     1263   2007   2043    440    237    -87       N  
ATOM   1154  CA  PRO A 150       0.738  36.161  22.101  1.00 14.87           C  
ANISOU 1154  CA  PRO A 150     1373   1901   2375    533    282      8       C  
ATOM   1155  C   PRO A 150       2.207  35.824  21.897  1.00 13.70           C  
ANISOU 1155  C   PRO A 150     1395   1809   2001    531    337    168       C  
ATOM   1156  O   PRO A 150       2.937  36.602  21.250  1.00 14.63           O  
ANISOU 1156  O   PRO A 150     1611   1849   2100    501    384    357       O  
ATOM   1157  CB  PRO A 150       0.596  37.262  23.139  1.00 16.74           C  
ANISOU 1157  CB  PRO A 150     1464   2096   2800    369    440   -389       C  
ATOM   1158  CG  PRO A 150       0.280  36.577  24.395  1.00 20.84           C  
ANISOU 1158  CG  PRO A 150     3110   2299   2508     30    392   -491       C  
ATOM   1159  CD  PRO A 150      -0.525  35.333  24.049  1.00 15.55           C  
ANISOU 1159  CD  PRO A 150     1601   2134   2173    550    354   -169       C  
ATOM   1160  N   HIS A 151       2.661  34.728  22.462  1.00 11.80           N  
ANISOU 1160  N   HIS A 151     1115   1561   1808    204    215     75       N  
ATOM   1161  CA  HIS A 151       4.021  34.269  22.357  1.00 11.55           C  
ANISOU 1161  CA  HIS A 151     1133   1737   1518    326    320     48       C  
ATOM   1162  C   HIS A 151       4.045  32.759  22.079  1.00 11.22           C  
ANISOU 1162  C   HIS A 151     1139   1715   1409    279    124     83       C  
ATOM   1163  O   HIS A 151       3.569  31.998  22.943  1.00 11.68           O  
ANISOU 1163  O   HIS A 151     1218   1756   1465    248    288     32       O  
ATOM   1164  CB  HIS A 151       4.769  34.583  23.654  1.00 11.74           C  
ANISOU 1164  CB  HIS A 151     1117   1690   1652    197    317      8       C  
ATOM   1165  CG  HIS A 151       4.781  36.038  24.033  1.00 12.21           C  
ANISOU 1165  CG  HIS A 151     1170   1740   1729    289    284    -68       C  
ATOM   1166  ND1 HIS A 151       5.454  36.995  23.385  1.00 13.59           N  
ANISOU 1166  ND1 HIS A 151     1467   1634   2063    155    400   -129       N  
ATOM   1167  CD2 HIS A 151       4.117  36.593  25.073  1.00 14.65           C  
ANISOU 1167  CD2 HIS A 151     1860   1989   1717    336    328   -174       C  
ATOM   1168  CE1 HIS A 151       5.203  38.170  23.993  1.00 14.24           C  
ANISOU 1168  CE1 HIS A 151     1646   1767   1997    364    394   -181       C  
ATOM   1169  NE2 HIS A 151       4.405  37.957  25.043  1.00 15.19           N  
ANISOU 1169  NE2 HIS A 151     1662   1964   2147    270    412   -316       N  
ATOM   1170  N   ILE A 152       4.578  32.348  20.959  1.00 10.97           N  
ANISOU 1170  N   ILE A 152     1109   1559   1499    258    183     48       N  
ATOM   1171  CA  ILE A 152       4.684  30.950  20.584  1.00 10.63           C  
ANISOU 1171  CA  ILE A 152     1068   1557   1413    107    252     82       C  
ATOM   1172  C   ILE A 152       6.140  30.641  20.268  1.00  9.95           C  
ANISOU 1172  C   ILE A 152     1124   1492   1164    196    180     60       C  
ATOM   1173  O   ILE A 152       6.718  31.276  19.401  1.00 11.49           O  
ANISOU 1173  O   ILE A 152     1121   1820   1425    157    240    300       O  
ATOM   1174  CB  ILE A 152       3.768  30.594  19.364  1.00 11.70           C  
ANISOU 1174  CB  ILE A 152     1059   1827   1560     75    221      6       C  
ATOM   1175  CG1 ILE A 152       2.298  30.943  19.673  1.00 13.50           C  
ANISOU 1175  CG1 ILE A 152      992   2111   2028    190     69     35       C  
ATOM   1176  CG2 ILE A 152       3.952  29.161  18.991  1.00 12.31           C  
ANISOU 1176  CG2 ILE A 152     1318   1819   1543    101    232   -153       C  
ATOM   1177  CD1 ILE A 152       1.337  30.725  18.548  1.00 15.37           C  
ANISOU 1177  CD1 ILE A 152     1196   2762   1883    477     55    -57       C  
ATOM   1178  N   LEU A 153       6.680  29.659  20.970  1.00 10.64           N  
ANISOU 1178  N   LEU A 153     1030   1651   1360    228    280    232       N  
ATOM   1179  CA  LEU A 153       8.063  29.206  20.770  1.00 10.10           C  
ANISOU 1179  CA  LEU A 153      941   1526   1370    157    164     42       C  
ATOM   1180  C   LEU A 153       8.079  27.918  19.996  1.00 10.18           C  
ANISOU 1180  C   LEU A 153     1037   1525   1307    235    153    149       C  
ATOM   1181  O   LEU A 153       7.426  26.923  20.377  1.00 11.49           O  
ANISOU 1181  O   LEU A 153     1267   1577   1522     89    238    115       O  
ATOM   1182  CB  LEU A 153       8.719  28.988  22.170  1.00 10.43           C  
ANISOU 1182  CB  LEU A 153     1106   1588   1268    182    267    164       C  
ATOM   1183  CG  LEU A 153      10.124  28.348  22.053  1.00 10.17           C  
ANISOU 1183  CG  LEU A 153      958   1528   1379     37    106    168       C  
ATOM   1184  CD1 LEU A 153      11.089  29.247  21.272  1.00  9.99           C  
ANISOU 1184  CD1 LEU A 153     1115   1494   1189     32    210     67       C  
ATOM   1185  CD2 LEU A 153      10.654  28.014  23.431  1.00 10.60           C  
ANISOU 1185  CD2 LEU A 153     1284   1498   1245    140    225    100       C  
ATOM   1186  N   ILE A 154       8.813  27.898  18.886  1.00 10.15           N  
ANISOU 1186  N   ILE A 154     1088   1455   1314    105    227     40       N  
ATOM   1187  CA  ILE A 154       9.083  26.696  18.097  1.00 10.50           C  
ANISOU 1187  CA  ILE A 154     1150   1483   1358    171    104    -33       C  
ATOM   1188  C   ILE A 154      10.393  26.115  18.579  1.00 10.00           C  
ANISOU 1188  C   ILE A 154     1067   1513   1220    198    246     -8       C  
ATOM   1189  O   ILE A 154      11.471  26.732  18.460  1.00 10.52           O  
ANISOU 1189  O   ILE A 154     1085   1538   1374     99    176     97       O  
ATOM   1190  CB  ILE A 154       9.152  27.000  16.591  1.00 11.76           C  
ANISOU 1190  CB  ILE A 154     1478   1675   1316    320     25    -22       C  
ATOM   1191  CG1 ILE A 154       7.897  27.721  16.091  1.00 13.28           C  
ANISOU 1191  CG1 ILE A 154     1642   1787   1619    248   -279     74       C  
ATOM   1192  CG2 ILE A 154       9.377  25.701  15.849  1.00 14.06           C  
ANISOU 1192  CG2 ILE A 154     2143   1837   1362    227     41   -209       C  
ATOM   1193  CD1 ILE A 154       8.062  28.331  14.706  1.00 15.95           C  
ANISOU 1193  CD1 ILE A 154     2303   2139   1618    370   -405    121       C  
ATOM   1194  N   ALA A 155      10.320  24.920  19.190  1.00  9.78           N  
ANISOU 1194  N   ALA A 155      989   1509   1218    139    239     92       N  
ATOM   1195  CA  ALA A 155      11.489  24.230  19.764  1.00  9.56           C  
ANISOU 1195  CA  ALA A 155      999   1373   1260    128    284    -62       C  
ATOM   1196  C   ALA A 155      11.407  22.748  19.404  1.00  9.54           C  
ANISOU 1196  C   ALA A 155      997   1410   1220    126    296   -105       C  
ATOM   1197  O   ALA A 155      11.488  21.869  20.240  1.00 10.13           O  
ANISOU 1197  O   ALA A 155     1080   1455   1314    119    194     14       O  
ATOM   1198  CB  ALA A 155      11.547  24.460  21.257  1.00 11.41           C  
ANISOU 1198  CB  ALA A 155     1606   1432   1296    191     86   -113       C  
ATOM   1199  N   THR A 156      11.281  22.469  18.090  1.00  9.91           N  
ANISOU 1199  N   THR A 156     1056   1482   1226    128    272   -127       N  
ATOM   1200  CA  THR A 156      10.974  21.157  17.592  1.00 10.36           C  
ANISOU 1200  CA  THR A 156     1033   1602   1302    111    128   -214       C  
ATOM   1201  C   THR A 156      12.195  20.313  17.246  1.00  9.60           C  
ANISOU 1201  C   THR A 156     1046   1517   1086     23    292   -223       C  
ATOM   1202  O   THR A 156      12.040  19.178  16.813  1.00 10.83           O  
ANISOU 1202  O   THR A 156     1159   1560   1396     71    262   -252       O  
ATOM   1203  CB  THR A 156      10.053  21.263  16.354  1.00 11.16           C  
ANISOU 1203  CB  THR A 156     1008   1947   1287     45    260   -140       C  
ATOM   1204  OG1 THR A 156      10.653  22.187  15.450  1.00 11.90           O  
ANISOU 1204  OG1 THR A 156     1382   1785   1353    118    181    -23       O  
ATOM   1205  CG2 THR A 156       8.663  21.763  16.798  1.00 11.81           C  
ANISOU 1205  CG2 THR A 156     1151   1873   1463    218     50   -300       C  
ATOM   1206  N   GLY A 157      13.401  20.837  17.418  1.00  9.75           N  
ANISOU 1206  N   GLY A 157     1016   1452   1236    112    217    -49       N  
ATOM   1207  CA  GLY A 157      14.590  20.063  17.218  1.00 10.82           C  
ANISOU 1207  CA  GLY A 157     1098   1746   1268    205    353   -151       C  
ATOM   1208  C   GLY A 157      14.838  19.635  15.786  1.00 10.50           C  
ANISOU 1208  C   GLY A 157     1027   1628   1333    167    210   -124       C  
ATOM   1209  O   GLY A 157      14.395  20.286  14.859  1.00 11.72           O  
ANISOU 1209  O   GLY A 157     1330   1866   1258    384    308    -27       O  
ATOM   1210  N   GLY A 158      15.577  18.539  15.668  1.00 11.67           N  
ANISOU 1210  N   GLY A 158     1345   1652   1437    282    271   -173       N  
ATOM   1211  CA  GLY A 158      15.969  17.980  14.370  1.00 12.77           C  
ANISOU 1211  CA  GLY A 158     1601   1704   1548    188    421   -306       C  
ATOM   1212  C   GLY A 158      15.998  16.464  14.453  1.00 11.84           C  
ANISOU 1212  C   GLY A 158     1248   1754   1499    211    363   -159       C  
ATOM   1213  O   GLY A 158      15.468  15.852  15.388  1.00 12.91           O  
ANISOU 1213  O   GLY A 158     1495   1768   1643    101    479   -249       O  
ATOM   1214  N   MET A 159      16.611  15.861  13.430  1.00 12.79           N  
ANISOU 1214  N   MET A 159     1695   1679   1487    270    406   -233       N  
ATOM   1215  CA  MET A 159      16.665  14.428  13.308  1.00 13.15           C  
ANISOU 1215  CA  MET A 159     1664   1692   1639     18    453   -300       C  
ATOM   1216  C   MET A 159      17.882  14.099  12.463  1.00 11.88           C  
ANISOU 1216  C   MET A 159     1599   1595   1321    206    311   -270       C  
ATOM   1217  O   MET A 159      18.456  14.953  11.764  1.00 13.71           O  
ANISOU 1217  O   MET A 159     1829   1763   1618    329    472    -16       O  
ATOM   1218  CB AMET A 159      15.456  13.869  12.552  0.50 17.73           C  
ANISOU 1218  CB AMET A 159     1647   2372   2718   -399    364   -348       C  
ATOM   1219  CB BMET A 159      15.393  13.829  12.712  0.50 14.90           C  
ANISOU 1219  CB BMET A 159     1561   1805   2296    168    228   -188       C  
ATOM   1220  CG AMET A 159      14.119  14.527  12.595  0.50 26.07           C  
ANISOU 1220  CG AMET A 159     2098   3440   4368    375   -556   -992       C  
ATOM   1221  CG BMET A 159      15.207  14.430  11.320  0.50 14.91           C  
ANISOU 1221  CG BMET A 159     1515   2157   1995    515    225   -439       C  
ATOM   1222  SD AMET A 159      13.693  15.811  11.367  0.50 36.77           S  
ANISOU 1222  SD AMET A 159     5683   4786   3501   3123   -591  -1509       S  
ATOM   1223  SD BMET A 159      13.661  13.922  10.569  0.50 30.47           S  
ANISOU 1223  SD BMET A 159     2883   5655   3040   -320   -805  -1264       S  
ATOM   1224  CE AMET A 159      12.354  14.932  10.591  0.50 40.40           C  
ANISOU 1224  CE AMET A 159     1525   9643   4184   1823    520   1388       C  
ATOM   1225  CE BMET A 159      13.172  15.568   9.970  0.50 39.71           C  
ANISOU 1225  CE BMET A 159     2219  10112   2756   2814   1281   2800       C  
ATOM   1226  N   PRO A 160      18.351  12.826  12.475  1.00 12.06           N  
ANISOU 1226  N   PRO A 160     1557   1684   1342    196    241   -147       N  
ATOM   1227  CA  PRO A 160      19.538  12.504  11.670  1.00 12.92           C  
ANISOU 1227  CA  PRO A 160     1630   1824   1457    325    335   -289       C  
ATOM   1228  C   PRO A 160      19.271  12.603  10.181  1.00 13.40           C  
ANISOU 1228  C   PRO A 160     1475   2082   1533    311    327   -336       C  
ATOM   1229  O   PRO A 160      18.169  12.236   9.754  1.00 15.18           O  
ANISOU 1229  O   PRO A 160     1628   2487   1652    168     52   -455       O  
ATOM   1230  CB  PRO A 160      19.856  11.067  12.044  1.00 14.60           C  
ANISOU 1230  CB  PRO A 160     1953   1828   1765    309    350   -277       C  
ATOM   1231  CG  PRO A 160      19.155  10.821  13.350  1.00 15.02           C  
ANISOU 1231  CG  PRO A 160     1972   1740   1995    335    465    -47       C  
ATOM   1232  CD  PRO A 160      17.916  11.701  13.290  1.00 14.34           C  
ANISOU 1232  CD  PRO A 160     1876   1786   1787    235    403     56       C  
ATOM   1233  N   SER A 161      20.292  13.032   9.434  1.00 14.75           N  
ANISOU 1233  N   SER A 161     1659   2517   1428    377    502   -321       N  
ATOM   1234  CA  SER A 161      20.238  12.955   7.996  1.00 16.77           C  
ANISOU 1234  CA  SER A 161     1900   3050   1421    758    401   -388       C  
ATOM   1235  C   SER A 161      20.565  11.581   7.434  1.00 15.68           C  
ANISOU 1235  C   SER A 161     1652   2890   1415    399    146   -417       C  
ATOM   1236  O   SER A 161      21.464  10.881   7.922  1.00 15.97           O  
ANISOU 1236  O   SER A 161     1811   2549   1709    255    -59   -368       O  
ATOM   1237  CB ASER A 161      21.238  13.945   7.362  0.55 25.24           C  
ANISOU 1237  CB ASER A 161     5071   3249   1270   -621    524    -11       C  
ATOM   1238  CB BSER A 161      21.410  13.836   7.507  0.45 19.31           C  
ANISOU 1238  CB BSER A 161     3325   2407   1604    605   1176   -212       C  
ATOM   1239  OG ASER A 161      20.992  15.281   7.801  0.55 29.69           O  
ANISOU 1239  OG ASER A 161     5738   3305   2238     15   1277    304       O  
ATOM   1240  OG BSER A 161      21.248  14.046   6.144  0.45 21.73           O  
ANISOU 1240  OG BSER A 161     2782   3801   1674     12    727   -367       O  
ATOM   1241  N   THR A 162      19.891  11.123   6.393  1.00 19.25           N  
ANISOU 1241  N   THR A 162     1833   3716   1765    893   -185   -876       N  
ATOM   1242  CA  THR A 162      20.257   9.939   5.662  1.00 19.76           C  
ANISOU 1242  CA  THR A 162     2306   3680   1523    760     75   -823       C  
ATOM   1243  C   THR A 162      20.350  10.272   4.165  1.00 17.53           C  
ANISOU 1243  C   THR A 162     2214   2731   1717    681     90   -474       C  
ATOM   1244  O   THR A 162      19.596  11.080   3.657  1.00 23.63           O  
ANISOU 1244  O   THR A 162     2956   4321   1703   1893   -281   -904       O  
ATOM   1245  CB ATHR A 162      19.313   8.738   5.828  0.44 20.64           C  
ANISOU 1245  CB ATHR A 162     2948   3281   1612    934    733   -387       C  
ATOM   1246  CB BTHR A 162      19.175   8.841   5.806  0.56 23.18           C  
ANISOU 1246  CB BTHR A 162     3537   3261   2011    485    200    109       C  
ATOM   1247  OG1ATHR A 162      18.034   9.171   5.379  0.44 27.23           O  
ANISOU 1247  OG1ATHR A 162     3428   3590   3329   -565  -1347    618       O  
ATOM   1248  OG1BTHR A 162      19.036   8.539   7.208  0.56 32.03           O  
ANISOU 1248  OG1BTHR A 162     4496   5829   1846   -599    -33     86       O  
ATOM   1249  CG2ATHR A 162      19.238   8.291   7.273  0.44 22.87           C  
ANISOU 1249  CG2ATHR A 162     2137   4978   1573   1386    645   -118       C  
ATOM   1250  CG2BTHR A 162      19.464   7.537   5.055  0.56 25.51           C  
ANISOU 1250  CG2BTHR A 162     3502   3407   2785    574   -363   -258       C  
ATOM   1251  N   PRO A 163      21.270   9.673   3.447  1.00 15.45           N  
ANISOU 1251  N   PRO A 163     2063   2245   1562    368    159   -535       N  
ATOM   1252  CA  PRO A 163      21.351   9.890   2.016  1.00 15.26           C  
ANISOU 1252  CA  PRO A 163     2118   2006   1675    167    183   -286       C  
ATOM   1253  C   PRO A 163      20.061   9.442   1.328  1.00 17.39           C  
ANISOU 1253  C   PRO A 163     2116   2789   1702    453     55   -465       C  
ATOM   1254  O   PRO A 163      19.404   8.494   1.682  1.00 19.87           O  
ANISOU 1254  O   PRO A 163     2160   3615   1774   -341    -14   -525       O  
ATOM   1255  CB  PRO A 163      22.479   8.958   1.559  1.00 16.88           C  
ANISOU 1255  CB  PRO A 163     2055   2593   1768    189    387   -569       C  
ATOM   1256  CG  PRO A 163      23.320   8.823   2.796  1.00 16.94           C  
ANISOU 1256  CG  PRO A 163     2240   2396   1799    475    360   -270       C  
ATOM   1257  CD  PRO A 163      22.339   8.752   3.901  1.00 15.39           C  
ANISOU 1257  CD  PRO A 163     1973   2176   1698    315    245   -346       C  
ATOM   1258  N   HIS A 164      19.753  10.148   0.222  1.00 19.43           N  
ANISOU 1258  N   HIS A 164     2673   2893   1817    745   -205   -591       N  
ATOM   1259  CA  HIS A 164      18.655   9.722  -0.640  1.00 24.30           C  
ANISOU 1259  CA  HIS A 164     3280   3955   2000   1140   -634  -1299       C  
ATOM   1260  C   HIS A 164      19.080   8.551  -1.517  1.00 19.90           C  
ANISOU 1260  C   HIS A 164     2576   3038   1946    629   -295   -714       C  
ATOM   1261  O   HIS A 164      20.252   8.495  -1.941  1.00 20.69           O  
ANISOU 1261  O   HIS A 164     2595   3322   1943    658   -285   -695       O  
ATOM   1262  CB  HIS A 164      18.185  10.850  -1.560  1.00 41.24           C  
ANISOU 1262  CB  HIS A 164     6414   4689   4566   3436  -3034  -1664       C  
ATOM   1263  CG  HIS A 164      17.483  11.963  -0.889  1.00 54.63           C  
ANISOU 1263  CG  HIS A 164     8821   6043   5894   4665  -2827  -2539       C  
ATOM   1264  ND1 HIS A 164      18.171  13.097  -0.509  1.00 61.38           N  
ANISOU 1264  ND1 HIS A 164    10370   5863   7089   4855  -3260  -3386       N  
ATOM   1265  CD2 HIS A 164      16.182  12.143  -0.554  1.00 60.54           C  
ANISOU 1265  CD2 HIS A 164     9700   7341   5963   5100  -1311  -2982       C  
ATOM   1266  CE1 HIS A 164      17.326  13.933   0.058  1.00 64.87           C  
ANISOU 1266  CE1 HIS A 164    11647   6231   6771   5596  -2595  -2784       C  
ATOM   1267  NE2 HIS A 164      16.122  13.382   0.041  1.00 65.97           N  
ANISOU 1267  NE2 HIS A 164    11610   7264   6190   5357  -1227  -2917       N  
ATOM   1268  N   GLU A 165      18.139   7.674  -1.821  1.00 22.06           N  
ANISOU 1268  N   GLU A 165     2654   3753   1974    442   -282   -955       N  
ATOM   1269  CA  GLU A 165      18.403   6.541  -2.682  1.00 21.38           C  
ANISOU 1269  CA  GLU A 165     3017   3103   2003     49   -245   -628       C  
ATOM   1270  C   GLU A 165      18.885   6.948  -4.070  1.00 20.98           C  
ANISOU 1270  C   GLU A 165     3208   2971   1794    499   -287   -720       C  
ATOM   1271  O   GLU A 165      19.604   6.175  -4.666  1.00 23.11           O  
ANISOU 1271  O   GLU A 165     2917   3530   2335    673   -132   -793       O  
ATOM   1272  CB AGLU A 165      17.153   5.677  -2.923  0.56 25.21           C  
ANISOU 1272  CB AGLU A 165     2997   3800   2782   -117   -379   -758       C  
ATOM   1273  CB BGLU A 165      17.099   5.750  -2.859  0.44 25.32           C  
ANISOU 1273  CB BGLU A 165     2882   3705   3033     -6   -338   -780       C  
ATOM   1274  CG AGLU A 165      16.547   5.117  -1.644  0.56 23.70           C  
ANISOU 1274  CG AGLU A 165     2116   3798   3092    247   -116   -658       C  
ATOM   1275  CG BGLU A 165      17.155   4.813  -4.044  0.44 30.42           C  
ANISOU 1275  CG BGLU A 165     3708   4252   3599   -430   -797  -1393       C  
ATOM   1276  CD AGLU A 165      17.418   4.037  -1.012  0.56 21.04           C  
ANISOU 1276  CD AGLU A 165     1413   4281   2300    214   -264   -883       C  
ATOM   1277  CD BGLU A 165      17.634   3.427  -3.649  0.44 30.13           C  
ANISOU 1277  CD BGLU A 165     3761   4784   2903    770   -398  -1886       C  
ATOM   1278  OE1AGLU A 165      17.917   3.180  -1.777  0.56 19.25           O  
ANISOU 1278  OE1AGLU A 165     1482   3575   2259   -177    214   -464       O  
ATOM   1279  OE1BGLU A 165      18.079   3.217  -2.506  0.44 35.91           O  
ANISOU 1279  OE1BGLU A 165     4465   5695   3485   1403  -1258  -1988       O  
ATOM   1280  OE2AGLU A 165      17.563   4.044   0.229  0.56 28.83           O  
ANISOU 1280  OE2AGLU A 165     3096   5553   2304    814   -208   -955       O  
ATOM   1281  OE2BGLU A 165      17.510   2.566  -4.540  0.44 28.22           O  
ANISOU 1281  OE2BGLU A 165     3263   4650   2808   -107    364  -1755       O  
ATOM   1282  N   SER A 166      18.402   8.075  -4.559  1.00 22.13           N  
ANISOU 1282  N   SER A 166     3102   3215   2093    536   -585   -520       N  
ATOM   1283  CA  SER A 166      18.816   8.507  -5.887  1.00 24.28           C  
ANISOU 1283  CA  SER A 166     3508   3368   2350    825   -388   -227       C  
ATOM   1284  C   SER A 166      20.301   8.809  -5.921  1.00 24.36           C  
ANISOU 1284  C   SER A 166     3754   3379   2124    442   -263   -119       C  
ATOM   1285  O   SER A 166      20.887   8.710  -7.002  1.00 26.45           O  
ANISOU 1285  O   SER A 166     3827   3899   2323    151   -180   -472       O  
ATOM   1286  CB  SER A 166      17.980   9.748  -6.287  1.00 29.48           C  
ANISOU 1286  CB  SER A 166     4618   3541   3044   1151  -1012   -113       C  
ATOM   1287  OG  SER A 166      18.204  10.769  -5.285  1.00 50.64           O  
ANISOU 1287  OG  SER A 166     8339   5016   5886   3656  -3494  -2402       O  
ATOM   1288  N   GLN A 167      20.846   9.145  -4.752  1.00 23.49           N  
ANISOU 1288  N   GLN A 167     3381   3258   2284    823   -293   -361       N  
ATOM   1289  CA  GLN A 167      22.280   9.446  -4.648  1.00 23.90           C  
ANISOU 1289  CA  GLN A 167     3662   2690   2729    166   -236    227       C  
ATOM   1290  C   GLN A 167      23.121   8.214  -4.312  1.00 19.89           C  
ANISOU 1290  C   GLN A 167     2908   2645   2004    110    156    -50       C  
ATOM   1291  O   GLN A 167      24.177   7.913  -4.884  1.00 25.17           O  
ANISOU 1291  O   GLN A 167     3621   3395   2548    239    875    119       O  
ATOM   1292  CB AGLN A 167      22.534  10.536  -3.600  0.60 28.27           C  
ANISOU 1292  CB AGLN A 167     4166   2520   4054    405   -664   -293       C  
ATOM   1293  CB BGLN A 167      22.515  10.553  -3.605  0.40 26.24           C  
ANISOU 1293  CB BGLN A 167     4202   2227   3542     74   -330    125       C  
ATOM   1294  CG AGLN A 167      21.929  11.873  -3.961  0.60 35.35           C  
ANISOU 1294  CG AGLN A 167     6747   2655   4030    729  -1270    189       C  
ATOM   1295  CG BGLN A 167      24.001  10.825  -3.521  0.40 26.81           C  
ANISOU 1295  CG BGLN A 167     4143   2044   4000    312   -475   -233       C  
ATOM   1296  CD AGLN A 167      22.262  12.338  -5.362  0.60 38.23           C  
ANISOU 1296  CD AGLN A 167     6091   3841   4592    754   -413    605       C  
ATOM   1297  CD BGLN A 167      24.482  11.692  -2.388  0.40 29.31           C  
ANISOU 1297  CD BGLN A 167     4155   2482   4498   -593    519   -885       C  
ATOM   1298  OE1AGLN A 167      23.398  12.428  -5.825  0.60 43.53           O  
ANISOU 1298  OE1AGLN A 167     5949   4468   6121   2432     50    889       O  
ATOM   1299  OE1BGLN A 167      25.290  12.580  -2.670  0.40 35.83           O  
ANISOU 1299  OE1BGLN A 167     2951   4505   6156  -1302    110   -551       O  
ATOM   1300  NE2AGLN A 167      21.197  12.652  -6.085  0.60 37.81           N  
ANISOU 1300  NE2AGLN A 167     5574   5060   3731   1346    842   1837       N  
ATOM   1301  NE2BGLN A 167      24.030  11.429  -1.166  0.40 25.03           N  
ANISOU 1301  NE2BGLN A 167     2388   3086   4037    751   -333   -495       N  
ATOM   1302  N   ILE A 168      22.639   7.459  -3.335  1.00 18.45           N  
ANISOU 1302  N   ILE A 168     2667   2538   1805    333    133   -164       N  
ATOM   1303  CA  ILE A 168      23.336   6.300  -2.770  1.00 16.63           C  
ANISOU 1303  CA  ILE A 168     2081   2498   1739    312    275   -268       C  
ATOM   1304  C   ILE A 168      22.315   5.184  -2.703  1.00 17.93           C  
ANISOU 1304  C   ILE A 168     2473   2443   1896    143    313   -531       C  
ATOM   1305  O   ILE A 168      21.596   5.058  -1.695  1.00 17.71           O  
ANISOU 1305  O   ILE A 168     2216   2572   1943    134    260   -283       O  
ATOM   1306  CB  ILE A 168      24.035   6.539  -1.425  1.00 16.68           C  
ANISOU 1306  CB  ILE A 168     2045   2448   1846    214    255   -213       C  
ATOM   1307  CG1 ILE A 168      25.053   7.691  -1.482  1.00 19.57           C  
ANISOU 1307  CG1 ILE A 168     2290   3123   2021   -238    337   -394       C  
ATOM   1308  CG2 ILE A 168      24.681   5.239  -0.952  1.00 18.03           C  
ANISOU 1308  CG2 ILE A 168     2494   2864   1492    583    146   -307       C  
ATOM   1309  CD1 ILE A 168      25.754   7.932  -0.150  1.00 19.19           C  
ANISOU 1309  CD1 ILE A 168     1939   3222   2132   -228    390   -505       C  
ATOM   1310  N   PRO A 169      22.210   4.378  -3.751  1.00 18.19           N  
ANISOU 1310  N   PRO A 169     2295   2801   1817    221     44   -430       N  
ATOM   1311  CA  PRO A 169      21.229   3.274  -3.705  1.00 18.94           C  
ANISOU 1311  CA  PRO A 169     2377   2852   1969    113   -198   -700       C  
ATOM   1312  C   PRO A 169      21.546   2.330  -2.549  1.00 18.01           C  
ANISOU 1312  C   PRO A 169     2115   2640   2089     64     98   -652       C  
ATOM   1313  O   PRO A 169      22.680   1.924  -2.319  1.00 17.98           O  
ANISOU 1313  O   PRO A 169     2144   2595   2094     33    217   -351       O  
ATOM   1314  CB  PRO A 169      21.340   2.627  -5.081  1.00 22.47           C  
ANISOU 1314  CB  PRO A 169     3077   3412   2048     63     -9   -885       C  
ATOM   1315  CG  PRO A 169      22.496   3.242  -5.765  1.00 24.35           C  
ANISOU 1315  CG  PRO A 169     3586   3234   2432     96    491   -877       C  
ATOM   1316  CD  PRO A 169      22.914   4.456  -5.041  1.00 19.28           C  
ANISOU 1316  CD  PRO A 169     2508   3184   1632    407     16   -529       C  
ATOM   1317  N   GLY A 170      20.501   1.929  -1.800  1.00 18.98           N  
ANISOU 1317  N   GLY A 170     1985   3142   2084   -131    -45   -707       N  
ATOM   1318  CA  GLY A 170      20.618   1.064  -0.648  1.00 19.20           C  
ANISOU 1318  CA  GLY A 170     2470   2666   2159   -268    223   -762       C  
ATOM   1319  C   GLY A 170      20.904   1.809   0.653  1.00 16.85           C  
ANISOU 1319  C   GLY A 170     1920   2438   2043     14    189   -674       C  
ATOM   1320  O   GLY A 170      21.067   1.190   1.705  1.00 17.44           O  
ANISOU 1320  O   GLY A 170     2197   2363   2066   -186    302   -581       O  
ATOM   1321  N   ALA A 171      20.969   3.165   0.615  1.00 16.78           N  
ANISOU 1321  N   ALA A 171     2006   2512   1859   -163    130   -570       N  
ATOM   1322  CA  ALA A 171      21.290   3.886   1.839  1.00 16.72           C  
ANISOU 1322  CA  ALA A 171     2052   2345   1957   -160    371   -650       C  
ATOM   1323  C   ALA A 171      20.297   3.579   2.961  1.00 16.23           C  
ANISOU 1323  C   ALA A 171     1782   2409   1974   -249    225   -774       C  
ATOM   1324  O   ALA A 171      20.677   3.612   4.140  1.00 16.23           O  
ANISOU 1324  O   ALA A 171     1850   2402   1914   -362    332   -786       O  
ATOM   1325  CB  ALA A 171      21.405   5.399   1.623  1.00 19.97           C  
ANISOU 1325  CB  ALA A 171     2656   2365   2566   -375    341   -487       C  
ATOM   1326  N   SER A 172      19.034   3.269   2.599  1.00 17.89           N  
ANISOU 1326  N   SER A 172     1639   2858   2302    -20    207   -767       N  
ATOM   1327  CA  SER A 172      18.033   2.948   3.656  1.00 19.13           C  
ANISOU 1327  CA  SER A 172     1782   3115   2373    -92    452   -988       C  
ATOM   1328  C   SER A 172      18.347   1.685   4.419  1.00 19.02           C  
ANISOU 1328  C   SER A 172     2073   2810   2343   -505    471  -1087       C  
ATOM   1329  O   SER A 172      17.689   1.477   5.458  1.00 20.40           O  
ANISOU 1329  O   SER A 172     1883   3284   2586   -221    493   -836       O  
ATOM   1330  CB  SER A 172      16.648   2.851   3.014  1.00 24.08           C  
ANISOU 1330  CB  SER A 172     1704   4768   2677    -67    542   -862       C  
ATOM   1331  OG  SER A 172      16.550   1.667   2.205  1.00 30.04           O  
ANISOU 1331  OG  SER A 172     2666   5633   3114  -1343    226  -1454       O  
ATOM   1332  N   LEU A 173      19.291   0.868   3.980  1.00 18.14           N  
ANISOU 1332  N   LEU A 173     2037   2791   2065   -320    271  -1020       N  
ATOM   1333  CA  LEU A 173      19.738  -0.310   4.724  1.00 18.51           C  
ANISOU 1333  CA  LEU A 173     2362   2567   2104   -588    775   -759       C  
ATOM   1334  C   LEU A 173      20.631   0.033   5.943  1.00 17.82           C  
ANISOU 1334  C   LEU A 173     2742   2313   1718   -178    742   -469       C  
ATOM   1335  O   LEU A 173      20.815  -0.797   6.844  1.00 21.21           O  
ANISOU 1335  O   LEU A 173     3381   2636   2043     70    980   -200       O  
ATOM   1336  CB  LEU A 173      20.503  -1.275   3.777  1.00 20.66           C  
ANISOU 1336  CB  LEU A 173     2923   2369   2556   -502    741  -1058       C  
ATOM   1337  CG  LEU A 173      19.674  -1.890   2.696  1.00 21.62           C  
ANISOU 1337  CG  LEU A 173     3244   2674   2298   -834    882   -888       C  
ATOM   1338  CD1 LEU A 173      20.562  -2.475   1.602  1.00 20.27           C  
ANISOU 1338  CD1 LEU A 173     2716   2692   2293   -590    490   -934       C  
ATOM   1339  CD2 LEU A 173      18.754  -2.977   3.253  1.00 29.24           C  
ANISOU 1339  CD2 LEU A 173     3832   4111   3169  -1966   1198  -1002       C  
ATOM   1340  N   GLY A 174      21.144   1.239   5.930  1.00 16.34           N  
ANISOU 1340  N   GLY A 174     2288   2274   1645    -21    428   -754       N  
ATOM   1341  CA  GLY A 174      21.882   1.773   7.055  1.00 16.61           C  
ANISOU 1341  CA  GLY A 174     1958   2732   1620    236    300   -669       C  
ATOM   1342  C   GLY A 174      20.911   2.271   8.142  1.00 16.62           C  
ANISOU 1342  C   GLY A 174     1788   2821   1705     67    308   -816       C  
ATOM   1343  O   GLY A 174      19.706   2.385   7.943  1.00 23.39           O  
ANISOU 1343  O   GLY A 174     1850   4715   2323    489    141  -1775       O  
ATOM   1344  N   ILE A 175      21.492   2.569   9.276  1.00 13.58           N  
ANISOU 1344  N   ILE A 175     1690   1832   1639    -13    442   -480       N  
ATOM   1345  CA  ILE A 175      20.824   3.128  10.420  1.00 12.50           C  
ANISOU 1345  CA  ILE A 175     1407   1823   1520   -163    321   -381       C  
ATOM   1346  C   ILE A 175      21.456   4.507  10.717  1.00 11.71           C  
ANISOU 1346  C   ILE A 175     1339   1613   1498    112    289   -255       C  
ATOM   1347  O   ILE A 175      22.460   4.870  10.117  1.00 13.34           O  
ANISOU 1347  O   ILE A 175     1403   1798   1867    -96    400   -351       O  
ATOM   1348  CB  ILE A 175      20.811   2.215  11.660  1.00 13.81           C  
ANISOU 1348  CB  ILE A 175     1719   1794   1736   -248    445   -248       C  
ATOM   1349  CG1 ILE A 175      22.222   1.935  12.221  1.00 13.89           C  
ANISOU 1349  CG1 ILE A 175     1702   1824   1749    137    498    -80       C  
ATOM   1350  CG2 ILE A 175      20.058   0.927  11.420  1.00 17.51           C  
ANISOU 1350  CG2 ILE A 175     2153   1949   2550   -560    548   -257       C  
ATOM   1351  CD1 ILE A 175      22.233   1.445  13.637  1.00 16.88           C  
ANISOU 1351  CD1 ILE A 175     2410   2301   1702    348    750     58       C  
ATOM   1352  N   THR A 176      20.868   5.207  11.661  1.00 11.94           N  
ANISOU 1352  N   THR A 176     1333   1691   1515    -41    330   -314       N  
ATOM   1353  CA  THR A 176      21.411   6.447  12.172  1.00 12.14           C  
ANISOU 1353  CA  THR A 176     1559   1617   1439    -87    447   -275       C  
ATOM   1354  C   THR A 176      21.607   6.317  13.684  1.00 12.28           C  
ANISOU 1354  C   THR A 176     1371   1891   1405   -163    374   -255       C  
ATOM   1355  O   THR A 176      21.365   5.224  14.265  1.00 12.53           O  
ANISOU 1355  O   THR A 176     1389   1776   1594   -136    441   -178       O  
ATOM   1356  CB  THR A 176      20.504   7.644  11.895  1.00 13.72           C  
ANISOU 1356  CB  THR A 176     1784   1892   1536    273    373   -310       C  
ATOM   1357  OG1 THR A 176      19.301   7.433  12.704  1.00 15.21           O  
ANISOU 1357  OG1 THR A 176     1781   2154   1845    367    487   -403       O  
ATOM   1358  CG2 THR A 176      20.175   7.748  10.414  1.00 15.81           C  
ANISOU 1358  CG2 THR A 176     2707   1711   1591    325    285   -214       C  
ATOM   1359  N   SER A 177      21.995   7.407  14.349  1.00 12.05           N  
ANISOU 1359  N   SER A 177     1405   1761   1411    -37    337   -320       N  
ATOM   1360  CA  SER A 177      22.078   7.369  15.810  1.00 12.03           C  
ANISOU 1360  CA  SER A 177     1448   1663   1459    -70    390   -251       C  
ATOM   1361  C   SER A 177      20.779   6.941  16.460  1.00 12.35           C  
ANISOU 1361  C   SER A 177     1432   1653   1607     -7    334   -171       C  
ATOM   1362  O   SER A 177      20.798   6.300  17.526  1.00 13.53           O  
ANISOU 1362  O   SER A 177     1573   1941   1627   -126    221     -8       O  
ATOM   1363  CB  SER A 177      22.579   8.711  16.356  1.00 12.89           C  
ANISOU 1363  CB  SER A 177     1797   1681   1421   -197    330   -183       C  
ATOM   1364  OG  SER A 177      21.731   9.778  15.973  1.00 13.08           O  
ANISOU 1364  OG  SER A 177     1878   1618   1472    -32    492   -216       O  
ATOM   1365  N   ASP A 178      19.643   7.258  15.854  1.00 12.27           N  
ANISOU 1365  N   ASP A 178     1386   1768   1509     40    400    -90       N  
ATOM   1366  CA  ASP A 178      18.374   6.788  16.436  1.00 13.18           C  
ANISOU 1366  CA  ASP A 178     1468   1912   1627    -85    360    -81       C  
ATOM   1367  C   ASP A 178      18.335   5.263  16.491  1.00 12.51           C  
ANISOU 1367  C   ASP A 178     1196   1918   1641    -76    378    -21       C  
ATOM   1368  O   ASP A 178      17.969   4.635  17.481  1.00 14.04           O  
ANISOU 1368  O   ASP A 178     1451   2122   1760   -231    445     47       O  
ATOM   1369  CB  ASP A 178      17.203   7.340  15.634  1.00 15.27           C  
ANISOU 1369  CB  ASP A 178     1428   2253   2122    243    441    145       C  
ATOM   1370  CG  ASP A 178      16.893   8.787  15.836  1.00 17.02           C  
ANISOU 1370  CG  ASP A 178     2165   2405   1897    530    658    -58       C  
ATOM   1371  OD1 ASP A 178      17.489   9.471  16.740  1.00 19.78           O  
ANISOU 1371  OD1 ASP A 178     2526   2663   2326    308    712   -414       O  
ATOM   1372  OD2 ASP A 178      16.056   9.338  15.057  1.00 22.50           O  
ANISOU 1372  OD2 ASP A 178     2525   2397   3628    517   -153    178       O  
ATOM   1373  N   GLY A 179      18.696   4.621  15.354  1.00 14.31           N  
ANISOU 1373  N   GLY A 179     1955   1847   1634     13    314    -74       N  
ATOM   1374  CA  GLY A 179      18.733   3.183  15.332  1.00 14.22           C  
ANISOU 1374  CA  GLY A 179     1715   1828   1860   -187    359     -8       C  
ATOM   1375  C   GLY A 179      19.791   2.601  16.230  1.00 13.16           C  
ANISOU 1375  C   GLY A 179     1652   1653   1697   -139    289   -262       C  
ATOM   1376  O   GLY A 179      19.637   1.475  16.722  1.00 13.80           O  
ANISOU 1376  O   GLY A 179     1772   1751   1720   -140    309   -199       O  
ATOM   1377  N   PHE A 180      20.893   3.299  16.469  1.00 12.79           N  
ANISOU 1377  N   PHE A 180     1671   1607   1583    -28    338    -70       N  
ATOM   1378  CA  PHE A 180      21.922   2.858  17.388  1.00 12.92           C  
ANISOU 1378  CA  PHE A 180     1431   1834   1643    -71    416   -126       C  
ATOM   1379  C   PHE A 180      21.300   2.571  18.763  1.00 12.16           C  
ANISOU 1379  C   PHE A 180     1537   1513   1573    -60    343    -92       C  
ATOM   1380  O   PHE A 180      21.587   1.567  19.384  1.00 13.28           O  
ANISOU 1380  O   PHE A 180     1605   1647   1792     59    405    -45       O  
ATOM   1381  CB  PHE A 180      23.003   3.936  17.509  1.00 13.95           C  
ANISOU 1381  CB  PHE A 180     1482   1973   1845    -62    364    -28       C  
ATOM   1382  CG  PHE A 180      24.094   3.628  18.521  1.00 13.78           C  
ANISOU 1382  CG  PHE A 180     1347   1808   2080    196    291     39       C  
ATOM   1383  CD1 PHE A 180      24.004   4.211  19.775  1.00 16.64           C  
ANISOU 1383  CD1 PHE A 180     1818   2211   2292    429   -102   -282       C  
ATOM   1384  CD2 PHE A 180      25.154   2.786  18.223  1.00 17.83           C  
ANISOU 1384  CD2 PHE A 180     1639   2390   2745    476    487   -118       C  
ATOM   1385  CE1 PHE A 180      24.978   4.002  20.737  1.00 21.22           C  
ANISOU 1385  CE1 PHE A 180     2194   3483   2386    930   -305   -190       C  
ATOM   1386  CE2 PHE A 180      26.138   2.560  19.156  1.00 21.81           C  
ANISOU 1386  CE2 PHE A 180     2176   3476   2634   1423    605    688       C  
ATOM   1387  CZ  PHE A 180      26.035   3.179  20.388  1.00 22.27           C  
ANISOU 1387  CZ  PHE A 180     1832   3990   2641    923    197    396       C  
ATOM   1388  N   PHE A 181      20.407   3.453  19.220  1.00 11.90           N  
ANISOU 1388  N   PHE A 181     1448   1597   1478    -39    270   -160       N  
ATOM   1389  CA  PHE A 181      19.786   3.313  20.505  1.00 12.26           C  
ANISOU 1389  CA  PHE A 181     1425   1803   1431    -50    296   -286       C  
ATOM   1390  C   PHE A 181      18.638   2.286  20.515  1.00 12.88           C  
ANISOU 1390  C   PHE A 181     1603   1750   1541   -140    260   -108       C  
ATOM   1391  O   PHE A 181      18.070   2.008  21.594  1.00 15.53           O  
ANISOU 1391  O   PHE A 181     1865   2387   1650   -417    347    -78       O  
ATOM   1392  CB  PHE A 181      19.313   4.667  21.072  1.00 13.37           C  
ANISOU 1392  CB  PHE A 181     1588   1736   1754    -10    371   -300       C  
ATOM   1393  CG  PHE A 181      20.513   5.572  21.356  1.00 12.63           C  
ANISOU 1393  CG  PHE A 181     1591   1847   1360   -110    434   -284       C  
ATOM   1394  CD1 PHE A 181      21.431   5.173  22.349  1.00 14.39           C  
ANISOU 1394  CD1 PHE A 181     1926   2168   1374   -197    193   -332       C  
ATOM   1395  CD2 PHE A 181      20.758   6.730  20.661  1.00 13.18           C  
ANISOU 1395  CD2 PHE A 181     1601   1860   1547    -18    601   -237       C  
ATOM   1396  CE1 PHE A 181      22.506   5.981  22.630  1.00 14.46           C  
ANISOU 1396  CE1 PHE A 181     1904   2280   1309   -283    184   -224       C  
ATOM   1397  CE2 PHE A 181      21.842   7.539  20.936  1.00 14.33           C  
ANISOU 1397  CE2 PHE A 181     1904   1835   1708   -166    459   -151       C  
ATOM   1398  CZ  PHE A 181      22.757   7.116  21.906  1.00 14.99           C  
ANISOU 1398  CZ  PHE A 181     1905   2098   1695   -157    362   -275       C  
ATOM   1399  N   GLN A 182      18.334   1.700  19.374  1.00 13.01           N  
ANISOU 1399  N   GLN A 182     1396   1782   1765   -190    231   -330       N  
ATOM   1400  CA  GLN A 182      17.411   0.572  19.318  1.00 14.20           C  
ANISOU 1400  CA  GLN A 182     1339   1913   2143   -168    337   -362       C  
ATOM   1401  C   GLN A 182      18.152  -0.759  19.205  1.00 14.57           C  
ANISOU 1401  C   GLN A 182     1485   1801   2248   -174    219   -124       C  
ATOM   1402  O   GLN A 182      17.530  -1.819  19.362  1.00 16.41           O  
ANISOU 1402  O   GLN A 182     1806   1926   2502   -264    290    -27       O  
ATOM   1403  CB AGLN A 182      16.444   0.702  18.131  0.58 16.56           C  
ANISOU 1403  CB AGLN A 182     1526   1903   2864    -13   -206   -684       C  
ATOM   1404  CB BGLN A 182      16.482   0.661  18.108  0.42 16.65           C  
ANISOU 1404  CB BGLN A 182     1421   1922   2984   -434   -241     33       C  
ATOM   1405  CG AGLN A 182      15.564   1.927  18.276  0.58 15.28           C  
ANISOU 1405  CG AGLN A 182      950   2053   2802   -128    265   -581       C  
ATOM   1406  CG BGLN A 182      15.403   1.712  18.098  0.42 21.72           C  
ANISOU 1406  CG BGLN A 182     2322   2430   3501    272   -603   -337       C  
ATOM   1407  CD AGLN A 182      14.694   2.217  17.083  0.58 24.95           C  
ANISOU 1407  CD AGLN A 182     2219   3457   3803    817   -903   -994       C  
ATOM   1408  CD BGLN A 182      14.377   1.588  19.194  0.42 22.37           C  
ANISOU 1408  CD BGLN A 182     1687   2609   4204    147   -445   -917       C  
ATOM   1409  OE1AGLN A 182      14.881   1.779  15.949  0.58 40.11           O  
ANISOU 1409  OE1AGLN A 182     5144   5956   4142   2657  -2413  -2431       O  
ATOM   1410  OE1BGLN A 182      13.552   0.677  19.220  0.42 32.06           O  
ANISOU 1410  OE1BGLN A 182     2239   3067   6875   -389    454  -1400       O  
ATOM   1411  NE2AGLN A 182      13.638   2.992  17.332  0.58 37.25           N  
ANISOU 1411  NE2AGLN A 182     2295   7213   4646   2265   -269   -192       N  
ATOM   1412  NE2BGLN A 182      14.344   2.504  20.139  0.42 32.96           N  
ANISOU 1412  NE2BGLN A 182     3703   4809   4013   -876   -185  -1916       N  
ATOM   1413  N   LEU A 183      19.449  -0.772  18.913  1.00 13.60           N  
ANISOU 1413  N   LEU A 183     1547   1875   1744     24    365     69       N  
ATOM   1414  CA  LEU A 183      20.189  -2.039  18.807  1.00 13.94           C  
ANISOU 1414  CA  LEU A 183     1608   1714   1974    -49    199     33       C  
ATOM   1415  C   LEU A 183      20.061  -2.908  20.068  1.00 14.03           C  
ANISOU 1415  C   LEU A 183     1503   1741   2087     35    477     70       C  
ATOM   1416  O   LEU A 183      20.251  -2.382  21.154  1.00 14.39           O  
ANISOU 1416  O   LEU A 183     1605   1980   1881    131    432    151       O  
ATOM   1417  CB  LEU A 183      21.660  -1.783  18.575  1.00 13.79           C  
ANISOU 1417  CB  LEU A 183     1636   1786   1819      5    520    -67       C  
ATOM   1418  CG  LEU A 183      22.073  -1.188  17.236  1.00 15.03           C  
ANISOU 1418  CG  LEU A 183     2056   1678   1977     96    562     31       C  
ATOM   1419  CD1 LEU A 183      23.553  -0.794  17.284  1.00 16.39           C  
ANISOU 1419  CD1 LEU A 183     1830   2078   2320    384    899    588       C  
ATOM   1420  CD2 LEU A 183      21.823  -2.195  16.120  1.00 19.98           C  
ANISOU 1420  CD2 LEU A 183     3437   2280   1872     92    957   -368       C  
ATOM   1421  N   GLU A 184      19.802  -4.185  19.893  1.00 15.66           N  
ANISOU 1421  N   GLU A 184     1721   1782   2447   -118    355    170       N  
ATOM   1422  CA  GLU A 184      19.611  -5.101  21.013  1.00 16.54           C  
ANISOU 1422  CA  GLU A 184     1974   1777   2533   -145    491    226       C  
ATOM   1423  C   GLU A 184      20.810  -6.006  21.203  1.00 15.88           C  
ANISOU 1423  C   GLU A 184     1868   1910   2254   -105    467    197       C  
ATOM   1424  O   GLU A 184      20.859  -6.729  22.176  1.00 19.89           O  
ANISOU 1424  O   GLU A 184     2302   2453   2801    -58    576    786       O  
ATOM   1425  CB AGLU A 184      18.364  -5.956  20.840  0.57 23.24           C  
ANISOU 1425  CB AGLU A 184     1824   2755   4252   -443     71   1339       C  
ATOM   1426  CB BGLU A 184      18.305  -5.869  20.832  0.43 22.44           C  
ANISOU 1426  CB BGLU A 184     1830   2612   4086   -355    273   1113       C  
ATOM   1427  CG AGLU A 184      17.015  -5.255  20.849  0.57 25.85           C  
ANISOU 1427  CG AGLU A 184     2016   2870   4937   -155    185   1150       C  
ATOM   1428  CG BGLU A 184      17.124  -4.901  20.914  0.43 26.14           C  
ANISOU 1428  CG BGLU A 184     2118   2446   5369   -151   -274   1159       C  
ATOM   1429  CD AGLU A 184      16.455  -5.036  22.235  0.57 29.96           C  
ANISOU 1429  CD AGLU A 184     2414   3813   5157    -37    411    772       C  
ATOM   1430  CD BGLU A 184      15.781  -5.580  20.961  0.43 28.60           C  
ANISOU 1430  CD BGLU A 184     1894   3372   5601   -186    279    429       C  
ATOM   1431  OE1AGLU A 184      17.155  -4.938  23.258  0.57 39.90           O  
ANISOU 1431  OE1AGLU A 184     3730   5995   5435   -907     56   -828       O  
ATOM   1432  OE1BGLU A 184      15.757  -6.796  20.699  0.43 40.01           O  
ANISOU 1432  OE1BGLU A 184     3106   3245   8852  -1049    271    380       O  
ATOM   1433  OE2AGLU A 184      15.200  -4.960  22.305  0.57 43.28           O  
ANISOU 1433  OE2AGLU A 184     2645   7382   6416   1002    847     76       O  
ATOM   1434  OE2BGLU A 184      14.772  -4.920  21.273  0.43 41.54           O  
ANISOU 1434  OE2BGLU A 184     2021   6503   7260    910   -554  -1236       O  
ATOM   1435  N   GLU A 185      21.782  -5.970  20.295  1.00 16.26           N  
ANISOU 1435  N   GLU A 185     1970   1942   2267   -176    567   -169       N  
ATOM   1436  CA  GLU A 185      23.006  -6.766  20.371  1.00 16.40           C  
ANISOU 1436  CA  GLU A 185     2103   1729   2401    -89    704    -14       C  
ATOM   1437  C   GLU A 185      24.179  -5.947  19.807  1.00 14.78           C  
ANISOU 1437  C   GLU A 185     1919   1431   2266    112    595     -4       C  
ATOM   1438  O   GLU A 185      23.977  -5.049  19.027  1.00 15.76           O  
ANISOU 1438  O   GLU A 185     1995   1845   2149    -89    434    148       O  
ATOM   1439  CB  GLU A 185      22.862  -8.052  19.561  1.00 22.98           C  
ANISOU 1439  CB  GLU A 185     2483   1704   4543   -194    460   -563       C  
ATOM   1440  CG  GLU A 185      21.723  -8.931  20.031  1.00 31.09           C  
ANISOU 1440  CG  GLU A 185     4414   2587   4811  -1366   1016   -395       C  
ATOM   1441  CD  GLU A 185      21.992  -9.516  21.424  1.00 37.93           C  
ANISOU 1441  CD  GLU A 185     4177   4052   6182  -1574    143   1178       C  
ATOM   1442  OE1 GLU A 185      23.049  -9.207  22.018  1.00 49.09           O  
ANISOU 1442  OE1 GLU A 185     3575   9128   5948  -1140    451   -241       O  
ATOM   1443  OE2 GLU A 185      21.130 -10.284  21.896  1.00 57.02           O  
ANISOU 1443  OE2 GLU A 185     5849   8229   7588  -3166    677   3263       O  
ATOM   1444  N   LEU A 186      25.371  -6.299  20.209  1.00 15.61           N  
ANISOU 1444  N   LEU A 186     1965   2023   1944     81    628    187       N  
ATOM   1445  CA  LEU A 186      26.590  -5.689  19.646  1.00 14.62           C  
ANISOU 1445  CA  LEU A 186     1866   1947   1743     46    650    -90       C  
ATOM   1446  C   LEU A 186      26.777  -6.118  18.206  1.00 14.78           C  
ANISOU 1446  C   LEU A 186     1961   1868   1787    -43    538   -190       C  
ATOM   1447  O   LEU A 186      26.867  -7.337  17.953  1.00 16.88           O  
ANISOU 1447  O   LEU A 186     2520   1850   2044     64    887   -109       O  
ATOM   1448  CB  LEU A 186      27.771  -6.180  20.455  1.00 17.66           C  
ANISOU 1448  CB  LEU A 186     1938   3011   1759     20    585    178       C  
ATOM   1449  CG  LEU A 186      29.147  -5.684  19.996  1.00 18.15           C  
ANISOU 1449  CG  LEU A 186     1904   2842   2151    -70    397    257       C  
ATOM   1450  CD1 LEU A 186      29.333  -4.213  20.277  1.00 18.72           C  
ANISOU 1450  CD1 LEU A 186     1906   3086   2121    -89    818   -261       C  
ATOM   1451  CD2 LEU A 186      30.224  -6.507  20.683  1.00 23.38           C  
ANISOU 1451  CD2 LEU A 186     1958   3647   3278     21    139    867       C  
ATOM   1452  N   PRO A 187      26.860  -5.212  17.234  1.00 13.88           N  
ANISOU 1452  N   PRO A 187     1909   1700   1664     11    415   -337       N  
ATOM   1453  CA  PRO A 187      27.175  -5.655  15.872  1.00 14.30           C  
ANISOU 1453  CA  PRO A 187     1891   1819   1724      8    380   -288       C  
ATOM   1454  C   PRO A 187      28.576  -6.243  15.805  1.00 14.46           C  
ANISOU 1454  C   PRO A 187     1920   1677   1897    -25    630   -140       C  
ATOM   1455  O   PRO A 187      29.528  -5.640  16.328  1.00 15.17           O  
ANISOU 1455  O   PRO A 187     1846   1939   1979   -129    652   -249       O  
ATOM   1456  CB  PRO A 187      27.055  -4.375  15.043  1.00 14.99           C  
ANISOU 1456  CB  PRO A 187     2021   1895   1779     51    489   -157       C  
ATOM   1457  CG  PRO A 187      26.381  -3.359  15.906  1.00 17.56           C  
ANISOU 1457  CG  PRO A 187     3099   1701   1870      7    682   -176       C  
ATOM   1458  CD  PRO A 187      26.642  -3.760  17.298  1.00 15.22           C  
ANISOU 1458  CD  PRO A 187     2097   1769   1916    176    762   -203       C  
ATOM   1459  N   GLY A 188      28.748  -7.303  15.053  1.00 14.88           N  
ANISOU 1459  N   GLY A 188     2029   1798   1824     41    543   -107       N  
ATOM   1460  CA  GLY A 188      30.087  -7.844  14.930  1.00 15.87           C  
ANISOU 1460  CA  GLY A 188     2225   1671   2134    142    915     25       C  
ATOM   1461  C   GLY A 188      31.025  -6.968  14.142  1.00 14.20           C  
ANISOU 1461  C   GLY A 188     1998   1528   1870    168    633    -52       C  
ATOM   1462  O   GLY A 188      32.219  -6.839  14.482  1.00 15.34           O  
ANISOU 1462  O   GLY A 188     2058   1916   1855     58    457     46       O  
ATOM   1463  N   ARG A 189      30.519  -6.345  13.096  1.00 13.86           N  
ANISOU 1463  N   ARG A 189     1944   1492   1831     46    605    -71       N  
ATOM   1464  CA  ARG A 189      31.240  -5.505  12.141  1.00 14.00           C  
ANISOU 1464  CA  ARG A 189     2203   1531   1587    100    502    -86       C  
ATOM   1465  C   ARG A 189      30.459  -4.213  11.903  1.00 12.32           C  
ANISOU 1465  C   ARG A 189     1638   1542   1502   -106    630    -25       C  
ATOM   1466  O   ARG A 189      29.301  -4.358  11.448  1.00 13.91           O  
ANISOU 1466  O   ARG A 189     1780   1705   1799   -202    379   -333       O  
ATOM   1467  CB  ARG A 189      31.506  -6.290  10.837  1.00 14.52           C  
ANISOU 1467  CB  ARG A 189     2154   1625   1738    -24    540   -245       C  
ATOM   1468  CG  ARG A 189      32.216  -5.509   9.761  1.00 15.62           C  
ANISOU 1468  CG  ARG A 189     2164   2068   1703     44    666   -322       C  
ATOM   1469  CD  ARG A 189      33.723  -5.493   9.971  1.00 16.34           C  
ANISOU 1469  CD  ARG A 189     2164   2083   1962    -52    520   -168       C  
ATOM   1470  NE  ARG A 189      34.403  -4.828   8.868  1.00 16.55           N  
ANISOU 1470  NE  ARG A 189     2288   2017   1983    123    753   -258       N  
ATOM   1471  CZ  ARG A 189      34.835  -3.595   8.849  1.00 14.90           C  
ANISOU 1471  CZ  ARG A 189     1983   1961   1717    243    528    -82       C  
ATOM   1472  NH1 ARG A 189      35.459  -3.136   7.761  1.00 17.78           N  
ANISOU 1472  NH1 ARG A 189     2664   2259   1833    -93    684    -94       N  
ATOM   1473  NH2 ARG A 189      34.677  -2.747   9.833  1.00 16.09           N  
ANISOU 1473  NH2 ARG A 189     2370   1893   1849    143    744    -66       N  
ATOM   1474  N   SER A 190      31.094  -3.107  12.206  1.00 12.40           N  
ANISOU 1474  N   SER A 190     1681   1452   1579    -22    416   -204       N  
ATOM   1475  CA  SER A 190      30.430  -1.795  12.061  1.00 12.79           C  
ANISOU 1475  CA  SER A 190     1632   1555   1672    164    284    -48       C  
ATOM   1476  C   SER A 190      31.199  -0.865  11.118  1.00 11.98           C  
ANISOU 1476  C   SER A 190     1552   1474   1525    270    398   -169       C  
ATOM   1477  O   SER A 190      32.435  -0.810  11.218  1.00 13.49           O  
ANISOU 1477  O   SER A 190     1542   1886   1699    295    468     86       O  
ATOM   1478  CB  SER A 190      30.309  -1.113  13.436  1.00 14.67           C  
ANISOU 1478  CB  SER A 190     2226   1569   1778    413    891     13       C  
ATOM   1479  OG  SER A 190      29.545  -1.889  14.342  1.00 14.68           O  
ANISOU 1479  OG  SER A 190     1818   1793   1968    -43    636    -58       O  
ATOM   1480  N   VAL A 191      30.458  -0.139  10.310  1.00 11.56           N  
ANISOU 1480  N   VAL A 191     1526   1470   1397    166    365   -143       N  
ATOM   1481  CA  VAL A 191      31.030   0.920   9.476  1.00 11.93           C  
ANISOU 1481  CA  VAL A 191     1562   1493   1479    100    414   -128       C  
ATOM   1482  C   VAL A 191      30.222   2.200   9.794  1.00 11.26           C  
ANISOU 1482  C   VAL A 191     1356   1499   1424    -37    352   -111       C  
ATOM   1483  O   VAL A 191      29.021   2.212   9.581  1.00 12.53           O  
ANISOU 1483  O   VAL A 191     1360   1613   1789     67    296   -201       O  
ATOM   1484  CB  VAL A 191      30.972   0.591   7.987  1.00 12.59           C  
ANISOU 1484  CB  VAL A 191     1709   1581   1494    157    512   -175       C  
ATOM   1485  CG1 VAL A 191      31.480   1.777   7.147  1.00 13.67           C  
ANISOU 1485  CG1 VAL A 191     1799   1829   1566     99    445     53       C  
ATOM   1486  CG2 VAL A 191      31.814  -0.669   7.699  1.00 14.51           C  
ANISOU 1486  CG2 VAL A 191     1950   1752   1810    256    681   -257       C  
ATOM   1487  N   ILE A 192      30.890   3.202  10.332  1.00 10.89           N  
ANISOU 1487  N   ILE A 192     1323   1557   1256    113    270   -167       N  
ATOM   1488  CA  ILE A 192      30.316   4.486  10.686  1.00 11.41           C  
ANISOU 1488  CA  ILE A 192     1382   1524   1431     63    297   -192       C  
ATOM   1489  C   ILE A 192      30.761   5.451   9.606  1.00 11.22           C  
ANISOU 1489  C   ILE A 192     1302   1478   1481      2    254   -204       C  
ATOM   1490  O   ILE A 192      31.951   5.544   9.328  1.00 12.55           O  
ANISOU 1490  O   ILE A 192     1281   1855   1631     85    334     56       O  
ATOM   1491  CB  ILE A 192      30.713   4.989  12.075  1.00 11.67           C  
ANISOU 1491  CB  ILE A 192     1297   1643   1493    -54    197   -238       C  
ATOM   1492  CG1 ILE A 192      30.273   4.024  13.156  1.00 14.54           C  
ANISOU 1492  CG1 ILE A 192     1802   2157   1565   -157    326     19       C  
ATOM   1493  CG2 ILE A 192      30.099   6.356  12.336  1.00 13.25           C  
ANISOU 1493  CG2 ILE A 192     1660   1817   1556     61    415   -460       C  
ATOM   1494  CD1 ILE A 192      31.076   2.819  13.384  1.00 19.44           C  
ANISOU 1494  CD1 ILE A 192     3328   2109   1950    368    472    229       C  
ATOM   1495  N   VAL A 193      29.806   6.188   9.011  1.00 10.98           N  
ANISOU 1495  N   VAL A 193     1243   1527   1402   -116    336   -176       N  
ATOM   1496  CA  VAL A 193      30.097   7.159   7.968  1.00 11.16           C  
ANISOU 1496  CA  VAL A 193     1292   1564   1384    -38    324   -138       C  
ATOM   1497  C   VAL A 193      29.955   8.557   8.541  1.00 10.70           C  
ANISOU 1497  C   VAL A 193     1338   1525   1203     62    228    -74       C  
ATOM   1498  O   VAL A 193      28.816   8.938   8.925  1.00 12.14           O  
ANISOU 1498  O   VAL A 193     1328   1662   1623     51    480    -56       O  
ATOM   1499  CB  VAL A 193      29.209   6.927   6.720  1.00 11.60           C  
ANISOU 1499  CB  VAL A 193     1350   1649   1408   -176    323   -233       C  
ATOM   1500  CG1 VAL A 193      29.613   7.929   5.636  1.00 13.11           C  
ANISOU 1500  CG1 VAL A 193     1519   1927   1534   -133    176    -35       C  
ATOM   1501  CG2 VAL A 193      29.319   5.521   6.200  1.00 13.51           C  
ANISOU 1501  CG2 VAL A 193     1778   1718   1638    -57    461   -388       C  
ATOM   1502  N   GLY A 194      30.998   9.349   8.529  1.00 11.79           N  
ANISOU 1502  N   GLY A 194     1266   1653   1560     15    340   -317       N  
ATOM   1503  CA  GLY A 194      30.981  10.712   9.011  1.00 12.71           C  
ANISOU 1503  CA  GLY A 194     1402   1781   1647    -68    259   -336       C  
ATOM   1504  C   GLY A 194      32.227  11.073   9.737  1.00 11.43           C  
ANISOU 1504  C   GLY A 194     1255   1654   1434    -18    264   -178       C  
ATOM   1505  O   GLY A 194      32.988  10.203  10.145  1.00 12.85           O  
ANISOU 1505  O   GLY A 194     1491   1731   1662     30    229     10       O  
ATOM   1506  N   ALA A 195      32.455  12.359   9.963  1.00 12.36           N  
ANISOU 1506  N   ALA A 195     1464   1645   1586     -5    199   -205       N  
ATOM   1507  CA  ALA A 195      33.675  12.825  10.538  1.00 12.01           C  
ANISOU 1507  CA  ALA A 195     1334   1771   1456   -128    382   -207       C  
ATOM   1508  C   ALA A 195      33.459  13.848  11.660  1.00 11.93           C  
ANISOU 1508  C   ALA A 195     1289   1834   1412   -157    285   -193       C  
ATOM   1509  O   ALA A 195      34.395  14.467  12.125  1.00 14.76           O  
ANISOU 1509  O   ALA A 195     1181   2423   2005   -192    319   -752       O  
ATOM   1510  CB  ALA A 195      34.613  13.371   9.477  1.00 14.27           C  
ANISOU 1510  CB  ALA A 195     1602   2253   1567   -121    619   -205       C  
ATOM   1511  N   GLY A 196      32.194  14.077  12.064  1.00 11.82           N  
ANISOU 1511  N   GLY A 196     1220   1820   1452   -167    243   -237       N  
ATOM   1512  CA  GLY A 196      31.872  14.952  13.153  1.00 12.05           C  
ANISOU 1512  CA  GLY A 196     1519   1612   1446    -50    308    -67       C  
ATOM   1513  C   GLY A 196      31.785  14.261  14.475  1.00 11.03           C  
ANISOU 1513  C   GLY A 196     1125   1650   1418     -1    222    -87       C  
ATOM   1514  O   GLY A 196      32.109  13.075  14.620  1.00 12.24           O  
ANISOU 1514  O   GLY A 196     1358   1647   1645    163    554     69       O  
ATOM   1515  N   TYR A 197      31.385  15.011  15.495  1.00 10.92           N  
ANISOU 1515  N   TYR A 197     1169   1550   1430     14    314    -91       N  
ATOM   1516  CA  TYR A 197      31.485  14.434  16.847  1.00 11.50           C  
ANISOU 1516  CA  TYR A 197     1170   1801   1399     84    192    -51       C  
ATOM   1517  C   TYR A 197      30.617  13.216  17.044  1.00 10.81           C  
ANISOU 1517  C   TYR A 197     1191   1721   1196    132    277   -130       C  
ATOM   1518  O   TYR A 197      31.015  12.298  17.768  1.00 11.55           O  
ANISOU 1518  O   TYR A 197     1311   1670   1409    223    262    -90       O  
ATOM   1519  CB  TYR A 197      31.244  15.485  17.933  1.00 12.45           C  
ANISOU 1519  CB  TYR A 197     1616   1711   1404    174     17   -117       C  
ATOM   1520  CG  TYR A 197      29.794  15.740  18.300  1.00 13.22           C  
ANISOU 1520  CG  TYR A 197     1844   1845   1335    296    347    -80       C  
ATOM   1521  CD1 TYR A 197      29.240  15.091  19.397  1.00 16.85           C  
ANISOU 1521  CD1 TYR A 197     2439   2543   1420    537    715    117       C  
ATOM   1522  CD2 TYR A 197      29.003  16.607  17.609  1.00 14.20           C  
ANISOU 1522  CD2 TYR A 197     1607   2037   1753    397    595     84       C  
ATOM   1523  CE1 TYR A 197      27.937  15.283  19.781  1.00 18.66           C  
ANISOU 1523  CE1 TYR A 197     2662   2379   2048    561   1043    165       C  
ATOM   1524  CE2 TYR A 197      27.673  16.831  17.975  1.00 17.22           C  
ANISOU 1524  CE2 TYR A 197     1663   2443   2438    377    944    418       C  
ATOM   1525  CZ  TYR A 197      27.165  16.142  19.076  1.00 18.07           C  
ANISOU 1525  CZ  TYR A 197     2154   2143   2567    454   1219    357       C  
ATOM   1526  OH  TYR A 197      25.884  16.344  19.480  1.00 22.56           O  
ANISOU 1526  OH  TYR A 197     2386   2972   3215    580   1696    450       O  
ATOM   1527  N   ILE A 198      29.419  13.182  16.464  1.00 11.33           N  
ANISOU 1527  N   ILE A 198     1158   1807   1339     51    276     23       N  
ATOM   1528  CA  ILE A 198      28.558  12.006  16.660  1.00 11.57           C  
ANISOU 1528  CA  ILE A 198     1191   1818   1387     18    384     32       C  
ATOM   1529  C   ILE A 198      29.195  10.776  16.049  1.00 10.93           C  
ANISOU 1529  C   ILE A 198     1125   1725   1301    -80    126     43       C  
ATOM   1530  O   ILE A 198      29.206   9.702  16.661  1.00 12.22           O  
ANISOU 1530  O   ILE A 198     1342   1719   1582    -35    173    150       O  
ATOM   1531  CB  ILE A 198      27.120  12.305  16.128  1.00 14.07           C  
ANISOU 1531  CB  ILE A 198     1082   1959   2304    -42    334    234       C  
ATOM   1532  CG1 ILE A 198      26.407  13.393  16.985  1.00 15.55           C  
ANISOU 1532  CG1 ILE A 198     1300   2254   2353    250    390    258       C  
ATOM   1533  CG2 ILE A 198      26.295  11.119  16.048  1.00 16.97           C  
ANISOU 1533  CG2 ILE A 198     1306   2446   2695   -185     83    -39       C  
ATOM   1534  CD1 ILE A 198      25.107  13.922  16.420  1.00 18.12           C  
ANISOU 1534  CD1 ILE A 198     1411   2726   2748    477    478    650       C  
ATOM   1535  N   ALA A 199      29.746  10.902  14.831  1.00 11.54           N  
ANISOU 1535  N   ALA A 199     1352   1629   1402     49    252      2       N  
ATOM   1536  CA  ALA A 199      30.420   9.772  14.190  1.00 12.09           C  
ANISOU 1536  CA  ALA A 199     1427   1730   1436    -18    189   -165       C  
ATOM   1537  C   ALA A 199      31.578   9.273  15.039  1.00 11.29           C  
ANISOU 1537  C   ALA A 199     1398   1568   1323     74    382   -191       C  
ATOM   1538  O   ALA A 199      31.787   8.084  15.236  1.00 11.78           O  
ANISOU 1538  O   ALA A 199     1611   1589   1277     37    373   -125       O  
ATOM   1539  CB  ALA A 199      30.904  10.206  12.810  1.00 12.95           C  
ANISOU 1539  CB  ALA A 199     1672   1845   1405    -53    265   -143       C  
ATOM   1540  N   VAL A 200      32.398  10.222  15.561  1.00 11.16           N  
ANISOU 1540  N   VAL A 200     1293   1616   1331     69    307    -55       N  
ATOM   1541  CA  VAL A 200      33.556   9.866  16.383  1.00 10.61           C  
ANISOU 1541  CA  VAL A 200     1156   1556   1320    136    438      6       C  
ATOM   1542  C   VAL A 200      33.120   9.110  17.617  1.00 10.32           C  
ANISOU 1542  C   VAL A 200     1085   1535   1300      1    297    -35       C  
ATOM   1543  O   VAL A 200      33.715   8.107  18.023  1.00 11.41           O  
ANISOU 1543  O   VAL A 200     1194   1529   1611    111    271     94       O  
ATOM   1544  CB  VAL A 200      34.374  11.132  16.704  1.00 10.87           C  
ANISOU 1544  CB  VAL A 200     1251   1505   1375    120    412     -4       C  
ATOM   1545  CG1 VAL A 200      35.393  10.882  17.774  1.00 12.47           C  
ANISOU 1545  CG1 VAL A 200     1195   1806   1738      5    266    -24       C  
ATOM   1546  CG2 VAL A 200      35.050  11.693  15.427  1.00 12.08           C  
ANISOU 1546  CG2 VAL A 200     1231   1761   1598    -39    539    -22       C  
ATOM   1547  N   GLU A 201      32.069   9.647  18.294  1.00 10.81           N  
ANISOU 1547  N   GLU A 201     1172   1668   1266     55    343    -37       N  
ATOM   1548  CA  GLU A 201      31.630   9.046  19.541  1.00 10.98           C  
ANISOU 1548  CA  GLU A 201     1210   1644   1319    108    321     60       C  
ATOM   1549  C   GLU A 201      31.075   7.656  19.284  1.00 10.83           C  
ANISOU 1549  C   GLU A 201     1140   1640   1335    102    360     46       C  
ATOM   1550  O   GLU A 201      31.356   6.694  20.043  1.00 11.76           O  
ANISOU 1550  O   GLU A 201     1395   1686   1388    148    290    214       O  
ATOM   1551  CB  GLU A 201      30.576   9.938  20.221  1.00 11.86           C  
ANISOU 1551  CB  GLU A 201     1332   1800   1374     70    413   -119       C  
ATOM   1552  CG  GLU A 201      31.138  11.220  20.789  1.00 11.97           C  
ANISOU 1552  CG  GLU A 201     1312   1890   1346     80    338   -117       C  
ATOM   1553  CD  GLU A 201      30.147  12.163  21.463  1.00 12.60           C  
ANISOU 1553  CD  GLU A 201     1170   1955   1663     60    230   -230       C  
ATOM   1554  OE1 GLU A 201      30.586  13.162  22.110  1.00 13.13           O  
ANISOU 1554  OE1 GLU A 201     1168   1891   1932     92     34   -332       O  
ATOM   1555  OE2 GLU A 201      28.924  11.878  21.363  1.00 14.90           O  
ANISOU 1555  OE2 GLU A 201     1226   2056   2380    -45    247   -318       O  
ATOM   1556  N   MET A 202      30.250   7.489  18.252  1.00 11.06           N  
ANISOU 1556  N   MET A 202     1234   1593   1376    116    305    108       N  
ATOM   1557  CA  MET A 202      29.651   6.182  18.000  1.00 12.29           C  
ANISOU 1557  CA  MET A 202     1286   1670   1713     72    332   -149       C  
ATOM   1558  C   MET A 202      30.745   5.157  17.615  1.00 11.25           C  
ANISOU 1558  C   MET A 202     1529   1598   1147     96    296     10       C  
ATOM   1559  O   MET A 202      30.689   4.017  18.095  1.00 11.98           O  
ANISOU 1559  O   MET A 202     1350   1619   1582     -3    265     34       O  
ATOM   1560  CB AMET A 202      28.712   6.392  16.800  0.52 11.19           C  
ANISOU 1560  CB AMET A 202     1161   1407   1684     14    510    -69       C  
ATOM   1561  CB BMET A 202      28.489   6.063  17.110  0.48 15.87           C  
ANISOU 1561  CB BMET A 202     1478   2049   2503   -295     31    204       C  
ATOM   1562  CG AMET A 202      27.455   7.177  17.080  0.52 11.50           C  
ANISOU 1562  CG AMET A 202      995   1338   2038   -129    458    -38       C  
ATOM   1563  CG BMET A 202      27.225   6.721  17.747  0.48 19.22           C  
ANISOU 1563  CG BMET A 202     1332   2586   3384    -10    163    606       C  
ATOM   1564  SD AMET A 202      26.300   6.290  18.087  0.52 16.02           S  
ANISOU 1564  SD AMET A 202     1557   2065   2465   -199    990    -44       S  
ATOM   1565  SD BMET A 202      25.802   6.673  16.590  0.48 23.09           S  
ANISOU 1565  SD BMET A 202     1808   3502   3462   -255   -115   1234       S  
ATOM   1566  CE AMET A 202      25.404   7.585  18.939  0.52 20.61           C  
ANISOU 1566  CE AMET A 202     2363   2472   2997    -40   1540   -271       C  
ATOM   1567  CE BMET A 202      26.505   7.836  15.561  0.48 45.96           C  
ANISOU 1567  CE BMET A 202     2548   7259   7655    421    -98   5839       C  
ATOM   1568  N   ALA A 203      31.697   5.548  16.765  1.00 11.44           N  
ANISOU 1568  N   ALA A 203     1493   1432   1423    191    406     20       N  
ATOM   1569  CA  ALA A 203      32.757   4.616  16.409  1.00 11.82           C  
ANISOU 1569  CA  ALA A 203     1538   1463   1488    226    386     48       C  
ATOM   1570  C   ALA A 203      33.568   4.181  17.604  1.00 11.47           C  
ANISOU 1570  C   ALA A 203     1233   1528   1599     85    404     65       C  
ATOM   1571  O   ALA A 203      33.935   3.010  17.749  1.00 12.59           O  
ANISOU 1571  O   ALA A 203     1588   1563   1632    177    292     43       O  
ATOM   1572  CB  ALA A 203      33.625   5.239  15.286  1.00 13.89           C  
ANISOU 1572  CB  ALA A 203     1894   1641   1743    163    746     67       C  
ATOM   1573  N   GLY A 204      33.896   5.134  18.485  1.00 12.04           N  
ANISOU 1573  N   GLY A 204     1447   1524   1604     86    276     52       N  
ATOM   1574  CA  GLY A 204      34.701   4.816  19.656  1.00 13.82           C  
ANISOU 1574  CA  GLY A 204     1617   1817   1816     -7     90     90       C  
ATOM   1575  C   GLY A 204      33.974   3.895  20.616  1.00 12.10           C  
ANISOU 1575  C   GLY A 204     1572   1609   1415    148     31    -36       C  
ATOM   1576  O   GLY A 204      34.646   3.008  21.186  1.00 13.98           O  
ANISOU 1576  O   GLY A 204     1603   1748   1962    161   -125     37       O  
ATOM   1577  N   ILE A 205      32.659   4.094  20.813  1.00 12.71           N  
ANISOU 1577  N   ILE A 205     1608   1715   1506    194    251   -131       N  
ATOM   1578  CA  ILE A 205      31.886   3.197  21.690  1.00 12.09           C  
ANISOU 1578  CA  ILE A 205     1691   1628   1276    227    167   -113       C  
ATOM   1579  C   ILE A 205      31.816   1.799  21.081  1.00 11.59           C  
ANISOU 1579  C   ILE A 205     1463   1649   1290    151    475    -61       C  
ATOM   1580  O   ILE A 205      32.090   0.810  21.787  1.00 12.55           O  
ANISOU 1580  O   ILE A 205     1590   1609   1571    180    499    124       O  
ATOM   1581  CB  ILE A 205      30.494   3.803  21.943  1.00 13.45           C  
ANISOU 1581  CB  ILE A 205     1857   1898   1357    457    373     -7       C  
ATOM   1582  CG1 ILE A 205      30.560   5.045  22.839  1.00 15.30           C  
ANISOU 1582  CG1 ILE A 205     2438   2177   1199    658    394   -133       C  
ATOM   1583  CG2 ILE A 205      29.582   2.742  22.526  1.00 16.18           C  
ANISOU 1583  CG2 ILE A 205     2077   2314   1756    364    756    169       C  
ATOM   1584  CD1 ILE A 205      29.335   5.921  22.785  1.00 18.44           C  
ANISOU 1584  CD1 ILE A 205     3078   1982   1946   1036   1065    371       C  
ATOM   1585  N   LEU A 206      31.453   1.724  19.807  1.00 11.69           N  
ANISOU 1585  N   LEU A 206     1479   1615   1346     39    453   -100       N  
ATOM   1586  CA  LEU A 206      31.310   0.390  19.205  1.00 11.89           C  
ANISOU 1586  CA  LEU A 206     1521   1549   1448     19    439   -108       C  
ATOM   1587  C   LEU A 206      32.613  -0.363  19.195  1.00 12.51           C  
ANISOU 1587  C   LEU A 206     1604   1647   1503    105    354    -19       C  
ATOM   1588  O   LEU A 206      32.655  -1.588  19.514  1.00 13.61           O  
ANISOU 1588  O   LEU A 206     1814   1594   1763    222    405     -2       O  
ATOM   1589  CB  LEU A 206      30.754   0.527  17.786  1.00 12.89           C  
ANISOU 1589  CB  LEU A 206     1635   1675   1590    120    301   -144       C  
ATOM   1590  CG  LEU A 206      29.253   0.786  17.727  1.00 13.13           C  
ANISOU 1590  CG  LEU A 206     1465   1847   1676    -88    382     42       C  
ATOM   1591  CD1 LEU A 206      28.837   1.312  16.355  1.00 15.46           C  
ANISOU 1591  CD1 LEU A 206     1991   2228   1654    259    146    -66       C  
ATOM   1592  CD2 LEU A 206      28.461  -0.473  18.072  1.00 15.89           C  
ANISOU 1592  CD2 LEU A 206     1816   1987   2235   -297    260    -60       C  
ATOM   1593  N   SER A 207      33.724   0.319  18.907  1.00 11.71           N  
ANISOU 1593  N   SER A 207     1460   1641   1348    167    376    -64       N  
ATOM   1594  CA  SER A 207      35.018  -0.374  18.897  1.00 12.64           C  
ANISOU 1594  CA  SER A 207     1671   1712   1421    239    502     31       C  
ATOM   1595  C   SER A 207      35.447  -0.815  20.276  1.00 12.56           C  
ANISOU 1595  C   SER A 207     1600   1612   1559    225    323    125       C  
ATOM   1596  O   SER A 207      35.935  -1.922  20.508  1.00 13.98           O  
ANISOU 1596  O   SER A 207     1892   1765   1657    453    584    163       O  
ATOM   1597  CB  SER A 207      36.064   0.565  18.264  1.00 13.36           C  
ANISOU 1597  CB  SER A 207     1513   1900   1663    252    491    131       C  
ATOM   1598  OG  SER A 207      37.265  -0.164  18.069  1.00 15.56           O  
ANISOU 1598  OG  SER A 207     1552   2243   2117    304    578    -20       O  
ATOM   1599  N   ALA A 208      35.290   0.076  21.280  1.00 12.34           N  
ANISOU 1599  N   ALA A 208     1560   1655   1475    181    330     60       N  
ATOM   1600  CA  ALA A 208      35.688  -0.266  22.654  1.00 13.35           C  
ANISOU 1600  CA  ALA A 208     1534   1921   1616    342    315    104       C  
ATOM   1601  C   ALA A 208      34.957  -1.496  23.139  1.00 13.45           C  
ANISOU 1601  C   ALA A 208     1800   1820   1492    436    455    123       C  
ATOM   1602  O   ALA A 208      35.478  -2.330  23.874  1.00 16.95           O  
ANISOU 1602  O   ALA A 208     2326   2160   1955    558    325    490       O  
ATOM   1603  CB  ALA A 208      35.455   0.927  23.572  1.00 14.11           C  
ANISOU 1603  CB  ALA A 208     1841   2096   1424    141    359    -21       C  
ATOM   1604  N   LEU A 209      33.668  -1.644  22.738  1.00 13.48           N  
ANISOU 1604  N   LEU A 209     1774   1981   1366    120    524      3       N  
ATOM   1605  CA  LEU A 209      32.810  -2.728  23.208  1.00 14.18           C  
ANISOU 1605  CA  LEU A 209     2072   1735   1582    146    490     76       C  
ATOM   1606  C   LEU A 209      32.965  -3.990  22.410  1.00 15.30           C  
ANISOU 1606  C   LEU A 209     2208   1814   1793    221    439     66       C  
ATOM   1607  O   LEU A 209      32.346  -5.016  22.772  1.00 18.92           O  
ANISOU 1607  O   LEU A 209     3327   1743   2118     71    978      7       O  
ATOM   1608  CB  LEU A 209      31.362  -2.265  23.274  1.00 14.36           C  
ANISOU 1608  CB  LEU A 209     1886   1849   1722   -143    562    -85       C  
ATOM   1609  CG  LEU A 209      31.120  -1.136  24.262  1.00 15.12           C  
ANISOU 1609  CG  LEU A 209     1902   1991   1850   -147    756   -224       C  
ATOM   1610  CD1 LEU A 209      29.675  -0.726  24.148  1.00 17.77           C  
ANISOU 1610  CD1 LEU A 209     2045   1923   2784    172    823    382       C  
ATOM   1611  CD2 LEU A 209      31.435  -1.536  25.689  1.00 16.38           C  
ANISOU 1611  CD2 LEU A 209     2195   2230   1799   -308    709   -140       C  
ATOM   1612  N   GLY A 210      33.820  -3.978  21.393  1.00 14.28           N  
ANISOU 1612  N   GLY A 210     2337   1605   1486    410    374    103       N  
ATOM   1613  CA  GLY A 210      34.269  -5.201  20.685  1.00 15.35           C  
ANISOU 1613  CA  GLY A 210     2131   1834   1869    391    195    -97       C  
ATOM   1614  C   GLY A 210      33.851  -5.301  19.254  1.00 14.51           C  
ANISOU 1614  C   GLY A 210     2093   1760   1659    320    533   -107       C  
ATOM   1615  O   GLY A 210      34.168  -6.344  18.624  1.00 19.06           O  
ANISOU 1615  O   GLY A 210     3394   1968   1882    959    310   -165       O  
ATOM   1616  N   SER A 211      33.142  -4.340  18.680  1.00 13.57           N  
ANISOU 1616  N   SER A 211     1864   1622   1671    185    423     -9       N  
ATOM   1617  CA  SER A 211      32.833  -4.438  17.251  1.00 13.95           C  
ANISOU 1617  CA  SER A 211     1906   1651   1741    300    410   -118       C  
ATOM   1618  C   SER A 211      34.074  -4.169  16.415  1.00 13.01           C  
ANISOU 1618  C   SER A 211     1899   1387   1656    289    399    -92       C  
ATOM   1619  O   SER A 211      34.888  -3.296  16.789  1.00 14.00           O  
ANISOU 1619  O   SER A 211     1917   1720   1681    116    461   -221       O  
ATOM   1620  CB  SER A 211      31.741  -3.420  16.900  1.00 13.56           C  
ANISOU 1620  CB  SER A 211     1833   1561   1758    262    326   -216       C  
ATOM   1621  OG  SER A 211      31.214  -3.675  15.604  1.00 15.00           O  
ANISOU 1621  OG  SER A 211     2135   1961   1605    354    344    -75       O  
ATOM   1622  N   LYS A 212      34.227  -4.864  15.298  1.00 13.68           N  
ANISOU 1622  N   LYS A 212     1919   1573   1705    170    461   -104       N  
ATOM   1623  CA  LYS A 212      35.309  -4.584  14.337  1.00 14.17           C  
ANISOU 1623  CA  LYS A 212     2072   1552   1760    270    627     -9       C  
ATOM   1624  C   LYS A 212      34.856  -3.366  13.521  1.00 12.48           C  
ANISOU 1624  C   LYS A 212     1576   1592   1575    273    538   -140       C  
ATOM   1625  O   LYS A 212      33.934  -3.465  12.720  1.00 13.36           O  
ANISOU 1625  O   LYS A 212     1700   1746   1631     81    454   -275       O  
ATOM   1626  CB ALYS A 212      35.675  -5.739  13.420  0.38 17.74           C  
ANISOU 1626  CB ALYS A 212     2917   1981   1843   1092    523    -90       C  
ATOM   1627  CB BLYS A 212      35.497  -5.779  13.400  0.62 14.29           C  
ANISOU 1627  CB BLYS A 212     1818   1579   2033    487    523    -58       C  
ATOM   1628  CG ALYS A 212      37.032  -5.671  12.743  0.38 20.75           C  
ANISOU 1628  CG ALYS A 212     3493   2276   2113    998   1124    -68       C  
ATOM   1629  CG BLYS A 212      36.537  -5.566  12.306  0.62 17.34           C  
ANISOU 1629  CG BLYS A 212     2134   2225   2231    585    788   -114       C  
ATOM   1630  CD ALYS A 212      38.098  -4.890  13.460  0.38 29.38           C  
ANISOU 1630  CD ALYS A 212     3221   4024   3919    270    577    292       C  
ATOM   1631  CD BLYS A 212      36.859  -6.853  11.566  0.62 24.61           C  
ANISOU 1631  CD BLYS A 212     3374   2969   3008    513   1442   -875       C  
ATOM   1632  CE ALYS A 212      38.595  -5.413  14.782  0.38 40.38           C  
ANISOU 1632  CE ALYS A 212     6449   4583   4309   1299  -1371   -769       C  
ATOM   1633  CE BLYS A 212      37.144  -6.647  10.086  0.62 34.28           C  
ANISOU 1633  CE BLYS A 212     6107   3932   2986   1765   1648   -795       C  
ATOM   1634  NZ ALYS A 212      38.568  -4.450  15.925  0.38 35.48           N  
ANISOU 1634  NZ ALYS A 212     6813   1510   5159    715  -2483    -58       N  
ATOM   1635  NZ BLYS A 212      37.084  -7.937   9.310  0.62 37.47           N  
ANISOU 1635  NZ BLYS A 212     8026   3611   2600   1172   1870   -436       N  
ATOM   1636  N   THR A 213      35.440  -2.225  13.830  1.00 12.53           N  
ANISOU 1636  N   THR A 213     1625   1599   1537    142    502    -27       N  
ATOM   1637  CA  THR A 213      34.846  -0.958  13.463  1.00 12.18           C  
ANISOU 1637  CA  THR A 213     1636   1534   1456    123    380    -55       C  
ATOM   1638  C   THR A 213      35.719  -0.179  12.475  1.00 12.57           C  
ANISOU 1638  C   THR A 213     1551   1701   1524    143    466    -65       C  
ATOM   1639  O   THR A 213      36.948  -0.072  12.681  1.00 14.00           O  
ANISOU 1639  O   THR A 213     1562   1878   1880    151    347    107       O  
ATOM   1640  CB  THR A 213      34.688  -0.125  14.754  1.00 12.83           C  
ANISOU 1640  CB  THR A 213     1754   1654   1467    146    492    -48       C  
ATOM   1641  OG1 THR A 213      33.864  -0.813  15.709  1.00 14.78           O  
ANISOU 1641  OG1 THR A 213     1876   2075   1665      6    693   -118       O  
ATOM   1642  CG2 THR A 213      34.032   1.212  14.484  1.00 14.16           C  
ANISOU 1642  CG2 THR A 213     1975   1728   1677    315    219   -244       C  
ATOM   1643  N   SER A 214      35.079   0.390  11.481  1.00 12.46           N  
ANISOU 1643  N   SER A 214     1581   1514   1640    114    422     48       N  
ATOM   1644  CA  SER A 214      35.676   1.332  10.552  1.00 12.61           C  
ANISOU 1644  CA  SER A 214     1579   1654   1560    168    487    -54       C  
ATOM   1645  C   SER A 214      34.903   2.665  10.621  1.00 11.76           C  
ANISOU 1645  C   SER A 214     1378   1612   1477    138    413     29       C  
ATOM   1646  O   SER A 214      33.676   2.662  10.802  1.00 14.20           O  
ANISOU 1646  O   SER A 214     1355   1871   2171     88    412     97       O  
ATOM   1647  CB  SER A 214      35.613   0.862   9.110  1.00 14.14           C  
ANISOU 1647  CB  SER A 214     1921   1815   1636    147    692   -104       C  
ATOM   1648  OG  SER A 214      36.186  -0.440   8.992  1.00 15.91           O  
ANISOU 1648  OG  SER A 214     2152   1948   1944    295    729   -239       O  
ATOM   1649  N   LEU A 215      35.608   3.761  10.446  1.00 11.88           N  
ANISOU 1649  N   LEU A 215     1190   1650   1675    162    416     35       N  
ATOM   1650  CA  LEU A 215      35.051   5.102  10.391  1.00 11.54           C  
ANISOU 1650  CA  LEU A 215     1124   1644   1617     71    335     57       C  
ATOM   1651  C   LEU A 215      35.453   5.673   9.032  1.00 11.69           C  
ANISOU 1651  C   LEU A 215     1286   1583   1572    164    395    -20       C  
ATOM   1652  O   LEU A 215      36.660   5.831   8.748  1.00 13.24           O  
ANISOU 1652  O   LEU A 215     1320   2140   1571    245    499    104       O  
ATOM   1653  CB  LEU A 215      35.611   5.919  11.533  1.00 12.12           C  
ANISOU 1653  CB  LEU A 215     1261   1829   1514    156    369    -92       C  
ATOM   1654  CG  LEU A 215      35.142   7.367  11.620  1.00 12.72           C  
ANISOU 1654  CG  LEU A 215     1568   1739   1526    152    500      4       C  
ATOM   1655  CD1 LEU A 215      33.644   7.467  11.824  1.00 14.26           C  
ANISOU 1655  CD1 LEU A 215     1481   1894   2043    372    407    191       C  
ATOM   1656  CD2 LEU A 215      35.917   8.121  12.672  1.00 15.70           C  
ANISOU 1656  CD2 LEU A 215     1722   2145   2098    -70    455   -442       C  
ATOM   1657  N   MET A 216      34.469   5.970   8.204  1.00 11.93           N  
ANISOU 1657  N   MET A 216     1339   1719   1473    155    450     28       N  
ATOM   1658  CA  MET A 216      34.707   6.429   6.832  1.00 11.94           C  
ANISOU 1658  CA  MET A 216     1450   1692   1395     50    570   -126       C  
ATOM   1659  C   MET A 216      34.541   7.930   6.730  1.00 11.61           C  
ANISOU 1659  C   MET A 216     1294   1723   1395    102    358     22       C  
ATOM   1660  O   MET A 216      33.447   8.435   6.989  1.00 13.13           O  
ANISOU 1660  O   MET A 216     1272   1782   1933    176    495    164       O  
ATOM   1661  CB  MET A 216      33.727   5.715   5.902  1.00 12.75           C  
ANISOU 1661  CB  MET A 216     1508   1823   1515     26    567   -228       C  
ATOM   1662  CG  MET A 216      34.141   5.890   4.434  1.00 13.89           C  
ANISOU 1662  CG  MET A 216     1751   1984   1543   -154    457   -203       C  
ATOM   1663  SD  MET A 216      32.916   5.288   3.261  1.00 15.18           S  
ANISOU 1663  SD  MET A 216     1942   2270   1556   -159    456   -106       S  
ATOM   1664  CE  MET A 216      32.729   3.612   3.854  1.00 14.30           C  
ANISOU 1664  CE  MET A 216     1769   2001   1662   -109     29   -149       C  
ATOM   1665  N   ILE A 217      35.608   8.604   6.340  1.00 11.50           N  
ANISOU 1665  N   ILE A 217     1354   1795   1219     86    488    -49       N  
ATOM   1666  CA  ILE A 217      35.666  10.066   6.353  1.00 11.98           C  
ANISOU 1666  CA  ILE A 217     1441   1765   1346    -35    503    -27       C  
ATOM   1667  C   ILE A 217      36.071  10.565   4.976  1.00 11.41           C  
ANISOU 1667  C   ILE A 217     1431   1655   1250     -5    475    -75       C  
ATOM   1668  O   ILE A 217      36.829   9.921   4.244  1.00 12.60           O  
ANISOU 1668  O   ILE A 217     1730   1741   1315     65    610   -154       O  
ATOM   1669  CB  ILE A 217      36.623  10.571   7.458  1.00 11.95           C  
ANISOU 1669  CB  ILE A 217     1408   1797   1337     64    497   -159       C  
ATOM   1670  CG1 ILE A 217      38.080  10.210   7.223  1.00 11.77           C  
ANISOU 1670  CG1 ILE A 217     1446   1805   1222   -101    487   -115       C  
ATOM   1671  CG2 ILE A 217      36.164  10.034   8.813  1.00 13.55           C  
ANISOU 1671  CG2 ILE A 217     1340   2346   1464   -139    547    -24       C  
ATOM   1672  CD1 ILE A 217      38.995  10.854   8.221  1.00 13.63           C  
ANISOU 1672  CD1 ILE A 217     1398   2119   1663     52    257   -326       C  
ATOM   1673  N   ARG A 218      35.586  11.754   4.615  1.00 11.99           N  
ANISOU 1673  N   ARG A 218     1633   1897   1025    172    366    -98       N  
ATOM   1674  CA  ARG A 218      35.786  12.309   3.291  1.00 12.24           C  
ANISOU 1674  CA  ARG A 218     1659   1819   1172     42    323     -5       C  
ATOM   1675  C   ARG A 218      37.194  12.862   3.071  1.00 11.80           C  
ANISOU 1675  C   ARG A 218     1645   1667   1171     95    333   -117       C  
ATOM   1676  O   ARG A 218      37.607  12.971   1.902  1.00 12.89           O  
ANISOU 1676  O   ARG A 218     1772   1871   1256    -12    453   -176       O  
ATOM   1677  CB  ARG A 218      34.726  13.368   2.998  1.00 13.46           C  
ANISOU 1677  CB  ARG A 218     1589   1888   1638     57    120     94       C  
ATOM   1678  CG  ARG A 218      33.327  12.836   2.833  1.00 14.40           C  
ANISOU 1678  CG  ARG A 218     1634   2122   1716    -39    342    143       C  
ATOM   1679  CD  ARG A 218      32.311  13.985   2.758  1.00 16.68           C  
ANISOU 1679  CD  ARG A 218     1529   2617   2193    145    435    394       C  
ATOM   1680  NE  ARG A 218      32.421  14.763   1.536  1.00 17.81           N  
ANISOU 1680  NE  ARG A 218     1794   2606   2367    350    184    551       N  
ATOM   1681  CZ  ARG A 218      31.842  14.504   0.366  1.00 23.28           C  
ANISOU 1681  CZ  ARG A 218     3311   2848   2687    386   -616    655       C  
ATOM   1682  NH1 ARG A 218      31.103  13.406   0.250  1.00 23.65           N  
ANISOU 1682  NH1 ARG A 218     2641   3464   2880    293   -343    -36       N  
ATOM   1683  NH2 ARG A 218      31.993  15.275  -0.718  1.00 25.58           N  
ANISOU 1683  NH2 ARG A 218     2867   4193   2660    928     27   1031       N  
ATOM   1684  N   HIS A 219      37.927  13.200   4.113  1.00 12.76           N  
ANISOU 1684  N   HIS A 219     1603   1976   1270   -192    369   -107       N  
ATOM   1685  CA  HIS A 219      39.243  13.792   3.998  1.00 12.87           C  
ANISOU 1685  CA  HIS A 219     1551   1923   1417    -59    440   -162       C  
ATOM   1686  C   HIS A 219      40.212  12.949   4.807  1.00 12.37           C  
ANISOU 1686  C   HIS A 219     1586   2023   1091    -19    528   -335       C  
ATOM   1687  O   HIS A 219      40.063  11.718   4.868  1.00 13.08           O  
ANISOU 1687  O   HIS A 219     1545   2023   1403    -25    471   -169       O  
ATOM   1688  CB  HIS A 219      39.201  15.281   4.369  1.00 13.54           C  
ANISOU 1688  CB  HIS A 219     1791   1962   1393   -274    189    -14       C  
ATOM   1689  CG  HIS A 219      38.270  16.096   3.581  1.00 14.72           C  
ANISOU 1689  CG  HIS A 219     2291   1765   1538    -35    224   -167       C  
ATOM   1690  ND1 HIS A 219      38.648  16.858   2.509  1.00 21.05           N  
ANISOU 1690  ND1 HIS A 219     2891   2947   2160    202    365    821       N  
ATOM   1691  CD2 HIS A 219      36.927  16.228   3.722  1.00 16.27           C  
ANISOU 1691  CD2 HIS A 219     2288   1964   1931    276     68    -12       C  
ATOM   1692  CE1 HIS A 219      37.580  17.485   1.999  1.00 21.27           C  
ANISOU 1692  CE1 HIS A 219     3149   3144   1790    679    416    373       C  
ATOM   1693  NE2 HIS A 219      36.549  17.086   2.730  1.00 19.22           N  
ANISOU 1693  NE2 HIS A 219     2855   2395   2051    322     72    339       N  
ATOM   1694  N   ASP A 220      41.244  13.565   5.395  1.00 12.79           N  
ANISOU 1694  N   ASP A 220     1668   1978   1212    -17    382   -296       N  
ATOM   1695  CA  ASP A 220      42.325  12.849   6.066  1.00 14.43           C  
ANISOU 1695  CA  ASP A 220     1384   2625   1475     39    450   -251       C  
ATOM   1696  C   ASP A 220      42.148  12.711   7.582  1.00 12.41           C  
ANISOU 1696  C   ASP A 220     1263   2071   1380    -24    437   -228       C  
ATOM   1697  O   ASP A 220      42.786  11.847   8.190  1.00 14.74           O  
ANISOU 1697  O   ASP A 220     1602   2407   1594    284    483   -217       O  
ATOM   1698  CB  ASP A 220      43.691  13.559   5.811  1.00 18.82           C  
ANISOU 1698  CB  ASP A 220     1564   4000   1586   -383    675     -2       C  
ATOM   1699  CG  ASP A 220      43.713  15.034   6.202  1.00 22.50           C  
ANISOU 1699  CG  ASP A 220     2593   3870   2084  -1297    481    209       C  
ATOM   1700  OD1 ASP A 220      44.798  15.555   6.542  1.00 28.97           O  
ANISOU 1700  OD1 ASP A 220     3000   5414   2593  -2016    554   -196       O  
ATOM   1701  OD2 ASP A 220      42.651  15.726   6.198  1.00 24.42           O  
ANISOU 1701  OD2 ASP A 220     3323   2971   2986  -1030    102   -168       O  
ATOM   1702  N   LYS A 221      41.315  13.555   8.188  1.00 12.56           N  
ANISOU 1702  N   LYS A 221     1386   2040   1347    170    378   -110       N  
ATOM   1703  CA  LYS A 221      41.188  13.690   9.626  1.00 12.36           C  
ANISOU 1703  CA  LYS A 221     1297   2094   1306     30    436   -215       C  
ATOM   1704  C   LYS A 221      39.738  13.873   9.999  1.00 11.33           C  
ANISOU 1704  C   LYS A 221     1278   1671   1357     41    359   -156       C  
ATOM   1705  O   LYS A 221      38.949  14.432   9.213  1.00 11.75           O  
ANISOU 1705  O   LYS A 221     1458   1758   1247     79    487    -10       O  
ATOM   1706  CB  LYS A 221      42.026  14.854  10.120  1.00 13.80           C  
ANISOU 1706  CB  LYS A 221     1440   2293   1510   -212    523   -331       C  
ATOM   1707  CG  LYS A 221      43.522  14.629   9.994  1.00 14.18           C  
ANISOU 1707  CG  LYS A 221     1442   2374   1571   -135    481   -296       C  
ATOM   1708  CD  LYS A 221      44.378  15.813  10.246  1.00 16.36           C  
ANISOU 1708  CD  LYS A 221     1653   2735   1826   -399    424   -499       C  
ATOM   1709  CE  LYS A 221      45.855  15.504  10.090  1.00 19.78           C  
ANISOU 1709  CE  LYS A 221     1585   3998   1932   -702    839   -658       C  
ATOM   1710  NZ  LYS A 221      46.629  16.741  10.216  1.00 22.23           N  
ANISOU 1710  NZ  LYS A 221     1984   4079   2383   -987    948   -596       N  
ATOM   1711  N   VAL A 222      39.399  13.528  11.229  1.00 11.81           N  
ANISOU 1711  N   VAL A 222     1313   1967   1207     83    379    -57       N  
ATOM   1712  CA  VAL A 222      38.105  13.826  11.819  1.00 11.68           C  
ANISOU 1712  CA  VAL A 222     1154   1948   1334    -68    303   -194       C  
ATOM   1713  C   VAL A 222      38.101  15.220  12.433  1.00 11.20           C  
ANISOU 1713  C   VAL A 222     1188   1915   1152      1    282   -159       C  
ATOM   1714  O   VAL A 222      39.134  15.881  12.646  1.00 12.24           O  
ANISOU 1714  O   VAL A 222     1193   1999   1457   -144    414   -162       O  
ATOM   1715  CB  VAL A 222      37.744  12.778  12.913  1.00 12.40           C  
ANISOU 1715  CB  VAL A 222     1404   1943   1365   -121    547   -269       C  
ATOM   1716  CG1 VAL A 222      37.656  11.408  12.335  1.00 15.76           C  
ANISOU 1716  CG1 VAL A 222     2314   1867   1808   -215    772   -250       C  
ATOM   1717  CG2 VAL A 222      38.670  12.857  14.129  1.00 12.88           C  
ANISOU 1717  CG2 VAL A 222     1289   2072   1532    144    447     78       C  
ATOM   1718  N   LEU A 223      36.899  15.716  12.742  1.00 11.48           N  
ANISOU 1718  N   LEU A 223     1159   1895   1306    -93    323   -171       N  
ATOM   1719  CA  LEU A 223      36.733  16.954  13.534  1.00 11.63           C  
ANISOU 1719  CA  LEU A 223     1264   1773   1382    -39    517    -73       C  
ATOM   1720  C   LEU A 223      37.473  18.115  12.898  1.00 11.91           C  
ANISOU 1720  C   LEU A 223     1287   1811   1429    -11    385    -17       C  
ATOM   1721  O   LEU A 223      38.157  18.901  13.551  1.00 12.91           O  
ANISOU 1721  O   LEU A 223     1471   1711   1721   -105    260     -4       O  
ATOM   1722  CB  LEU A 223      37.130  16.767  15.004  1.00 11.90           C  
ANISOU 1722  CB  LEU A 223     1346   1768   1406    101    460   -129       C  
ATOM   1723  CG  LEU A 223      36.374  15.662  15.754  1.00 12.17           C  
ANISOU 1723  CG  LEU A 223     1299   1790   1534    -61    357    -62       C  
ATOM   1724  CD1 LEU A 223      36.860  15.666  17.211  1.00 13.86           C  
ANISOU 1724  CD1 LEU A 223     1418   2270   1580    -17    386    119       C  
ATOM   1725  CD2 LEU A 223      34.888  15.788  15.688  1.00 13.21           C  
ANISOU 1725  CD2 LEU A 223     1231   2174   1616    198    375    205       C  
ATOM   1726  N   ARG A 224      37.342  18.268  11.579  1.00 12.89           N  
ANISOU 1726  N   ARG A 224     1788   1678   1433    -23    421    119       N  
ATOM   1727  CA  ARG A 224      38.068  19.297  10.854  1.00 14.14           C  
ANISOU 1727  CA  ARG A 224     1997   1809   1565   -162    637     -6       C  
ATOM   1728  C   ARG A 224      37.652  20.706  11.246  1.00 15.02           C  
ANISOU 1728  C   ARG A 224     2330   1735   1643    -99    495    -23       C  
ATOM   1729  O   ARG A 224      38.465  21.616  11.004  1.00 18.36           O  
ANISOU 1729  O   ARG A 224     2870   1868   2238   -331    803    -79       O  
ATOM   1730  CB  ARG A 224      37.944  19.050   9.338  1.00 15.86           C  
ANISOU 1730  CB  ARG A 224     2568   2022   1435      7    628     66       C  
ATOM   1731  CG  ARG A 224      38.683  17.745   8.956  1.00 17.13           C  
ANISOU 1731  CG  ARG A 224     2575   2039   1896   -132    741   -262       C  
ATOM   1732  CD  ARG A 224      38.819  17.528   7.499  1.00 22.91           C  
ANISOU 1732  CD  ARG A 224     3782   2833   2091    209   1282   -447       C  
ATOM   1733  NE  ARG A 224      37.752  18.018   6.716  1.00 33.06           N  
ANISOU 1733  NE  ARG A 224     6637   3953   1970   1235    -32   -457       N  
ATOM   1734  CZ  ARG A 224      37.685  18.829   5.695  1.00 27.82           C  
ANISOU 1734  CZ  ARG A 224     5377   2821   2373    464    535   -560       C  
ATOM   1735  NH1 ARG A 224      36.478  19.073   5.200  1.00 37.44           N  
ANISOU 1735  NH1 ARG A 224     6036   4115   4073    223   -604    759       N  
ATOM   1736  NH2 ARG A 224      38.747  19.403   5.141  1.00 39.27           N  
ANISOU 1736  NH2 ARG A 224     6501   4855   3563  -1227   1335  -1721       N  
ATOM   1737  N   SER A 225      36.484  20.904  11.829  1.00 14.95           N  
ANISOU 1737  N   SER A 225     2207   2016   1457    130    244    -73       N  
ATOM   1738  CA  SER A 225      36.126  22.241  12.287  1.00 15.62           C  
ANISOU 1738  CA  SER A 225     2234   2117   1582    252    169   -119       C  
ATOM   1739  C   SER A 225      36.752  22.615  13.635  1.00 14.84           C  
ANISOU 1739  C   SER A 225     2099   2012   1527    360    152   -187       C  
ATOM   1740  O   SER A 225      36.652  23.767  14.046  1.00 18.23           O  
ANISOU 1740  O   SER A 225     2929   1904   2093    271    -55   -151       O  
ATOM   1741  CB  SER A 225      34.601  22.378  12.440  1.00 18.41           C  
ANISOU 1741  CB  SER A 225     2156   2568   2268    444   -190   -117       C  
ATOM   1742  OG  SER A 225      34.103  21.435  13.395  1.00 22.50           O  
ANISOU 1742  OG  SER A 225     2258   3860   2431    494    604    225       O  
ATOM   1743  N   PHE A 226      37.353  21.639  14.305  1.00 12.80           N  
ANISOU 1743  N   PHE A 226     1584   1773   1505    -11    343   -111       N  
ATOM   1744  CA  PHE A 226      38.025  21.892  15.584  1.00 12.55           C  
ANISOU 1744  CA  PHE A 226     1508   1697   1564    -48    297      6       C  
ATOM   1745  C   PHE A 226      39.439  22.373  15.312  1.00 13.33           C  
ANISOU 1745  C   PHE A 226     1586   1901   1576   -134    348     22       C  
ATOM   1746  O   PHE A 226      39.894  22.435  14.161  1.00 14.55           O  
ANISOU 1746  O   PHE A 226     1659   2225   1645   -238    452     75       O  
ATOM   1747  CB  PHE A 226      38.055  20.625  16.415  1.00 13.17           C  
ANISOU 1747  CB  PHE A 226     1622   1841   1541   -132    337     29       C  
ATOM   1748  CG  PHE A 226      36.716  20.213  17.017  1.00 13.54           C  
ANISOU 1748  CG  PHE A 226     1880   1760   1506   -270    487    -68       C  
ATOM   1749  CD1 PHE A 226      35.619  19.930  16.275  1.00 14.60           C  
ANISOU 1749  CD1 PHE A 226     1653   2245   1647    -90    501   -109       C  
ATOM   1750  CD2 PHE A 226      36.638  20.128  18.425  1.00 15.54           C  
ANISOU 1750  CD2 PHE A 226     2238   2206   1462   -320    488     41       C  
ATOM   1751  CE1 PHE A 226      34.422  19.521  16.848  1.00 15.05           C  
ANISOU 1751  CE1 PHE A 226     1736   2108   1872    -16    682    -22       C  
ATOM   1752  CE2 PHE A 226      35.441  19.749  19.021  1.00 17.77           C  
ANISOU 1752  CE2 PHE A 226     2594   2482   1674   -550    744    -91       C  
ATOM   1753  CZ  PHE A 226      34.324  19.470  18.222  1.00 15.49           C  
ANISOU 1753  CZ  PHE A 226     1998   1966   1920    -28    800    126       C  
ATOM   1754  N   ASP A 227      40.131  22.827  16.366  1.00 13.68           N  
ANISOU 1754  N   ASP A 227     1644   1748   1806   -224    335   -154       N  
ATOM   1755  CA  ASP A 227      41.509  23.243  16.187  1.00 13.66           C  
ANISOU 1755  CA  ASP A 227     1641   1861   1688   -227    287     56       C  
ATOM   1756  C   ASP A 227      42.304  22.132  15.517  1.00 14.03           C  
ANISOU 1756  C   ASP A 227     1537   2015   1777   -160    362    100       C  
ATOM   1757  O   ASP A 227      42.096  20.939  15.834  1.00 14.00           O  
ANISOU 1757  O   ASP A 227     1527   1961   1831    -93    411     72       O  
ATOM   1758  CB  ASP A 227      42.114  23.595  17.552  1.00 13.93           C  
ANISOU 1758  CB  ASP A 227     1539   1978   1776   -155    223     43       C  
ATOM   1759  CG  ASP A 227      43.501  24.188  17.415  1.00 15.04           C  
ANISOU 1759  CG  ASP A 227     1553   2085   2077   -212    224    -67       C  
ATOM   1760  OD1 ASP A 227      43.612  25.434  17.297  1.00 18.94           O  
ANISOU 1760  OD1 ASP A 227     1863   2140   3195   -335    228    141       O  
ATOM   1761  OD2 ASP A 227      44.475  23.447  17.457  1.00 15.78           O  
ANISOU 1761  OD2 ASP A 227     1553   2292   2150   -184    206   -147       O  
ATOM   1762  N   SER A 228      43.250  22.544  14.661  1.00 14.84           N  
ANISOU 1762  N   SER A 228     1583   2142   1913   -243    515     19       N  
ATOM   1763  CA  SER A 228      44.044  21.551  13.975  1.00 16.18           C  
ANISOU 1763  CA  SER A 228     2286   2091   1771   -213    812     90       C  
ATOM   1764  C   SER A 228      44.719  20.514  14.885  1.00 14.84           C  
ANISOU 1764  C   SER A 228     1488   2165   1983   -273    722     27       C  
ATOM   1765  O   SER A 228      44.875  19.365  14.483  1.00 15.41           O  
ANISOU 1765  O   SER A 228     1600   2255   2000   -156    577   -115       O  
ATOM   1766  CB  SER A 228      45.124  22.220  13.094  1.00 19.01           C  
ANISOU 1766  CB  SER A 228     1925   2723   2574     34    994    530       C  
ATOM   1767  OG  SER A 228      46.010  22.978  13.867  1.00 24.65           O  
ANISOU 1767  OG  SER A 228     2100   3508   3758   -493    718    364       O  
ATOM   1768  N   MET A 229      45.175  20.954  16.069  1.00 15.75           N  
ANISOU 1768  N   MET A 229     1772   2083   2129   -361    492    -18       N  
ATOM   1769  CA  MET A 229      45.814  19.998  16.981  1.00 15.79           C  
ANISOU 1769  CA  MET A 229     1642   2030   2330   -329    170   -197       C  
ATOM   1770  C   MET A 229      44.864  18.880  17.426  1.00 14.36           C  
ANISOU 1770  C   MET A 229     1583   1918   1955   -167     71    -97       C  
ATOM   1771  O   MET A 229      45.268  17.707  17.542  1.00 16.13           O  
ANISOU 1771  O   MET A 229     1960   1978   2191    -86    285    -46       O  
ATOM   1772  CB  MET A 229      46.330  20.713  18.268  1.00 16.99           C  
ANISOU 1772  CB  MET A 229     1775   1917   2765   -139   -106   -384       C  
ATOM   1773  CG  MET A 229      46.858  19.711  19.385  1.00 23.54           C  
ANISOU 1773  CG  MET A 229     2883   2553   3506   1354  -1465  -1006       C  
ATOM   1774  SD  MET A 229      47.223  20.695  20.891  1.00 21.60           S  
ANISOU 1774  SD  MET A 229     3012   2414   2780     -2   -425   -162       S  
ATOM   1775  CE  MET A 229      45.507  20.708  21.486  1.00 23.93           C  
ANISOU 1775  CE  MET A 229     3431   2892   2767  -1226    193   -183       C  
ATOM   1776  N   ILE A 230      43.608  19.252  17.687  1.00 13.90           N  
ANISOU 1776  N   ILE A 230     1581   1742   1958   -251    147   -113       N  
ATOM   1777  CA  ILE A 230      42.585  18.303  18.082  1.00 14.09           C  
ANISOU 1777  CA  ILE A 230     1861   1798   1694   -218    509   -163       C  
ATOM   1778  C   ILE A 230      42.218  17.389  16.915  1.00 12.61           C  
ANISOU 1778  C   ILE A 230     1241   1713   1836    -84    380   -140       C  
ATOM   1779  O   ILE A 230      42.078  16.175  17.099  1.00 13.32           O  
ANISOU 1779  O   ILE A 230     1413   1825   1824   -205    621   -195       O  
ATOM   1780  CB AILE A 230      41.288  19.043  18.514  0.28 16.17           C  
ANISOU 1780  CB AILE A 230     2049   2473   1623     19    746   -197       C  
ATOM   1781  CB BILE A 230      41.366  19.046  18.681  0.71 13.98           C  
ANISOU 1781  CB BILE A 230     2125   1744   1442   -118    670     82       C  
ATOM   1782  CG1AILE A 230      41.283  19.756  19.872  0.28 15.73           C  
ANISOU 1782  CG1AILE A 230     2237   2146   1595    204    478    -85       C  
ATOM   1783  CG1BILE A 230      41.808  19.849  19.921  0.71 15.96           C  
ANISOU 1783  CG1BILE A 230     2452   1978   1633    -27    466   -161       C  
ATOM   1784  CG2AILE A 230      40.106  18.069  18.440  0.28 14.29           C  
ANISOU 1784  CG2AILE A 230     1888   2050   1493    308   1227   -475       C  
ATOM   1785  CG2BILE A 230      40.175  18.140  18.972  0.71 14.83           C  
ANISOU 1785  CG2BILE A 230     1992   2175   1467   -167    745     76       C  
ATOM   1786  CD1AILE A 230      39.983  20.506  20.176  0.28 13.89           C  
ANISOU 1786  CD1AILE A 230     1797   1476   2004   -527    898   -103       C  
ATOM   1787  CD1BILE A 230      42.342  18.976  21.037  0.71 17.12           C  
ANISOU 1787  CD1BILE A 230     2486   2247   1771   -293    121    -66       C  
ATOM   1788  N   SER A 231      42.022  17.975  15.731  1.00 12.89           N  
ANISOU 1788  N   SER A 231     1255   1912   1732    -34    350   -140       N  
ATOM   1789  CA  SER A 231      41.716  17.131  14.593  1.00 12.88           C  
ANISOU 1789  CA  SER A 231     1324   1944   1628    -62    618    -27       C  
ATOM   1790  C   SER A 231      42.777  16.066  14.369  1.00 12.89           C  
ANISOU 1790  C   SER A 231     1293   2074   1531   -154    419   -251       C  
ATOM   1791  O   SER A 231      42.472  14.876  14.159  1.00 13.62           O  
ANISOU 1791  O   SER A 231     1410   2042   1721    -40    440   -360       O  
ATOM   1792  CB  SER A 231      41.496  18.061  13.372  1.00 14.23           C  
ANISOU 1792  CB  SER A 231     1594   2288   1526   -189    556     34       C  
ATOM   1793  OG  SER A 231      41.324  17.341  12.189  1.00 14.82           O  
ANISOU 1793  OG  SER A 231     1583   2298   1749   -149    458   -118       O  
ATOM   1794  N   THR A 232      44.053  16.468  14.398  1.00 12.81           N  
ANISOU 1794  N   THR A 232     1312   2203   1353   -134    436     47       N  
ATOM   1795  CA  THR A 232      45.151  15.511  14.238  1.00 13.06           C  
ANISOU 1795  CA  THR A 232     1271   2267   1422   -121    468   -206       C  
ATOM   1796  C   THR A 232      45.163  14.468  15.368  1.00 12.85           C  
ANISOU 1796  C   THR A 232     1246   2121   1517    -54    361   -198       C  
ATOM   1797  O   THR A 232      45.233  13.256  15.115  1.00 13.86           O  
ANISOU 1797  O   THR A 232     1348   2099   1818     54    518   -325       O  
ATOM   1798  CB  THR A 232      46.461  16.268  14.205  1.00 13.97           C  
ANISOU 1798  CB  THR A 232     1310   2342   1654   -161    490    -92       C  
ATOM   1799  OG1 THR A 232      46.461  17.144  13.073  1.00 15.62           O  
ANISOU 1799  OG1 THR A 232     1460   2708   1768   -243    617     41       O  
ATOM   1800  CG2 THR A 232      47.625  15.274  14.098  1.00 16.82           C  
ANISOU 1800  CG2 THR A 232     1230   2700   2461    -91    509   -151       C  
ATOM   1801  N   ASN A 233      45.122  14.936  16.612  1.00 12.24           N  
ANISOU 1801  N   ASN A 233     1223   1965   1463    -36    282   -145       N  
ATOM   1802  CA  ASN A 233      45.253  14.034  17.746  1.00 12.21           C  
ANISOU 1802  CA  ASN A 233     1140   2039   1461     29    266   -200       C  
ATOM   1803  C   ASN A 233      44.104  13.057  17.803  1.00 12.24           C  
ANISOU 1803  C   ASN A 233     1215   1987   1449     -2    391   -139       C  
ATOM   1804  O   ASN A 233      44.305  11.869  18.117  1.00 13.27           O  
ANISOU 1804  O   ASN A 233     1405   2024   1615    -48    164    -63       O  
ATOM   1805  CB  ASN A 233      45.374  14.840  19.032  1.00 12.81           C  
ANISOU 1805  CB  ASN A 233     1234   2237   1398   -141    243   -237       C  
ATOM   1806  CG  ASN A 233      45.769  13.937  20.151  1.00 12.70           C  
ANISOU 1806  CG  ASN A 233     1005   2330   1491   -128    191   -155       C  
ATOM   1807  OD1 ASN A 233      46.928  13.535  20.235  1.00 16.16           O  
ANISOU 1807  OD1 ASN A 233     1221   3109   1810    204    212    -77       O  
ATOM   1808  ND2 ASN A 233      44.836  13.647  21.037  1.00 14.16           N  
ANISOU 1808  ND2 ASN A 233     1317   2491   1572     39    371     49       N  
ATOM   1809  N   CYS A 234      42.891  13.522  17.567  1.00 11.68           N  
ANISOU 1809  N   CYS A 234     1193   1905   1341     -3    316   -154       N  
ATOM   1810  CA  CYS A 234      41.705  12.637  17.657  1.00 12.02           C  
ANISOU 1810  CA  CYS A 234     1299   1973   1296    -87    247   -107       C  
ATOM   1811  C   CYS A 234      41.792  11.533  16.617  1.00 11.63           C  
ANISOU 1811  C   CYS A 234     1293   1917   1211    -23    296    -18       C  
ATOM   1812  O   CYS A 234      41.453  10.357  16.889  1.00 12.66           O  
ANISOU 1812  O   CYS A 234     1334   1877   1598    -42    319    -80       O  
ATOM   1813  CB  CYS A 234      40.440  13.452  17.554  1.00 12.55           C  
ANISOU 1813  CB  CYS A 234     1195   1941   1632   -163    329   -189       C  
ATOM   1814  SG  CYS A 234      38.930  12.510  17.794  1.00 15.91           S  
ANISOU 1814  SG  CYS A 234     1353   2321   2370   -244    736   -535       S  
ATOM   1815  N   THR A 235      42.231  11.870  15.428  1.00 11.90           N  
ANISOU 1815  N   THR A 235     1337   1874   1311     22    384   -110       N  
ATOM   1816  CA  THR A 235      42.387  10.872  14.386  1.00 11.91           C  
ANISOU 1816  CA  THR A 235     1206   2014   1304    -22    308   -152       C  
ATOM   1817  C   THR A 235      43.402   9.811  14.773  1.00 12.64           C  
ANISOU 1817  C   THR A 235     1335   2016   1453     92    384   -215       C  
ATOM   1818  O   THR A 235      43.187   8.608  14.610  1.00 13.99           O  
ANISOU 1818  O   THR A 235     1397   2129   1788    166    420   -298       O  
ATOM   1819  CB  THR A 235      42.767  11.556  13.051  1.00 12.70           C  
ANISOU 1819  CB  THR A 235     1351   2141   1334    139    369   -229       C  
ATOM   1820  OG1 THR A 235      41.881  12.611  12.714  1.00 12.82           O  
ANISOU 1820  OG1 THR A 235     1351   2168   1351    107    442    -36       O  
ATOM   1821  CG2 THR A 235      42.731  10.562  11.886  1.00 14.28           C  
ANISOU 1821  CG2 THR A 235     1886   2180   1359     13    496   -290       C  
ATOM   1822  N   GLU A 236      44.555  10.245  15.291  1.00 13.22           N  
ANISOU 1822  N   GLU A 236     1250   2130   1641    193    351    -76       N  
ATOM   1823  CA  GLU A 236      45.577   9.345  15.732  1.00 13.78           C  
ANISOU 1823  CA  GLU A 236     1339   2122   1773    325    361   -190       C  
ATOM   1824  C   GLU A 236      45.079   8.447  16.873  1.00 13.86           C  
ANISOU 1824  C   GLU A 236     1363   2092   1811    380    193    -60       C  
ATOM   1825  O   GLU A 236      45.368   7.237  16.891  1.00 15.04           O  
ANISOU 1825  O   GLU A 236     1578   2127   2009    298    330    -53       O  
ATOM   1826  CB  GLU A 236      46.826  10.135  16.214  1.00 15.98           C  
ANISOU 1826  CB  GLU A 236     1202   2396   2475    301    272   -164       C  
ATOM   1827  CG  GLU A 236      47.550  10.853  15.087  1.00 19.13           C  
ANISOU 1827  CG  GLU A 236     1350   2930   2989    160    643    -75       C  
ATOM   1828  CD  GLU A 236      48.644  11.821  15.475  1.00 23.35           C  
ANISOU 1828  CD  GLU A 236     1401   4342   3129   -486    420     87       C  
ATOM   1829  OE1 GLU A 236      49.388  12.263  14.566  1.00 26.97           O  
ANISOU 1829  OE1 GLU A 236     1711   4500   4037   -343    667    913       O  
ATOM   1830  OE2 GLU A 236      48.757  12.162  16.671  1.00 32.57           O  
ANISOU 1830  OE2 GLU A 236     3646   5422   3307  -1387   -274   -112       O  
ATOM   1831  N   GLU A 237      44.352   8.999  17.851  1.00 13.61           N  
ANISOU 1831  N   GLU A 237     1457   1958   1755    228    218    -51       N  
ATOM   1832  CA  GLU A 237      43.865   8.227  18.966  1.00 14.58           C  
ANISOU 1832  CA  GLU A 237     1582   2205   1751    139    214    142       C  
ATOM   1833  C   GLU A 237      42.848   7.169  18.523  1.00 13.47           C  
ANISOU 1833  C   GLU A 237     1411   2256   1449    252    377     98       C  
ATOM   1834  O   GLU A 237      42.870   6.057  19.023  1.00 14.95           O  
ANISOU 1834  O   GLU A 237     1628   2190   1863     74    111    162       O  
ATOM   1835  CB  GLU A 237      43.323   9.122  20.058  1.00 17.66           C  
ANISOU 1835  CB  GLU A 237     1989   2689   2034   -175    443   -269       C  
ATOM   1836  CG  GLU A 237      44.366   9.842  20.911  1.00 19.49           C  
ANISOU 1836  CG  GLU A 237     1980   3212   2215    122    -48   -413       C  
ATOM   1837  CD  GLU A 237      45.118   9.027  21.942  1.00 21.00           C  
ANISOU 1837  CD  GLU A 237     2200   3588   2192    124    292     88       C  
ATOM   1838  OE1 GLU A 237      45.817   9.642  22.784  1.00 23.03           O  
ANISOU 1838  OE1 GLU A 237     2414   3909   2430    493   -302     19       O  
ATOM   1839  OE2 GLU A 237      45.103   7.741  21.995  1.00 38.84           O  
ANISOU 1839  OE2 GLU A 237     6414   3651   4694   -349  -2155    766       O  
ATOM   1840  N   LEU A 238      41.981   7.511  17.558  1.00 13.43           N  
ANISOU 1840  N   LEU A 238     1468   1944   1691    266    318     -7       N  
ATOM   1841  CA  LEU A 238      41.062   6.540  17.002  1.00 12.49           C  
ANISOU 1841  CA  LEU A 238     1326   1820   1601    189    429    113       C  
ATOM   1842  C   LEU A 238      41.829   5.347  16.425  1.00 13.67           C  
ANISOU 1842  C   LEU A 238     1339   2065   1788    326    321    -58       C  
ATOM   1843  O   LEU A 238      41.535   4.173  16.704  1.00 13.88           O  
ANISOU 1843  O   LEU A 238     1579   1930   1763    275    125    -76       O  
ATOM   1844  CB  LEU A 238      40.196   7.142  15.905  1.00 12.91           C  
ANISOU 1844  CB  LEU A 238     1302   1886   1719    242    372      9       C  
ATOM   1845  CG  LEU A 238      39.016   7.990  16.440  1.00 13.34           C  
ANISOU 1845  CG  LEU A 238     1385   1995   1691    287    326   -299       C  
ATOM   1846  CD1 LEU A 238      38.578   8.978  15.370  1.00 14.34           C  
ANISOU 1846  CD1 LEU A 238     1417   2112   1921    448    139   -268       C  
ATOM   1847  CD2 LEU A 238      37.874   7.099  16.901  1.00 15.35           C  
ANISOU 1847  CD2 LEU A 238     1382   2377   2073    254    507   -277       C  
ATOM   1848  N   GLU A 239      42.828   5.663  15.596  1.00 13.38           N  
ANISOU 1848  N   GLU A 239     1368   1996   1720    324    397   -225       N  
ATOM   1849  CA  GLU A 239      43.613   4.589  15.001  1.00 15.02           C  
ANISOU 1849  CA  GLU A 239     1388   2107   2212    473    362   -370       C  
ATOM   1850  C   GLU A 239      44.354   3.742  16.048  1.00 16.89           C  
ANISOU 1850  C   GLU A 239     1360   2259   2797    527    210   -161       C  
ATOM   1851  O   GLU A 239      44.404   2.513  15.998  1.00 19.13           O  
ANISOU 1851  O   GLU A 239     1721   2228   3319    549     98     41       O  
ATOM   1852  CB  GLU A 239      44.600   5.204  13.986  1.00 17.07           C  
ANISOU 1852  CB  GLU A 239     1572   2523   2390    576    659   -439       C  
ATOM   1853  CG  GLU A 239      43.864   5.812  12.797  1.00 22.01           C  
ANISOU 1853  CG  GLU A 239     2598   3162   2602   1205    784    236       C  
ATOM   1854  CD  GLU A 239      44.497   6.242  11.523  1.00 25.55           C  
ANISOU 1854  CD  GLU A 239     3133   3666   2909    982   1403    218       C  
ATOM   1855  OE1 GLU A 239      44.623   5.421  10.560  1.00 34.25           O  
ANISOU 1855  OE1 GLU A 239     4126   5431   3458    265   1651   -928       O  
ATOM   1856  OE2 GLU A 239      44.898   7.389  11.252  1.00 31.78           O  
ANISOU 1856  OE2 GLU A 239     3377   4164   4535    414   1879    534       O  
ATOM   1857  N   ASN A 240      44.938   4.392  17.057  1.00 16.57           N  
ANISOU 1857  N   ASN A 240     1598   2329   2371    551    230    127       N  
ATOM   1858  CA  ASN A 240      45.657   3.668  18.090  1.00 19.53           C  
ANISOU 1858  CA  ASN A 240     1555   2661   3204    648   -159    353       C  
ATOM   1859  C   ASN A 240      44.693   2.794  18.898  1.00 18.54           C  
ANISOU 1859  C   ASN A 240     2046   2752   2247    523   -423    389       C  
ATOM   1860  O   ASN A 240      45.132   1.793  19.454  1.00 23.66           O  
ANISOU 1860  O   ASN A 240     2332   3293   3366    733   -129   1000       O  
ATOM   1861  CB  ASN A 240      46.340   4.642  19.029  1.00 21.69           C  
ANISOU 1861  CB  ASN A 240     1906   3193   3143    375   -519    565       C  
ATOM   1862  CG  ASN A 240      47.515   5.360  18.426  1.00 24.68           C  
ANISOU 1862  CG  ASN A 240     1761   3958   3659     87   -250     57       C  
ATOM   1863  OD1 ASN A 240      47.967   5.025  17.307  1.00 30.62           O  
ANISOU 1863  OD1 ASN A 240     2293   5240   4101   -117    325   -370       O  
ATOM   1864  ND2 ASN A 240      47.990   6.383  19.147  1.00 31.82           N  
ANISOU 1864  ND2 ASN A 240     3304   4852   3933  -1006   -557    -54       N  
ATOM   1865  N   ALA A 241      43.411   3.122  18.978  1.00 18.32           N  
ANISOU 1865  N   ALA A 241     1987   2668   2306    132   -178    619       N  
ATOM   1866  CA  ALA A 241      42.490   2.277  19.683  1.00 20.25           C  
ANISOU 1866  CA  ALA A 241     2502   2632   2561    -66   -184    734       C  
ATOM   1867  C   ALA A 241      41.909   1.171  18.799  1.00 19.70           C  
ANISOU 1867  C   ALA A 241     2122   2318   3043    259     65    450       C  
ATOM   1868  O   ALA A 241      41.044   0.419  19.275  1.00 25.09           O  
ANISOU 1868  O   ALA A 241     2952   2624   3957   -276    764    283       O  
ATOM   1869  CB  ALA A 241      41.338   3.123  20.184  1.00 21.65           C  
ANISOU 1869  CB  ALA A 241     2830   3246   2148   -453    471   -158       C  
ATOM   1870  N   GLY A 242      42.317   1.068  17.558  1.00 19.64           N  
ANISOU 1870  N   GLY A 242     2379   2428   2656    110   -457    624       N  
ATOM   1871  CA  GLY A 242      41.779  -0.024  16.761  1.00 19.12           C  
ANISOU 1871  CA  GLY A 242     2145   2158   2963    206   -322    561       C  
ATOM   1872  C   GLY A 242      40.632   0.343  15.845  1.00 16.03           C  
ANISOU 1872  C   GLY A 242     1910   1919   2261    139     39    412       C  
ATOM   1873  O   GLY A 242      40.118  -0.574  15.212  1.00 16.78           O  
ANISOU 1873  O   GLY A 242     1797   1957   2621    150    242     82       O  
ATOM   1874  N   VAL A 243      40.206   1.586  15.753  1.00 14.59           N  
ANISOU 1874  N   VAL A 243     1673   1994   1876    289    206    105       N  
ATOM   1875  CA  VAL A 243      39.235   2.005  14.747  1.00 13.68           C  
ANISOU 1875  CA  VAL A 243     1428   1953   1816    224    437    266       C  
ATOM   1876  C   VAL A 243      39.994   2.173  13.438  1.00 13.61           C  
ANISOU 1876  C   VAL A 243     1383   1980   1808    145    314    153       C  
ATOM   1877  O   VAL A 243      41.002   2.880  13.375  1.00 16.43           O  
ANISOU 1877  O   VAL A 243     1516   2656   2071    -90    464    277       O  
ATOM   1878  CB  VAL A 243      38.557   3.300  15.172  1.00 14.22           C  
ANISOU 1878  CB  VAL A 243     1628   1899   1878    179    457    215       C  
ATOM   1879  CG1 VAL A 243      37.600   3.808  14.082  1.00 14.14           C  
ANISOU 1879  CG1 VAL A 243     1510   1787   2076    163    302    168       C  
ATOM   1880  CG2 VAL A 243      37.785   3.152  16.498  1.00 15.18           C  
ANISOU 1880  CG2 VAL A 243     1801   2135   1830    -83    552   -147       C  
ATOM   1881  N   GLU A 244      39.518   1.489  12.404  1.00 14.43           N  
ANISOU 1881  N   GLU A 244     1708   1910   1867    247    474    107       N  
ATOM   1882  CA  GLU A 244      40.077   1.654  11.061  1.00 14.99           C  
ANISOU 1882  CA  GLU A 244     1721   2147   1829    413    501    131       C  
ATOM   1883  C   GLU A 244      39.535   2.924  10.466  1.00 13.83           C  
ANISOU 1883  C   GLU A 244     1442   2097   1714    280    579     93       C  
ATOM   1884  O   GLU A 244      38.320   2.972  10.164  1.00 16.53           O  
ANISOU 1884  O   GLU A 244     1372   2203   2706    199    419    201       O  
ATOM   1885  CB  GLU A 244      39.740   0.443  10.181  1.00 16.55           C  
ANISOU 1885  CB  GLU A 244     2097   2197   1995    613    497     33       C  
ATOM   1886  CG  GLU A 244      40.283   0.555   8.788  1.00 18.89           C  
ANISOU 1886  CG  GLU A 244     2137   2955   2084    712    764   -222       C  
ATOM   1887  CD  GLU A 244      39.808  -0.568   7.898  1.00 20.20           C  
ANISOU 1887  CD  GLU A 244     2708   2673   2292    376   1023   -232       C  
ATOM   1888  OE1 GLU A 244      38.636  -1.009   7.998  1.00 21.75           O  
ANISOU 1888  OE1 GLU A 244     2576   2955   2735    421   1008   -284       O  
ATOM   1889  OE2 GLU A 244      40.624  -0.990   7.051  1.00 25.32           O  
ANISOU 1889  OE2 GLU A 244     2512   3675   3432    566   1017  -1171       O  
ATOM   1890  N   VAL A 245      40.365   3.954  10.266  1.00 13.73           N  
ANISOU 1890  N   VAL A 245     1409   2195   1613    146    357    -26       N  
ATOM   1891  CA  VAL A 245      39.890   5.196   9.682  1.00 13.17           C  
ANISOU 1891  CA  VAL A 245     1424   2111   1468    103    411    -25       C  
ATOM   1892  C   VAL A 245      40.150   5.156   8.175  1.00 13.93           C  
ANISOU 1892  C   VAL A 245     1406   2342   1546     58    583    -85       C  
ATOM   1893  O   VAL A 245      41.291   5.098   7.722  1.00 16.15           O  
ANISOU 1893  O   VAL A 245     1455   2948   1732    186    641   -103       O  
ATOM   1894  CB  VAL A 245      40.580   6.434  10.317  1.00 13.44           C  
ANISOU 1894  CB  VAL A 245     1247   2182   1679    117    492   -114       C  
ATOM   1895  CG1 VAL A 245      40.089   7.727   9.655  1.00 14.54           C  
ANISOU 1895  CG1 VAL A 245     1468   2126   1932     -8    388    -83       C  
ATOM   1896  CG2 VAL A 245      40.312   6.407  11.818  1.00 14.88           C  
ANISOU 1896  CG2 VAL A 245     1655   2357   1643     68    441   -261       C  
ATOM   1897  N   LEU A 246      39.050   5.118   7.430  1.00 13.00           N  
ANISOU 1897  N   LEU A 246     1530   1935   1476    185    526    -60       N  
ATOM   1898  CA  LEU A 246      39.063   5.000   5.963  1.00 12.93           C  
ANISOU 1898  CA  LEU A 246     1647   1745   1522    235    569   -123       C  
ATOM   1899  C   LEU A 246      39.031   6.415   5.395  1.00 13.26           C  
ANISOU 1899  C   LEU A 246     1540   1927   1572    215    556     71       C  
ATOM   1900  O   LEU A 246      37.969   7.080   5.361  1.00 13.03           O  
ANISOU 1900  O   LEU A 246     1527   1829   1593    209    538     74       O  
ATOM   1901  CB  LEU A 246      37.878   4.178   5.491  1.00 13.74           C  
ANISOU 1901  CB  LEU A 246     1730   1972   1520    138    534    -72       C  
ATOM   1902  CG  LEU A 246      37.839   2.729   6.010  1.00 15.52           C  
ANISOU 1902  CG  LEU A 246     2271   1916   1708    -70    430    -85       C  
ATOM   1903  CD1 LEU A 246      36.492   2.110   5.683  1.00 17.54           C  
ANISOU 1903  CD1 LEU A 246     2421   2367   1876   -396    669   -176       C  
ATOM   1904  CD2 LEU A 246      38.988   1.905   5.417  1.00 17.90           C  
ANISOU 1904  CD2 LEU A 246     2500   1805   2496    185    542     53       C  
ATOM   1905  N   LYS A 247      40.184   6.917   5.019  1.00 12.87           N  
ANISOU 1905  N   LYS A 247     1560   1937   1391    200    664      6       N  
ATOM   1906  CA  LYS A 247      40.375   8.318   4.617  1.00 13.22           C  
ANISOU 1906  CA  LYS A 247     1666   1950   1408     75    581    -94       C  
ATOM   1907  C   LYS A 247      40.010   8.513   3.156  1.00 11.87           C  
ANISOU 1907  C   LYS A 247     1423   1769   1317    191    638   -179       C  
ATOM   1908  O   LYS A 247      40.137   7.630   2.312  1.00 12.94           O  
ANISOU 1908  O   LYS A 247     1630   1770   1516     59    631   -314       O  
ATOM   1909  CB  LYS A 247      41.819   8.727   4.890  1.00 13.98           C  
ANISOU 1909  CB  LYS A 247     1611   2116   1582     60    530   -149       C  
ATOM   1910  CG  LYS A 247      42.118   8.615   6.409  1.00 15.47           C  
ANISOU 1910  CG  LYS A 247     1715   2565   1597    174    461     48       C  
ATOM   1911  CD  LYS A 247      43.593   8.804   6.742  1.00 16.13           C  
ANISOU 1911  CD  LYS A 247     1670   2693   1765    205    536   -344       C  
ATOM   1912  CE  LYS A 247      43.781   8.461   8.214  1.00 19.06           C  
ANISOU 1912  CE  LYS A 247     1894   3446   1902    385    303   -118       C  
ATOM   1913  NZ  LYS A 247      45.205   8.644   8.661  1.00 26.10           N  
ANISOU 1913  NZ  LYS A 247     1811   5430   2675    940     35   -455       N  
ATOM   1914  N   PHE A 248      39.565   9.719   2.833  1.00 11.90           N  
ANISOU 1914  N   PHE A 248     1522   1712   1289     48    586   -218       N  
ATOM   1915  CA  PHE A 248      39.224  10.109   1.483  1.00 12.72           C  
ANISOU 1915  CA  PHE A 248     1739   1788   1306   -127    564    -38       C  
ATOM   1916  C   PHE A 248      38.262   9.117   0.830  1.00 12.04           C  
ANISOU 1916  C   PHE A 248     1523   1672   1380    127    527   -209       C  
ATOM   1917  O   PHE A 248      38.411   8.719  -0.328  1.00 13.24           O  
ANISOU 1917  O   PHE A 248     1757   1980   1294      1    676   -249       O  
ATOM   1918  CB  PHE A 248      40.471  10.323   0.589  1.00 13.82           C  
ANISOU 1918  CB  PHE A 248     1788   1987   1474   -246    682   -220       C  
ATOM   1919  CG  PHE A 248      41.286  11.526   1.061  1.00 14.15           C  
ANISOU 1919  CG  PHE A 248     1993   2000   1383   -337    818   -431       C  
ATOM   1920  CD1 PHE A 248      42.412  11.330   1.808  1.00 16.06           C  
ANISOU 1920  CD1 PHE A 248     2098   2708   1297   -569    739   -326       C  
ATOM   1921  CD2 PHE A 248      40.887  12.809   0.675  1.00 16.38           C  
ANISOU 1921  CD2 PHE A 248     2501   1991   1731   -451    958   -261       C  
ATOM   1922  CE1 PHE A 248      43.165  12.445   2.260  1.00 19.60           C  
ANISOU 1922  CE1 PHE A 248     2524   3184   1738   -972    586   -496       C  
ATOM   1923  CE2 PHE A 248      41.599  13.923   1.122  1.00 18.41           C  
ANISOU 1923  CE2 PHE A 248     3079   2040   1876   -589   1243   -513       C  
ATOM   1924  CZ  PHE A 248      42.705  13.702   1.901  1.00 19.64           C  
ANISOU 1924  CZ  PHE A 248     2762   2904   1796  -1110   1289   -674       C  
ATOM   1925  N   SER A 249      37.257   8.670   1.631  1.00 12.62           N  
ANISOU 1925  N   SER A 249     1432   1935   1426     13    503   -220       N  
ATOM   1926  CA  SER A 249      36.419   7.560   1.242  1.00 12.60           C  
ANISOU 1926  CA  SER A 249     1545   1927   1315     11    446   -341       C  
ATOM   1927  C   SER A 249      34.927   7.924   1.357  1.00 12.67           C  
ANISOU 1927  C   SER A 249     1533   1716   1564    -40    507   -348       C  
ATOM   1928  O   SER A 249      34.527   8.601   2.315  1.00 14.49           O  
ANISOU 1928  O   SER A 249     1708   2289   1510    143    577   -371       O  
ATOM   1929  CB  SER A 249      36.780   6.361   2.114  1.00 13.29           C  
ANISOU 1929  CB  SER A 249     1559   1953   1536     16    522   -238       C  
ATOM   1930  OG  SER A 249      38.057   5.842   1.773  1.00 13.87           O  
ANISOU 1930  OG  SER A 249     1707   1990   1571     89    636   -210       O  
ATOM   1931  N   GLN A 250      34.125   7.450   0.439  1.00 12.84           N  
ANISOU 1931  N   GLN A 250     1588   1768   1523   -133    476   -186       N  
ATOM   1932  CA  GLN A 250      32.693   7.733   0.314  1.00 14.07           C  
ANISOU 1932  CA  GLN A 250     1571   1842   1932    -14    520   -265       C  
ATOM   1933  C   GLN A 250      31.938   6.484  -0.101  1.00 13.44           C  
ANISOU 1933  C   GLN A 250     1552   1893   1663    -40    553   -329       C  
ATOM   1934  O   GLN A 250      32.470   5.639  -0.855  1.00 16.15           O  
ANISOU 1934  O   GLN A 250     1790   2188   2158    -66    801   -619       O  
ATOM   1935  CB  GLN A 250      32.429   8.832  -0.726  1.00 18.00           C  
ANISOU 1935  CB  GLN A 250     1794   1928   3115    -65     79    211       C  
ATOM   1936  CG  GLN A 250      33.059  10.147  -0.425  1.00 16.15           C  
ANISOU 1936  CG  GLN A 250     2054   1826   2258    126     36   -119       C  
ATOM   1937  CD  GLN A 250      32.994  11.193  -1.499  1.00 20.20           C  
ANISOU 1937  CD  GLN A 250     2604   1946   3125     78   -173    449       C  
ATOM   1938  OE1 GLN A 250      33.929  12.040  -1.622  1.00 22.59           O  
ANISOU 1938  OE1 GLN A 250     3086   2551   2947   -358    535    294       O  
ATOM   1939  NE2 GLN A 250      31.880  11.227  -2.180  1.00 25.24           N  
ANISOU 1939  NE2 GLN A 250     3607   2642   3340   -283   -943    986       N  
ATOM   1940  N   VAL A 251      30.722   6.322   0.385  1.00 13.01           N  
ANISOU 1940  N   VAL A 251     1523   1856   1564    -44    527   -420       N  
ATOM   1941  CA  VAL A 251      29.870   5.207  -0.001  1.00 13.16           C  
ANISOU 1941  CA  VAL A 251     1696   1707   1598    -38    442   -191       C  
ATOM   1942  C   VAL A 251      29.191   5.509  -1.327  1.00 13.97           C  
ANISOU 1942  C   VAL A 251     1833   1935   1539    -17    364   -185       C  
ATOM   1943  O   VAL A 251      28.579   6.560  -1.532  1.00 16.13           O  
ANISOU 1943  O   VAL A 251     2127   2271   1732    287    213   -207       O  
ATOM   1944  CB  VAL A 251      28.790   4.930   1.068  1.00 13.70           C  
ANISOU 1944  CB  VAL A 251     1677   2003   1526   -212    459   -352       C  
ATOM   1945  CG1 VAL A 251      27.903   3.793   0.641  1.00 14.13           C  
ANISOU 1945  CG1 VAL A 251     1693   1837   1838   -190    163    -79       C  
ATOM   1946  CG2 VAL A 251      29.420   4.642   2.434  1.00 13.21           C  
ANISOU 1946  CG2 VAL A 251     1470   1964   1584     92    433   -321       C  
ATOM   1947  N   LYS A 252      29.307   4.537  -2.239  1.00 15.57           N  
ANISOU 1947  N   LYS A 252     2581   1877   1458   -309    465   -186       N  
ATOM   1948  CA  LYS A 252      28.588   4.627  -3.518  1.00 17.66           C  
ANISOU 1948  CA  LYS A 252     2638   2579   1495   -453    374   -227       C  
ATOM   1949  C   LYS A 252      27.290   3.838  -3.575  1.00 16.31           C  
ANISOU 1949  C   LYS A 252     2257   2221   1720    -50    551   -258       C  
ATOM   1950  O   LYS A 252      26.320   4.208  -4.252  1.00 18.16           O  
ANISOU 1950  O   LYS A 252     2469   2469   1962     39    385   -158       O  
ATOM   1951  CB ALYS A 252      29.483   4.159  -4.673  0.62 23.59           C  
ANISOU 1951  CB ALYS A 252     2833   4528   1601  -1291    811   -677       C  
ATOM   1952  CB BLYS A 252      29.549   4.117  -4.606  0.38 23.08           C  
ANISOU 1952  CB BLYS A 252     2699   4470   1600   -965    771   -530       C  
ATOM   1953  CG ALYS A 252      30.628   5.103  -4.964  0.62 23.56           C  
ANISOU 1953  CG ALYS A 252     2419   4559   1972  -1206    298   -438       C  
ATOM   1954  CG BLYS A 252      28.947   4.080  -5.992  0.38 26.96           C  
ANISOU 1954  CG BLYS A 252     3077   5602   1566  -1405    726   -553       C  
ATOM   1955  CD ALYS A 252      30.269   6.566  -5.006  0.62 35.31           C  
ANISOU 1955  CD ALYS A 252     3978   4509   4930  -1236    -56    277       C  
ATOM   1956  CD BLYS A 252      29.892   3.623  -7.074  0.38 35.19           C  
ANISOU 1956  CD BLYS A 252     4211   7283   1876   -220    606  -1410       C  
ATOM   1957  CE ALYS A 252      30.976   7.488  -5.965  0.62 43.56           C  
ANISOU 1957  CE ALYS A 252     4016   5357   7176  -2174   -312   1393       C  
ATOM   1958  CE BLYS A 252      29.437   2.342  -7.748  0.38 39.63           C  
ANISOU 1958  CE BLYS A 252     4248   7985   2823   -371    540  -2203       C  
ATOM   1959  NZ ALYS A 252      31.130   8.858  -5.356  0.62 55.09           N  
ANISOU 1959  NZ ALYS A 252     5487   5560   9883  -3029  -1623    952       N  
ATOM   1960  NZ BLYS A 252      28.102   2.461  -8.407  0.38 55.51           N  
ANISOU 1960  NZ BLYS A 252     5903  10877   4312   -443  -1532  -2626       N  
ATOM   1961  N   GLU A 253      27.185   2.725  -2.867  1.00 15.86           N  
ANISOU 1961  N   GLU A 253     2214   2184   1630   -140    445   -317       N  
ATOM   1962  CA  GLU A 253      26.020   1.845  -2.912  1.00 16.09           C  
ANISOU 1962  CA  GLU A 253     2009   2378   1725   -124    393   -217       C  
ATOM   1963  C   GLU A 253      26.084   0.916  -1.710  1.00 15.61           C  
ANISOU 1963  C   GLU A 253     1950   2100   1881    -95    466   -267       C  
ATOM   1964  O   GLU A 253      27.186   0.621  -1.238  1.00 16.08           O  
ANISOU 1964  O   GLU A 253     2007   2228   1875   -243    443    -41       O  
ATOM   1965  CB  GLU A 253      26.032   0.957  -4.191  1.00 19.85           C  
ANISOU 1965  CB  GLU A 253     3003   2726   1815   -627    -12   -291       C  
ATOM   1966  CG  GLU A 253      24.811   0.103  -4.374  1.00 23.42           C  
ANISOU 1966  CG  GLU A 253     3466   3196   2236  -1166    691   -671       C  
ATOM   1967  CD  GLU A 253      24.530  -0.400  -5.764  1.00 28.36           C  
ANISOU 1967  CD  GLU A 253     3825   4692   2259  -1990    332   -710       C  
ATOM   1968  OE1 GLU A 253      25.524  -0.487  -6.509  1.00 36.45           O  
ANISOU 1968  OE1 GLU A 253     5063   6156   2629  -2435   1298  -1722       O  
ATOM   1969  OE2 GLU A 253      23.327  -0.676  -6.073  1.00 32.74           O  
ANISOU 1969  OE2 GLU A 253     3679   3673   5088   -192  -1021  -1441       O  
ATOM   1970  N   VAL A 254      24.934   0.419  -1.280  1.00 14.69           N  
ANISOU 1970  N   VAL A 254     1892   1924   1766      4    411   -274       N  
ATOM   1971  CA  VAL A 254      24.807  -0.560  -0.221  1.00 15.81           C  
ANISOU 1971  CA  VAL A 254     2307   1970   1730   -388    466   -431       C  
ATOM   1972  C   VAL A 254      23.880  -1.672  -0.709  1.00 16.46           C  
ANISOU 1972  C   VAL A 254     2254   2043   1958   -338    396   -515       C  
ATOM   1973  O   VAL A 254      22.831  -1.366  -1.286  1.00 17.06           O  
ANISOU 1973  O   VAL A 254     2293   2005   2186   -458    298   -403       O  
ATOM   1974  CB  VAL A 254      24.273   0.065   1.089  1.00 14.45           C  
ANISOU 1974  CB  VAL A 254     1807   1964   1720   -327    446   -405       C  
ATOM   1975  CG1 VAL A 254      24.384  -0.950   2.200  1.00 16.58           C  
ANISOU 1975  CG1 VAL A 254     2331   2148   1820   -558    503   -267       C  
ATOM   1976  CG2 VAL A 254      24.993   1.342   1.505  1.00 16.39           C  
ANISOU 1976  CG2 VAL A 254     2440   1822   1965   -256    368   -473       C  
ATOM   1977  N   LYS A 255      24.269  -2.922  -0.495  1.00 15.90           N  
ANISOU 1977  N   LYS A 255     2215   2041   1785   -511    341   -418       N  
ATOM   1978  CA  LYS A 255      23.436  -4.050  -0.888  1.00 18.16           C  
ANISOU 1978  CA  LYS A 255     2893   2042   1964   -588    170   -591       C  
ATOM   1979  C   LYS A 255      23.302  -5.040   0.269  1.00 16.90           C  
ANISOU 1979  C   LYS A 255     2455   1811   2156   -455    330   -606       C  
ATOM   1980  O   LYS A 255      24.207  -5.224   1.086  1.00 18.91           O  
ANISOU 1980  O   LYS A 255     2583   2621   1981   -882    270   -281       O  
ATOM   1981  CB  LYS A 255      23.998  -4.754  -2.145  1.00 20.33           C  
ANISOU 1981  CB  LYS A 255     3701   1882   2140   -254    423   -512       C  
ATOM   1982  CG  LYS A 255      24.067  -3.887  -3.393  1.00 27.62           C  
ANISOU 1982  CG  LYS A 255     6205   2468   1823   -326    413   -599       C  
ATOM   1983  CD  LYS A 255      24.585  -4.687  -4.578  1.00 32.02           C  
ANISOU 1983  CD  LYS A 255     6902   3198   2065    429    772   -564       C  
ATOM   1984  CE  LYS A 255      24.963  -3.867  -5.788  1.00 38.02           C  
ANISOU 1984  CE  LYS A 255     8638   3802   2007    289   1064   -413       C  
ATOM   1985  NZ  LYS A 255      25.363  -4.770  -6.899  1.00 53.35           N  
ANISOU 1985  NZ  LYS A 255    13440   4671   2160    -35   1959   -939       N  
ATOM   1986  N   LYS A 256      22.100  -5.646   0.333  1.00 18.45           N  
ANISOU 1986  N   LYS A 256     2557   2135   2317   -606    114   -403       N  
ATOM   1987  CA  LYS A 256      21.898  -6.667   1.322  1.00 19.37           C  
ANISOU 1987  CA  LYS A 256     2735   2412   2213   -709    249   -315       C  
ATOM   1988  C   LYS A 256      22.553  -7.938   0.804  1.00 20.17           C  
ANISOU 1988  C   LYS A 256     3484   2141   2038   -710    142   -270       C  
ATOM   1989  O   LYS A 256      22.398  -8.328  -0.350  1.00 24.32           O  
ANISOU 1989  O   LYS A 256     4739   2151   2350   -494   -419   -484       O  
ATOM   1990  CB  LYS A 256      20.420  -6.932   1.566  1.00 23.58           C  
ANISOU 1990  CB  LYS A 256     2861   2803   3294  -1086    285   -109       C  
ATOM   1991  CG  LYS A 256      20.215  -7.881   2.730  1.00 26.83           C  
ANISOU 1991  CG  LYS A 256     3689   3413   3092  -1203    921   -136       C  
ATOM   1992  CD  LYS A 256      20.385  -7.193   4.060  1.00 38.75           C  
ANISOU 1992  CD  LYS A 256     6577   4914   3231  -1739   -209   -309       C  
ATOM   1993  CE  LYS A 256      20.224  -8.122   5.241  1.00 36.78           C  
ANISOU 1993  CE  LYS A 256     5240   5652   3083    542   1366    -82       C  
ATOM   1994  NZ  LYS A 256      21.142  -9.324   5.250  1.00 30.95           N  
ANISOU 1994  NZ  LYS A 256     2971   5016   3774   -721    785   -801       N  
ATOM   1995  N   THR A 257      23.269  -8.625   1.666  1.00 18.86           N  
ANISOU 1995  N   THR A 257     3216   2055   1895   -890    272   -296       N  
ATOM   1996  CA  THR A 257      23.927  -9.888   1.421  1.00 19.05           C  
ANISOU 1996  CA  THR A 257     3226   2068   1944   -830    311   -207       C  
ATOM   1997  C   THR A 257      23.458 -10.938   2.397  1.00 21.03           C  
ANISOU 1997  C   THR A 257     3912   1995   2084  -1000    586   -357       C  
ATOM   1998  O   THR A 257      22.721 -10.691   3.363  1.00 22.66           O  
ANISOU 1998  O   THR A 257     3824   2471   2314   -894    813   -234       O  
ATOM   1999  CB  THR A 257      25.466  -9.742   1.490  1.00 20.87           C  
ANISOU 1999  CB  THR A 257     3258   2300   2370   -868    414   -515       C  
ATOM   2000  OG1 THR A 257      25.869  -9.337   2.820  1.00 27.35           O  
ANISOU 2000  OG1 THR A 257     3596   4014   2783   -305   -276   -992       O  
ATOM   2001  CG2 THR A 257      25.957  -8.761   0.441  1.00 24.47           C  
ANISOU 2001  CG2 THR A 257     3790   2198   3308  -1091    964   -351       C  
ATOM   2002  N   LEU A 258      23.896 -12.184   2.200  1.00 21.56           N  
ANISOU 2002  N   LEU A 258     4110   1991   2092  -1013    518   -339       N  
ATOM   2003  CA  LEU A 258      23.399 -13.275   3.059  1.00 23.96           C  
ANISOU 2003  CA  LEU A 258     4980   1899   2225  -1273    583   -457       C  
ATOM   2004  C   LEU A 258      23.779 -13.066   4.511  1.00 27.67           C  
ANISOU 2004  C   LEU A 258     6283   2061   2168  -1295    368   -164       C  
ATOM   2005  O   LEU A 258      23.046 -13.455   5.434  1.00 36.35           O  
ANISOU 2005  O   LEU A 258     8217   3210   2386  -2508    795    147       O  
ATOM   2006  CB  LEU A 258      23.998 -14.583   2.535  1.00 21.75           C  
ANISOU 2006  CB  LEU A 258     3837   2087   2338   -962    325   -232       C  
ATOM   2007  CG  LEU A 258      23.506 -15.074   1.194  1.00 22.21           C  
ANISOU 2007  CG  LEU A 258     4167   2073   2197   -804    588   -390       C  
ATOM   2008  CD1 LEU A 258      24.315 -16.325   0.849  1.00 24.69           C  
ANISOU 2008  CD1 LEU A 258     4673   2036   2670   -582    858   -192       C  
ATOM   2009  CD2 LEU A 258      22.011 -15.339   1.222  1.00 27.10           C  
ANISOU 2009  CD2 LEU A 258     4001   2216   4081   -561   -843    269       C  
ATOM   2010  N  ASER A 259      24.924 -12.425   4.651  0.51 27.30           N  
ANISOU 2010  N  ASER A 259     6331   2175   1865  -1272   -237     92       N  
ATOM   2011  N  BSER A 259      24.947 -12.474   4.784  0.49 26.55           N  
ANISOU 2011  N  BSER A 259     5732   2464   1892   -604    -34   -374       N  
ATOM   2012  CA ASER A 259      25.466 -11.889   5.867  0.51 33.54           C  
ANISOU 2012  CA ASER A 259     7501   2565   2680   -662   -955   -666       C  
ATOM   2013  CA BSER A 259      25.269 -12.396   6.211  0.49 31.40           C  
ANISOU 2013  CA BSER A 259     7247   2618   2064   -100   -459   -333       C  
ATOM   2014  C  ASER A 259      25.381 -10.364   5.821  0.51 26.87           C  
ANISOU 2014  C  ASER A 259     5338   2499   2370  -1061    558   -589       C  
ATOM   2015  C  BSER A 259      25.085 -10.976   6.734  0.49 28.77           C  
ANISOU 2015  C  BSER A 259     6681   2364   1886  -1039   -175   -331       C  
ATOM   2016  O  ASER A 259      26.143  -9.800   5.048  0.51 33.85           O  
ANISOU 2016  O  ASER A 259     5266   3285   4310  -1050   2106  -1136       O  
ATOM   2017  O  BSER A 259      25.172 -10.764   7.948  0.49 34.51           O  
ANISOU 2017  O  BSER A 259     7999   3310   1804    232    -75   -432       O  
ATOM   2018  CB ASER A 259      26.934 -12.288   6.041  0.51 35.24           C  
ANISOU 2018  CB ASER A 259     7917   2635   2837   -372  -1833    405       C  
ATOM   2019  CB BSER A 259      26.695 -12.869   6.488  0.49 37.07           C  
ANISOU 2019  CB BSER A 259     7673   3559   2855    212  -1390   -502       C  
ATOM   2020  OG ASER A 259      27.810 -11.288   5.535  0.51 45.10           O  
ANISOU 2020  OG ASER A 259     7116   2876   7142  -1686  -4217    899       O  
ATOM   2021  OG BSER A 259      27.262 -11.990   7.462  0.49 51.46           O  
ANISOU 2021  OG BSER A 259    10274   5529   3750   1387  -3688  -1626       O  
ATOM   2022  N  AGLY A 260      24.518  -9.715   6.576  0.51 23.41           N  
ANISOU 2022  N  AGLY A 260     3877   2673   2344  -1357    528     33       N  
ATOM   2023  N  BGLY A 260      24.838 -10.044   5.813  0.49 22.96           N  
ANISOU 2023  N  BGLY A 260     4652   2374   1698   -791    510   -409       N  
ATOM   2024  CA AGLY A 260      24.535  -8.269   6.685  0.51 20.62           C  
ANISOU 2024  CA AGLY A 260     3260   2704   1871  -1045    662   -245       C  
ATOM   2025  CA BGLY A 260      24.626  -8.682   6.285  0.49 18.85           C  
ANISOU 2025  CA BGLY A 260     3179   2483   1501   -733   1040   -340       C  
ATOM   2026  C  AGLY A 260      24.466  -7.565   5.349  0.51 19.36           C  
ANISOU 2026  C  AGLY A 260     3105   2370   1881  -1055    322   -373       C  
ATOM   2027  C  BGLY A 260      24.531  -7.663   5.176  0.49 17.55           C  
ANISOU 2027  C  BGLY A 260     2647   2445   1575   -786    478   -366       C  
ATOM   2028  O  AGLY A 260      23.630  -7.937   4.505  0.51 23.05           O  
ANISOU 2028  O  AGLY A 260     4432   2477   1849  -1890    157   -602       O  
ATOM   2029  O  BGLY A 260      23.548  -7.659   4.414  0.49 18.41           O  
ANISOU 2029  O  BGLY A 260     1744   2902   2349    122    711   -724       O  
ATOM   2030  N  ALEU A 261      25.321  -6.568   5.169  0.51 15.42           N  
ANISOU 2030  N  ALEU A 261     2093   1939   1825   -379    508   -466       N  
ATOM   2031  N  BLEU A 261      25.548  -6.814   5.097  0.49 16.28           N  
ANISOU 2031  N  BLEU A 261     2830   1835   1520   -651    433   -559       N  
ATOM   2032  CA ALEU A 261      25.371  -5.724   3.996  0.51 14.99           C  
ANISOU 2032  CA ALEU A 261     1876   2037   1783   -470    325   -449       C  
ATOM   2033  CA BLEU A 261      25.586  -5.736   4.127  0.49 15.00           C  
ANISOU 2033  CA BLEU A 261     2092   2057   1552   -499    155   -383       C  
ATOM   2034  C  ALEU A 261      26.752  -5.761   3.359  0.51 15.14           C  
ANISOU 2034  C  ALEU A 261     2011   2144   1598   -478    403   -693       C  
ATOM   2035  C  BLEU A 261      26.923  -5.667   3.402  0.49 16.73           C  
ANISOU 2035  C  BLEU A 261     2360   2253   1741   -539    412   -460       C  
ATOM   2036  O  ALEU A 261      27.744  -6.107   4.047  0.51 16.41           O  
ANISOU 2036  O  ALEU A 261     1988   2456   1790   -263    398   -635       O  
ATOM   2037  O  BLEU A 261      28.002  -5.822   4.012  0.49 18.89           O  
ANISOU 2037  O  BLEU A 261     2115   3388   1674   -686    498   -614       O  
ATOM   2038  CB ALEU A 261      25.062  -4.265   4.376  0.51 15.50           C  
ANISOU 2038  CB ALEU A 261     2171   2072   1645   -179    278   -328       C  
ATOM   2039  CB BLEU A 261      25.373  -4.354   4.789  0.49 14.40           C  
ANISOU 2039  CB BLEU A 261     1924   1880   1668   -500     31   -244       C  
ATOM   2040  CG ALEU A 261      23.794  -4.002   5.200  0.51 14.40           C  
ANISOU 2040  CG ALEU A 261     2248   1677   1546   -363    340   -200       C  
ATOM   2041  CG BLEU A 261      24.135  -4.261   5.685  0.49 15.47           C  
ANISOU 2041  CG BLEU A 261     2196   2257   1424   -433     73   -456       C  
ATOM   2042  CD1ALEU A 261      23.834  -2.631   5.869  0.51 18.17           C  
ANISOU 2042  CD1ALEU A 261     3609   1827   1467   -417    562   -404       C  
ATOM   2043  CD1BLEU A 261      24.024  -2.915   6.384  0.49 20.53           C  
ANISOU 2043  CD1BLEU A 261     3286   2632   1884    590   -683   -882       C  
ATOM   2044  CD2ALEU A 261      22.583  -4.145   4.296  0.51 14.50           C  
ANISOU 2044  CD2ALEU A 261     2202   1462   1846   -194    159    220       C  
ATOM   2045  CD2BLEU A 261      22.896  -4.530   4.840  0.49 14.86           C  
ANISOU 2045  CD2BLEU A 261     1913   1908   1825   -361     -6     66       C  
ATOM   2046  N   GLU A 262      26.868  -5.370   2.097  1.00 16.19           N  
ANISOU 2046  N   GLU A 262     2355   2048   1747   -348    563   -445       N  
ATOM   2047  CA  GLU A 262      28.097  -5.053   1.371  1.00 16.59           C  
ANISOU 2047  CA  GLU A 262     2371   1902   2030   -318    666   -435       C  
ATOM   2048  C   GLU A 262      28.055  -3.582   1.052  1.00 15.61           C  
ANISOU 2048  C   GLU A 262     2151   1888   1892   -201    596   -472       C  
ATOM   2049  O   GLU A 262      27.097  -3.104   0.453  1.00 16.88           O  
ANISOU 2049  O   GLU A 262     2182   2009   2221   -369    425   -278       O  
ATOM   2050  CB AGLU A 262      28.287  -5.803   0.054  0.70 20.04           C  
ANISOU 2050  CB AGLU A 262     3391   1974   2250   -135   1281   -563       C  
ATOM   2051  CB BGLU A 262      28.307  -5.915   0.134  0.30 19.25           C  
ANISOU 2051  CB BGLU A 262     2846   2018   2450   -515   1172   -738       C  
ATOM   2052  CG AGLU A 262      29.292  -5.285  -0.987  0.70 23.26           C  
ANISOU 2052  CG AGLU A 262     2858   3212   2768   -459   1417   -804       C  
ATOM   2053  CG BGLU A 262      29.710  -5.763  -0.464  0.30 21.94           C  
ANISOU 2053  CG BGLU A 262     3274   2732   2330   -779   1546   -191       C  
ATOM   2054  CD AGLU A 262      29.097  -5.767  -2.398  0.70 28.91           C  
ANISOU 2054  CD AGLU A 262     4854   3782   2349   -293   1746   -464       C  
ATOM   2055  CD BGLU A 262      30.113  -6.952  -1.307  0.30 24.25           C  
ANISOU 2055  CD BGLU A 262     3084   3675   2455   -494   1660   -714       C  
ATOM   2056  OE1AGLU A 262      28.297  -5.311  -3.260  0.70 31.48           O  
ANISOU 2056  OE1AGLU A 262     6997   2744   2220    106   1104   -636       O  
ATOM   2057  OE1BGLU A 262      29.241  -7.523  -2.006  0.30 30.23           O  
ANISOU 2057  OE1BGLU A 262     4483   4563   2440   1264   -424  -1407       O  
ATOM   2058  OE2AGLU A 262      29.824  -6.743  -2.722  0.70 31.58           O  
ANISOU 2058  OE2AGLU A 262     5674   4125   2200    227   1380   -756       O  
ATOM   2059  OE2BGLU A 262      31.308  -7.326  -1.260  0.30 30.68           O  
ANISOU 2059  OE2BGLU A 262     2894   3632   5130   -775   1793  -1040       O  
ATOM   2060  N   VAL A 263      29.105  -2.875   1.472  1.00 14.86           N  
ANISOU 2060  N   VAL A 263     2197   1851   1600   -163    433   -223       N  
ATOM   2061  CA  VAL A 263      29.231  -1.454   1.228  1.00 14.08           C  
ANISOU 2061  CA  VAL A 263     1926   1693   1733     62    449   -218       C  
ATOM   2062  C   VAL A 263      30.227  -1.247   0.102  1.00 15.58           C  
ANISOU 2062  C   VAL A 263     2191   1689   2039     92    706   -132       C  
ATOM   2063  O   VAL A 263      31.384  -1.689   0.220  1.00 18.14           O  
ANISOU 2063  O   VAL A 263     2096   2546   2248    102    731    327       O  
ATOM   2064  CB  VAL A 263      29.661  -0.736   2.514  1.00 15.70           C  
ANISOU 2064  CB  VAL A 263     2164   1803   1998    -77    358   -310       C  
ATOM   2065  CG1 VAL A 263      29.839   0.761   2.286  1.00 18.53           C  
ANISOU 2065  CG1 VAL A 263     2399   1819   2821   -130   -189   -450       C  
ATOM   2066  CG2 VAL A 263      28.685  -0.983   3.667  1.00 17.53           C  
ANISOU 2066  CG2 VAL A 263     2191   2628   1840    369    393   -341       C  
ATOM   2067  N   SER A 264      29.781  -0.561  -0.967  1.00 14.95           N  
ANISOU 2067  N   SER A 264     2139   1792   1750   -105    549   -312       N  
ATOM   2068  CA  SER A 264      30.673  -0.215  -2.066  1.00 15.77           C  
ANISOU 2068  CA  SER A 264     2192   1887   1913   -188    592   -168       C  
ATOM   2069  C   SER A 264      31.243   1.174  -1.793  1.00 14.64           C  
ANISOU 2069  C   SER A 264     1960   1844   1759      3    631   -318       C  
ATOM   2070  O   SER A 264      30.477   2.127  -1.618  1.00 17.22           O  
ANISOU 2070  O   SER A 264     2160   1957   2423    140    425   -444       O  
ATOM   2071  CB ASER A 264      29.935  -0.180  -3.400  0.78 17.80           C  
ANISOU 2071  CB ASER A 264     2595   2403   1765   -696    590   -391       C  
ATOM   2072  CB BSER A 264      29.909  -0.266  -3.382  0.22 19.10           C  
ANISOU 2072  CB BSER A 264     2928   2626   1704   -434    558   -590       C  
ATOM   2073  OG ASER A 264      29.367  -1.429  -3.712  0.78 20.89           O  
ANISOU 2073  OG ASER A 264     3297   2451   2191   -916    900   -799       O  
ATOM   2074  OG BSER A 264      30.697   0.169  -4.471  0.22 20.82           O  
ANISOU 2074  OG BSER A 264     2788   3375   1749    291    859   -510       O  
ATOM   2075  N   MET A 265      32.549   1.291  -1.677  1.00 15.74           N  
ANISOU 2075  N   MET A 265     1901   2016   2062   -145    972   -309       N  
ATOM   2076  CA  MET A 265      33.243   2.474  -1.311  1.00 17.63           C  
ANISOU 2076  CA  MET A 265     2456   2297   1945   -592   1143   -376       C  
ATOM   2077  C   MET A 265      34.136   2.936  -2.451  1.00 14.64           C  
ANISOU 2077  C   MET A 265     1788   2023   1753   -155    837   -322       C  
ATOM   2078  O   MET A 265      34.733   2.161  -3.173  1.00 18.42           O  
ANISOU 2078  O   MET A 265     2730   2065   2204    163   1365   -181       O  
ATOM   2079  CB  MET A 265      34.158   2.142  -0.086  1.00 21.00           C  
ANISOU 2079  CB  MET A 265     2963   3321   1697  -1014   1059   -262       C  
ATOM   2080  CG  MET A 265      35.080   3.222   0.414  1.00 19.65           C  
ANISOU 2080  CG  MET A 265     2727   2647   2094   -484    690     46       C  
ATOM   2081  SD  MET A 265      35.872   2.782   1.933  1.00 19.07           S  
ANISOU 2081  SD  MET A 265     2599   2384   2261     62    743    170       S  
ATOM   2082  CE  MET A 265      36.960   1.414   1.612  1.00 21.29           C  
ANISOU 2082  CE  MET A 265     2836   2997   2258    241    763   -602       C  
ATOM   2083  N   VAL A 266      34.246   4.254  -2.605  1.00 13.90           N  
ANISOU 2083  N   VAL A 266     1753   1973   1557    -52    602   -327       N  
ATOM   2084  CA  VAL A 266      35.252   4.863  -3.488  1.00 14.36           C  
ANISOU 2084  CA  VAL A 266     2102   1838   1517   -126    612   -276       C  
ATOM   2085  C   VAL A 266      36.247   5.648  -2.635  1.00 13.44           C  
ANISOU 2085  C   VAL A 266     1922   1948   1237   -138    754   -248       C  
ATOM   2086  O   VAL A 266      35.830   6.443  -1.774  1.00 14.42           O  
ANISOU 2086  O   VAL A 266     1779   2155   1546     55    590   -477       O  
ATOM   2087  CB AVAL A 266      34.666   5.760  -4.571  0.46 15.48           C  
ANISOU 2087  CB AVAL A 266     2382   2171   1329      4    512   -355       C  
ATOM   2088  CB BVAL A 266      34.677   5.899  -4.451  0.54 18.99           C  
ANISOU 2088  CB BVAL A 266     2881   2497   1837   -542     -8    178       C  
ATOM   2089  CG1AVAL A 266      33.668   6.756  -4.005  0.46 18.16           C  
ANISOU 2089  CG1AVAL A 266     2048   2542   2309    278    383   -422       C  
ATOM   2090  CG1BVAL A 266      35.748   6.298  -5.488  0.54 23.26           C  
ANISOU 2090  CG1BVAL A 266     4272   3532   1035  -1473     78     31       C  
ATOM   2091  CG2AVAL A 266      35.788   6.534  -5.285  0.46 16.84           C  
ANISOU 2091  CG2AVAL A 266     2651   1950   1797    333    819     75       C  
ATOM   2092  CG2BVAL A 266      33.431   5.458  -5.183  0.54 31.47           C  
ANISOU 2092  CG2BVAL A 266     3505   5563   2888  -1119  -1021    654       C  
ATOM   2093  N   THR A 267      37.515   5.391  -2.818  1.00 14.43           N  
ANISOU 2093  N   THR A 267     1952   1994   1536   -230    915   -467       N  
ATOM   2094  CA  THR A 267      38.599   6.059  -2.115  1.00 14.42           C  
ANISOU 2094  CA  THR A 267     1924   1906   1650   -184    857   -446       C  
ATOM   2095  C   THR A 267      39.420   6.844  -3.130  1.00 14.30           C  
ANISOU 2095  C   THR A 267     1935   2104   1393   -332    755   -446       C  
ATOM   2096  O   THR A 267      39.792   6.311  -4.172  1.00 16.38           O  
ANISOU 2096  O   THR A 267     2228   2323   1671   -410   1017   -634       O  
ATOM   2097  CB  THR A 267      39.504   5.061  -1.404  1.00 15.72           C  
ANISOU 2097  CB  THR A 267     2107   1975   1890    -95    765   -310       C  
ATOM   2098  OG1 THR A 267      38.685   4.315  -0.448  1.00 16.40           O  
ANISOU 2098  OG1 THR A 267     1976   2292   1963     38    758   -150       O  
ATOM   2099  CG2 THR A 267      40.659   5.682  -0.667  1.00 17.28           C  
ANISOU 2099  CG2 THR A 267     2022   2681   1864   -102    772   -565       C  
ATOM   2100  N   ALA A 268      39.682   8.119  -2.830  1.00 14.14           N  
ANISOU 2100  N   ALA A 268     1922   2020   1430   -296    721   -364       N  
ATOM   2101  CA  ALA A 268      40.374   8.998  -3.766  1.00 14.09           C  
ANISOU 2101  CA  ALA A 268     2119   1858   1376     13    629   -123       C  
ATOM   2102  C   ALA A 268      41.358   9.880  -3.001  1.00 14.30           C  
ANISOU 2102  C   ALA A 268     2135   1924   1375   -194    750   -114       C  
ATOM   2103  O   ALA A 268      41.093  11.043  -2.682  1.00 16.18           O  
ANISOU 2103  O   ALA A 268     2430   2038   1678   -138    876   -265       O  
ATOM   2104  CB  ALA A 268      39.394   9.786  -4.586  1.00 16.74           C  
ANISOU 2104  CB  ALA A 268     2212   2027   2120     45    372    -30       C  
ATOM   2105  N   VAL A 269      42.510   9.297  -2.681  1.00 14.23           N  
ANISOU 2105  N   VAL A 269     1953   1955   1499   -339    755   -345       N  
ATOM   2106  CA  VAL A 269      43.551   9.991  -1.942  1.00 15.77           C  
ANISOU 2106  CA  VAL A 269     2064   2185   1742   -415    763   -641       C  
ATOM   2107  C   VAL A 269      44.314  10.925  -2.860  1.00 17.92           C  
ANISOU 2107  C   VAL A 269     2176   2744   1887   -920    825   -814       C  
ATOM   2108  O   VAL A 269      44.762  10.459  -3.951  1.00 18.01           O  
ANISOU 2108  O   VAL A 269     2308   2581   1955   -620    983   -632       O  
ATOM   2109  CB  VAL A 269      44.494   8.959  -1.326  1.00 17.36           C  
ANISOU 2109  CB  VAL A 269     1876   2866   1853   -278    640   -742       C  
ATOM   2110  CG1 VAL A 269      45.631   9.657  -0.594  1.00 20.59           C  
ANISOU 2110  CG1 VAL A 269     2174   3339   2309   -660    392   -578       C  
ATOM   2111  CG2 VAL A 269      43.769   8.037  -0.353  1.00 18.33           C  
ANISOU 2111  CG2 VAL A 269     2341   2699   1925   -375    286   -287       C  
ATOM   2112  N   PRO A 270      44.564  12.154  -2.458  1.00 18.53           N  
ANISOU 2112  N   PRO A 270     2577   2454   2010   -722   1150   -631       N  
ATOM   2113  CA  PRO A 270      45.398  13.037  -3.287  1.00 20.83           C  
ANISOU 2113  CA  PRO A 270     3244   2593   2076   -893   1442   -592       C  
ATOM   2114  C   PRO A 270      46.740  12.399  -3.617  1.00 21.03           C  
ANISOU 2114  C   PRO A 270     2663   3059   2268  -1355   1107  -1058       C  
ATOM   2115  O   PRO A 270      47.415  11.817  -2.783  1.00 23.81           O  
ANISOU 2115  O   PRO A 270     2734   4030   2282   -859    911  -1382       O  
ATOM   2116  CB  PRO A 270      45.575  14.309  -2.451  1.00 23.07           C  
ANISOU 2116  CB  PRO A 270     3713   2594   2458  -1123   1502   -628       C  
ATOM   2117  CG  PRO A 270      44.411  14.300  -1.477  1.00 23.26           C  
ANISOU 2117  CG  PRO A 270     3448   2551   2837   -685   1471   -943       C  
ATOM   2118  CD  PRO A 270      44.066  12.861  -1.243  1.00 22.41           C  
ANISOU 2118  CD  PRO A 270     3459   2712   2343   -884   1784   -840       C  
ATOM   2119  N   GLY A 271      47.092  12.491  -4.903  1.00 21.57           N  
ANISOU 2119  N   GLY A 271     2831   2883   2482  -1119   1424  -1014       N  
ATOM   2120  CA  GLY A 271      48.313  11.947  -5.432  1.00 22.61           C  
ANISOU 2120  CA  GLY A 271     2576   3076   2938  -1136   1433   -887       C  
ATOM   2121  C   GLY A 271      48.197  10.515  -5.893  1.00 21.43           C  
ANISOU 2121  C   GLY A 271     2308   3361   2475  -1061   1186  -1312       C  
ATOM   2122  O   GLY A 271      49.171  10.028  -6.466  1.00 24.24           O  
ANISOU 2122  O   GLY A 271     2502   3601   3106   -539   1343   -915       O  
ATOM   2123  N   ARG A 272      47.094   9.844  -5.672  1.00 20.53           N  
ANISOU 2123  N   ARG A 272     2341   3215   2246  -1062    927   -971       N  
ATOM   2124  CA  ARG A 272      46.852   8.464  -6.056  1.00 18.60           C  
ANISOU 2124  CA  ARG A 272     1869   3081   2119   -645    510   -919       C  
ATOM   2125  C   ARG A 272      45.671   8.464  -7.010  1.00 16.49           C  
ANISOU 2125  C   ARG A 272     2255   2216   1794   -560    460   -315       C  
ATOM   2126  O   ARG A 272      45.038   9.499  -7.198  1.00 18.67           O  
ANISOU 2126  O   ARG A 272     2758   2236   2102   -312    452   -603       O  
ATOM   2127  CB AARG A 272      46.506   7.612  -4.835  0.31 21.95           C  
ANISOU 2127  CB AARG A 272     2946   3164   2232   -856   -654   -385       C  
ATOM   2128  CB BARG A 272      46.593   7.575  -4.838  0.69 18.56           C  
ANISOU 2128  CB BARG A 272     2055   2723   2276    275    -62   -609       C  
ATOM   2129  CG AARG A 272      47.523   6.577  -4.426  0.31 27.50           C  
ANISOU 2129  CG AARG A 272     3082   4062   3304   -362   -966   -404       C  
ATOM   2130  CG BARG A 272      47.666   7.606  -3.764  0.69 23.30           C  
ANISOU 2130  CG BARG A 272     2468   3692   2695   -250   -408   -835       C  
ATOM   2131  CD AARG A 272      47.153   5.802  -3.166  0.31 29.29           C  
ANISOU 2131  CD AARG A 272     3489   3569   4071   -453  -1417    292       C  
ATOM   2132  CD BARG A 272      47.582   6.436  -2.811  0.69 29.84           C  
ANISOU 2132  CD BARG A 272     4141   4010   3188     61  -1628   -268       C  
ATOM   2133  NE AARG A 272      47.867   4.532  -3.118  0.31 32.58           N  
ANISOU 2133  NE AARG A 272     3687   4145   4547    119   -909    -70       N  
ATOM   2134  NE BARG A 272      48.245   5.205  -3.255  0.69 36.16           N  
ANISOU 2134  NE BARG A 272     4935   3967   4838    199  -1347   -456       N  
ATOM   2135  CZ AARG A 272      47.479   3.295  -2.886  0.31 26.03           C  
ANISOU 2135  CZ AARG A 272     2357   3790   3742   1082    -18   -242       C  
ATOM   2136  CZ BARG A 272      49.433   4.779  -3.623  0.69 37.40           C  
ANISOU 2136  CZ BARG A 272     4662   3873   5674    535  -2055   -657       C  
ATOM   2137  NH1AARG A 272      48.398   2.328  -2.918  0.31 32.40           N  
ANISOU 2137  NH1AARG A 272     2398   4818   5095   1642    366   -655       N  
ATOM   2138  NH1BARG A 272      50.508   5.563  -3.691  0.69 45.04           N  
ANISOU 2138  NH1BARG A 272     4200   5286   7628    196  -2925  -1239       N  
ATOM   2139  NH2AARG A 272      46.216   3.003  -2.626  0.31 18.77           N  
ANISOU 2139  NH2AARG A 272     2163   3144   1824   1264   -282  -1509       N  
ATOM   2140  NH2BARG A 272      49.644   3.505  -3.972  0.69 39.18           N  
ANISOU 2140  NH2BARG A 272     6187   4308   4391    849  -2155  -1162       N  
ATOM   2141  N   LEU A 273      45.344   7.340  -7.556  1.00 15.48           N  
ANISOU 2141  N   LEU A 273     2162   2258   1462   -239    273   -480       N  
ATOM   2142  CA  LEU A 273      44.139   7.165  -8.392  1.00 13.91           C  
ANISOU 2142  CA  LEU A 273     1991   1885   1408    -54    448   -351       C  
ATOM   2143  C   LEU A 273      42.958   6.681  -7.575  1.00 14.45           C  
ANISOU 2143  C   LEU A 273     2238   2034   1218   -227    527   -443       C  
ATOM   2144  O   LEU A 273      43.120   5.936  -6.588  1.00 15.40           O  
ANISOU 2144  O   LEU A 273     2399   2104   1347     18    733   -355       O  
ATOM   2145  CB  LEU A 273      44.441   6.161  -9.523  1.00 13.18           C  
ANISOU 2145  CB  LEU A 273     1609   2046   1352   -163    400   -374       C  
ATOM   2146  CG  LEU A 273      45.381   6.672 -10.628  1.00 15.64           C  
ANISOU 2146  CG  LEU A 273     1745   2665   1532   -223    544   -339       C  
ATOM   2147  CD1 LEU A 273      45.594   5.570 -11.623  1.00 17.88           C  
ANISOU 2147  CD1 LEU A 273     1828   3292   1672   -424    642   -870       C  
ATOM   2148  CD2 LEU A 273      44.827   7.921 -11.307  1.00 20.57           C  
ANISOU 2148  CD2 LEU A 273     2985   3044   1787     10    985    302       C  
ATOM   2149  N   PRO A 274      41.729   7.081  -7.971  1.00 14.47           N  
ANISOU 2149  N   PRO A 274     2144   1925   1430   -151    699   -325       N  
ATOM   2150  CA  PRO A 274      40.529   6.552  -7.296  1.00 14.95           C  
ANISOU 2150  CA  PRO A 274     2315   1935   1430    -58    877   -276       C  
ATOM   2151  C   PRO A 274      40.427   5.044  -7.437  1.00 14.83           C  
ANISOU 2151  C   PRO A 274     2108   1886   1640    -74    905   -363       C  
ATOM   2152  O   PRO A 274      40.744   4.452  -8.463  1.00 15.31           O  
ANISOU 2152  O   PRO A 274     2140   2071   1607   -183    911   -375       O  
ATOM   2153  CB  PRO A 274      39.408   7.283  -8.029  1.00 17.59           C  
ANISOU 2153  CB  PRO A 274     2180   2100   2403    148    884   -160       C  
ATOM   2154  CG  PRO A 274      39.986   8.481  -8.676  1.00 18.82           C  
ANISOU 2154  CG  PRO A 274     2404   2609   2137     96    749    330       C  
ATOM   2155  CD  PRO A 274      41.394   8.104  -8.950  1.00 15.53           C  
ANISOU 2155  CD  PRO A 274     2387   2096   1417    -50    720   -193       C  
ATOM   2156  N   VAL A 275      39.896   4.422  -6.375  1.00 14.84           N  
ANISOU 2156  N   VAL A 275     2082   1890   1667   -291    943   -430       N  
ATOM   2157  CA  VAL A 275      39.765   2.969  -6.309  1.00 14.89           C  
ANISOU 2157  CA  VAL A 275     2046   1842   1771    -59    879   -380       C  
ATOM   2158  C   VAL A 275      38.437   2.623  -5.658  1.00 14.16           C  
ANISOU 2158  C   VAL A 275     2116   1894   1369   -179    723   -215       C  
ATOM   2159  O   VAL A 275      38.022   3.264  -4.673  1.00 17.05           O  
ANISOU 2159  O   VAL A 275     2580   2184   1714   -445   1143   -571       O  
ATOM   2160  CB  VAL A 275      40.943   2.345  -5.554  1.00 18.12           C  
ANISOU 2160  CB  VAL A 275     2137   2333   2414     34    614   -287       C  
ATOM   2161  CG1 VAL A 275      41.225   2.949  -4.229  1.00 21.99           C  
ANISOU 2161  CG1 VAL A 275     2357   3589   2409    245    395   -521       C  
ATOM   2162  CG2 VAL A 275      40.696   0.839  -5.422  1.00 22.60           C  
ANISOU 2162  CG2 VAL A 275     2294   2303   3992    402    356      5       C  
ATOM   2163  N   MET A 276      37.788   1.591  -6.171  1.00 15.48           N  
ANISOU 2163  N   MET A 276     2302   1942   1639   -278    934   -439       N  
ATOM   2164  CA  MET A 276      36.557   1.041  -5.630  1.00 17.05           C  
ANISOU 2164  CA  MET A 276     2330   2139   2010   -326    948   -409       C  
ATOM   2165  C   MET A 276      36.885  -0.175  -4.766  1.00 17.79           C  
ANISOU 2165  C   MET A 276     2651   1850   2259   -276   1319   -398       C  
ATOM   2166  O   MET A 276      37.626  -1.027  -5.291  1.00 22.66           O  
ANISOU 2166  O   MET A 276     3857   2075   2677    187   1956   -244       O  
ATOM   2167  CB AMET A 276      35.547   0.745  -6.706  0.46 27.25           C  
ANISOU 2167  CB AMET A 276     3492   2677   4185  -1084   -730   -177       C  
ATOM   2168  CB BMET A 276      35.604   0.491  -6.664  0.54 20.26           C  
ANISOU 2168  CB BMET A 276     2142   3435   2121   -689   1158   -669       C  
ATOM   2169  CG AMET A 276      34.241   0.079  -6.504  0.46 33.14           C  
ANISOU 2169  CG AMET A 276     3299   4968   4324  -1354   -613    623       C  
ATOM   2170  CG BMET A 276      35.257   1.501  -7.748  0.54 22.19           C  
ANISOU 2170  CG BMET A 276     2222   3355   2855   -115    200   -818       C  
ATOM   2171  SD AMET A 276      33.114   0.572  -5.220  0.46 57.95           S  
ANISOU 2171  SD AMET A 276     5637  13431   2952  -3970    369  -1634       S  
ATOM   2172  SD BMET A 276      34.519   2.944  -6.986  0.54 43.48           S  
ANISOU 2172  SD BMET A 276     5670   4948   5904   2077  -1597  -2832       S  
ATOM   2173  CE AMET A 276      32.941   2.328  -5.524  0.46 65.07           C  
ANISOU 2173  CE AMET A 276     6843  13765   4116   1943   4165  -3581       C  
ATOM   2174  CE BMET A 276      33.029   2.220  -6.238  0.54 63.80           C  
ANISOU 2174  CE BMET A 276     8127  11245   4871   2729   3360  -4262       C  
ATOM   2175  N   THR A 277      36.331  -0.250  -3.587  1.00 17.12           N  
ANISOU 2175  N   THR A 277     2150   1976   2379     31   1254    -95       N  
ATOM   2176  CA  THR A 277      36.528  -1.322  -2.633  1.00 18.89           C  
ANISOU 2176  CA  THR A 277     2479   2242   2458    240   1216      4       C  
ATOM   2177  C   THR A 277      35.160  -1.800  -2.171  1.00 17.73           C  
ANISOU 2177  C   THR A 277     2519   2084   2134    -37   1146   -183       C  
ATOM   2178  O   THR A 277      34.347  -0.944  -1.814  1.00 18.93           O  
ANISOU 2178  O   THR A 277     2599   2003   2589    -32   1260   -403       O  
ATOM   2179  CB  THR A 277      37.383  -0.874  -1.412  1.00 22.86           C  
ANISOU 2179  CB  THR A 277     2474   3188   3025   -215    683    509       C  
ATOM   2180  OG1 THR A 277      38.616  -0.392  -1.961  1.00 25.73           O  
ANISOU 2180  OG1 THR A 277     2426   3572   3778   -139    817    603       O  
ATOM   2181  CG2 THR A 277      37.663  -2.032  -0.471  1.00 31.56           C  
ANISOU 2181  CG2 THR A 277     3350   4145   4496  -1020   -520   1660       C  
ATOM   2182  N   MET A 278      34.925  -3.095  -2.107  1.00 18.84           N  
ANISOU 2182  N   MET A 278     2932   2031   2195     32   1186   -293       N  
ATOM   2183  CA  MET A 278      33.745  -3.621  -1.454  1.00 18.25           C  
ANISOU 2183  CA  MET A 278     2955   1864   2116    -55    981    -67       C  
ATOM   2184  C   MET A 278      34.104  -3.963  -0.028  1.00 18.15           C  
ANISOU 2184  C   MET A 278     2659   2071   2167    300   1052    -82       C  
ATOM   2185  O   MET A 278      35.131  -4.609   0.290  1.00 23.84           O  
ANISOU 2185  O   MET A 278     2878   3490   2689    959   1457    776       O  
ATOM   2186  CB AMET A 278      33.359  -4.962  -2.084  0.62 22.99           C  
ANISOU 2186  CB AMET A 278     4407   2020   2307   -637    883    -21       C  
ATOM   2187  CB BMET A 278      33.221  -4.789  -2.290  0.38 21.42           C  
ANISOU 2187  CB BMET A 278     2691   2685   2763   -121   1005   -825       C  
ATOM   2188  CG AMET A 278      32.759  -4.967  -3.452  0.62 25.00           C  
ANISOU 2188  CG AMET A 278     5021   2179   2297     44    743   -587       C  
ATOM   2189  CG BMET A 278      32.438  -4.433  -3.526  0.38 25.35           C  
ANISOU 2189  CG BMET A 278     4663   2230   2738    271    416  -1047       C  
ATOM   2190  SD AMET A 278      31.447  -3.723  -3.554  0.62 23.99           S  
ANISOU 2190  SD AMET A 278     3787   2630   2698   -366    749   -708       S  
ATOM   2191  SD BMET A 278      32.995  -3.040  -4.506  0.38 42.34           S  
ANISOU 2191  SD BMET A 278     8683   4035   3370  -1250    350    104       S  
ATOM   2192  CE AMET A 278      30.668  -4.194  -5.071  0.62 30.83           C  
ANISOU 2192  CE AMET A 278     2690   4323   4701   -179    155  -2859       C  
ATOM   2193  CE BMET A 278      34.336  -3.735  -5.473  0.38 77.06           C  
ANISOU 2193  CE BMET A 278     8435  12972   7873  -7673   4721  -6392       C  
ATOM   2194  N   ILE A 279      33.281  -3.567   0.916  1.00 16.57           N  
ANISOU 2194  N   ILE A 279     2076   2186   2034   -128    763   -368       N  
ATOM   2195  CA  ILE A 279      33.419  -3.953   2.315  1.00 16.59           C  
ANISOU 2195  CA  ILE A 279     2251   1980   2074     13    932   -194       C  
ATOM   2196  C   ILE A 279      32.310  -4.988   2.603  1.00 15.56           C  
ANISOU 2196  C   ILE A 279     2179   1808   1926     14    557   -233       C  
ATOM   2197  O   ILE A 279      31.151  -4.625   2.686  1.00 16.84           O  
ANISOU 2197  O   ILE A 279     2178   1837   2385   -138    535   -240       O  
ATOM   2198  CB  ILE A 279      33.283  -2.771   3.281  1.00 16.49           C  
ANISOU 2198  CB  ILE A 279     1998   2144   2122   -264    513   -402       C  
ATOM   2199  CG1 ILE A 279      34.156  -1.578   2.883  1.00 17.09           C  
ANISOU 2199  CG1 ILE A 279     1969   2433   2093   -403    453   -337       C  
ATOM   2200  CG2 ILE A 279      33.587  -3.279   4.680  1.00 17.55           C  
ANISOU 2200  CG2 ILE A 279     2204   2321   2144   -131    639   -272       C  
ATOM   2201  CD1 ILE A 279      33.925  -0.369   3.776  1.00 19.65           C  
ANISOU 2201  CD1 ILE A 279     2297   2246   2922   -286    276   -540       C  
ATOM   2202  N   PRO A 280      32.655  -6.256   2.762  1.00 17.39           N  
ANISOU 2202  N   PRO A 280     2655   1872   2080    115    865   -209       N  
ATOM   2203  CA  PRO A 280      31.661  -7.309   2.969  1.00 17.19           C  
ANISOU 2203  CA  PRO A 280     2935   1682   1916    105    635   -209       C  
ATOM   2204  C   PRO A 280      31.316  -7.524   4.427  1.00 16.52           C  
ANISOU 2204  C   PRO A 280     2630   1736   1911    308    761   -167       C  
ATOM   2205  O   PRO A 280      32.065  -7.071   5.299  1.00 18.88           O  
ANISOU 2205  O   PRO A 280     3008   2146   2020    108    653   -221       O  
ATOM   2206  CB  PRO A 280      32.360  -8.598   2.445  1.00 20.69           C  
ANISOU 2206  CB  PRO A 280     3717   1881   2263     99   1280   -362       C  
ATOM   2207  CG  PRO A 280      33.776  -8.319   2.881  1.00 22.70           C  
ANISOU 2207  CG  PRO A 280     3246   1975   3406    465   1609   -180       C  
ATOM   2208  CD  PRO A 280      34.004  -6.833   2.687  1.00 19.67           C  
ANISOU 2208  CD  PRO A 280     2812   2014   2647    384    646    149       C  
ATOM   2209  N   ASP A 281      30.239  -8.229   4.656  1.00 20.46           N  
ANISOU 2209  N   ASP A 281     3506   1981   2286   -410   1197   -642       N  
ATOM   2210  CA  ASP A 281      29.894  -8.793   5.954  1.00 20.41           C  
ANISOU 2210  CA  ASP A 281     3546   1998   2211   -301   1146   -523       C  
ATOM   2211  C   ASP A 281      29.734  -7.688   6.998  1.00 17.38           C  
ANISOU 2211  C   ASP A 281     2776   1823   2004   -236    873   -285       C  
ATOM   2212  O   ASP A 281      30.054  -7.882   8.167  1.00 20.24           O  
ANISOU 2212  O   ASP A 281     3660   1975   2056    101    524   -313       O  
ATOM   2213  CB  ASP A 281      30.904  -9.855   6.422  1.00 27.47           C  
ANISOU 2213  CB  ASP A 281     5329   1955   3154    464    770   -554       C  
ATOM   2214  CG  ASP A 281      31.249 -10.885   5.355  1.00 31.56           C  
ANISOU 2214  CG  ASP A 281     5808   2902   3280   1013   1604   -589       C  
ATOM   2215  OD1 ASP A 281      32.454 -11.219   5.112  1.00 45.12           O  
ANISOU 2215  OD1 ASP A 281     6660   4495   5991   1761   3375    436       O  
ATOM   2216  OD2 ASP A 281      30.262 -11.370   4.746  1.00 39.97           O  
ANISOU 2216  OD2 ASP A 281     7497   3490   4200  -1757   2653  -1936       O  
ATOM   2217  N   VAL A 282      29.161  -6.571   6.610  1.00 16.42           N  
ANISOU 2217  N   VAL A 282     2621   1887   1731   -281    716   -356       N  
ATOM   2218  CA  VAL A 282      28.903  -5.455   7.544  1.00 15.26           C  
ANISOU 2218  CA  VAL A 282     2276   1940   1582   -233    537   -407       C  
ATOM   2219  C   VAL A 282      27.572  -5.693   8.252  1.00 15.43           C  
ANISOU 2219  C   VAL A 282     2199   2031   1630   -204    432   -335       C  
ATOM   2220  O   VAL A 282      26.506  -5.887   7.623  1.00 18.81           O  
ANISOU 2220  O   VAL A 282     2390   2983   1775   -716    358   -523       O  
ATOM   2221  CB  VAL A 282      28.925  -4.128   6.809  1.00 14.61           C  
ANISOU 2221  CB  VAL A 282     1893   1898   1760   -145    334   -347       C  
ATOM   2222  CG1 VAL A 282      28.555  -3.007   7.796  1.00 15.69           C  
ANISOU 2222  CG1 VAL A 282     1804   2036   2121   -202    485   -560       C  
ATOM   2223  CG2 VAL A 282      30.276  -3.841   6.185  1.00 15.11           C  
ANISOU 2223  CG2 VAL A 282     1995   2092   1656     98    486   -207       C  
ATOM   2224  N   ASP A 283      27.608  -5.715   9.595  1.00 14.19           N  
ANISOU 2224  N   ASP A 283     1995   1792   1606   -185    554   -449       N  
ATOM   2225  CA  ASP A 283      26.373  -5.857  10.382  1.00 15.37           C  
ANISOU 2225  CA  ASP A 283     2040   1947   1855   -284    542   -237       C  
ATOM   2226  C   ASP A 283      25.685  -4.536  10.615  1.00 16.85           C  
ANISOU 2226  C   ASP A 283     1975   2038   2391   -148    844   -280       C  
ATOM   2227  O   ASP A 283      24.455  -4.519  10.584  1.00 23.29           O  
ANISOU 2227  O   ASP A 283     1966   2532   4349   -260    555   -874       O  
ATOM   2228  CB  ASP A 283      26.682  -6.548  11.730  1.00 16.19           C  
ANISOU 2228  CB  ASP A 283     2353   2152   1646   -325    611   -282       C  
ATOM   2229  CG  ASP A 283      27.349  -7.891  11.516  1.00 18.01           C  
ANISOU 2229  CG  ASP A 283     2877   2053   1914   -260    317   -205       C  
ATOM   2230  OD1 ASP A 283      28.474  -8.056  12.003  1.00 19.55           O  
ANISOU 2230  OD1 ASP A 283     2863   2235   2329      3    293   -187       O  
ATOM   2231  OD2 ASP A 283      26.701  -8.754  10.842  1.00 23.52           O  
ANISOU 2231  OD2 ASP A 283     3292   2254   3391   -484    203   -797       O  
ATOM   2232  N   CYS A 284      26.433  -3.483  10.873  1.00 15.43           N  
ANISOU 2232  N   CYS A 284     1936   1765   2161     54    617    -12       N  
ATOM   2233  CA  CYS A 284      25.863  -2.173  11.170  1.00 14.66           C  
ANISOU 2233  CA  CYS A 284     1615   1777   2178     40    423    -80       C  
ATOM   2234  C   CYS A 284      26.524  -1.156  10.283  1.00 13.47           C  
ANISOU 2234  C   CYS A 284     1599   1722   1799     18    332   -184       C  
ATOM   2235  O   CYS A 284      27.718  -0.943  10.424  1.00 14.72           O  
ANISOU 2235  O   CYS A 284     1614   1944   2036     40    339    130       O  
ATOM   2236  CB  CYS A 284      26.031  -1.864  12.649  1.00 15.80           C  
ANISOU 2236  CB  CYS A 284     2026   2032   1945    202    598     45       C  
ATOM   2237  SG  CYS A 284      25.454  -0.265  13.185  1.00 18.71           S  
ANISOU 2237  SG  CYS A 284     2601   2283   2226    480    817   -120       S  
ATOM   2238  N   LEU A 285      25.724  -0.476   9.447  1.00 13.00           N  
ANISOU 2238  N   LEU A 285     1598   1668   1675     12    315   -346       N  
ATOM   2239  CA  LEU A 285      26.185   0.692   8.686  1.00 12.48           C  
ANISOU 2239  CA  LEU A 285     1576   1506   1659     -2    269   -425       C  
ATOM   2240  C   LEU A 285      25.475   1.849   9.309  1.00 11.87           C  
ANISOU 2240  C   LEU A 285     1378   1697   1436    165    172   -343       C  
ATOM   2241  O   LEU A 285      24.236   1.885   9.283  1.00 13.98           O  
ANISOU 2241  O   LEU A 285     1434   1933   1944     37    159   -515       O  
ATOM   2242  CB  LEU A 285      25.827   0.552   7.205  1.00 13.06           C  
ANISOU 2242  CB  LEU A 285     1588   1731   1644    -46    223   -486       C  
ATOM   2243  CG  LEU A 285      26.081   1.787   6.365  1.00 15.14           C  
ANISOU 2243  CG  LEU A 285     2164   1922   1665    100    284   -281       C  
ATOM   2244  CD1 LEU A 285      27.558   2.129   6.281  1.00 16.12           C  
ANISOU 2244  CD1 LEU A 285     2484   1938   1702   -424    417   -384       C  
ATOM   2245  CD2 LEU A 285      25.459   1.619   4.970  1.00 16.80           C  
ANISOU 2245  CD2 LEU A 285     2391   2414   1578    199    324   -461       C  
ATOM   2246  N   LEU A 286      26.195   2.788   9.865  1.00 11.66           N  
ANISOU 2246  N   LEU A 286     1353   1614   1462     96    295   -252       N  
ATOM   2247  CA  LEU A 286      25.629   3.904  10.640  1.00 11.59           C  
ANISOU 2247  CA  LEU A 286     1270   1550   1585     40    381   -302       C  
ATOM   2248  C   LEU A 286      25.972   5.203   9.908  1.00 11.56           C  
ANISOU 2248  C   LEU A 286     1280   1562   1550     12    449   -333       C  
ATOM   2249  O   LEU A 286      27.158   5.605   9.837  1.00 13.38           O  
ANISOU 2249  O   LEU A 286     1280   1730   2073    -10    447    -54       O  
ATOM   2250  CB  LEU A 286      26.146   3.890  12.088  1.00 13.47           C  
ANISOU 2250  CB  LEU A 286     1677   1968   1472   -145    402   -260       C  
ATOM   2251  CG  LEU A 286      25.400   4.693  13.172  1.00 17.54           C  
ANISOU 2251  CG  LEU A 286     2723   2232   1710    -84    358   -680       C  
ATOM   2252  CD1 LEU A 286      25.897   4.201  14.544  1.00 29.56           C  
ANISOU 2252  CD1 LEU A 286     6362   3470   1399   -129    540    -90       C  
ATOM   2253  CD2 LEU A 286      25.528   6.160  12.982  1.00 19.43           C  
ANISOU 2253  CD2 LEU A 286     2473   2303   2607     79   1008   -458       C  
ATOM   2254  N   TRP A 287      24.972   5.918   9.432  1.00 10.96           N  
ANISOU 2254  N   TRP A 287     1249   1558   1358    -59    410   -243       N  
ATOM   2255  CA  TRP A 287      25.101   7.230   8.843  1.00 11.27           C  
ANISOU 2255  CA  TRP A 287     1269   1615   1399    -90    300   -227       C  
ATOM   2256  C   TRP A 287      25.161   8.279   9.931  1.00 11.43           C  
ANISOU 2256  C   TRP A 287     1360   1524   1460     12    467   -239       C  
ATOM   2257  O   TRP A 287      24.148   8.425  10.656  1.00 12.78           O  
ANISOU 2257  O   TRP A 287     1461   1832   1563      9    548   -364       O  
ATOM   2258  CB  TRP A 287      23.946   7.540   7.915  1.00 12.36           C  
ANISOU 2258  CB  TRP A 287     1430   1856   1409    103    325   -219       C  
ATOM   2259  CG  TRP A 287      23.773   6.647   6.766  1.00 11.84           C  
ANISOU 2259  CG  TRP A 287     1574   1722   1203    123    207    -98       C  
ATOM   2260  CD1 TRP A 287      22.751   5.750   6.595  1.00 13.80           C  
ANISOU 2260  CD1 TRP A 287     1646   2113   1484    -95    421   -310       C  
ATOM   2261  CD2 TRP A 287      24.586   6.509   5.598  1.00 12.08           C  
ANISOU 2261  CD2 TRP A 287     1512   1822   1255     80    246   -256       C  
ATOM   2262  NE1 TRP A 287      22.870   5.075   5.408  1.00 14.52           N  
ANISOU 2262  NE1 TRP A 287     1834   2270   1411   -385    292   -299       N  
ATOM   2263  CE2 TRP A 287      24.019   5.544   4.774  1.00 13.31           C  
ANISOU 2263  CE2 TRP A 287     1620   1919   1517   -123    424   -377       C  
ATOM   2264  CE3 TRP A 287      25.746   7.147   5.179  1.00 12.64           C  
ANISOU 2264  CE3 TRP A 287     1428   1956   1420     50    235   -284       C  
ATOM   2265  CZ2 TRP A 287      24.568   5.155   3.542  1.00 14.37           C  
ANISOU 2265  CZ2 TRP A 287     1718   2251   1490     21    240   -598       C  
ATOM   2266  CZ3 TRP A 287      26.284   6.770   3.952  1.00 14.39           C  
ANISOU 2266  CZ3 TRP A 287     1727   2400   1339    -34    356   -267       C  
ATOM   2267  CH2 TRP A 287      25.695   5.805   3.176  1.00 14.19           C  
ANISOU 2267  CH2 TRP A 287     1664   2322   1405    219    444   -402       C  
ATOM   2268  N   ALA A 288      26.257   9.006  10.045  1.00 11.25           N  
ANISOU 2268  N   ALA A 288     1232   1572   1470     95    335   -290       N  
ATOM   2269  CA  ALA A 288      26.442  10.113  11.004  1.00 11.35           C  
ANISOU 2269  CA  ALA A 288     1222   1731   1360    -33    340   -272       C  
ATOM   2270  C   ALA A 288      26.977  11.311  10.211  1.00 11.70           C  
ANISOU 2270  C   ALA A 288     1300   1738   1405     72    394   -232       C  
ATOM   2271  O   ALA A 288      28.087  11.790  10.509  1.00 13.23           O  
ANISOU 2271  O   ALA A 288     1313   1843   1871    -56    391   -294       O  
ATOM   2272  CB  ALA A 288      27.326   9.703  12.151  1.00 12.44           C  
ANISOU 2272  CB  ALA A 288     1393   1836   1498    121    240   -215       C  
ATOM   2273  N   ILE A 289      26.167  11.754   9.272  1.00 12.40           N  
ANISOU 2273  N   ILE A 289     1331   1898   1485    -70    377    -36       N  
ATOM   2274  CA  ILE A 289      26.558  12.728   8.256  1.00 13.13           C  
ANISOU 2274  CA  ILE A 289     1609   1678   1703    -70    471    -31       C  
ATOM   2275  C   ILE A 289      25.892  14.079   8.427  1.00 13.78           C  
ANISOU 2275  C   ILE A 289     1704   1799   1733    -41    510    -18       C  
ATOM   2276  O   ILE A 289      26.172  15.011   7.655  1.00 20.43           O  
ANISOU 2276  O   ILE A 289     3551   1966   2245    337   1479    219       O  
ATOM   2277  CB  ILE A 289      26.303  12.179   6.857  1.00 13.95           C  
ANISOU 2277  CB  ILE A 289     1851   1892   1556    172    429    116       C  
ATOM   2278  CG1 ILE A 289      24.812  11.941   6.597  1.00 15.26           C  
ANISOU 2278  CG1 ILE A 289     1870   2398   1530     89    440   -333       C  
ATOM   2279  CG2 ILE A 289      27.103  10.931   6.616  1.00 16.17           C  
ANISOU 2279  CG2 ILE A 289     2035   2248   1859    284    546   -235       C  
ATOM   2280  CD1 ILE A 289      24.502  11.581   5.176  1.00 19.76           C  
ANISOU 2280  CD1 ILE A 289     2441   3443   1626   -291    420   -502       C  
ATOM   2281  N   GLY A 290      25.051  14.281   9.389  1.00 13.62           N  
ANISOU 2281  N   GLY A 290     1570   1791   1814    223    510    151       N  
ATOM   2282  CA  GLY A 290      24.459  15.566   9.706  1.00 15.03           C  
ANISOU 2282  CA  GLY A 290     1885   1872   1954    145    743     14       C  
ATOM   2283  C   GLY A 290      23.088  15.419  10.311  1.00 14.02           C  
ANISOU 2283  C   GLY A 290     1707   1859   1763    259    456    -37       C  
ATOM   2284  O   GLY A 290      22.627  14.307  10.574  1.00 14.82           O  
ANISOU 2284  O   GLY A 290     1466   1996   2169    175    450     63       O  
ATOM   2285  N   ARG A 291      22.472  16.562  10.548  1.00 14.71           N  
ANISOU 2285  N   ARG A 291     1835   1898   1857    272    607    -69       N  
ATOM   2286  CA  ARG A 291      21.170  16.697  11.186  1.00 13.86           C  
ANISOU 2286  CA  ARG A 291     1705   1974   1585    253    475     33       C  
ATOM   2287  C   ARG A 291      20.277  17.587  10.344  1.00 14.26           C  
ANISOU 2287  C   ARG A 291     2090   1773   1556    318    530     17       C  
ATOM   2288  O   ARG A 291      20.771  18.582   9.783  1.00 17.80           O  
ANISOU 2288  O   ARG A 291     2478   2214   2072    494    974    461       O  
ATOM   2289  CB  ARG A 291      21.278  17.343  12.582  1.00 18.00           C  
ANISOU 2289  CB  ARG A 291     2281   2941   1617    693    488   -247       C  
ATOM   2290  CG  ARG A 291      22.251  16.703  13.546  1.00 16.61           C  
ANISOU 2290  CG  ARG A 291     2131   2315   1864     24    263   -211       C  
ATOM   2291  CD  ARG A 291      21.635  15.441  14.185  1.00 17.34           C  
ANISOU 2291  CD  ARG A 291     1354   1674   3559    150     82   -137       C  
ATOM   2292  NE  ARG A 291      20.430  15.812  15.047  1.00 15.77           N  
ANISOU 2292  NE  ARG A 291     1964   1745   2284    297     96     71       N  
ATOM   2293  CZ  ARG A 291      19.667  14.906  15.623  1.00 14.43           C  
ANISOU 2293  CZ  ARG A 291     1767   1879   1837    528     44    -60       C  
ATOM   2294  NH1 ARG A 291      18.567  15.273  16.331  1.00 16.68           N  
ANISOU 2294  NH1 ARG A 291     1838   2182   2319    559    165   -472       N  
ATOM   2295  NH2 ARG A 291      19.931  13.619  15.523  1.00 14.10           N  
ANISOU 2295  NH2 ARG A 291     1763   1760   1833    200    139   -260       N  
ATOM   2296  N   VAL A 292      18.994  17.280  10.267  1.00 14.74           N  
ANISOU 2296  N   VAL A 292     1939   2099   1564    628    437     87       N  
ATOM   2297  CA  VAL A 292      17.999  18.047   9.531  1.00 16.86           C  
ANISOU 2297  CA  VAL A 292     2312   2743   1352   1073    656     84       C  
ATOM   2298  C   VAL A 292      16.970  18.565  10.524  1.00 13.25           C  
ANISOU 2298  C   VAL A 292     1779   1914   1343    496    484    -23       C  
ATOM   2299  O   VAL A 292      16.550  17.839  11.412  1.00 15.18           O  
ANISOU 2299  O   VAL A 292     2268   2042   1458    633    651     57       O  
ATOM   2300  CB AVAL A 292      17.482  17.284   8.303  0.54 21.68           C  
ANISOU 2300  CB AVAL A 292     2677   4288   1273   2190    260   -523       C  
ATOM   2301  CB BVAL A 292      17.215  16.991   8.673  0.46 20.65           C  
ANISOU 2301  CB BVAL A 292     3114   3802    931   1380     58   -553       C  
ATOM   2302  CG1AVAL A 292      18.594  17.232   7.251  0.54 28.83           C  
ANISOU 2302  CG1AVAL A 292     3604   5903   1446   1495    900   -471       C  
ATOM   2303  CG1BVAL A 292      16.072  17.614   7.895  0.46 19.34           C  
ANISOU 2303  CG1BVAL A 292     3578   2602   1168   1348     45   -352       C  
ATOM   2304  CG2AVAL A 292      17.031  15.933   8.767  0.54 27.59           C  
ANISOU 2304  CG2AVAL A 292     2394   5164   2926   -399    -69  -1411       C  
ATOM   2305  CG2BVAL A 292      18.115  16.179   7.752  0.46 18.76           C  
ANISOU 2305  CG2BVAL A 292     3008   2683   1436    849    804     42       C  
ATOM   2306  N   PRO A 293      16.531  19.816  10.391  1.00 12.21           N  
ANISOU 2306  N   PRO A 293     1521   1843   1275    248    359    -69       N  
ATOM   2307  CA  PRO A 293      15.574  20.375  11.359  1.00 12.00           C  
ANISOU 2307  CA  PRO A 293     1429   1629   1503    241    275   -148       C  
ATOM   2308  C   PRO A 293      14.161  19.811  11.164  1.00 12.18           C  
ANISOU 2308  C   PRO A 293     1414   1791   1421    203    214    -26       C  
ATOM   2309  O   PRO A 293      13.769  19.488  10.041  1.00 14.36           O  
ANISOU 2309  O   PRO A 293     1572   2337   1547   -122    288   -213       O  
ATOM   2310  CB  PRO A 293      15.611  21.854  11.037  1.00 13.26           C  
ANISOU 2310  CB  PRO A 293     1553   1819   1666    154    339     45       C  
ATOM   2311  CG  PRO A 293      15.918  21.888   9.568  1.00 14.08           C  
ANISOU 2311  CG  PRO A 293     1750   1941   1657    283    451     75       C  
ATOM   2312  CD  PRO A 293      16.947  20.789   9.388  1.00 14.31           C  
ANISOU 2312  CD  PRO A 293     1756   2073   1609    365    356    211       C  
ATOM   2313  N   ASN A 294      13.392  19.722  12.234  1.00 12.85           N  
ANISOU 2313  N   ASN A 294     1328   2005   1551    232    301   -114       N  
ATOM   2314  CA  ASN A 294      12.073  19.158  12.203  1.00 13.00           C  
ANISOU 2314  CA  ASN A 294     1420   2205   1313    -64    242   -283       C  
ATOM   2315  C   ASN A 294      11.038  20.268  11.972  1.00 13.38           C  
ANISOU 2315  C   ASN A 294     1337   2323   1423     24    334   -397       C  
ATOM   2316  O   ASN A 294      10.442  20.785  12.901  1.00 14.65           O  
ANISOU 2316  O   ASN A 294     1662   2350   1555    -14    349   -517       O  
ATOM   2317  CB AASN A 294      11.872  18.391  13.507  0.50 14.24           C  
ANISOU 2317  CB AASN A 294     1616   2349   1446   -277    263   -223       C  
ATOM   2318  CB BASN A 294      11.770  18.404  13.500  0.50 20.14           C  
ANISOU 2318  CB BASN A 294     2444   3113   2094  -1033   -163    664       C  
ATOM   2319  CG AASN A 294      10.784  17.371  13.472  0.50 13.24           C  
ANISOU 2319  CG AASN A 294     1309   2401   1319   -152    645   -532       C  
ATOM   2320  CG BASN A 294      12.159  16.956  13.251  0.50 19.70           C  
ANISOU 2320  CG BASN A 294     1683   3165   2637   -788     71   1160       C  
ATOM   2321  OD1AASN A 294       9.955  17.434  12.573  0.50 15.80           O  
ANISOU 2321  OD1AASN A 294     1550   1952   2503   -104    -61   -149       O  
ATOM   2322  OD1BASN A 294      11.597  16.375  12.355  0.50 29.16           O  
ANISOU 2322  OD1BASN A 294     4162   3913   3003   -638    344   -413       O  
ATOM   2323  ND2AASN A 294      10.725  16.468  14.471  0.50 13.70           N  
ANISOU 2323  ND2AASN A 294     1238   2460   1509   -371    379   -444       N  
ATOM   2324  ND2BASN A 294      13.049  16.392  13.997  0.50 45.08           N  
ANISOU 2324  ND2BASN A 294     3313   3721  10093  -1890  -3361   3512       N  
ATOM   2325  N   THR A 295      10.866  20.674  10.681  1.00 14.11           N  
ANISOU 2325  N   THR A 295     1297   2590   1476    208    216   -354       N  
ATOM   2326  CA  THR A 295       9.970  21.744  10.297  1.00 14.12           C  
ANISOU 2326  CA  THR A 295     1319   2448   1598    180    169   -502       C  
ATOM   2327  C   THR A 295       9.041  21.381   9.156  1.00 15.87           C  
ANISOU 2327  C   THR A 295     1327   3094   1609    106     48   -433       C  
ATOM   2328  O   THR A 295       8.102  22.155   8.929  1.00 18.10           O  
ANISOU 2328  O   THR A 295     1653   3429   1797    276   -159   -369       O  
ATOM   2329  CB  THR A 295      10.745  23.036   9.942  1.00 14.88           C  
ANISOU 2329  CB  THR A 295     1347   2634   1674    193    237   -150       C  
ATOM   2330  OG1 THR A 295      11.628  22.714   8.845  1.00 16.16           O  
ANISOU 2330  OG1 THR A 295     1855   2745   1539     72    261   -182       O  
ATOM   2331  CG2 THR A 295      11.585  23.562  11.072  1.00 15.49           C  
ANISOU 2331  CG2 THR A 295     1731   2267   1887    -26    368   -460       C  
ATOM   2332  N   LYS A 296       9.179  20.267   8.478  1.00 18.71           N  
ANISOU 2332  N   LYS A 296     1580   3712   1818    119     78   -978       N  
ATOM   2333  CA  LYS A 296       8.416  20.020   7.285  1.00 22.76           C  
ANISOU 2333  CA  LYS A 296     1811   4931   1906    -77    199  -1472       C  
ATOM   2334  C   LYS A 296       6.926  19.994   7.502  1.00 20.90           C  
ANISOU 2334  C   LYS A 296     1698   4113   2128   -153     86   -862       C  
ATOM   2335  O   LYS A 296       6.184  20.323   6.569  1.00 22.60           O  
ANISOU 2335  O   LYS A 296     2101   4263   2221    168     48   -585       O  
ATOM   2336  CB  LYS A 296       8.840  18.689   6.626  1.00 25.99           C  
ANISOU 2336  CB  LYS A 296     1840   5435   2598    186   -108  -2107       C  
ATOM   2337  N   ASP A 297       6.462  19.514   8.654  1.00 20.95           N  
ANISOU 2337  N   ASP A 297     2144   3647   2170    186    418   -811       N  
ATOM   2338  CA  ASP A 297       5.012  19.362   8.805  1.00 21.13           C  
ANISOU 2338  CA  ASP A 297     2220   3224   2585    -56    569   -580       C  
ATOM   2339  C   ASP A 297       4.406  20.399   9.762  1.00 17.83           C  
ANISOU 2339  C   ASP A 297     1766   3039   1970    184    134   -261       C  
ATOM   2340  O   ASP A 297       3.295  20.158  10.294  1.00 19.59           O  
ANISOU 2340  O   ASP A 297     1945   3004   2495    -20    422   -526       O  
ATOM   2341  CB  ASP A 297       4.781  17.939   9.280  1.00 27.44           C  
ANISOU 2341  CB  ASP A 297     3821   3121   3484    -26   1622   -665       C  
ATOM   2342  CG  ASP A 297       5.151  16.910   8.206  1.00 32.58           C  
ANISOU 2342  CG  ASP A 297     5033   3416   3929    156   2017   -925       C  
ATOM   2343  OD1 ASP A 297       4.969  17.181   7.001  1.00 56.56           O  
ANISOU 2343  OD1 ASP A 297    13592   4250   3648  -1969    870  -1503       O  
ATOM   2344  OD2 ASP A 297       5.575  15.834   8.665  1.00 46.97           O  
ANISOU 2344  OD2 ASP A 297     6345   4232   7268   2003   1126  -1123       O  
ATOM   2345  N   LEU A 298       5.097  21.522   9.960  1.00 16.22           N  
ANISOU 2345  N   LEU A 298     1540   3102   1520    200    190   -140       N  
ATOM   2346  CA  LEU A 298       4.622  22.568  10.851  1.00 15.59           C  
ANISOU 2346  CA  LEU A 298     1374   3042   1509     27    171   -180       C  
ATOM   2347  C   LEU A 298       3.669  23.543  10.172  1.00 15.99           C  
ANISOU 2347  C   LEU A 298     1572   3001   1505    161     58   -389       C  
ATOM   2348  O   LEU A 298       3.140  24.411  10.883  1.00 16.79           O  
ANISOU 2348  O   LEU A 298     1716   3082   1583    157    214   -371       O  
ATOM   2349  CB  LEU A 298       5.776  23.446  11.388  1.00 17.15           C  
ANISOU 2349  CB  LEU A 298     1474   3161   1880   -114     65    -10       C  
ATOM   2350  CG  LEU A 298       6.509  22.867  12.554  1.00 17.30           C  
ANISOU 2350  CG  LEU A 298     1768   2996   1808   -446      7    243       C  
ATOM   2351  CD1 LEU A 298       7.740  23.731  12.846  1.00 15.30           C  
ANISOU 2351  CD1 LEU A 298     1654   2342   1817    -89     73   -152       C  
ATOM   2352  CD2 LEU A 298       5.620  22.755  13.779  1.00 18.34           C  
ANISOU 2352  CD2 LEU A 298     1584   3412   1974   -209     30    273       C  
ATOM   2353  N   SER A 299       3.525  23.464   8.871  1.00 15.52           N  
ANISOU 2353  N   SER A 299     1758   2609   1530   -105    -90   -288       N  
ATOM   2354  CA  SER A 299       2.702  24.447   8.141  1.00 16.75           C  
ANISOU 2354  CA  SER A 299     1828   2778   1757     55    -78   -160       C  
ATOM   2355  C   SER A 299       3.190  25.867   8.332  1.00 16.35           C  
ANISOU 2355  C   SER A 299     1716   2705   1793    106    -56    -88       C  
ATOM   2356  O   SER A 299       2.436  26.831   8.456  1.00 17.34           O  
ANISOU 2356  O   SER A 299     1753   2744   2091    147     39     65       O  
ATOM   2357  CB  SER A 299       1.189  24.391   8.436  1.00 18.08           C  
ANISOU 2357  CB  SER A 299     1718   3155   1997    -94   -249   -254       C  
ATOM   2358  OG  SER A 299       0.689  23.120   8.026  1.00 21.91           O  
ANISOU 2358  OG  SER A 299     2039   3370   2917   -233   -381   -498       O  
ATOM   2359  N   LEU A 300       4.533  26.058   8.330  1.00 15.84           N  
ANISOU 2359  N   LEU A 300     1794   2539   1684     59    234   -323       N  
ATOM   2360  CA  LEU A 300       5.129  27.391   8.480  1.00 15.81           C  
ANISOU 2360  CA  LEU A 300     1520   2478   2007    230    211   -237       C  
ATOM   2361  C   LEU A 300       4.676  28.355   7.401  1.00 16.53           C  
ANISOU 2361  C   LEU A 300     1604   2505   2172    154    193   -162       C  
ATOM   2362  O   LEU A 300       4.541  29.560   7.631  1.00 17.42           O  
ANISOU 2362  O   LEU A 300     1837   2531   2252    160    149     29       O  
ATOM   2363  CB  LEU A 300       6.657  27.285   8.480  1.00 16.46           C  
ANISOU 2363  CB  LEU A 300     1612   2446   2194    159    144   -289       C  
ATOM   2364  CG  LEU A 300       7.328  26.472   9.566  1.00 16.33           C  
ANISOU 2364  CG  LEU A 300     1499   2391   2315    162    206   -161       C  
ATOM   2365  CD1 LEU A 300       8.815  26.427   9.269  1.00 18.80           C  
ANISOU 2365  CD1 LEU A 300     1439   2671   3034    170    221   -201       C  
ATOM   2366  CD2 LEU A 300       7.063  27.060  10.936  1.00 16.96           C  
ANISOU 2366  CD2 LEU A 300     1946   2261   2238    336    194     55       C  
ATOM   2367  N   ASN A 301       4.406  27.854   6.189  1.00 18.02           N  
ANISOU 2367  N   ASN A 301     2066   2879   1901    207    385      3       N  
ATOM   2368  CA  ASN A 301       3.983  28.708   5.104  1.00 21.38           C  
ANISOU 2368  CA  ASN A 301     2630   3563   1930    504    542    209       C  
ATOM   2369  C   ASN A 301       2.643  29.371   5.374  1.00 20.62           C  
ANISOU 2369  C   ASN A 301     2328   3674   1833    502     51    -40       C  
ATOM   2370  O   ASN A 301       2.380  30.420   4.755  1.00 24.01           O  
ANISOU 2370  O   ASN A 301     3043   4058   2023    822     34    237       O  
ATOM   2371  CB AASN A 301       4.036  28.020   3.744  0.38 23.39           C  
ANISOU 2371  CB AASN A 301     3286   3817   1785    466    806    321       C  
ATOM   2372  CB BASN A 301       3.765  27.788   3.889  0.62 27.42           C  
ANISOU 2372  CB BASN A 301     3627   4635   2156   1660   -211   -399       C  
ATOM   2373  CG AASN A 301       5.388  27.797   3.122  0.38 27.68           C  
ANISOU 2373  CG AASN A 301     3649   4793   2076    821   1173    329       C  
ATOM   2374  CG BASN A 301       2.500  26.932   3.986  0.62 37.01           C  
ANISOU 2374  CG BASN A 301     6458   5423   2180   -773   -744   -644       C  
ATOM   2375  OD1AASN A 301       5.553  26.832   2.349  0.38 35.17           O  
ANISOU 2375  OD1AASN A 301     4813   6008   2540    786   1651   -570       O  
ATOM   2376  OD1BASN A 301       2.277  26.136   4.912  0.62 33.78           O  
ANISOU 2376  OD1BASN A 301     3958   6881   1995    932    483   -131       O  
ATOM   2377  ND2AASN A 301       6.421  28.593   3.354  0.38 31.53           N  
ANISOU 2377  ND2AASN A 301     2791   7258   1930    802    640   -558       N  
ATOM   2378  ND2BASN A 301       1.604  27.060   2.996  0.62 47.10           N  
ANISOU 2378  ND2BASN A 301     7471   7480   2946  -3575  -1709   1382       N  
ATOM   2379  N   LYS A 302       1.859  28.813   6.292  1.00 19.44           N  
ANISOU 2379  N   LYS A 302     1977   3507   1902    233   -116   -371       N  
ATOM   2380  CA  LYS A 302       0.544  29.436   6.511  1.00 19.81           C  
ANISOU 2380  CA  LYS A 302     2141   3567   1818    256     35   -279       C  
ATOM   2381  C   LYS A 302       0.707  30.812   7.154  1.00 19.39           C  
ANISOU 2381  C   LYS A 302     1724   3483   2159    447   -181   -179       C  
ATOM   2382  O   LYS A 302      -0.260  31.593   7.082  1.00 22.61           O  
ANISOU 2382  O   LYS A 302     2055   3387   3151    554   -600    153       O  
ATOM   2383  CB  LYS A 302      -0.353  28.512   7.334  1.00 19.86           C  
ANISOU 2383  CB  LYS A 302     2037   3365   2143    614    -30    173       C  
ATOM   2384  CG  LYS A 302      -0.806  27.268   6.572  1.00 23.15           C  
ANISOU 2384  CG  LYS A 302     2756   3839   2199    -99   -549    327       C  
ATOM   2385  CD  LYS A 302      -1.882  26.503   7.325  1.00 24.21           C  
ANISOU 2385  CD  LYS A 302     2481   4095   2621    -18   -611    729       C  
ATOM   2386  CE  LYS A 302      -2.411  25.335   6.543  1.00 31.87           C  
ANISOU 2386  CE  LYS A 302     3578   4883   3650  -1043   -212    165       C  
ATOM   2387  NZ  LYS A 302      -3.495  24.570   7.213  1.00 38.46           N  
ANISOU 2387  NZ  LYS A 302     2753   6366   5493  -1496   -897   1068       N  
ATOM   2388  N   LEU A 303       1.821  31.080   7.819  1.00 18.70           N  
ANISOU 2388  N   LEU A 303     1655   3297   2154    271   -114    -62       N  
ATOM   2389  CA  LEU A 303       2.099  32.359   8.428  1.00 18.17           C  
ANISOU 2389  CA  LEU A 303     1865   3041   1997    392    -21    111       C  
ATOM   2390  C   LEU A 303       3.295  33.079   7.814  1.00 17.04           C  
ANISOU 2390  C   LEU A 303     1808   2667   1999    621    -49    229       C  
ATOM   2391  O   LEU A 303       3.719  34.133   8.270  1.00 19.46           O  
ANISOU 2391  O   LEU A 303     2070   2733   2591    493    -50     86       O  
ATOM   2392  CB  LEU A 303       2.343  32.209   9.918  1.00 17.92           C  
ANISOU 2392  CB  LEU A 303     1890   2945   1975    513    175    -19       C  
ATOM   2393  CG  LEU A 303       1.090  31.855  10.714  1.00 19.41           C  
ANISOU 2393  CG  LEU A 303     1941   3309   2127    628    221    212       C  
ATOM   2394  CD1 LEU A 303       1.482  31.476  12.140  1.00 25.04           C  
ANISOU 2394  CD1 LEU A 303     2034   5160   2319     46     29    773       C  
ATOM   2395  CD2 LEU A 303       0.080  32.984  10.694  1.00 26.49           C  
ANISOU 2395  CD2 LEU A 303     2559   3922   3586   1241   1281    942       C  
ATOM   2396  N   GLY A 304       3.904  32.502   6.783  1.00 17.31           N  
ANISOU 2396  N   GLY A 304     1649   3094   1836    671   -117    202       N  
ATOM   2397  CA  GLY A 304       5.043  33.090   6.106  1.00 20.35           C  
ANISOU 2397  CA  GLY A 304     1809   3775   2149    560     -8    635       C  
ATOM   2398  C   GLY A 304       6.330  33.056   6.993  1.00 18.40           C  
ANISOU 2398  C   GLY A 304     1859   3115   2019    194    -65    826       C  
ATOM   2399  O   GLY A 304       7.178  33.937   6.843  1.00 18.60           O  
ANISOU 2399  O   GLY A 304     2374   2675   2018    183   -113    711       O  
ATOM   2400  N   ILE A 305       6.456  32.071   7.899  1.00 15.22           N  
ANISOU 2400  N   ILE A 305     1556   2529   1698    289    243    365       N  
ATOM   2401  CA  ILE A 305       7.643  32.021   8.753  1.00 14.13           C  
ANISOU 2401  CA  ILE A 305     1682   2103   1586    369    223    342       C  
ATOM   2402  C   ILE A 305       8.861  31.608   7.903  1.00 14.17           C  
ANISOU 2402  C   ILE A 305     1692   2112   1580    381    227    215       C  
ATOM   2403  O   ILE A 305       8.825  30.619   7.170  1.00 16.82           O  
ANISOU 2403  O   ILE A 305     1873   2271   2247    234    262   -121       O  
ATOM   2404  CB  ILE A 305       7.406  31.068   9.925  1.00 14.03           C  
ANISOU 2404  CB  ILE A 305     1460   2243   1626    247    168    334       C  
ATOM   2405  CG1 ILE A 305       6.272  31.562  10.844  1.00 15.43           C  
ANISOU 2405  CG1 ILE A 305     1604   2720   1540    363    208    435       C  
ATOM   2406  CG2 ILE A 305       8.680  30.777  10.708  1.00 14.91           C  
ANISOU 2406  CG2 ILE A 305     1605   2432   1629    308     89    288       C  
ATOM   2407  CD1 ILE A 305       5.605  30.489  11.673  1.00 16.06           C  
ANISOU 2407  CD1 ILE A 305     1760   2525   1818    364    433    336       C  
ATOM   2408  N   GLN A 306       9.922  32.370   8.031  1.00 13.78           N  
ANISOU 2408  N   GLN A 306     1733   2042   1459    373    236    215       N  
ATOM   2409  CA  GLN A 306      11.118  32.240   7.190  1.00 14.07           C  
ANISOU 2409  CA  GLN A 306     1695   2267   1384    285    158    270       C  
ATOM   2410  C   GLN A 306      11.994  31.093   7.598  1.00 12.78           C  
ANISOU 2410  C   GLN A 306     1411   2115   1330    118    210    215       C  
ATOM   2411  O   GLN A 306      12.304  30.891   8.785  1.00 13.04           O  
ANISOU 2411  O   GLN A 306     1573   2120   1261    265    210    196       O  
ATOM   2412  CB  GLN A 306      11.872  33.549   7.283  1.00 14.90           C  
ANISOU 2412  CB  GLN A 306     1983   2143   1536    325    383    233       C  
ATOM   2413  CG  GLN A 306      13.072  33.601   6.337  1.00 16.53           C  
ANISOU 2413  CG  GLN A 306     2219   2300   1763     88    577    149       C  
ATOM   2414  CD  GLN A 306      13.839  34.898   6.519  1.00 16.04           C  
ANISOU 2414  CD  GLN A 306     2217   2500   1376     25    364    108       C  
ATOM   2415  OE1 GLN A 306      13.381  35.828   7.211  1.00 18.35           O  
ANISOU 2415  OE1 GLN A 306     2861   2184   1929    -92    901    164       O  
ATOM   2416  NE2 GLN A 306      15.002  34.997   5.906  1.00 17.68           N  
ANISOU 2416  NE2 GLN A 306     2537   2267   1914    -41    691    545       N  
ATOM   2417  N   THR A 307      12.432  30.328   6.592  1.00 13.75           N  
ANISOU 2417  N   THR A 307     1696   2348   1178    247    206    213       N  
ATOM   2418  CA  THR A 307      13.380  29.217   6.760  1.00 13.40           C  
ANISOU 2418  CA  THR A 307     1806   2098   1189    168    341    180       C  
ATOM   2419  C   THR A 307      14.540  29.374   5.739  1.00 14.60           C  
ANISOU 2419  C   THR A 307     2157   2140   1251    360    561    259       C  
ATOM   2420  O   THR A 307      14.377  30.067   4.730  1.00 16.71           O  
ANISOU 2420  O   THR A 307     2373   2636   1341    551    664    442       O  
ATOM   2421  CB  THR A 307      12.751  27.820   6.582  1.00 15.22           C  
ANISOU 2421  CB  THR A 307     2097   2254   1432     53    367     -6       C  
ATOM   2422  OG1 THR A 307      12.138  27.758   5.301  1.00 18.52           O  
ANISOU 2422  OG1 THR A 307     2932   2626   1481   -196    152    -74       O  
ATOM   2423  CG2 THR A 307      11.701  27.515   7.631  1.00 16.57           C  
ANISOU 2423  CG2 THR A 307     2269   2537   1491   -444    450   -204       C  
ATOM   2424  N   ASP A 308      15.657  28.696   6.026  1.00 14.39           N  
ANISOU 2424  N   ASP A 308     2096   1935   1436    366    521    147       N  
ATOM   2425  CA  ASP A 308      16.731  28.564   5.002  1.00 15.68           C  
ANISOU 2425  CA  ASP A 308     2146   2286   1527    147    708    247       C  
ATOM   2426  C   ASP A 308      16.378  27.402   4.096  1.00 18.17           C  
ANISOU 2426  C   ASP A 308     2592   2626   1687     88    850    -59       C  
ATOM   2427  O   ASP A 308      15.346  26.740   4.240  1.00 17.58           O  
ANISOU 2427  O   ASP A 308     2428   2675   1577     18    550   -144       O  
ATOM   2428  CB  ASP A 308      18.098  28.438   5.626  1.00 16.76           C  
ANISOU 2428  CB  ASP A 308     2072   2362   1935     96    772    447       C  
ATOM   2429  CG  ASP A 308      18.376  27.217   6.391  1.00 14.62           C  
ANISOU 2429  CG  ASP A 308     1834   2106   1614    130    812    135       C  
ATOM   2430  OD1 ASP A 308      17.581  26.254   6.330  1.00 16.40           O  
ANISOU 2430  OD1 ASP A 308     2320   2185   1724    -75    805     30       O  
ATOM   2431  OD2 ASP A 308      19.423  27.167   7.041  1.00 17.97           O  
ANISOU 2431  OD2 ASP A 308     1942   2625   2262    175    598    390       O  
ATOM   2432  N   ASP A 309      17.289  27.146   3.137  1.00 20.81           N  
ANISOU 2432  N   ASP A 309     3090   2871   1945    125   1265     29       N  
ATOM   2433  CA  ASP A 309      17.024  26.085   2.164  1.00 22.70           C  
ANISOU 2433  CA  ASP A 309     3914   3222   1487    407   1099     45       C  
ATOM   2434  C   ASP A 309      17.075  24.686   2.753  1.00 22.98           C  
ANISOU 2434  C   ASP A 309     4459   2955   1319    283    868   -311       C  
ATOM   2435  O   ASP A 309      16.571  23.759   2.118  1.00 29.38           O  
ANISOU 2435  O   ASP A 309     5811   3442   1911   -247    -80   -234       O  
ATOM   2436  CB AASP A 309      18.074  26.222   1.058  0.70 25.89           C  
ANISOU 2436  CB AASP A 309     4212   3674   1950   1317   1533    514       C  
ATOM   2437  CB BASP A 309      17.936  26.205   0.951  0.29 25.79           C  
ANISOU 2437  CB BASP A 309     4160   3545   2094    950   1654    192       C  
ATOM   2438  CG AASP A 309      19.554  26.044   1.393  0.70 30.38           C  
ANISOU 2438  CG AASP A 309     4012   3924   3607   1228   1543   -821       C  
ATOM   2439  CG BASP A 309      17.647  27.387   0.047  0.29 22.55           C  
ANISOU 2439  CG BASP A 309     3167   3327   2075    626   2034    188       C  
ATOM   2440  OD1AASP A 309      19.912  26.269   2.577  0.70 38.71           O  
ANISOU 2440  OD1AASP A 309     3811   6943   3956  -1017    995   -296       O  
ATOM   2441  OD1BASP A 309      16.467  27.734  -0.177  0.29 30.48           O  
ANISOU 2441  OD1BASP A 309     3511   5357   2715   1118   1621    977       O  
ATOM   2442  OD2AASP A 309      20.405  25.719   0.516  0.70 42.39           O  
ANISOU 2442  OD2AASP A 309     4002   6362   5742   -468   2877  -1899       O  
ATOM   2443  OD2BASP A 309      18.646  27.953  -0.450  0.29 31.66           O  
ANISOU 2443  OD2BASP A 309     3876   5611   2543  -1551    787    703       O  
ATOM   2444  N   LYS A 310      17.632  24.536   3.917  1.00 18.79           N  
ANISOU 2444  N   LYS A 310     2882   2664   1593    248    956   -222       N  
ATOM   2445  CA  LYS A 310      17.650  23.280   4.657  1.00 19.23           C  
ANISOU 2445  CA  LYS A 310     2813   2720   1773    204    805   -128       C  
ATOM   2446  C   LYS A 310      16.480  23.094   5.634  1.00 17.65           C  
ANISOU 2446  C   LYS A 310     2883   2028   1797    217    843   -299       C  
ATOM   2447  O   LYS A 310      16.372  22.026   6.245  1.00 20.23           O  
ANISOU 2447  O   LYS A 310     3308   2230   2149    384    949     42       O  
ATOM   2448  CB ALYS A 310      18.997  23.194   5.379  0.40 22.39           C  
ANISOU 2448  CB ALYS A 310     2817   3133   2557    486    581   -184       C  
ATOM   2449  CB BLYS A 310      18.989  23.187   5.383  0.60 21.41           C  
ANISOU 2449  CB BLYS A 310     2836   3036   2265    548    649   -391       C  
ATOM   2450  CG ALYS A 310      20.164  23.300   4.411  0.40 25.10           C  
ANISOU 2450  CG ALYS A 310     2813   3751   2974    606    754   -146       C  
ATOM   2451  CG BLYS A 310      20.199  23.022   4.506  0.60 23.74           C  
ANISOU 2451  CG BLYS A 310     2927   3463   2631    596    875   -171       C  
ATOM   2452  CD ALYS A 310      20.425  21.964   3.745  0.40 26.91           C  
ANISOU 2452  CD ALYS A 310     3047   3858   3320    784   1117   -200       C  
ATOM   2453  CD BLYS A 310      21.503  23.394   5.192  0.60 31.15           C  
ANISOU 2453  CD BLYS A 310     2839   4937   4059    495    574   -338       C  
ATOM   2454  CE ALYS A 310      21.469  22.024   2.625  0.40 28.85           C  
ANISOU 2454  CE ALYS A 310     2861   4458   3641    885   1216   -204       C  
ATOM   2455  CE BLYS A 310      22.713  22.616   4.705  0.60 36.85           C  
ANISOU 2455  CE BLYS A 310     3090   5677   5234   1042   -124  -1492       C  
ATOM   2456  NZ ALYS A 310      21.315  20.810   1.773  0.40 30.28           N  
ANISOU 2456  NZ ALYS A 310     2845   4732   3927    927   1522   -553       N  
ATOM   2457  NZ BLYS A 310      23.882  23.470   4.324  0.60 45.48           N  
ANISOU 2457  NZ BLYS A 310     3097   8081   6104   1027   1345   -487       N  
ATOM   2458  N   GLY A 311      15.617  24.070   5.764  1.00 16.53           N  
ANISOU 2458  N   GLY A 311     2506   2285   1488    273    483    -70       N  
ATOM   2459  CA  GLY A 311      14.482  23.949   6.683  1.00 15.66           C  
ANISOU 2459  CA  GLY A 311     2023   2375   1553    -60    268   -303       C  
ATOM   2460  C   GLY A 311      14.661  24.581   8.038  1.00 13.26           C  
ANISOU 2460  C   GLY A 311     1856   1752   1431     68    322    -57       C  
ATOM   2461  O   GLY A 311      13.749  24.455   8.869  1.00 14.24           O  
ANISOU 2461  O   GLY A 311     1642   2192   1578    140    350    -51       O  
ATOM   2462  N   HIS A 312      15.823  25.184   8.313  1.00 12.92           N  
ANISOU 2462  N   HIS A 312     1760   1804   1345     80    305     26       N  
ATOM   2463  CA  HIS A 312      16.013  25.785   9.627  1.00 11.83           C  
ANISOU 2463  CA  HIS A 312     1553   1574   1369    145    249     30       C  
ATOM   2464  C   HIS A 312      15.148  27.036   9.773  1.00 11.53           C  
ANISOU 2464  C   HIS A 312     1407   1703   1271    144    317    196       C  
ATOM   2465  O   HIS A 312      15.079  27.820   8.823  1.00 13.31           O  
ANISOU 2465  O   HIS A 312     1912   1818   1326    384    552    299       O  
ATOM   2466  CB  HIS A 312      17.455  26.163   9.875  1.00 12.22           C  
ANISOU 2466  CB  HIS A 312     1514   1711   1417    113    318     99       C  
ATOM   2467  CG  HIS A 312      18.429  25.047   9.858  1.00 13.11           C  
ANISOU 2467  CG  HIS A 312     1559   1940   1482    252    429    189       C  
ATOM   2468  ND1 HIS A 312      19.326  24.881   8.804  1.00 16.46           N  
ANISOU 2468  ND1 HIS A 312     1895   2409   1950    476    824    344       N  
ATOM   2469  CD2 HIS A 312      18.662  24.019  10.720  1.00 14.09           C  
ANISOU 2469  CD2 HIS A 312     1545   2018   1790    467    389    240       C  
ATOM   2470  CE1 HIS A 312      20.054  23.775   9.050  1.00 16.18           C  
ANISOU 2470  CE1 HIS A 312     1670   2233   2245    278    663    164       C  
ATOM   2471  NE2 HIS A 312      19.705  23.243  10.204  1.00 14.87           N  
ANISOU 2471  NE2 HIS A 312     1645   1934   2072    382    448     49       N  
ATOM   2472  N   ILE A 313      14.596  27.252  10.950  1.00 11.79           N  
ANISOU 2472  N   ILE A 313     1411   1775   1293    266    335    188       N  
ATOM   2473  CA  ILE A 313      13.888  28.506  11.207  1.00 11.29           C  
ANISOU 2473  CA  ILE A 313     1296   1793   1202    255    270    241       C  
ATOM   2474  C   ILE A 313      14.912  29.623  11.356  1.00 11.33           C  
ANISOU 2474  C   ILE A 313     1388   1677   1238    267    337    243       C  
ATOM   2475  O   ILE A 313      15.880  29.467  12.134  1.00 12.55           O  
ANISOU 2475  O   ILE A 313     1534   1824   1412    135    155    368       O  
ATOM   2476  CB AILE A 313      13.103  28.428  12.540  0.54 11.38           C  
ANISOU 2476  CB AILE A 313     1420   1702   1203    263    323    402       C  
ATOM   2477  CB BILE A 313      12.856  28.376  12.323  0.46 11.44           C  
ANISOU 2477  CB BILE A 313     1306   1842   1199    176    265    292       C  
ATOM   2478  CG1AILE A 313      12.156  27.248  12.659  0.54 12.99           C  
ANISOU 2478  CG1AILE A 313     1276   2028   1631    173    331    392       C  
ATOM   2479  CG1BILE A 313      11.885  27.258  11.935  0.46 12.79           C  
ANISOU 2479  CG1BILE A 313     1450   2024   1384      0    -65    429       C  
ATOM   2480  CG2AILE A 313      12.450  29.788  12.779  0.54 13.06           C  
ANISOU 2480  CG2AILE A 313     1742   2015   1206    560   -122   -119       C  
ATOM   2481  CG2BILE A 313      12.195  29.716  12.575  0.46 11.58           C  
ANISOU 2481  CG2BILE A 313     1054   1897   1447     91    606    503       C  
ATOM   2482  CD1AILE A 313      11.041  27.309  11.639  0.54 14.71           C  
ANISOU 2482  CD1AILE A 313     1644   2062   1882    341     12    -76       C  
ATOM   2483  CD1BILE A 313      10.961  26.920  13.084  0.46 12.86           C  
ANISOU 2483  CD1BILE A 313     1222   1890   1774    186    277    112       C  
ATOM   2484  N   ILE A 314      14.711  30.729  10.641  1.00 11.01           N  
ANISOU 2484  N   ILE A 314     1367   1808   1007    127    340    231       N  
ATOM   2485  CA  ILE A 314      15.626  31.861  10.732  1.00 10.67           C  
ANISOU 2485  CA  ILE A 314     1291   1624   1140    253    221    188       C  
ATOM   2486  C   ILE A 314      15.258  32.720  11.949  1.00 11.40           C  
ANISOU 2486  C   ILE A 314     1464   1774   1094    173    402    196       C  
ATOM   2487  O   ILE A 314      14.076  33.010  12.154  1.00 12.31           O  
ANISOU 2487  O   ILE A 314     1337   2015   1324    230    358    202       O  
ATOM   2488  CB  ILE A 314      15.610  32.707   9.453  1.00 11.92           C  
ANISOU 2488  CB  ILE A 314     1570   1861   1097     52    359    259       C  
ATOM   2489  CG1 ILE A 314      15.893  31.791   8.206  1.00 12.92           C  
ANISOU 2489  CG1 ILE A 314     1902   1859   1147      6    370    257       C  
ATOM   2490  CG2 ILE A 314      16.569  33.862   9.527  1.00 13.35           C  
ANISOU 2490  CG2 ILE A 314     2156   1826   1091    -86    343    269       C  
ATOM   2491  CD1 ILE A 314      17.159  30.994   8.342  1.00 15.23           C  
ANISOU 2491  CD1 ILE A 314     1843   2520   1425    185    590   -219       C  
ATOM   2492  N   VAL A 315      16.272  33.118  12.738  1.00 10.95           N  
ANISOU 2492  N   VAL A 315     1395   1615   1150    153    371    209       N  
ATOM   2493  CA  VAL A 315      16.042  33.969  13.883  1.00 11.14           C  
ANISOU 2493  CA  VAL A 315     1240   1860   1133     87    331    168       C  
ATOM   2494  C   VAL A 315      17.051  35.086  13.915  1.00 11.26           C  
ANISOU 2494  C   VAL A 315     1304   1704   1269    133    408    264       C  
ATOM   2495  O   VAL A 315      18.144  34.978  13.315  1.00 12.42           O  
ANISOU 2495  O   VAL A 315     1451   1769   1500     80    550    271       O  
ATOM   2496  CB  VAL A 315      16.051  33.162  15.182  1.00 11.16           C  
ANISOU 2496  CB  VAL A 315     1339   1671   1231    127    327    202       C  
ATOM   2497  CG1 VAL A 315      14.872  32.218  15.313  1.00 11.54           C  
ANISOU 2497  CG1 VAL A 315     1451   1568   1366     72    312    170       C  
ATOM   2498  CG2 VAL A 315      17.409  32.459  15.408  1.00 12.22           C  
ANISOU 2498  CG2 VAL A 315     1377   1749   1516    132    341    261       C  
ATOM   2499  N   ASP A 316      16.731  36.126  14.663  1.00 11.97           N  
ANISOU 2499  N   ASP A 316     1445   1750   1353     61    480    231       N  
ATOM   2500  CA  ASP A 316      17.634  37.176  15.038  1.00 12.16           C  
ANISOU 2500  CA  ASP A 316     1598   1581   1440     51    464    355       C  
ATOM   2501  C   ASP A 316      18.357  36.814  16.366  1.00 11.26           C  
ANISOU 2501  C   ASP A 316     1389   1513   1376    212    474    203       C  
ATOM   2502  O   ASP A 316      18.192  35.731  16.942  1.00 12.26           O  
ANISOU 2502  O   ASP A 316     1501   1660   1498    201    480    319       O  
ATOM   2503  CB  ASP A 316      16.960  38.564  15.081  1.00 12.83           C  
ANISOU 2503  CB  ASP A 316     1736   1704   1433    276    304    401       C  
ATOM   2504  CG  ASP A 316      16.007  38.740  16.260  1.00 12.78           C  
ANISOU 2504  CG  ASP A 316     1689   1470   1697    128    390    255       C  
ATOM   2505  OD1 ASP A 316      15.285  39.796  16.234  1.00 14.48           O  
ANISOU 2505  OD1 ASP A 316     1885   1692   1925    357    550    411       O  
ATOM   2506  OD2 ASP A 316      15.924  37.857  17.139  1.00 12.19           O  
ANISOU 2506  OD2 ASP A 316     1545   1655   1433    189    338    325       O  
ATOM   2507  N   GLU A 317      19.125  37.742  16.912  1.00 12.47           N  
ANISOU 2507  N   GLU A 317     1591   1569   1580    139    402    279       N  
ATOM   2508  CA  GLU A 317      19.926  37.506  18.135  1.00 12.63           C  
ANISOU 2508  CA  GLU A 317     1366   1835   1599    -29    365    300       C  
ATOM   2509  C   GLU A 317      19.064  37.318  19.395  1.00 11.86           C  
ANISOU 2509  C   GLU A 317     1453   1566   1487     34    299    162       C  
ATOM   2510  O   GLU A 317      19.570  36.785  20.381  1.00 12.10           O  
ANISOU 2510  O   GLU A 317     1319   1680   1599     32    353    253       O  
ATOM   2511  CB  GLU A 317      20.885  38.667  18.340  1.00 13.81           C  
ANISOU 2511  CB  GLU A 317     1500   1895   1853   -102    427    460       C  
ATOM   2512  CG  GLU A 317      20.282  39.969  18.672  1.00 16.94           C  
ANISOU 2512  CG  GLU A 317     2247   1852   2339   -105    298    293       C  
ATOM   2513  CD  GLU A 317      21.158  41.177  18.845  1.00 26.12           C  
ANISOU 2513  CD  GLU A 317     3652   2186   4088   -694     39    -35       C  
ATOM   2514  OE1 GLU A 317      20.743  42.273  18.376  1.00 35.57           O  
ANISOU 2514  OE1 GLU A 317     5382   2007   6127   -282   1801    776       O  
ATOM   2515  OE2 GLU A 317      22.241  41.035  19.416  1.00 53.70           O  
ANISOU 2515  OE2 GLU A 317     6354   6573   7477  -4070  -3877   3357       O  
ATOM   2516  N   PHE A 318      17.787  37.713  19.329  1.00 11.26           N  
ANISOU 2516  N   PHE A 318     1419   1495   1365     52    368    127       N  
ATOM   2517  CA  PHE A 318      16.838  37.531  20.381  1.00 10.79           C  
ANISOU 2517  CA  PHE A 318     1302   1478   1319     80    312    105       C  
ATOM   2518  C   PHE A 318      15.899  36.330  20.174  1.00 10.57           C  
ANISOU 2518  C   PHE A 318     1180   1542   1293     84    241    146       C  
ATOM   2519  O   PHE A 318      14.896  36.188  20.910  1.00 11.71           O  
ANISOU 2519  O   PHE A 318     1407   1583   1459    203    643    151       O  
ATOM   2520  CB  PHE A 318      15.989  38.830  20.492  1.00 12.48           C  
ANISOU 2520  CB  PHE A 318     1532   1549   1659    177    382    119       C  
ATOM   2521  CG  PHE A 318      16.827  40.008  20.958  1.00 13.60           C  
ANISOU 2521  CG  PHE A 318     1376   1595   2196     95    587     53       C  
ATOM   2522  CD1 PHE A 318      17.145  41.001  20.045  1.00 19.12           C  
ANISOU 2522  CD1 PHE A 318     2629   1883   2754   -221   1134    254       C  
ATOM   2523  CD2 PHE A 318      17.219  40.115  22.269  1.00 15.65           C  
ANISOU 2523  CD2 PHE A 318     1566   2118   2261     67    430   -428       C  
ATOM   2524  CE1 PHE A 318      17.897  42.082  20.491  1.00 23.89           C  
ANISOU 2524  CE1 PHE A 318     2862   1732   4481   -309   1299      1       C  
ATOM   2525  CE2 PHE A 318      17.985  41.160  22.739  1.00 20.91           C  
ANISOU 2525  CE2 PHE A 318     1795   2360   3792    229   -167   -975       C  
ATOM   2526  CZ  PHE A 318      18.292  42.151  21.800  1.00 25.02           C  
ANISOU 2526  CZ  PHE A 318     2390   2162   4955   -376    760  -1010       C  
ATOM   2527  N   GLN A 319      16.197  35.473  19.221  1.00 10.68           N  
ANISOU 2527  N   GLN A 319     1227   1430   1400    184    365     49       N  
ATOM   2528  CA  GLN A 319      15.390  34.296  18.900  1.00 10.18           C  
ANISOU 2528  CA  GLN A 319     1298   1424   1145    241    256    166       C  
ATOM   2529  C   GLN A 319      14.055  34.636  18.297  1.00  9.47           C  
ANISOU 2529  C   GLN A 319     1124   1386   1090    253    337    198       C  
ATOM   2530  O   GLN A 319      13.163  33.782  18.184  1.00 10.76           O  
ANISOU 2530  O   GLN A 319     1220   1502   1365    145    318    196       O  
ATOM   2531  CB  GLN A 319      15.215  33.339  20.111  1.00 10.68           C  
ANISOU 2531  CB  GLN A 319     1201   1636   1222    207    256    218       C  
ATOM   2532  CG  GLN A 319      16.524  33.057  20.861  1.00 10.16           C  
ANISOU 2532  CG  GLN A 319     1198   1425   1238    111    290    195       C  
ATOM   2533  CD  GLN A 319      17.643  32.328  20.151  1.00 10.13           C  
ANISOU 2533  CD  GLN A 319     1054   1429   1368    105    339    296       C  
ATOM   2534  OE1 GLN A 319      18.810  32.522  20.470  1.00 11.73           O  
ANISOU 2534  OE1 GLN A 319     1120   1772   1564     44    276    -83       O  
ATOM   2535  NE2 GLN A 319      17.295  31.426  19.217  1.00 10.25           N  
ANISOU 2535  NE2 GLN A 319     1033   1624   1239    206    301     91       N  
ATOM   2536  N   ASN A 320      13.862  35.835  17.788  1.00 10.43           N  
ANISOU 2536  N   ASN A 320     1354   1460   1147    190    269    269       N  
ATOM   2537  CA  ASN A 320      12.665  36.201  17.034  1.00 10.54           C  
ANISOU 2537  CA  ASN A 320     1148   1516   1339    242    197    215       C  
ATOM   2538  C   ASN A 320      12.721  35.578  15.642  1.00 10.24           C  
ANISOU 2538  C   ASN A 320     1216   1426   1248    279    258    229       C  
ATOM   2539  O   ASN A 320      13.762  35.697  14.975  1.00 12.06           O  
ANISOU 2539  O   ASN A 320     1441   1786   1355    241    463    216       O  
ATOM   2540  CB  ASN A 320      12.531  37.713  16.806  1.00 11.03           C  
ANISOU 2540  CB  ASN A 320     1418   1496   1278    142    277    284       C  
ATOM   2541  CG  ASN A 320      12.343  38.485  18.092  1.00 11.72           C  
ANISOU 2541  CG  ASN A 320     1460   1553   1439    298    353    186       C  
ATOM   2542  OD1 ASN A 320      11.443  38.202  18.901  1.00 12.84           O  
ANISOU 2542  OD1 ASN A 320     1690   1694   1495    260    574    191       O  
ATOM   2543  ND2 ASN A 320      13.200  39.484  18.310  1.00 12.89           N  
ANISOU 2543  ND2 ASN A 320     1475   1792   1632    166    374      7       N  
ATOM   2544  N   THR A 321      11.606  35.002  15.178  1.00 11.28           N  
ANISOU 2544  N   THR A 321     1306   1779   1202    223    263    188       N  
ATOM   2545  CA  THR A 321      11.403  34.696  13.780  1.00 11.49           C  
ANISOU 2545  CA  THR A 321     1307   1877   1181    356    197    112       C  
ATOM   2546  C   THR A 321      11.092  35.979  13.023  1.00 12.29           C  
ANISOU 2546  C   THR A 321     1487   1932   1249    407    364    187       C  
ATOM   2547  O   THR A 321      11.117  37.072  13.606  1.00 13.41           O  
ANISOU 2547  O   THR A 321     1701   1846   1547    355    259    201       O  
ATOM   2548  CB  THR A 321      10.261  33.688  13.573  1.00 11.52           C  
ANISOU 2548  CB  THR A 321     1316   1806   1255    423    168    122       C  
ATOM   2549  OG1 THR A 321       8.995  34.344  13.787  1.00 12.51           O  
ANISOU 2549  OG1 THR A 321     1273   1967   1516    305    198    257       O  
ATOM   2550  CG2 THR A 321      10.382  32.439  14.401  1.00 12.24           C  
ANISOU 2550  CG2 THR A 321     1507   1718   1427    478    242    106       C  
ATOM   2551  N   ASN A 322      10.815  35.885  11.728  1.00 12.66           N  
ANISOU 2551  N   ASN A 322     1646   1888   1275    237    249    288       N  
ATOM   2552  CA  ASN A 322      10.329  37.051  10.981  1.00 14.05           C  
ANISOU 2552  CA  ASN A 322     1913   2075   1348    330    303    388       C  
ATOM   2553  C   ASN A 322       8.874  37.410  11.280  1.00 14.42           C  
ANISOU 2553  C   ASN A 322     2002   2111   1364    494    238    475       C  
ATOM   2554  O   ASN A 322       8.388  38.390  10.690  1.00 17.34           O  
ANISOU 2554  O   ASN A 322     2097   2443   2050    607    473    903       O  
ATOM   2555  CB  ASN A 322      10.528  36.861   9.465  1.00 14.73           C  
ANISOU 2555  CB  ASN A 322     2152   2148   1297    373    271    384       C  
ATOM   2556  CG  ASN A 322       9.586  35.791   8.905  1.00 14.33           C  
ANISOU 2556  CG  ASN A 322     1916   2171   1358    481    210    400       C  
ATOM   2557  OD1 ASN A 322       9.468  34.736   9.536  1.00 15.07           O  
ANISOU 2557  OD1 ASN A 322     2052   2166   1507    421    189    460       O  
ATOM   2558  ND2 ASN A 322       9.017  36.088   7.771  1.00 17.18           N  
ANISOU 2558  ND2 ASN A 322     2317   2570   1640    325   -131    601       N  
ATOM   2559  N   VAL A 323       8.151  36.662  12.122  1.00 13.70           N  
ANISOU 2559  N   VAL A 323     1741   2008   1455    532    206    388       N  
ATOM   2560  CA  VAL A 323       6.766  36.910  12.443  1.00 13.92           C  
ANISOU 2560  CA  VAL A 323     1615   1985   1689    704    109    419       C  
ATOM   2561  C   VAL A 323       6.625  37.317  13.920  1.00 14.13           C  
ANISOU 2561  C   VAL A 323     1782   1869   1717    511    402    538       C  
ATOM   2562  O   VAL A 323       7.069  36.594  14.806  1.00 13.95           O  
ANISOU 2562  O   VAL A 323     1642   1932   1726    581    305    483       O  
ATOM   2563  CB  VAL A 323       5.881  35.698  12.108  1.00 14.92           C  
ANISOU 2563  CB  VAL A 323     1671   2200   1796    607    167    404       C  
ATOM   2564  CG1 VAL A 323       4.424  35.911  12.525  1.00 15.60           C  
ANISOU 2564  CG1 VAL A 323     1631   2320   1975    542    161    542       C  
ATOM   2565  CG2 VAL A 323       5.982  35.362  10.639  1.00 16.35           C  
ANISOU 2565  CG2 VAL A 323     1789   2468   1953    471    101     80       C  
ATOM   2566  N   LYS A 324       6.009  38.481  14.159  1.00 15.31           N  
ANISOU 2566  N   LYS A 324     2031   2041   1746    732    377    520       N  
ATOM   2567  CA  LYS A 324       5.794  38.972  15.516  1.00 16.10           C  
ANISOU 2567  CA  LYS A 324     2386   1854   1877    569    504    422       C  
ATOM   2568  C   LYS A 324       5.095  37.920  16.362  1.00 14.84           C  
ANISOU 2568  C   LYS A 324     2005   1941   1693    584    468    321       C  
ATOM   2569  O   LYS A 324       4.108  37.312  15.929  1.00 15.52           O  
ANISOU 2569  O   LYS A 324     1727   2295   1877    677    227    434       O  
ATOM   2570  CB ALYS A 324       4.935  40.242  15.479  0.68 19.84           C  
ANISOU 2570  CB ALYS A 324     3216   1994   2328    982    540    452       C  
ATOM   2571  CB BLYS A 324       4.979  40.263  15.424  0.32 20.52           C  
ANISOU 2571  CB BLYS A 324     3639   1941   2219   1049    375    362       C  
ATOM   2572  CG ALYS A 324       4.523  40.786  16.835  0.68 22.99           C  
ANISOU 2572  CG ALYS A 324     3841   2335   2559   1179    735    245       C  
ATOM   2573  CG BLYS A 324       5.789  41.509  15.201  0.32 23.64           C  
ANISOU 2573  CG BLYS A 324     5209   1966   1809    597     45    896       C  
ATOM   2574  CD ALYS A 324       3.534  41.944  16.651  0.68 26.09           C  
ANISOU 2574  CD ALYS A 324     3890   2387   3637   1329    575   -137       C  
ATOM   2575  CD BLYS A 324       6.737  41.586  14.051  0.32 28.49           C  
ANISOU 2575  CD BLYS A 324     4553   3673   2598   -274    200    702       C  
ATOM   2576  CE ALYS A 324       3.013  42.426  17.967  0.68 26.16           C  
ANISOU 2576  CE ALYS A 324     3610   2487   3843   1131   1041     78       C  
ATOM   2577  CE BLYS A 324       8.177  41.438  14.484  0.32 30.55           C  
ANISOU 2577  CE BLYS A 324     4936   3520   3151    672   -219    758       C  
ATOM   2578  NZ ALYS A 324       4.027  43.013  18.868  0.68 39.83           N  
ANISOU 2578  NZ ALYS A 324     7649   2585   4899     63   -471   -887       N  
ATOM   2579  NZ BLYS A 324       8.992  40.830  13.400  0.32 27.97           N  
ANISOU 2579  NZ BLYS A 324     4623   2813   3189    485   -915      1       N  
ATOM   2580  N   GLY A 325       5.573  37.725  17.571  1.00 14.39           N  
ANISOU 2580  N   GLY A 325     1940   1789   1739    560    319    306       N  
ATOM   2581  CA  GLY A 325       4.998  36.812  18.528  1.00 13.76           C  
ANISOU 2581  CA  GLY A 325     1783   1796   1650    561    359    298       C  
ATOM   2582  C   GLY A 325       5.381  35.372  18.341  1.00 12.05           C  
ANISOU 2582  C   GLY A 325     1328   1832   1418    550    254    376       C  
ATOM   2583  O   GLY A 325       4.854  34.500  19.053  1.00 12.67           O  
ANISOU 2583  O   GLY A 325     1422   1849   1544    464    255    381       O  
ATOM   2584  N   ILE A 326       6.311  35.069  17.421  1.00 12.16           N  
ANISOU 2584  N   ILE A 326     1425   1715   1480    435    335    262       N  
ATOM   2585  CA  ILE A 326       6.781  33.711  17.163  1.00 11.48           C  
ANISOU 2585  CA  ILE A 326     1189   1571   1603    335    109    227       C  
ATOM   2586  C   ILE A 326       8.277  33.702  17.278  1.00 10.14           C  
ANISOU 2586  C   ILE A 326     1246   1517   1089    288    272    235       C  
ATOM   2587  O   ILE A 326       8.967  34.582  16.700  1.00 11.65           O  
ANISOU 2587  O   ILE A 326     1348   1708   1370    343    257    326       O  
ATOM   2588  CB  ILE A 326       6.295  33.179  15.807  1.00 12.35           C  
ANISOU 2588  CB  ILE A 326     1346   1787   1559    414     29    204       C  
ATOM   2589  CG1 ILE A 326       4.763  33.387  15.681  1.00 13.72           C  
ANISOU 2589  CG1 ILE A 326     1439   2051   1724    510     11    -51       C  
ATOM   2590  CG2 ILE A 326       6.673  31.710  15.648  1.00 13.05           C  
ANISOU 2590  CG2 ILE A 326     1442   1827   1689    349    208     11       C  
ATOM   2591  CD1 ILE A 326       4.208  32.765  14.422  1.00 16.11           C  
ANISOU 2591  CD1 ILE A 326     1561   2556   2003    486   -151   -264       C  
ATOM   2592  N   TYR A 327       8.834  32.737  17.989  1.00  9.76           N  
ANISOU 2592  N   TYR A 327     1018   1518   1171    221    243    173       N  
ATOM   2593  CA  TYR A 327      10.221  32.624  18.327  1.00 10.24           C  
ANISOU 2593  CA  TYR A 327     1096   1552   1241    231    175     64       C  
ATOM   2594  C   TYR A 327      10.693  31.219  17.989  1.00 10.05           C  
ANISOU 2594  C   TYR A 327     1164   1454   1201    189    315    168       C  
ATOM   2595  O   TYR A 327       9.870  30.316  17.846  1.00 10.46           O  
ANISOU 2595  O   TYR A 327     1159   1487   1328    166    194    156       O  
ATOM   2596  CB  TYR A 327      10.451  32.908  19.874  1.00 10.50           C  
ANISOU 2596  CB  TYR A 327     1126   1595   1270    232    201    188       C  
ATOM   2597  CG  TYR A 327       9.636  34.060  20.330  1.00 10.62           C  
ANISOU 2597  CG  TYR A 327     1181   1569   1284    248    294    264       C  
ATOM   2598  CD1 TYR A 327       8.365  33.889  20.813  1.00 11.97           C  
ANISOU 2598  CD1 TYR A 327     1197   1804   1548    114    374   -185       C  
ATOM   2599  CD2 TYR A 327      10.092  35.361  20.154  1.00 11.19           C  
ANISOU 2599  CD2 TYR A 327     1385   1596   1271    214    480    147       C  
ATOM   2600  CE1 TYR A 327       7.565  34.952  21.189  1.00 12.72           C  
ANISOU 2600  CE1 TYR A 327     1186   1896   1751     86    345   -205       C  
ATOM   2601  CE2 TYR A 327       9.273  36.446  20.509  1.00 12.13           C  
ANISOU 2601  CE2 TYR A 327     1491   1583   1536    250    504    157       C  
ATOM   2602  CZ  TYR A 327       8.022  36.225  21.032  1.00 11.92           C  
ANISOU 2602  CZ  TYR A 327     1298   1788   1441    410    306    135       C  
ATOM   2603  OH  TYR A 327       7.213  37.293  21.376  1.00 13.89           O  
ANISOU 2603  OH  TYR A 327     1409   1953   1913    539    274     -8       O  
ATOM   2604  N   ALA A 328      12.015  30.984  17.992  1.00  9.77           N  
ANISOU 2604  N   ALA A 328     1113   1349   1251    149    361    116       N  
ATOM   2605  CA  ALA A 328      12.552  29.652  17.837  1.00  9.88           C  
ANISOU 2605  CA  ALA A 328     1087   1424   1242    176    266    182       C  
ATOM   2606  C   ALA A 328      13.872  29.529  18.583  1.00  9.84           C  
ANISOU 2606  C   ALA A 328     1074   1411   1254    214    308     89       C  
ATOM   2607  O   ALA A 328      14.641  30.492  18.617  1.00  9.95           O  
ANISOU 2607  O   ALA A 328     1082   1375   1325    162    218    125       O  
ATOM   2608  CB  ALA A 328      12.707  29.254  16.383  1.00 10.75           C  
ANISOU 2608  CB  ALA A 328     1238   1615   1231    270    326    -39       C  
ATOM   2609  N   VAL A 329      14.114  28.353  19.203  1.00  9.39           N  
ANISOU 2609  N   VAL A 329      986   1346   1237    151    270    146       N  
ATOM   2610  CA  VAL A 329      15.379  28.083  19.870  1.00  9.74           C  
ANISOU 2610  CA  VAL A 329      999   1384   1318    185    261     46       C  
ATOM   2611  C   VAL A 329      15.782  26.651  19.594  1.00  9.83           C  
ANISOU 2611  C   VAL A 329     1199   1454   1080    234    213     -3       C  
ATOM   2612  O   VAL A 329      14.934  25.808  19.245  1.00 10.43           O  
ANISOU 2612  O   VAL A 329     1055   1480   1428    234     83      2       O  
ATOM   2613  CB  VAL A 329      15.333  28.304  21.399  1.00 11.34           C  
ANISOU 2613  CB  VAL A 329     1559   1590   1158    132    355     12       C  
ATOM   2614  CG1 VAL A 329      14.919  29.698  21.801  1.00 12.46           C  
ANISOU 2614  CG1 VAL A 329     1578   1675   1481    200    257    -80       C  
ATOM   2615  CG2 VAL A 329      14.532  27.267  22.119  1.00 13.23           C  
ANISOU 2615  CG2 VAL A 329     1664   1796   1569     96    529    164       C  
ATOM   2616  N   GLY A 330      17.049  26.349  19.850  1.00 10.09           N  
ANISOU 2616  N   GLY A 330     1103   1481   1251    222    221     11       N  
ATOM   2617  CA  GLY A 330      17.552  25.003  19.808  1.00  9.62           C  
ANISOU 2617  CA  GLY A 330     1018   1420   1217    152    227     50       C  
ATOM   2618  C   GLY A 330      17.904  24.524  18.428  1.00  9.32           C  
ANISOU 2618  C   GLY A 330      954   1437   1151    221    195     65       C  
ATOM   2619  O   GLY A 330      18.183  25.286  17.486  1.00 10.36           O  
ANISOU 2619  O   GLY A 330     1149   1565   1223    141    372    222       O  
ATOM   2620  N   ASP A 331      17.912  23.197  18.263  1.00 10.05           N  
ANISOU 2620  N   ASP A 331     1154   1435   1230    238    347    154       N  
ATOM   2621  CA  ASP A 331      18.399  22.574  17.046  1.00 10.37           C  
ANISOU 2621  CA  ASP A 331     1193   1494   1253    260    430    107       C  
ATOM   2622  C   ASP A 331      17.620  22.975  15.809  1.00 10.61           C  
ANISOU 2622  C   ASP A 331     1267   1521   1244    258    362      9       C  
ATOM   2623  O   ASP A 331      18.183  22.920  14.692  1.00 12.02           O  
ANISOU 2623  O   ASP A 331     1544   1783   1238    499    516    135       O  
ATOM   2624  CB  ASP A 331      18.433  21.054  17.186  1.00 11.50           C  
ANISOU 2624  CB  ASP A 331     1442   1553   1374    364    346     49       C  
ATOM   2625  CG  ASP A 331      19.509  20.409  17.993  1.00 11.27           C  
ANISOU 2625  CG  ASP A 331     1212   1469   1600    231    423    145       C  
ATOM   2626  OD1 ASP A 331      19.590  19.167  17.913  1.00 12.58           O  
ANISOU 2626  OD1 ASP A 331     1495   1659   1626    314    420     10       O  
ATOM   2627  OD2 ASP A 331      20.254  21.157  18.695  1.00 12.26           O  
ANISOU 2627  OD2 ASP A 331     1353   1695   1611    229    341     48       O  
ATOM   2628  N   VAL A 332      16.355  23.352  15.946  1.00 10.86           N  
ANISOU 2628  N   VAL A 332     1303   1533   1290    257    385    168       N  
ATOM   2629  CA  VAL A 332      15.561  23.751  14.770  1.00 10.85           C  
ANISOU 2629  CA  VAL A 332     1352   1549   1223    229    379    115       C  
ATOM   2630  C   VAL A 332      16.126  24.960  14.064  1.00 11.23           C  
ANISOU 2630  C   VAL A 332     1429   1676   1163    211    435    181       C  
ATOM   2631  O   VAL A 332      15.828  25.177  12.899  1.00 11.88           O  
ANISOU 2631  O   VAL A 332     1548   1784   1181    260    437    236       O  
ATOM   2632  CB  VAL A 332      14.081  23.940  15.169  1.00 10.68           C  
ANISOU 2632  CB  VAL A 332     1207   1591   1259    119    276     94       C  
ATOM   2633  CG1 VAL A 332      13.863  25.266  15.892  1.00 11.00           C  
ANISOU 2633  CG1 VAL A 332     1307   1696   1179    232    279     18       C  
ATOM   2634  CG2 VAL A 332      13.165  23.758  13.946  1.00 12.83           C  
ANISOU 2634  CG2 VAL A 332     1543   1814   1519    -51     50      9       C  
ATOM   2635  N   CYS A 333      16.971  25.762  14.730  1.00 11.07           N  
ANISOU 2635  N   CYS A 333     1365   1581   1262    272    475    187       N  
ATOM   2636  CA  CYS A 333      17.598  26.914  14.144  1.00 11.77           C  
ANISOU 2636  CA  CYS A 333     1379   1774   1320    194    521    290       C  
ATOM   2637  C   CYS A 333      18.997  26.614  13.561  1.00 11.94           C  
ANISOU 2637  C   CYS A 333     1352   1969   1215    283    449    381       C  
ATOM   2638  O   CYS A 333      19.552  27.456  12.843  1.00 13.46           O  
ANISOU 2638  O   CYS A 333     1394   2108   1614    299    561    493       O  
ATOM   2639  CB  CYS A 333      17.739  28.067  15.127  1.00 11.88           C  
ANISOU 2639  CB  CYS A 333     1254   1721   1539    210    447    198       C  
ATOM   2640  SG  CYS A 333      16.142  28.609  15.813  1.00 14.00           S  
ANISOU 2640  SG  CYS A 333     1555   1847   1917    240    650     76       S  
ATOM   2641  N   GLY A 334      19.572  25.441  13.822  1.00 12.61           N  
ANISOU 2641  N   GLY A 334     1287   1951   1553    309    419    287       N  
ATOM   2642  CA  GLY A 334      20.786  25.045  13.152  1.00 13.10           C  
ANISOU 2642  CA  GLY A 334     1453   1963   1562    299    465    341       C  
ATOM   2643  C   GLY A 334      22.078  25.647  13.671  1.00 13.99           C  
ANISOU 2643  C   GLY A 334     1306   2166   1846    382    506    234       C  
ATOM   2644  O   GLY A 334      23.099  25.389  12.990  1.00 19.54           O  
ANISOU 2644  O   GLY A 334     1619   3574   2232     66    824   -413       O  
ATOM   2645  N   LYS A 335      22.096  26.342  14.769  1.00 13.74           N  
ANISOU 2645  N   LYS A 335     1378   2210   1633    215    418    290       N  
ATOM   2646  CA  LYS A 335      23.269  27.028  15.295  1.00 14.82           C  
ANISOU 2646  CA  LYS A 335     1513   2316   1801   -167    483    632       C  
ATOM   2647  C   LYS A 335      23.636  26.428  16.651  1.00 13.04           C  
ANISOU 2647  C   LYS A 335     1281   2048   1626     76    464    345       C  
ATOM   2648  O   LYS A 335      22.791  26.422  17.578  1.00 14.90           O  
ANISOU 2648  O   LYS A 335     1170   2736   1756    336    494    682       O  
ATOM   2649  CB ALYS A 335      23.057  28.536  15.446  0.57 20.51           C  
ANISOU 2649  CB ALYS A 335     2884   2141   2767   -505    -72   1002       C  
ATOM   2650  CB BLYS A 335      23.021  28.547  15.444  0.43 15.66           C  
ANISOU 2650  CB BLYS A 335     1586   2258   2107   -201    455    825       C  
ATOM   2651  CG ALYS A 335      22.402  29.230  14.285  0.57 21.29           C  
ANISOU 2651  CG ALYS A 335     2750   2845   2493    578    689   1031       C  
ATOM   2652  CG BLYS A 335      24.275  29.297  15.884  0.43 20.14           C  
ANISOU 2652  CG BLYS A 335     2056   2480   3115   -433      7    627       C  
ATOM   2653  CD ALYS A 335      23.276  29.285  13.041  0.57 26.51           C  
ANISOU 2653  CD ALYS A 335     2308   5267   2496   1327    611    976       C  
ATOM   2654  CD BLYS A 335      24.101  30.813  15.887  0.43 26.32           C  
ANISOU 2654  CD BLYS A 335     4183   2348   3470   -932    -79   1162       C  
ATOM   2655  CE ALYS A 335      22.728  30.349  12.096  0.57 27.92           C  
ANISOU 2655  CE ALYS A 335     3757   4768   2082   1708   1584   1040       C  
ATOM   2656  CE BLYS A 335      25.445  31.498  16.155  0.43 28.03           C  
ANISOU 2656  CE BLYS A 335     4213   2599   3840  -1027    536     65       C  
ATOM   2657  NZ ALYS A 335      23.115  31.722  12.561  0.57 38.68           N  
ANISOU 2657  NZ ALYS A 335     6164   5107   3426   2267   -413    145       N  
ATOM   2658  NZ BLYS A 335      25.366  32.880  15.590  0.43 34.19           N  
ANISOU 2658  NZ BLYS A 335     3478   3435   6077  -1594   -616   1549       N  
ATOM   2659  N   ALA A 336      24.843  25.935  16.854  1.00 12.85           N  
ANISOU 2659  N   ALA A 336     1316   1865   1702    104    599    227       N  
ATOM   2660  CA  ALA A 336      25.369  25.477  18.144  1.00 12.74           C  
ANISOU 2660  CA  ALA A 336     1325   1743   1774    215    575    316       C  
ATOM   2661  C   ALA A 336      24.435  24.386  18.712  1.00 11.92           C  
ANISOU 2661  C   ALA A 336     1256   1811   1461    149    583    171       C  
ATOM   2662  O   ALA A 336      23.751  24.602  19.727  1.00 11.87           O  
ANISOU 2662  O   ALA A 336     1210   1729   1571    179    493    218       O  
ATOM   2663  CB  ALA A 336      25.600  26.608  19.082  1.00 15.08           C  
ANISOU 2663  CB  ALA A 336     1557   2324   1849   -432    607     29       C  
ATOM   2664  N   LEU A 337      24.481  23.215  18.104  1.00 12.04           N  
ANISOU 2664  N   LEU A 337     1330   1856   1390    106    385     83       N  
ATOM   2665  CA  LEU A 337      23.501  22.133  18.387  1.00 11.94           C  
ANISOU 2665  CA  LEU A 337     1377   1774   1384    222    488    230       C  
ATOM   2666  C   LEU A 337      23.915  21.341  19.628  1.00 10.50           C  
ANISOU 2666  C   LEU A 337      913   1673   1405    178    441    110       C  
ATOM   2667  O   LEU A 337      24.480  20.244  19.553  1.00 12.03           O  
ANISOU 2667  O   LEU A 337     1447   1757   1365    312    376     25       O  
ATOM   2668  CB ALEU A 337      23.297  21.265  17.163  0.41 11.78           C  
ANISOU 2668  CB ALEU A 337     1247   1861   1370    -19    496    238       C  
ATOM   2669  CB BLEU A 337      23.394  21.177  17.231  0.59 15.51           C  
ANISOU 2669  CB BLEU A 337     2145   2160   1590   -139     60    -25       C  
ATOM   2670  CG ALEU A 337      22.448  21.876  16.043  0.41 17.00           C  
ANISOU 2670  CG ALEU A 337     2688   1976   1795   -446   -257    638       C  
ATOM   2671  CG BLEU A 337      23.212  21.763  15.835  0.59 23.24           C  
ANISOU 2671  CG BLEU A 337     4134   2915   1779    588   -836    -50       C  
ATOM   2672  CD1ALEU A 337      23.348  22.803  15.230  0.41 13.46           C  
ANISOU 2672  CD1ALEU A 337     1561   1826   1727    518    416    445       C  
ATOM   2673  CD1BLEU A 337      23.037  20.632  14.827  0.59 24.75           C  
ANISOU 2673  CD1BLEU A 337     4525   3356   1522   -114    -48   -164       C  
ATOM   2674  CD2ALEU A 337      21.856  20.804  15.147  0.41 16.34           C  
ANISOU 2674  CD2ALEU A 337     1094   3482   1632   -429    560   -341       C  
ATOM   2675  CD2BLEU A 337      22.012  22.699  15.870  0.59 19.07           C  
ANISOU 2675  CD2BLEU A 337     2775   2830   1641   -275   -299    440       C  
ATOM   2676  N   LEU A 338      23.673  21.946  20.779  1.00 10.28           N  
ANISOU 2676  N   LEU A 338     1067   1494   1344    213    440    154       N  
ATOM   2677  CA  LEU A 338      24.013  21.404  22.082  1.00 10.04           C  
ANISOU 2677  CA  LEU A 338     1049   1432   1335    184    402    173       C  
ATOM   2678  C   LEU A 338      22.814  21.621  23.024  1.00  9.29           C  
ANISOU 2678  C   LEU A 338      964   1405   1160    147    170     11       C  
ATOM   2679  O   LEU A 338      22.088  22.627  22.954  1.00 10.39           O  
ANISOU 2679  O   LEU A 338     1064   1441   1444    166    299    179       O  
ATOM   2680  CB  LEU A 338      25.205  22.121  22.656  1.00 11.57           C  
ANISOU 2680  CB  LEU A 338     1040   1762   1595     31    400    276       C  
ATOM   2681  CG  LEU A 338      26.516  21.923  21.874  1.00 12.96           C  
ANISOU 2681  CG  LEU A 338     1036   2324   1564     95    319     78       C  
ATOM   2682  CD1 LEU A 338      27.534  22.992  22.309  1.00 18.90           C  
ANISOU 2682  CD1 LEU A 338     1367   3729   2085   -805    669   -379       C  
ATOM   2683  CD2 LEU A 338      27.039  20.512  22.018  1.00 16.61           C  
ANISOU 2683  CD2 LEU A 338     1312   2885   2114    681    682    725       C  
ATOM   2684  N   THR A 339      22.654  20.745  24.001  1.00  9.28           N  
ANISOU 2684  N   THR A 339      998   1374   1153     81    342     50       N  
ATOM   2685  CA  THR A 339      21.571  20.854  24.993  1.00  9.18           C  
ANISOU 2685  CA  THR A 339      878   1477   1131     92    153     -1       C  
ATOM   2686  C   THR A 339      21.681  22.140  25.811  1.00  8.77           C  
ANISOU 2686  C   THR A 339      881   1366   1083     -3    258    105       C  
ATOM   2687  O   THR A 339      20.672  22.870  25.923  1.00  9.69           O  
ANISOU 2687  O   THR A 339      928   1438   1317    116    240     63       O  
ATOM   2688  CB  THR A 339      21.497  19.590  25.854  1.00  9.38           C  
ANISOU 2688  CB  THR A 339      958   1401   1207     23    255     73       C  
ATOM   2689  OG1 THR A 339      20.711  18.644  25.133  1.00 13.29           O  
ANISOU 2689  OG1 THR A 339     2084   1572   1395   -392    199     17       O  
ATOM   2690  CG2 THR A 339      20.874  19.807  27.190  1.00 11.30           C  
ANISOU 2690  CG2 THR A 339     1267   1580   1446     53    418     55       C  
ATOM   2691  N   PRO A 340      22.831  22.504  26.365  1.00  9.38           N  
ANISOU 2691  N   PRO A 340      914   1393   1258     84    208     45       N  
ATOM   2692  CA  PRO A 340      22.870  23.697  27.207  1.00  9.42           C  
ANISOU 2692  CA  PRO A 340      985   1409   1184     -2    213     15       C  
ATOM   2693  C   PRO A 340      22.609  24.975  26.450  1.00  9.20           C  
ANISOU 2693  C   PRO A 340      832   1373   1289    -46    295     21       C  
ATOM   2694  O   PRO A 340      22.233  25.999  27.079  1.00 10.26           O  
ANISOU 2694  O   PRO A 340      993   1447   1460     39    294   -111       O  
ATOM   2695  CB  PRO A 340      24.296  23.659  27.798  1.00 11.20           C  
ANISOU 2695  CB  PRO A 340     1180   1736   1340    138     52     15       C  
ATOM   2696  CG  PRO A 340      24.657  22.234  27.832  1.00 12.57           C  
ANISOU 2696  CG  PRO A 340     1182   1717   1876    269    -73   -232       C  
ATOM   2697  CD  PRO A 340      24.064  21.674  26.545  1.00 10.50           C  
ANISOU 2697  CD  PRO A 340     1036   1471   1483    266    113    170       C  
ATOM   2698  N   VAL A 341      22.875  24.984  25.144  1.00  9.39           N  
ANISOU 2698  N   VAL A 341      845   1383   1341    194    293     56       N  
ATOM   2699  CA  VAL A 341      22.611  26.144  24.293  1.00  9.76           C  
ANISOU 2699  CA  VAL A 341     1000   1488   1221     64    312     44       C  
ATOM   2700  C   VAL A 341      21.102  26.317  24.135  1.00  9.67           C  
ANISOU 2700  C   VAL A 341      985   1350   1338     79    380    260       C  
ATOM   2701  O   VAL A 341      20.569  27.435  24.298  1.00 10.57           O  
ANISOU 2701  O   VAL A 341     1108   1360   1550     81    453    120       O  
ATOM   2702  CB  VAL A 341      23.365  26.011  22.989  1.00 10.35           C  
ANISOU 2702  CB  VAL A 341      998   1546   1390    128    400    142       C  
ATOM   2703  CG1 VAL A 341      23.003  27.171  22.079  1.00 12.03           C  
ANISOU 2703  CG1 VAL A 341     1217   1837   1518    172    588    419       C  
ATOM   2704  CG2 VAL A 341      24.873  25.998  23.210  1.00 11.29           C  
ANISOU 2704  CG2 VAL A 341      988   1791   1511    -61    411     52       C  
ATOM   2705  N   ALA A 342      20.385  25.232  23.810  1.00  9.55           N  
ANISOU 2705  N   ALA A 342      854   1353   1421    143    297     -3       N  
ATOM   2706  CA  ALA A 342      18.948  25.287  23.733  1.00  9.56           C  
ANISOU 2706  CA  ALA A 342      897   1449   1287    262    232    163       C  
ATOM   2707  C   ALA A 342      18.338  25.799  25.068  1.00  9.39           C  
ANISOU 2707  C   ALA A 342      876   1335   1356    161    224    135       C  
ATOM   2708  O   ALA A 342      17.431  26.643  25.077  1.00  9.85           O  
ANISOU 2708  O   ALA A 342      918   1299   1525    145    254     26       O  
ATOM   2709  CB  ALA A 342      18.358  23.917  23.368  1.00 10.24           C  
ANISOU 2709  CB  ALA A 342      991   1660   1240     22    321    -42       C  
ATOM   2710  N   ILE A 343      18.846  25.251  26.170  1.00  9.18           N  
ANISOU 2710  N   ILE A 343      856   1310   1320    211    301     43       N  
ATOM   2711  CA  ILE A 343      18.357  25.606  27.498  1.00  9.68           C  
ANISOU 2711  CA  ILE A 343      906   1415   1356    125    263      2       C  
ATOM   2712  C   ILE A 343      18.599  27.080  27.769  1.00  9.66           C  
ANISOU 2712  C   ILE A 343     1001   1390   1280     94    243     27       C  
ATOM   2713  O   ILE A 343      17.671  27.800  28.212  1.00 10.12           O  
ANISOU 2713  O   ILE A 343     1071   1475   1299    145    334     85       O  
ATOM   2714  CB  ILE A 343      18.985  24.705  28.577  1.00  9.38           C  
ANISOU 2714  CB  ILE A 343      952   1288   1326     81    179    -96       C  
ATOM   2715  CG1 ILE A 343      18.462  23.254  28.430  1.00 10.38           C  
ANISOU 2715  CG1 ILE A 343     1267   1355   1321    114    277    -30       C  
ATOM   2716  CG2 ILE A 343      18.774  25.265  29.937  1.00 10.11           C  
ANISOU 2716  CG2 ILE A 343     1075   1424   1342    113    279    -51       C  
ATOM   2717  CD1 ILE A 343      19.068  22.287  29.382  1.00 11.66           C  
ANISOU 2717  CD1 ILE A 343     1358   1468   1603    222    253    181       C  
ATOM   2718  N   ALA A 344      19.818  27.558  27.557  1.00  9.70           N  
ANISOU 2718  N   ALA A 344     1052   1331   1302     82    363   -138       N  
ATOM   2719  CA  ALA A 344      20.162  28.938  27.903  1.00 10.11           C  
ANISOU 2719  CA  ALA A 344     1103   1445   1294    -24    203    -72       C  
ATOM   2720  C   ALA A 344      19.394  29.892  27.005  1.00 10.04           C  
ANISOU 2720  C   ALA A 344     1112   1288   1416    -34    510    -16       C  
ATOM   2721  O   ALA A 344      18.903  30.933  27.463  1.00 11.16           O  
ANISOU 2721  O   ALA A 344     1193   1420   1630     83    510   -107       O  
ATOM   2722  CB  ALA A 344      21.649  29.154  27.830  1.00 11.87           C  
ANISOU 2722  CB  ALA A 344     1198   1635   1678    -74    212   -148       C  
ATOM   2723  N   ALA A 345      19.312  29.614  25.698  1.00 10.21           N  
ANISOU 2723  N   ALA A 345     1075   1419   1386    277    429    103       N  
ATOM   2724  CA  ALA A 345      18.558  30.472  24.800  1.00 10.22           C  
ANISOU 2724  CA  ALA A 345     1110   1285   1491    207    414     95       C  
ATOM   2725  C   ALA A 345      17.086  30.506  25.226  1.00  9.68           C  
ANISOU 2725  C   ALA A 345     1088   1308   1281    139    350    -38       C  
ATOM   2726  O   ALA A 345      16.463  31.566  25.195  1.00 10.51           O  
ANISOU 2726  O   ALA A 345     1090   1481   1422    147    395    127       O  
ATOM   2727  CB  ALA A 345      18.691  30.015  23.371  1.00 11.59           C  
ANISOU 2727  CB  ALA A 345     1139   1971   1293    241    374    235       C  
ATOM   2728  N   GLY A 346      16.520  29.372  25.620  1.00  9.85           N  
ANISOU 2728  N   GLY A 346     1038   1451   1255    123    400     39       N  
ATOM   2729  CA  GLY A 346      15.150  29.314  26.073  1.00  9.48           C  
ANISOU 2729  CA  GLY A 346      999   1462   1142     67    215    -29       C  
ATOM   2730  C   GLY A 346      14.883  30.076  27.357  1.00  9.27           C  
ANISOU 2730  C   GLY A 346      960   1291   1271    125    271     33       C  
ATOM   2731  O   GLY A 346      13.863  30.741  27.482  1.00  9.68           O  
ANISOU 2731  O   GLY A 346      933   1426   1319    125    252     -4       O  
ATOM   2732  N   ARG A 347      15.817  29.970  28.296  1.00  9.55           N  
ANISOU 2732  N   ARG A 347      967   1445   1218    184    246      5       N  
ATOM   2733  CA  ARG A 347      15.672  30.740  29.548  1.00  9.60           C  
ANISOU 2733  CA  ARG A 347     1014   1368   1263    123    298     20       C  
ATOM   2734  C   ARG A 347      15.825  32.234  29.323  1.00  9.92           C  
ANISOU 2734  C   ARG A 347     1199   1306   1265    164    312     -9       C  
ATOM   2735  O   ARG A 347      15.055  33.025  29.885  1.00 10.15           O  
ANISOU 2735  O   ARG A 347     1207   1362   1288    106    354    -16       O  
ATOM   2736  CB  ARG A 347      16.669  30.233  30.577  1.00  9.85           C  
ANISOU 2736  CB  ARG A 347     1109   1418   1214    240    287     69       C  
ATOM   2737  CG  ARG A 347      16.332  28.876  31.145  1.00  9.99           C  
ANISOU 2737  CG  ARG A 347      963   1419   1414    172    381    126       C  
ATOM   2738  CD  ARG A 347      17.436  28.289  31.976  1.00 10.20           C  
ANISOU 2738  CD  ARG A 347     1097   1422   1356    162    228     87       C  
ATOM   2739  NE  ARG A 347      17.037  27.041  32.620  1.00 10.42           N  
ANISOU 2739  NE  ARG A 347     1138   1459   1360     77    218     62       N  
ATOM   2740  CZ  ARG A 347      17.863  26.148  33.120  1.00 10.97           C  
ANISOU 2740  CZ  ARG A 347     1321   1449   1397    192     71     45       C  
ATOM   2741  NH1 ARG A 347      17.384  25.026  33.661  1.00 12.70           N  
ANISOU 2741  NH1 ARG A 347     1448   1633   1744    171    151    275       N  
ATOM   2742  NH2 ARG A 347      19.172  26.378  33.132  1.00 11.86           N  
ANISOU 2742  NH2 ARG A 347     1223   1767   1517    228     81    120       N  
ATOM   2743  N   LYS A 348      16.825  32.636  28.527  1.00  9.88           N  
ANISOU 2743  N   LYS A 348     1180   1317   1256    182    313     61       N  
ATOM   2744  CA  LYS A 348      17.005  34.063  28.250  1.00 10.05           C  
ANISOU 2744  CA  LYS A 348     1164   1341   1316    127    262     36       C  
ATOM   2745  C   LYS A 348      15.784  34.645  27.567  1.00  9.67           C  
ANISOU 2745  C   LYS A 348     1080   1209   1386     12    360     -8       C  
ATOM   2746  O   LYS A 348      15.387  35.786  27.839  1.00  9.96           O  
ANISOU 2746  O   LYS A 348     1126   1245   1414     96    332   -107       O  
ATOM   2747  CB ALYS A 348      18.294  34.295  27.461  0.67 10.63           C  
ANISOU 2747  CB ALYS A 348     1056   1339   1643     79    390   -188       C  
ATOM   2748  CB BLYS A 348      18.265  34.320  27.415  0.33 11.77           C  
ANISOU 2748  CB BLYS A 348     1000   1589   1882     49    268    229       C  
ATOM   2749  CG ALYS A 348      19.576  33.958  28.227  0.67 12.78           C  
ANISOU 2749  CG ALYS A 348     1054   1258   2543     62    167   -118       C  
ATOM   2750  CG BLYS A 348      19.567  34.381  28.203  0.33 14.16           C  
ANISOU 2750  CG BLYS A 348     1073   2005   2303    358     36   -416       C  
ATOM   2751  CD ALYS A 348      19.910  35.007  29.263  0.67 18.38           C  
ANISOU 2751  CD ALYS A 348     1923   2470   2590    295   -605   -587       C  
ATOM   2752  CD BLYS A 348      19.723  35.653  29.019  0.33 24.54           C  
ANISOU 2752  CD BLYS A 348     3811   2518   2995    957  -1640   -974       C  
ATOM   2753  CE ALYS A 348      21.418  35.085  29.512  0.67 21.92           C  
ANISOU 2753  CE ALYS A 348     2252   2672   3406    545  -1577   -273       C  
ATOM   2754  CE BLYS A 348      21.186  35.921  29.366  0.33 24.91           C  
ANISOU 2754  CE BLYS A 348     4261   2612   2590    195  -1879  -1079       C  
ATOM   2755  NZ ALYS A 348      21.768  36.356  30.185  0.67 42.02           N  
ANISOU 2755  NZ ALYS A 348     6047   3207   6712  -1215  -4148   -287       N  
ATOM   2756  NZ BLYS A 348      21.766  34.777  30.129  0.33 29.83           N  
ANISOU 2756  NZ BLYS A 348     3105   4988   3241   -223  -1510   1205       N  
ATOM   2757  N   LEU A 349      15.173  33.875  26.683  1.00  9.02           N  
ANISOU 2757  N   LEU A 349     1060   1143   1223    227    282    -29       N  
ATOM   2758  CA  LEU A 349      13.954  34.302  25.976  1.00  9.72           C  
ANISOU 2758  CA  LEU A 349     1021   1326   1346    218    331    123       C  
ATOM   2759  C   LEU A 349      12.812  34.492  26.985  1.00  9.50           C  
ANISOU 2759  C   LEU A 349      956   1292   1361    126    242    145       C  
ATOM   2760  O   LEU A 349      12.085  35.474  26.933  1.00 10.23           O  
ANISOU 2760  O   LEU A 349     1125   1306   1455    192    240     44       O  
ATOM   2761  CB  LEU A 349      13.583  33.316  24.885  1.00  9.91           C  
ANISOU 2761  CB  LEU A 349     1105   1473   1187    272    297     81       C  
ATOM   2762  CG  LEU A 349      12.309  33.610  24.138  1.00 10.19           C  
ANISOU 2762  CG  LEU A 349     1134   1477   1259    219    288    106       C  
ATOM   2763  CD1 LEU A 349      12.393  34.946  23.386  1.00 11.24           C  
ANISOU 2763  CD1 LEU A 349     1301   1663   1306    382    358    242       C  
ATOM   2764  CD2 LEU A 349      11.999  32.482  23.179  1.00 10.74           C  
ANISOU 2764  CD2 LEU A 349     1168   1672   1240    207    178    140       C  
ATOM   2765  N   ALA A 350      12.645  33.539  27.913  1.00  9.23           N  
ANISOU 2765  N   ALA A 350     1045   1183   1279    171    334     16       N  
ATOM   2766  CA  ALA A 350      11.591  33.691  28.927  1.00  9.82           C  
ANISOU 2766  CA  ALA A 350     1105   1381   1245     17    272     22       C  
ATOM   2767  C   ALA A 350      11.760  34.945  29.750  1.00  9.75           C  
ANISOU 2767  C   ALA A 350     1079   1360   1264     43    370    -11       C  
ATOM   2768  O   ALA A 350      10.769  35.648  30.041  1.00 10.37           O  
ANISOU 2768  O   ALA A 350     1069   1498   1373    147    377    -32       O  
ATOM   2769  CB  ALA A 350      11.564  32.454  29.824  1.00 10.28           C  
ANISOU 2769  CB  ALA A 350     1292   1417   1198     66    354     49       C  
ATOM   2770  N   HIS A 351      12.991  35.290  30.144  1.00  9.91           N  
ANISOU 2770  N   HIS A 351     1104   1398   1264     86    308    -61       N  
ATOM   2771  CA  HIS A 351      13.183  36.548  30.876  1.00 10.21           C  
ANISOU 2771  CA  HIS A 351     1094   1526   1258     86    277   -101       C  
ATOM   2772  C   HIS A 351      12.879  37.745  29.993  1.00 10.17           C  
ANISOU 2772  C   HIS A 351     1085   1461   1317     -1    363    -24       C  
ATOM   2773  O   HIS A 351      12.345  38.759  30.514  1.00 11.27           O  
ANISOU 2773  O   HIS A 351     1321   1472   1487    166    487   -160       O  
ATOM   2774  CB  HIS A 351      14.624  36.660  31.444  1.00 11.31           C  
ANISOU 2774  CB  HIS A 351     1228   1779   1289    -33    110    -65       C  
ATOM   2775  CG  HIS A 351      14.848  35.742  32.581  1.00 11.49           C  
ANISOU 2775  CG  HIS A 351     1300   1712   1354     40     59   -205       C  
ATOM   2776  ND1 HIS A 351      14.431  36.084  33.896  1.00 12.73           N  
ANISOU 2776  ND1 HIS A 351     1610   1919   1308     -9    257    -35       N  
ATOM   2777  CD2 HIS A 351      15.388  34.517  32.712  1.00 13.53           C  
ANISOU 2777  CD2 HIS A 351     1536   1897   1707    130    299     76       C  
ATOM   2778  CE1 HIS A 351      14.732  35.103  34.714  1.00 13.85           C  
ANISOU 2778  CE1 HIS A 351     1751   2007   1504    165    -34     34       C  
ATOM   2779  NE2 HIS A 351      15.309  34.106  34.025  1.00 14.06           N  
ANISOU 2779  NE2 HIS A 351     1706   1841   1795     -8    147    162       N  
ATOM   2780  N   ARG A 352      13.221  37.717  28.721  1.00 10.29           N  
ANISOU 2780  N   ARG A 352     1127   1514   1267    101    400    -74       N  
ATOM   2781  CA  ARG A 352      12.896  38.817  27.851  1.00 10.38           C  
ANISOU 2781  CA  ARG A 352     1274   1330   1339    -21    340    -72       C  
ATOM   2782  C   ARG A 352      11.387  39.017  27.781  1.00 10.11           C  
ANISOU 2782  C   ARG A 352     1234   1351   1256     49    435     25       C  
ATOM   2783  O   ARG A 352      10.860  40.152  27.878  1.00 12.18           O  
ANISOU 2783  O   ARG A 352     1594   1412   1620    251    616     35       O  
ATOM   2784  CB  ARG A 352      13.474  38.594  26.424  1.00 10.89           C  
ANISOU 2784  CB  ARG A 352     1213   1564   1359    158    416     84       C  
ATOM   2785  CG  ARG A 352      13.249  39.792  25.551  1.00 10.74           C  
ANISOU 2785  CG  ARG A 352     1226   1295   1559     66    376     47       C  
ATOM   2786  CD  ARG A 352      14.050  39.742  24.270  1.00 12.13           C  
ANISOU 2786  CD  ARG A 352     1597   1581   1432    160    346    124       C  
ATOM   2787  NE  ARG A 352      13.719  38.668  23.328  1.00 11.36           N  
ANISOU 2787  NE  ARG A 352     1398   1590   1329    157    368    179       N  
ATOM   2788  CZ  ARG A 352      12.758  38.765  22.438  1.00 11.60           C  
ANISOU 2788  CZ  ARG A 352     1438   1592   1377    262    396    254       C  
ATOM   2789  NH1 ARG A 352      12.575  37.793  21.571  1.00 11.84           N  
ANISOU 2789  NH1 ARG A 352     1429   1648   1422    225    208    152       N  
ATOM   2790  NH2 ARG A 352      11.927  39.808  22.389  1.00 12.84           N  
ANISOU 2790  NH2 ARG A 352     1530   1570   1778    342    284    215       N  
ATOM   2791  N   LEU A 353      10.629  37.950  27.541  1.00 10.25           N  
ANISOU 2791  N   LEU A 353     1067   1439   1390    125    330     43       N  
ATOM   2792  CA  LEU A 353       9.204  38.050  27.291  1.00 10.43           C  
ANISOU 2792  CA  LEU A 353     1103   1465   1394     75    354     37       C  
ATOM   2793  C   LEU A 353       8.366  38.283  28.556  1.00 10.97           C  
ANISOU 2793  C   LEU A 353     1230   1394   1545    115    423    101       C  
ATOM   2794  O   LEU A 353       7.346  38.982  28.480  1.00 12.98           O  
ANISOU 2794  O   LEU A 353     1342   1786   1805    422    538    188       O  
ATOM   2795  CB  LEU A 353       8.714  36.813  26.564  1.00 10.74           C  
ANISOU 2795  CB  LEU A 353     1075   1463   1542    211    239     33       C  
ATOM   2796  CG  LEU A 353       9.362  36.483  25.219  1.00 10.70           C  
ANISOU 2796  CG  LEU A 353     1102   1634   1328    175    209      9       C  
ATOM   2797  CD1 LEU A 353       8.721  35.208  24.687  1.00 12.89           C  
ANISOU 2797  CD1 LEU A 353     1318   1894   1686    142    193   -211       C  
ATOM   2798  CD2 LEU A 353       9.290  37.616  24.230  1.00 13.49           C  
ANISOU 2798  CD2 LEU A 353     1564   1971   1592    466    282    282       C  
ATOM   2799  N   PHE A 354       8.794  37.646  29.655  1.00 10.72           N  
ANISOU 2799  N   PHE A 354     1189   1436   1448     93    391     46       N  
ATOM   2800  CA  PHE A 354       7.939  37.593  30.820  1.00 10.97           C  
ANISOU 2800  CA  PHE A 354     1345   1403   1422     68    476    -12       C  
ATOM   2801  C   PHE A 354       8.509  38.299  32.028  1.00 10.89           C  
ANISOU 2801  C   PHE A 354     1319   1368   1450     59    571    -24       C  
ATOM   2802  O   PHE A 354       7.832  38.549  33.025  1.00 12.87           O  
ANISOU 2802  O   PHE A 354     1467   1812   1611   -153    682   -243       O  
ATOM   2803  CB  PHE A 354       7.574  36.125  31.185  1.00 11.44           C  
ANISOU 2803  CB  PHE A 354     1242   1449   1656     73    431     55       C  
ATOM   2804  CG  PHE A 354       6.867  35.472  30.036  1.00 11.70           C  
ANISOU 2804  CG  PHE A 354     1333   1351   1760    -36    257    120       C  
ATOM   2805  CD1 PHE A 354       5.596  35.895  29.675  1.00 14.30           C  
ANISOU 2805  CD1 PHE A 354     1418   1716   2299    217    109   -194       C  
ATOM   2806  CD2 PHE A 354       7.469  34.503  29.261  1.00 12.06           C  
ANISOU 2806  CD2 PHE A 354     1447   1384   1751    -21    344     99       C  
ATOM   2807  CE1 PHE A 354       4.967  35.332  28.570  1.00 15.29           C  
ANISOU 2807  CE1 PHE A 354     1322   1957   2531     65     28   -176       C  
ATOM   2808  CE2 PHE A 354       6.827  33.940  28.174  1.00 12.87           C  
ANISOU 2808  CE2 PHE A 354     1601   1523   1768     13    378     32       C  
ATOM   2809  CZ  PHE A 354       5.578  34.395  27.844  1.00 14.07           C  
ANISOU 2809  CZ  PHE A 354     1744   1643   1959    -37     55     63       C  
ATOM   2810  N   GLU A 355       9.792  38.769  31.972  1.00 12.21           N  
ANISOU 2810  N   GLU A 355     1449   1659   1530   -147    491   -255       N  
ATOM   2811  CA  GLU A 355      10.344  39.724  32.915  1.00 12.99           C  
ANISOU 2811  CA  GLU A 355     1506   1836   1594   -197    624   -309       C  
ATOM   2812  C   GLU A 355      10.613  41.035  32.238  1.00 13.14           C  
ANISOU 2812  C   GLU A 355     1497   1725   1772   -216    664   -492       C  
ATOM   2813  O   GLU A 355      11.115  41.994  32.893  1.00 15.55           O  
ANISOU 2813  O   GLU A 355     1978   1925   2005   -471    613   -550       O  
ATOM   2814  CB  GLU A 355      11.545  39.149  33.651  1.00 14.80           C  
ANISOU 2814  CB  GLU A 355     1426   2439   1759   -242    452   -289       C  
ATOM   2815  CG  GLU A 355      11.678  39.553  35.041  1.00 21.35           C  
ANISOU 2815  CG  GLU A 355     3012   3525   1578    861    467   -178       C  
ATOM   2816  CD  GLU A 355      12.866  39.131  35.821  1.00 26.12           C  
ANISOU 2816  CD  GLU A 355     4589   3659   1677   1879   -302   -273       C  
ATOM   2817  OE1 GLU A 355      13.048  39.547  37.000  1.00 39.53           O  
ANISOU 2817  OE1 GLU A 355     5493   6912   2616   2613   -984  -2109       O  
ATOM   2818  OE2 GLU A 355      13.676  38.338  35.276  1.00 24.10           O  
ANISOU 2818  OE2 GLU A 355     3584   2714   2860    942   -290   -814       O  
ATOM   2819  N   TYR A 356      10.396  41.171  30.940  1.00 12.41           N  
ANISOU 2819  N   TYR A 356     1288   1573   1856    -91    602   -251       N  
ATOM   2820  CA  TYR A 356      10.489  42.417  30.208  1.00 13.72           C  
ANISOU 2820  CA  TYR A 356     1468   1501   2242    -94    761   -178       C  
ATOM   2821  C   TYR A 356      11.911  42.920  30.102  1.00 14.55           C  
ANISOU 2821  C   TYR A 356     1446   1502   2578   -164    672   -359       C  
ATOM   2822  O   TYR A 356      12.141  44.128  30.033  1.00 17.49           O  
ANISOU 2822  O   TYR A 356     1705   1563   3378   -221   1123   -349       O  
ATOM   2823  CB  TYR A 356       9.535  43.537  30.767  1.00 14.72           C  
ANISOU 2823  CB  TYR A 356     1678   1604   2309     42    821   -218       C  
ATOM   2824  CG  TYR A 356       8.133  42.968  30.885  1.00 13.78           C  
ANISOU 2824  CG  TYR A 356     1650   1505   2078    124    864   -310       C  
ATOM   2825  CD1 TYR A 356       7.333  42.731  29.789  1.00 16.36           C  
ANISOU 2825  CD1 TYR A 356     1795   2255   2168    -76    581    366       C  
ATOM   2826  CD2 TYR A 356       7.646  42.534  32.119  1.00 13.53           C  
ANISOU 2826  CD2 TYR A 356     1479   1680   1983    -24    639   -354       C  
ATOM   2827  CE1 TYR A 356       6.066  42.179  29.896  1.00 15.64           C  
ANISOU 2827  CE1 TYR A 356     1756   2316   1870    -19    552    197       C  
ATOM   2828  CE2 TYR A 356       6.400  41.962  32.233  1.00 13.04           C  
ANISOU 2828  CE2 TYR A 356     1373   1773   1809     74    592   -146       C  
ATOM   2829  CZ  TYR A 356       5.603  41.773  31.115  1.00 12.96           C  
ANISOU 2829  CZ  TYR A 356     1554   1631   1739    -37    536    -23       C  
ATOM   2830  OH  TYR A 356       4.370  41.199  31.193  1.00 14.46           O  
ANISOU 2830  OH  TYR A 356     1555   2128   1812    -89    407    -34       O  
ATOM   2831  N   LYS A 357      12.884  42.012  30.123  1.00 13.59           N  
ANISOU 2831  N   LYS A 357     1515   1611   2039    -50    693   -317       N  
ATOM   2832  CA  LYS A 357      14.300  42.348  30.058  1.00 14.25           C  
ANISOU 2832  CA  LYS A 357     1451   1743   2220   -154    724   -475       C  
ATOM   2833  C   LYS A 357      14.717  42.393  28.592  1.00 14.07           C  
ANISOU 2833  C   LYS A 357     1423   1647   2274    -36    734    -98       C  
ATOM   2834  O   LYS A 357      15.032  41.366  27.955  1.00 13.20           O  
ANISOU 2834  O   LYS A 357     1414   1649   1952    -12    683    -92       O  
ATOM   2835  CB ALYS A 357      15.097  41.358  30.899  0.53 15.37           C  
ANISOU 2835  CB ALYS A 357     1534   2091   2215   -477    330   -215       C  
ATOM   2836  CB BLYS A 357      15.062  41.276  30.831  0.47 14.89           C  
ANISOU 2836  CB BLYS A 357     1484   2221   1953   -279    470   -291       C  
ATOM   2837  CG ALYS A 357      14.971  41.653  32.390  0.53 18.01           C  
ANISOU 2837  CG ALYS A 357     1568   3009   2266  -1259     28   -559       C  
ATOM   2838  CG BLYS A 357      14.593  41.102  32.269  0.47 15.86           C  
ANISOU 2838  CG BLYS A 357     1280   2707   2039  -1131    532   -292       C  
ATOM   2839  CD ALYS A 357      15.591  40.574  33.260  0.53 22.92           C  
ANISOU 2839  CD ALYS A 357     2901   3643   2166   -965   -316   -323       C  
ATOM   2840  CD BLYS A 357      15.301  42.100  33.183  0.47 21.47           C  
ANISOU 2840  CD BLYS A 357     3027   2932   2201  -1539    382   -578       C  
ATOM   2841  CE ALYS A 357      17.055  40.313  32.982  0.53 29.84           C  
ANISOU 2841  CE ALYS A 357     2770   4658   3909   -449   -674   1008       C  
ATOM   2842  CE BLYS A 357      15.259  41.629  34.637  0.47 29.70           C  
ANISOU 2842  CE BLYS A 357     5713   3423   2149   -696   -303   -594       C  
ATOM   2843  NZ ALYS A 357      17.546  39.026  33.599  0.53 45.47           N  
ANISOU 2843  NZ ALYS A 357     5720   6933   4626   1640   -826   2252       N  
ATOM   2844  NZ BLYS A 357      16.583  41.816  35.311  0.47 44.61           N  
ANISOU 2844  NZ BLYS A 357     7384   6128   3438  -1824  -2000   -456       N  
ATOM   2845  N   GLU A 358      14.647  43.593  27.990  1.00 15.52           N  
ANISOU 2845  N   GLU A 358     1628   1538   2729     30    717   -136       N  
ATOM   2846  CA  GLU A 358      14.782  43.716  26.554  1.00 17.21           C  
ANISOU 2846  CA  GLU A 358     1964   1694   2879    426    711    373       C  
ATOM   2847  C   GLU A 358      16.167  43.325  26.042  1.00 16.13           C  
ANISOU 2847  C   GLU A 358     2027   1722   2379    135    720    184       C  
ATOM   2848  O   GLU A 358      16.228  43.028  24.849  1.00 19.93           O  
ANISOU 2848  O   GLU A 358     2440   2757   2376    397    693    165       O  
ATOM   2849  CB AGLU A 358      14.541  45.181  26.085  0.65 22.93           C  
ANISOU 2849  CB AGLU A 358     2825   1816   4071    467   1081    777       C  
ATOM   2850  CB BGLU A 358      14.511  45.175  26.117  0.35 22.22           C  
ANISOU 2850  CB BGLU A 358     2744   1726   3971    435    802    630       C  
ATOM   2851  CG AGLU A 358      13.035  45.423  25.907  0.65 32.91           C  
ANISOU 2851  CG AGLU A 358     3367   1885   7254    912   -979    382       C  
ATOM   2852  CG BGLU A 358      15.536  46.134  26.681  0.35 23.38           C  
ANISOU 2852  CG BGLU A 358     2691   1863   4329   -118   1482    741       C  
ATOM   2853  CD AGLU A 358      12.792  45.809  24.444  0.65 55.99           C  
ANISOU 2853  CD AGLU A 358     9736   3683   7856   1710  -4500   -448       C  
ATOM   2854  CD BGLU A 358      15.356  46.498  28.135  0.35 27.40           C  
ANISOU 2854  CD BGLU A 358     2403   3588   4420   -593    893     67       C  
ATOM   2855  OE1AGLU A 358      13.157  45.017  23.536  0.65 72.81           O  
ANISOU 2855  OE1AGLU A 358    13671   6410   7584   2412  -5196  -1911       O  
ATOM   2856  OE1BGLU A 358      16.375  46.955  28.726  0.35 40.80           O  
ANISOU 2856  OE1BGLU A 358     2810   6778   5914  -1412    453   -641       O  
ATOM   2857  OE2AGLU A 358      12.250  46.908  24.214  0.65 90.03           O  
ANISOU 2857  OE2AGLU A 358    20386   3718  10103   3855  -8767   -690       O  
ATOM   2858  OE2BGLU A 358      14.241  46.260  28.665  0.35 22.49           O  
ANISOU 2858  OE2BGLU A 358     2146   2262   4137    245   1040   -698       O  
ATOM   2859  N   ASP A 359      17.186  43.329  26.875  1.00 15.66           N  
ANISOU 2859  N   ASP A 359     1735   1741   2475   -144    867     12       N  
ATOM   2860  CA  ASP A 359      18.514  42.949  26.422  1.00 15.98           C  
ANISOU 2860  CA  ASP A 359     1785   1778   2507   -287    912      8       C  
ATOM   2861  C   ASP A 359      18.844  41.488  26.759  1.00 15.09           C  
ANISOU 2861  C   ASP A 359     1417   1819   2497   -191    616   -124       C  
ATOM   2862  O   ASP A 359      20.021  41.080  26.556  1.00 18.64           O  
ANISOU 2862  O   ASP A 359     1401   2221   3460   -150    874   -199       O  
ATOM   2863  CB AASP A 359      19.578  43.904  26.976  0.65 22.71           C  
ANISOU 2863  CB AASP A 359     1991   2185   4453   -717    846   -231       C  
ATOM   2864  CB BASP A 359      19.584  43.863  27.024  0.35 20.53           C  
ANISOU 2864  CB BASP A 359     1810   1873   4119   -275    785   -485       C  
ATOM   2865  CG AASP A 359      19.732  45.267  26.339  0.65 36.95           C  
ANISOU 2865  CG AASP A 359     5579   2424   6036  -1874   -958    365       C  
ATOM   2866  CG BASP A 359      19.953  43.594  28.459  0.35 30.15           C  
ANISOU 2866  CG BASP A 359     5010   1504   4940   -542  -1458   -647       C  
ATOM   2867  OD1AASP A 359      19.733  45.410  25.094  0.65 49.62           O  
ANISOU 2867  OD1AASP A 359     9556   2954   6342  -1263  -2607   1608       O  
ATOM   2868  OD1BASP A 359      19.325  42.792  29.169  0.35 42.12           O  
ANISOU 2868  OD1BASP A 359     6688   5391   3924  -1899  -1664    640       O  
ATOM   2869  OD2AASP A 359      19.897  46.271  27.091  0.65 66.76           O  
ANISOU 2869  OD2AASP A 359    14688   2561   8116  -2438  -3594    -93       O  
ATOM   2870  OD2BASP A 359      20.920  44.209  28.972  0.35 38.53           O  
ANISOU 2870  OD2BASP A 359     4344   4564   5732   -558   -610  -2999       O  
ATOM   2871  N   SER A 360      17.887  40.723  27.264  1.00 12.91           N  
ANISOU 2871  N   SER A 360     1415   1561   1928   -134    437    -99       N  
ATOM   2872  CA  SER A 360      18.145  39.321  27.645  1.00 12.30           C  
ANISOU 2872  CA  SER A 360     1323   1603   1748     36    339    -93       C  
ATOM   2873  C   SER A 360      18.244  38.462  26.391  1.00 11.55           C  
ANISOU 2873  C   SER A 360     1144   1463   1780    -89    289   -130       C  
ATOM   2874  O   SER A 360      17.270  38.331  25.652  1.00 13.89           O  
ANISOU 2874  O   SER A 360     1246   1823   2210    224     74   -336       O  
ATOM   2875  CB  SER A 360      17.036  38.843  28.546  1.00 12.51           C  
ANISOU 2875  CB  SER A 360     1463   1534   1755     -4    385    -42       C  
ATOM   2876  OG  SER A 360      17.234  37.475  28.919  1.00 13.10           O  
ANISOU 2876  OG  SER A 360     1483   1505   1988     37    163     90       O  
ATOM   2877  N   LYS A 361      19.400  37.867  26.160  1.00 12.15           N  
ANISOU 2877  N   LYS A 361     1169   1703   1744     30    156   -258       N  
ATOM   2878  CA  LYS A 361      19.707  37.031  25.018  1.00 11.46           C  
ANISOU 2878  CA  LYS A 361     1333   1489   1532    126    143   -109       C  
ATOM   2879  C   LYS A 361      20.935  36.175  25.339  1.00 11.63           C  
ANISOU 2879  C   LYS A 361     1277   1461   1682      4     51    -32       C  
ATOM   2880  O   LYS A 361      21.667  36.481  26.244  1.00 15.33           O  
ANISOU 2880  O   LYS A 361     1557   2141   2128    388   -227   -621       O  
ATOM   2881  CB ALYS A 361      19.981  37.898  23.792  0.56 13.41           C  
ANISOU 2881  CB ALYS A 361     1642   1701   1753    235    168    124       C  
ATOM   2882  CB BLYS A 361      19.902  37.800  23.722  0.44 13.00           C  
ANISOU 2882  CB BLYS A 361     1206   1862   1872    270    420    301       C  
ATOM   2883  CG ALYS A 361      21.150  38.852  24.026  0.56 14.17           C  
ANISOU 2883  CG ALYS A 361     1730   1889   1763     40    608    -83       C  
ATOM   2884  CG BLYS A 361      21.124  38.697  23.639  0.44 15.82           C  
ANISOU 2884  CG BLYS A 361     2063   2080   1868   -345     75    311       C  
ATOM   2885  CD ALYS A 361      21.497  39.678  22.810  0.56 19.30           C  
ANISOU 2885  CD ALYS A 361     2232   2860   2241   -326    694    414       C  
ATOM   2886  CD BLYS A 361      21.167  39.429  22.291  0.44 17.46           C  
ANISOU 2886  CD BLYS A 361     2102   2560   1973   -188    766    463       C  
ATOM   2887  CE ALYS A 361      22.481  40.782  23.101  0.56 21.19           C  
ANISOU 2887  CE ALYS A 361     2102   2967   2981   -422    476    849       C  
ATOM   2888  CE BLYS A 361      21.827  40.780  22.453  0.44 23.44           C  
ANISOU 2888  CE BLYS A 361     2934   2957   3014   -943    -21   1132       C  
ATOM   2889  NZ ALYS A 361      22.043  42.107  22.560  0.56 33.96           N  
ANISOU 2889  NZ ALYS A 361     5277   2493   5134    155    158    533       N  
ATOM   2890  NZ BLYS A 361      23.205  40.674  22.998  0.44 22.70           N  
ANISOU 2890  NZ BLYS A 361     2364   3498   2764   -635    741    180       N  
ATOM   2891  N   LEU A 362      21.104  35.115  24.556  1.00 11.94           N  
ANISOU 2891  N   LEU A 362     1210   1620   1707     72    204   -235       N  
ATOM   2892  CA  LEU A 362      22.265  34.259  24.717  1.00 12.15           C  
ANISOU 2892  CA  LEU A 362     1172   1716   1728     85    181    -47       C  
ATOM   2893  C   LEU A 362      23.423  34.791  23.883  1.00 11.84           C  
ANISOU 2893  C   LEU A 362     1167   1555   1776    174    189    206       C  
ATOM   2894  O   LEU A 362      23.259  35.019  22.682  1.00 14.12           O  
ANISOU 2894  O   LEU A 362     1313   2240   1812    203    222    355       O  
ATOM   2895  CB  LEU A 362      21.965  32.813  24.284  1.00 11.46           C  
ANISOU 2895  CB  LEU A 362     1092   1680   1581     42    189   -125       C  
ATOM   2896  CG  LEU A 362      23.132  31.827  24.407  1.00 12.40           C  
ANISOU 2896  CG  LEU A 362     1239   1673   1800    165    350    218       C  
ATOM   2897  CD1 LEU A 362      23.708  31.736  25.801  1.00 14.40           C  
ANISOU 2897  CD1 LEU A 362     1514   1828   2129     36      9    495       C  
ATOM   2898  CD2 LEU A 362      22.748  30.476  23.874  1.00 13.51           C  
ANISOU 2898  CD2 LEU A 362     1487   1582   2064     91    433    250       C  
ATOM   2899  N   ASP A 363      24.609  34.908  24.486  1.00 12.40           N  
ANISOU 2899  N   ASP A 363     1194   1847   1669     81    176     69       N  
ATOM   2900  CA  ASP A 363      25.874  35.138  23.788  1.00 13.31           C  
ANISOU 2900  CA  ASP A 363     1223   1766   2067    -63    224     60       C  
ATOM   2901  C   ASP A 363      26.356  33.775  23.219  1.00 12.17           C  
ANISOU 2901  C   ASP A 363      949   1640   2034    -59    326    323       C  
ATOM   2902  O   ASP A 363      26.590  32.857  23.989  1.00 13.65           O  
ANISOU 2902  O   ASP A 363     1240   1887   2058     92    182    462       O  
ATOM   2903  CB  ASP A 363      26.884  35.724  24.759  1.00 16.99           C  
ANISOU 2903  CB  ASP A 363     1501   2290   2665   -315     78   -199       C  
ATOM   2904  CG  ASP A 363      28.230  36.066  24.167  1.00 18.28           C  
ANISOU 2904  CG  ASP A 363     1491   2458   2998   -468    109    -64       C  
ATOM   2905  OD1 ASP A 363      28.466  35.833  22.948  1.00 18.83           O  
ANISOU 2905  OD1 ASP A 363     1669   2300   3185   -155    454   -102       O  
ATOM   2906  OD2 ASP A 363      29.078  36.676  24.892  1.00 25.98           O  
ANISOU 2906  OD2 ASP A 363     1926   4374   3570  -1049    -81   -418       O  
ATOM   2907  N   TYR A 364      26.484  33.677  21.905  1.00 12.74           N  
ANISOU 2907  N   TYR A 364     1108   1790   1944    -65    363    259       N  
ATOM   2908  CA  TYR A 364      26.899  32.440  21.266  1.00 13.61           C  
ANISOU 2908  CA  TYR A 364     1198   1879   2093    -30    439    197       C  
ATOM   2909  C   TYR A 364      28.414  32.336  21.175  1.00 14.31           C  
ANISOU 2909  C   TYR A 364     1236   1867   2336    100    327    251       C  
ATOM   2910  O   TYR A 364      28.907  31.311  20.637  1.00 17.27           O  
ANISOU 2910  O   TYR A 364     1307   2276   2979    133    559    -39       O  
ATOM   2911  CB  TYR A 364      26.216  32.252  19.902  1.00 13.65           C  
ANISOU 2911  CB  TYR A 364     1290   1797   2099     80    481     11       C  
ATOM   2912  CG  TYR A 364      24.775  31.805  20.018  1.00 13.21           C  
ANISOU 2912  CG  TYR A 364     1150   1880   1987    133    308    200       C  
ATOM   2913  CD1 TYR A 364      23.745  32.747  20.279  1.00 13.46           C  
ANISOU 2913  CD1 TYR A 364     1275   1846   1994    108    178     77       C  
ATOM   2914  CD2 TYR A 364      24.366  30.502  19.857  1.00 13.29           C  
ANISOU 2914  CD2 TYR A 364     1227   1986   1836    102    347   -126       C  
ATOM   2915  CE1 TYR A 364      22.411  32.340  20.383  1.00 13.09           C  
ANISOU 2915  CE1 TYR A 364     1222   1789   1962    225    315   -209       C  
ATOM   2916  CE2 TYR A 364      23.049  30.087  19.943  1.00 13.00           C  
ANISOU 2916  CE2 TYR A 364     1237   1752   1952    239    280    138       C  
ATOM   2917  CZ  TYR A 364      22.055  30.999  20.192  1.00 11.68           C  
ANISOU 2917  CZ  TYR A 364     1167   1751   1519    176    272     72       C  
ATOM   2918  OH  TYR A 364      20.758  30.581  20.305  1.00 12.28           O  
ANISOU 2918  OH  TYR A 364     1180   1760   1725     80    313    157       O  
ATOM   2919  N   ASN A 365      29.184  33.280  21.621  1.00 13.85           N  
ANISOU 2919  N   ASN A 365     1163   1895   2205     47    278    577       N  
ATOM   2920  CA  ASN A 365      30.643  33.170  21.691  1.00 14.98           C  
ANISOU 2920  CA  ASN A 365     1173   2050   2466     29    346    757       C  
ATOM   2921  C   ASN A 365      31.040  32.466  22.966  1.00 13.23           C  
ANISOU 2921  C   ASN A 365     1177   1626   2226     56    365    373       C  
ATOM   2922  O   ASN A 365      30.378  32.541  24.015  1.00 14.01           O  
ANISOU 2922  O   ASN A 365     1303   1822   2198    140    415    199       O  
ATOM   2923  CB  ASN A 365      31.262  34.564  21.716  1.00 18.59           C  
ANISOU 2923  CB  ASN A 365     1461   2255   3346   -274     -1   1014       C  
ATOM   2924  CG  ASN A 365      30.997  35.229  20.388  1.00 22.83           C  
ANISOU 2924  CG  ASN A 365     2061   2774   3840   -575    156   1725       C  
ATOM   2925  OD1 ASN A 365      31.315  34.738  19.321  1.00 35.72           O  
ANISOU 2925  OD1 ASN A 365     3571   6454   3549   1734   1454   2581       O  
ATOM   2926  ND2 ASN A 365      30.273  36.352  20.450  1.00 37.28           N  
ANISOU 2926  ND2 ASN A 365     5951   3164   5051    992    121   2144       N  
ATOM   2927  N   ASN A 366      32.184  31.754  22.905  1.00 13.35           N  
ANISOU 2927  N   ASN A 366     1099   1751   2221     62    298    285       N  
ATOM   2928  CA  ASN A 366      32.737  31.108  24.071  1.00 13.12           C  
ANISOU 2928  CA  ASN A 366     1043   1679   2264    142    175     32       C  
ATOM   2929  C   ASN A 366      31.870  30.088  24.716  1.00 13.61           C  
ANISOU 2929  C   ASN A 366     1186   1676   2309    105     72    241       C  
ATOM   2930  O   ASN A 366      31.914  29.901  25.925  1.00 15.47           O  
ANISOU 2930  O   ASN A 366     1495   1967   2416    153   -178    457       O  
ATOM   2931  CB  ASN A 366      33.225  32.154  25.069  1.00 15.12           C  
ANISOU 2931  CB  ASN A 366     1612   1705   2429    101     54     16       C  
ATOM   2932  CG  ASN A 366      34.387  32.963  24.617  1.00 18.18           C  
ANISOU 2932  CG  ASN A 366     1595   1875   3438   -140    -83     16       C  
ATOM   2933  OD1 ASN A 366      34.434  34.211  24.792  1.00 23.28           O  
ANISOU 2933  OD1 ASN A 366     2844   1922   4079   -437    800   -224       O  
ATOM   2934  ND2 ASN A 366      35.387  32.304  24.110  1.00 18.81           N  
ANISOU 2934  ND2 ASN A 366     1186   2021   3939   -327    -89   -244       N  
ATOM   2935  N   ILE A 367      31.105  29.377  23.904  1.00 12.83           N  
ANISOU 2935  N   ILE A 367     1111   1500   2262     90    287    173       N  
ATOM   2936  CA  ILE A 367      30.344  28.198  24.340  1.00 12.05           C  
ANISOU 2936  CA  ILE A 367     1011   1589   1979     90    383    292       C  
ATOM   2937  C   ILE A 367      31.316  27.009  24.401  1.00 11.31           C  
ANISOU 2937  C   ILE A 367      878   1544   1876    -39    299    317       C  
ATOM   2938  O   ILE A 367      31.925  26.702  23.377  1.00 12.29           O  
ANISOU 2938  O   ILE A 367     1089   1770   1810    186    315    292       O  
ATOM   2939  CB  ILE A 367      29.175  27.879  23.409  1.00 13.79           C  
ANISOU 2939  CB  ILE A 367      926   1777   2535      5    130    471       C  
ATOM   2940  CG1 ILE A 367      28.129  29.012  23.404  1.00 17.29           C  
ANISOU 2940  CG1 ILE A 367     1141   2019   3407    227    248    894       C  
ATOM   2941  CG2 ILE A 367      28.546  26.540  23.794  1.00 15.24           C  
ANISOU 2941  CG2 ILE A 367      960   1890   2940   -117     45    605       C  
ATOM   2942  CD1 ILE A 367      27.074  28.939  22.357  1.00 23.23           C  
ANISOU 2942  CD1 ILE A 367     1141   2761   4926   -284   -555   1533       C  
ATOM   2943  N   PRO A 368      31.444  26.345  25.550  1.00 11.38           N  
ANISOU 2943  N   PRO A 368     1132   1430   1761    142    287    163       N  
ATOM   2944  CA  PRO A 368      32.348  25.182  25.618  1.00 11.35           C  
ANISOU 2944  CA  PRO A 368      967   1567   1778    125    356     95       C  
ATOM   2945  C   PRO A 368      31.646  23.924  25.099  1.00 11.40           C  
ANISOU 2945  C   PRO A 368     1089   1513   1730    160    248    124       C  
ATOM   2946  O   PRO A 368      30.424  23.784  25.211  1.00 12.92           O  
ANISOU 2946  O   PRO A 368      959   1798   2153     68    389    125       O  
ATOM   2947  CB  PRO A 368      32.644  25.089  27.135  1.00 12.43           C  
ANISOU 2947  CB  PRO A 368     1263   1653   1808    310    164     64       C  
ATOM   2948  CG  PRO A 368      31.340  25.560  27.764  1.00 12.65           C  
ANISOU 2948  CG  PRO A 368     1407   1797   1602    240    364      0       C  
ATOM   2949  CD  PRO A 368      30.827  26.650  26.859  1.00 12.68           C  
ANISOU 2949  CD  PRO A 368     1245   1734   1839    306    415    174       C  
ATOM   2950  N  ATHR A 369      32.456  23.017  24.573  0.60 11.06           N  
ANISOU 2950  N  ATHR A 369     1028   1510   1664    135    235     95       N  
ATOM   2951  N  BTHR A 369      32.460  22.987  24.639  0.40 11.84           N  
ANISOU 2951  N  BTHR A 369      897   1532   2071    112    166     54       N  
ATOM   2952  CA ATHR A 369      32.108  21.717  23.982  0.60 11.18           C  
ANISOU 2952  CA ATHR A 369      775   1587   1887     65    111    -10       C  
ATOM   2953  CA BTHR A 369      31.888  21.683  24.293  0.40 10.93           C  
ANISOU 2953  CA BTHR A 369      809   1549   1796     74    218     94       C  
ATOM   2954  C  ATHR A 369      32.991  20.637  24.587  0.60 10.43           C  
ANISOU 2954  C  ATHR A 369      806   1417   1740      0    136   -125       C  
ATOM   2955  C  BTHR A 369      32.933  20.605  24.479  0.40 10.71           C  
ANISOU 2955  C  BTHR A 369     1020   1551   1499    183    411    210       C  
ATOM   2956  O  ATHR A 369      34.230  20.787  24.743  0.60  9.09           O  
ANISOU 2956  O  ATHR A 369      840   1532   1082    -28    140    -57       O  
ATOM   2957  O  BTHR A 369      34.120  20.792  24.208  0.40  9.07           O  
ANISOU 2957  O  BTHR A 369      893   1322   1232    102    -20    341       O  
ATOM   2958  CB ATHR A 369      32.262  21.752  22.458  0.60 13.71           C  
ANISOU 2958  CB ATHR A 369     1401   1949   1857    516    -54   -256       C  
ATOM   2959  CB BTHR A 369      31.388  21.622  22.850  0.40 13.39           C  
ANISOU 2959  CB BTHR A 369     1166   1975   1946    276    -55    -36       C  
ATOM   2960  OG1ATHR A 369      31.427  22.739  21.814  0.60 19.97           O  
ANISOU 2960  OG1ATHR A 369     2858   2728   2002   1212   -130     78       O  
ATOM   2961  OG1BTHR A 369      30.616  20.432  22.641  0.40 16.11           O  
ANISOU 2961  OG1BTHR A 369     1683   2283   2156   -101   -274     23       O  
ATOM   2962  CG2ATHR A 369      31.878  20.412  21.793  0.60 15.79           C  
ANISOU 2962  CG2ATHR A 369     1711   2221   2067   -209    548   -378       C  
ATOM   2963  CG2BTHR A 369      32.607  21.659  21.937  0.40 15.51           C  
ANISOU 2963  CG2BTHR A 369     1495   2755   1644     98     74   -270       C  
ATOM   2964  N   VAL A 370      32.407  19.482  24.910  1.00 11.21           N  
ANISOU 2964  N   VAL A 370      783   1518   1957    105    263     62       N  
ATOM   2965  CA  VAL A 370      33.147  18.256  25.147  1.00 10.55           C  
ANISOU 2965  CA  VAL A 370      815   1433   1759     75    227    101       C  
ATOM   2966  C   VAL A 370      32.705  17.223  24.114  1.00 11.30           C  
ANISOU 2966  C   VAL A 370     1016   1479   1797     -6     87     92       C  
ATOM   2967  O   VAL A 370      31.514  17.052  23.847  1.00 14.81           O  
ANISOU 2967  O   VAL A 370      928   1958   2742    201    -72   -353       O  
ATOM   2968  CB  VAL A 370      32.995  17.710  26.586  1.00 11.33           C  
ANISOU 2968  CB  VAL A 370      861   1671   1772    -77    429    245       C  
ATOM   2969  CG1 VAL A 370      33.430  16.269  26.736  1.00 12.78           C  
ANISOU 2969  CG1 VAL A 370     1235   1789   1834    151    380    309       C  
ATOM   2970  CG2 VAL A 370      33.765  18.629  27.524  1.00 12.27           C  
ANISOU 2970  CG2 VAL A 370     1159   1858   1646    -58    412    184       C  
ATOM   2971  N   VAL A 371      33.683  16.512  23.523  1.00 10.68           N  
ANISOU 2971  N   VAL A 371     1005   1580   1471   -101    222    -18       N  
ATOM   2972  CA  VAL A 371      33.421  15.342  22.684  1.00 10.12           C  
ANISOU 2972  CA  VAL A 371      885   1604   1356    -74     51     29       C  
ATOM   2973  C   VAL A 371      33.861  14.129  23.470  1.00 10.13           C  
ANISOU 2973  C   VAL A 371      908   1456   1486     68    311    -41       C  
ATOM   2974  O   VAL A 371      35.007  14.046  23.937  1.00 11.18           O  
ANISOU 2974  O   VAL A 371     1031   1528   1691    -14     88    -12       O  
ATOM   2975  CB  VAL A 371      34.145  15.437  21.327  1.00 11.41           C  
ANISOU 2975  CB  VAL A 371     1133   1844   1360   -145    123    -90       C  
ATOM   2976  CG1 VAL A 371      33.898  14.191  20.509  1.00 12.52           C  
ANISOU 2976  CG1 VAL A 371     1395   1882   1480    108    227   -172       C  
ATOM   2977  CG2 VAL A 371      33.725  16.681  20.557  1.00 14.96           C  
ANISOU 2977  CG2 VAL A 371     2313   1871   1501   -478     73    183       C  
ATOM   2978  N   PHE A 372      32.950  13.150  23.602  1.00 10.26           N  
ANISOU 2978  N   PHE A 372      940   1638   1319     -3    179     85       N  
ATOM   2979  CA  PHE A 372      33.202  11.970  24.374  1.00 10.49           C  
ANISOU 2979  CA  PHE A 372      993   1586   1408    -25    246    130       C  
ATOM   2980  C   PHE A 372      33.883  10.893  23.501  1.00 11.07           C  
ANISOU 2980  C   PHE A 372     1169   1574   1461    -67    210   -164       C  
ATOM   2981  O   PHE A 372      33.359   9.835  23.228  1.00 11.92           O  
ANISOU 2981  O   PHE A 372     1305   1550   1675   -155    196    -45       O  
ATOM   2982  CB  PHE A 372      31.918  11.527  25.049  1.00 11.79           C  
ANISOU 2982  CB  PHE A 372     1211   1663   1608   -171    338     40       C  
ATOM   2983  CG  PHE A 372      31.506  12.451  26.186  1.00 13.01           C  
ANISOU 2983  CG  PHE A 372     1118   2059   1765   -404    554   -185       C  
ATOM   2984  CD1 PHE A 372      32.131  12.373  27.437  1.00 16.31           C  
ANISOU 2984  CD1 PHE A 372     2024   2474   1698  -1082    355    -83       C  
ATOM   2985  CD2 PHE A 372      30.550  13.397  25.960  1.00 15.23           C  
ANISOU 2985  CD2 PHE A 372     1320   2119   2347   -259    868   -325       C  
ATOM   2986  CE1 PHE A 372      31.760  13.277  28.458  1.00 19.82           C  
ANISOU 2986  CE1 PHE A 372     2480   3206   1844  -1614    781   -426       C  
ATOM   2987  CE2 PHE A 372      30.107  14.277  26.942  1.00 19.63           C  
ANISOU 2987  CE2 PHE A 372     2121   2379   2960   -269   1320   -711       C  
ATOM   2988  CZ  PHE A 372      30.728  14.159  28.157  1.00 21.06           C  
ANISOU 2988  CZ  PHE A 372     2626   2761   2612  -1353   1376   -891       C  
ATOM   2989  N   SER A 373      35.095  11.281  23.038  1.00 12.31           N  
ANISOU 2989  N   SER A 373     1022   1808   1848    -92    320   -155       N  
ATOM   2990  CA  SER A 373      36.040  10.347  22.448  1.00 11.61           C  
ANISOU 2990  CA  SER A 373     1112   1714   1584    -24    225   -267       C  
ATOM   2991  C   SER A 373      36.809   9.618  23.535  1.00 10.97           C  
ANISOU 2991  C   SER A 373     1056   1613   1500   -165    250   -245       C  
ATOM   2992  O   SER A 373      36.465   9.745  24.718  1.00 12.31           O  
ANISOU 2992  O   SER A 373     1106   2014   1557   -233    385   -190       O  
ATOM   2993  CB ASER A 373      36.907  11.241  21.555  0.62 12.40           C  
ANISOU 2993  CB ASER A 373     1338   1664   1711    -25    369   -143       C  
ATOM   2994  CB BSER A 373      37.005  10.952  21.422  0.38 13.42           C  
ANISOU 2994  CB BSER A 373     1142   2506   1450    239    264     20       C  
ATOM   2995  OG ASER A 373      37.304  12.403  22.252  0.62 11.88           O  
ANISOU 2995  OG ASER A 373     1402   1735   1379    -49    328    -97       O  
ATOM   2996  OG BSER A 373      37.603   9.962  20.567  0.38 13.14           O  
ANISOU 2996  OG BSER A 373     1260   2127   1605     75    378     75       O  
ATOM   2997  N   HIS A 374      37.827   8.868  23.163  1.00 11.96           N  
ANISOU 2997  N   HIS A 374     1319   1718   1507     50    284   -253       N  
ATOM   2998  CA  HIS A 374      38.669   8.123  24.054  1.00 12.17           C  
ANISOU 2998  CA  HIS A 374     1305   1854   1464    -11    251   -277       C  
ATOM   2999  C   HIS A 374      40.136   8.483  23.841  1.00 12.73           C  
ANISOU 2999  C   HIS A 374     1156   1739   1942     95    245   -332       C  
ATOM   3000  O   HIS A 374      40.740   7.994  22.847  1.00 15.54           O  
ANISOU 3000  O   HIS A 374     1514   2320   2071   -115    594   -466       O  
ATOM   3001  CB  HIS A 374      38.538   6.600  23.872  1.00 13.24           C  
ANISOU 3001  CB  HIS A 374     1313   1827   1890   -104    275    -67       C  
ATOM   3002  CG  HIS A 374      37.106   6.176  24.102  1.00 14.13           C  
ANISOU 3002  CG  HIS A 374     1297   1958   2116    -37    227    141       C  
ATOM   3003  ND1 HIS A 374      36.618   5.920  25.368  1.00 18.46           N  
ANISOU 3003  ND1 HIS A 374     1534   3263   2217   -521    211    676       N  
ATOM   3004  CD2 HIS A 374      36.086   6.077  23.238  1.00 16.74           C  
ANISOU 3004  CD2 HIS A 374     1280   2977   2105   -338    353   -216       C  
ATOM   3005  CE1 HIS A 374      35.300   5.609  25.270  1.00 17.14           C  
ANISOU 3005  CE1 HIS A 374     1544   2769   2201   -392     70    423       C  
ATOM   3006  NE2 HIS A 374      34.993   5.690  24.004  1.00 16.36           N  
ANISOU 3006  NE2 HIS A 374     1465   2742   2011   -268    386     53       N  
ATOM   3007  N   PRO A 375      40.713   9.359  24.603  1.00 12.53           N  
ANISOU 3007  N   PRO A 375     1157   1613   1993     91    168   -170       N  
ATOM   3008  CA  PRO A 375      40.155  10.118  25.743  1.00 11.72           C  
ANISOU 3008  CA  PRO A 375     1315   1464   1673    134    124    -89       C  
ATOM   3009  C   PRO A 375      39.286  11.274  25.239  1.00 10.59           C  
ANISOU 3009  C   PRO A 375     1027   1521   1476    -46    206     53       C  
ATOM   3010  O   PRO A 375      39.286  11.630  24.069  1.00 10.77           O  
ANISOU 3010  O   PRO A 375     1004   1621   1468    -27    330     28       O  
ATOM   3011  CB  PRO A 375      41.398  10.601  26.464  1.00 14.21           C  
ANISOU 3011  CB  PRO A 375     1333   1892   2175    360   -161   -145       C  
ATOM   3012  CG  PRO A 375      42.473  10.559  25.524  1.00 18.14           C  
ANISOU 3012  CG  PRO A 375     1677   3024   2191   -743    134   -214       C  
ATOM   3013  CD  PRO A 375      42.154   9.695  24.391  1.00 13.01           C  
ANISOU 3013  CD  PRO A 375     1104   1614   2227     32    178     44       C  
ATOM   3014  N   PRO A 376      38.539  11.905  26.160  1.00 10.47           N  
ANISOU 3014  N   PRO A 376     1108   1452   1419     22    303     27       N  
ATOM   3015  CA  PRO A 376      37.634  12.995  25.774  1.00 10.09           C  
ANISOU 3015  CA  PRO A 376      860   1636   1337    -38    198     89       C  
ATOM   3016  C   PRO A 376      38.389  14.255  25.353  1.00  9.17           C  
ANISOU 3016  C   PRO A 376      853   1360   1270    154    366    -76       C  
ATOM   3017  O   PRO A 376      39.528  14.516  25.734  1.00 10.67           O  
ANISOU 3017  O   PRO A 376      836   1731   1488     46    239    231       O  
ATOM   3018  CB  PRO A 376      36.797  13.242  27.028  1.00 11.96           C  
ANISOU 3018  CB  PRO A 376      973   1920   1652     68    364      4       C  
ATOM   3019  CG  PRO A 376      37.638  12.684  28.123  1.00 14.18           C  
ANISOU 3019  CG  PRO A 376     1944   2017   1427    433    555    199       C  
ATOM   3020  CD  PRO A 376      38.395  11.535  27.581  1.00 11.48           C  
ANISOU 3020  CD  PRO A 376     1177   1735   1450    -16    177    149       C  
ATOM   3021  N   ILE A 377      37.677  15.080  24.605  1.00  9.70           N  
ANISOU 3021  N   ILE A 377      820   1419   1445     -1    145     -3       N  
ATOM   3022  CA  ILE A 377      38.100  16.376  24.064  1.00  9.80           C  
ANISOU 3022  CA  ILE A 377      927   1482   1314    -40    264     35       C  
ATOM   3023  C   ILE A 377      37.314  17.468  24.748  1.00  9.96           C  
ANISOU 3023  C   ILE A 377      891   1420   1475     40    345     34       C  
ATOM   3024  O   ILE A 377      36.108  17.362  24.917  1.00 10.56           O  
ANISOU 3024  O   ILE A 377      800   1637   1577    -32    231     48       O  
ATOM   3025  CB  ILE A 377      37.852  16.443  22.548  1.00 10.97           C  
ANISOU 3025  CB  ILE A 377      989   1818   1362     22    298      8       C  
ATOM   3026  CG1 ILE A 377      38.726  15.460  21.803  1.00 12.23           C  
ANISOU 3026  CG1 ILE A 377     1048   2096   1504    -33    397   -314       C  
ATOM   3027  CG2 ILE A 377      37.952  17.866  21.989  1.00 12.49           C  
ANISOU 3027  CG2 ILE A 377     1126   2029   1591    -43    155    340       C  
ATOM   3028  CD1 ILE A 377      38.261  15.115  20.436  1.00 14.02           C  
ANISOU 3028  CD1 ILE A 377     1351   2517   1460    -49    328   -334       C  
ATOM   3029  N   GLY A 378      37.995  18.565  25.102  1.00 10.06           N  
ANISOU 3029  N   GLY A 378      835   1485   1503     55    248    -10       N  
ATOM   3030  CA  GLY A 378      37.336  19.785  25.535  1.00 10.72           C  
ANISOU 3030  CA  GLY A 378      965   1529   1579     22    371    -32       C  
ATOM   3031  C   GLY A 378      37.813  20.979  24.761  1.00 11.10           C  
ANISOU 3031  C   GLY A 378      975   1486   1756     62    287    108       C  
ATOM   3032  O   GLY A 378      39.032  21.129  24.505  1.00 12.90           O  
ANISOU 3032  O   GLY A 378      888   1544   2468     58    303    195       O  
ATOM   3033  N   THR A 379      36.924  21.887  24.382  1.00 10.81           N  
ANISOU 3033  N   THR A 379      896   1489   1724    -13    336    130       N  
ATOM   3034  CA  THR A 379      37.296  23.084  23.676  1.00 11.30           C  
ANISOU 3034  CA  THR A 379     1011   1500   1783     89    462    170       C  
ATOM   3035  C   THR A 379      36.395  24.253  24.043  1.00 10.58           C  
ANISOU 3035  C   THR A 379      921   1473   1627     47    224    183       C  
ATOM   3036  O   THR A 379      35.197  24.079  24.254  1.00 11.03           O  
ANISOU 3036  O   THR A 379      952   1516   1722      4    369    177       O  
ATOM   3037  CB  THR A 379      37.308  22.839  22.151  1.00 12.78           C  
ANISOU 3037  CB  THR A 379     1326   1724   1804     85    488    117       C  
ATOM   3038  OG1 THR A 379      37.751  23.975  21.430  1.00 15.11           O  
ANISOU 3038  OG1 THR A 379     1588   2048   2107   -134    419    426       O  
ATOM   3039  CG2 THR A 379      35.955  22.484  21.613  1.00 14.68           C  
ANISOU 3039  CG2 THR A 379     1433   2203   1943    -70    283    111       C  
ATOM   3040  N   VAL A 380      36.996  25.426  24.112  1.00 11.02           N  
ANISOU 3040  N   VAL A 380     1021   1501   1665     14    387    210       N  
ATOM   3041  CA  VAL A 380      36.211  26.661  24.229  1.00 11.09           C  
ANISOU 3041  CA  VAL A 380      947   1457   1811    -14    315    185       C  
ATOM   3042  C   VAL A 380      36.940  27.755  23.491  1.00 10.74           C  
ANISOU 3042  C   VAL A 380     1175   1400   1507    -60    170    147       C  
ATOM   3043  O   VAL A 380      38.166  27.849  23.515  1.00 12.21           O  
ANISOU 3043  O   VAL A 380     1034   1663   1940   -105    300    248       O  
ATOM   3044  CB  VAL A 380      35.902  27.030  25.694  1.00 11.33           C  
ANISOU 3044  CB  VAL A 380     1123   1599   1582     -5    230    233       C  
ATOM   3045  CG1 VAL A 380      37.153  27.325  26.501  1.00 13.47           C  
ANISOU 3045  CG1 VAL A 380     1135   2021   1963     82    229     98       C  
ATOM   3046  CG2 VAL A 380      34.887  28.155  25.789  1.00 12.99           C  
ANISOU 3046  CG2 VAL A 380     1264   1660   2011    102    254     51       C  
ATOM   3047  N   GLY A 381      36.204  28.659  22.860  1.00 11.86           N  
ANISOU 3047  N   GLY A 381     1110   1540   1859    -36    229    277       N  
ATOM   3048  CA  GLY A 381      36.783  29.802  22.142  1.00 12.64           C  
ANISOU 3048  CA  GLY A 381     1417   1430   1955    109    394    346       C  
ATOM   3049  C   GLY A 381      37.308  29.435  20.765  1.00 11.77           C  
ANISOU 3049  C   GLY A 381     1162   1439   1871    109    205    328       C  
ATOM   3050  O   GLY A 381      36.918  28.482  20.142  1.00 14.38           O  
ANISOU 3050  O   GLY A 381     1739   1774   1951   -276    408    156       O  
ATOM   3051  N   LEU A 382      38.225  30.298  20.316  1.00 12.85           N  
ANISOU 3051  N   LEU A 382     1268   1826   1789   -165    267    350       N  
ATOM   3052  CA  LEU A 382      38.722  30.280  18.949  1.00 13.09           C  
ANISOU 3052  CA  LEU A 382     1317   1866   1791    -41    312    520       C  
ATOM   3053  C   LEU A 382      39.820  29.283  18.751  1.00 13.45           C  
ANISOU 3053  C   LEU A 382     1584   1727   1800     17    335    574       C  
ATOM   3054  O   LEU A 382      40.726  29.110  19.566  1.00 13.43           O  
ANISOU 3054  O   LEU A 382     1455   1746   1901     92    317    364       O  
ATOM   3055  CB  LEU A 382      39.322  31.680  18.636  1.00 14.33           C  
ANISOU 3055  CB  LEU A 382     1477   1809   2160     -7    270    670       C  
ATOM   3056  CG  LEU A 382      38.319  32.814  18.710  1.00 16.19           C  
ANISOU 3056  CG  LEU A 382     1646   1907   2598    163    539    625       C  
ATOM   3057  CD1 LEU A 382      39.032  34.094  18.238  1.00 21.37           C  
ANISOU 3057  CD1 LEU A 382     2321   1883   3917     25    525   1000       C  
ATOM   3058  CD2 LEU A 382      37.040  32.562  17.944  1.00 21.22           C  
ANISOU 3058  CD2 LEU A 382     1905   2270   3887    407   -174    287       C  
ATOM   3059  N   THR A 383      39.811  28.623  17.602  1.00 13.52           N  
ANISOU 3059  N   THR A 383     1403   1863   1872      5    175    473       N  
ATOM   3060  CA  THR A 383      40.940  27.866  17.127  1.00 13.76           C  
ANISOU 3060  CA  THR A 383     1511   1927   1792     19    283    489       C  
ATOM   3061  C   THR A 383      42.104  28.829  16.843  1.00 14.14           C  
ANISOU 3061  C   THR A 383     1534   2041   1798    -26    332    503       C  
ATOM   3062  O   THR A 383      41.907  30.037  16.694  1.00 14.57           O  
ANISOU 3062  O   THR A 383     1595   1993   1950   -138    271    465       O  
ATOM   3063  CB  THR A 383      40.656  27.040  15.850  1.00 15.60           C  
ANISOU 3063  CB  THR A 383     1877   2163   1888    -56    273    270       C  
ATOM   3064  OG1 THR A 383      40.485  27.996  14.761  1.00 16.42           O  
ANISOU 3064  OG1 THR A 383     2107   2365   1766    -86    265    338       O  
ATOM   3065  CG2 THR A 383      39.435  26.200  15.965  1.00 16.68           C  
ANISOU 3065  CG2 THR A 383     2220   2089   2029   -208    184    310       C  
ATOM   3066  N   GLU A 384      43.308  28.262  16.779  1.00 14.23           N  
ANISOU 3066  N   GLU A 384     1523   1951   1931   -139    339    257       N  
ATOM   3067  CA  GLU A 384      44.458  29.105  16.412  1.00 14.50           C  
ANISOU 3067  CA  GLU A 384     1532   2146   1830   -189    370    250       C  
ATOM   3068  C   GLU A 384      44.244  29.844  15.086  1.00 15.87           C  
ANISOU 3068  C   GLU A 384     1601   2423   2008     -9    442    493       C  
ATOM   3069  O   GLU A 384      44.482  31.016  14.924  1.00 17.46           O  
ANISOU 3069  O   GLU A 384     1714   2600   2320   -185    426    778       O  
ATOM   3070  CB  GLU A 384      45.722  28.263  16.364  1.00 15.57           C  
ANISOU 3070  CB  GLU A 384     1550   2189   2177   -118    283    360       C  
ATOM   3071  CG  GLU A 384      46.963  29.014  16.056  1.00 17.94           C  
ANISOU 3071  CG  GLU A 384     1597   2917   2303   -188    402    641       C  
ATOM   3072  CD  GLU A 384      48.244  28.212  16.098  1.00 22.19           C  
ANISOU 3072  CD  GLU A 384     1638   3493   3299     25    730    806       C  
ATOM   3073  OE1 GLU A 384      49.297  28.819  15.723  1.00 26.20           O  
ANISOU 3073  OE1 GLU A 384     1770   4343   3842   -145   1008    948       O  
ATOM   3074  OE2 GLU A 384      48.226  27.020  16.486  1.00 22.04           O  
ANISOU 3074  OE2 GLU A 384     1719   3240   3415    216    574    473       O  
ATOM   3075  N   ASP A 385      43.739  29.109  14.107  1.00 17.74           N  
ANISOU 3075  N   ASP A 385     2122   2857   1760     15    387    421       N  
ATOM   3076  CA  ASP A 385      43.521  29.779  12.807  1.00 19.55           C  
ANISOU 3076  CA  ASP A 385     2248   3180   2000    -70    277    639       C  
ATOM   3077  C   ASP A 385      42.431  30.828  12.853  1.00 18.69           C  
ANISOU 3077  C   ASP A 385     2258   3010   1832   -130    354    866       C  
ATOM   3078  O   ASP A 385      42.550  31.877  12.216  1.00 20.58           O  
ANISOU 3078  O   ASP A 385     2563   3080   2177   -470    153   1026       O  
ATOM   3079  CB  ASP A 385      43.178  28.744  11.757  1.00 24.59           C  
ANISOU 3079  CB  ASP A 385     3441   4213   1688    154    706    -16       C  
ATOM   3080  CG  ASP A 385      44.365  27.876  11.390  1.00 33.86           C  
ANISOU 3080  CG  ASP A 385     4492   6007   2366   1304   1011   -516       C  
ATOM   3081  OD1 ASP A 385      44.070  26.767  10.893  1.00 43.72           O  
ANISOU 3081  OD1 ASP A 385     5200   6272   5139   1401   1826  -1719       O  
ATOM   3082  OD2 ASP A 385      45.534  28.289  11.600  1.00 37.14           O  
ANISOU 3082  OD2 ASP A 385     3997   5251   4862   1575   1484    621       O  
ATOM   3083  N   GLU A 386      41.364  30.589  13.594  1.00 17.32           N  
ANISOU 3083  N   GLU A 386     1887   2448   2244   -202    125    715       N  
ATOM   3084  CA  GLU A 386      40.329  31.635  13.748  1.00 17.40           C  
ANISOU 3084  CA  GLU A 386     2066   2505   2041    -39     67    878       C  
ATOM   3085  C   GLU A 386      40.856  32.861  14.433  1.00 16.63           C  
ANISOU 3085  C   GLU A 386     1501   2476   2343    132    262    788       C  
ATOM   3086  O   GLU A 386      40.558  34.001  14.062  1.00 18.11           O  
ANISOU 3086  O   GLU A 386     2018   2444   2419    125      4    890       O  
ATOM   3087  CB  GLU A 386      39.156  31.075  14.545  1.00 17.83           C  
ANISOU 3087  CB  GLU A 386     1925   2535   2317   -109    101    750       C  
ATOM   3088  CG  GLU A 386      38.271  30.079  13.805  1.00 18.73           C  
ANISOU 3088  CG  GLU A 386     2159   2526   2431   -128    224    500       C  
ATOM   3089  CD  GLU A 386      37.306  29.264  14.651  1.00 21.17           C  
ANISOU 3089  CD  GLU A 386     2278   3216   2552   -639    144    408       C  
ATOM   3090  OE1 GLU A 386      36.405  28.628  14.019  1.00 33.53           O  
ANISOU 3090  OE1 GLU A 386     3475   5833   3431  -2308  -1169   1444       O  
ATOM   3091  OE2 GLU A 386      37.446  29.213  15.923  1.00 18.53           O  
ANISOU 3091  OE2 GLU A 386     2095   2475   2470   -239    259    302       O  
ATOM   3092  N   ALA A 387      41.730  32.653  15.440  1.00 16.07           N  
ANISOU 3092  N   ALA A 387     1961   2014   2130     50    226    698       N  
ATOM   3093  CA  ALA A 387      42.336  33.787  16.127  1.00 15.63           C  
ANISOU 3093  CA  ALA A 387     2073   1800   2065    124    286    754       C  
ATOM   3094  C   ALA A 387      43.282  34.531  15.202  1.00 16.65           C  
ANISOU 3094  C   ALA A 387     1807   2418   2101    -48    169    898       C  
ATOM   3095  O   ALA A 387      43.302  35.776  15.200  1.00 17.82           O  
ANISOU 3095  O   ALA A 387     1842   2315   2611   -140     46   1135       O  
ATOM   3096  CB  ALA A 387      43.100  33.321  17.386  1.00 15.71           C  
ANISOU 3096  CB  ALA A 387     1845   2246   1878    207    474    695       C  
ATOM   3097  N   ILE A 388      44.066  33.830  14.405  1.00 17.54           N  
ANISOU 3097  N   ILE A 388     2058   2540   2064   -142    354    923       N  
ATOM   3098  CA  ILE A 388      44.947  34.533  13.441  1.00 18.45           C  
ANISOU 3098  CA  ILE A 388     2022   2700   2286   -202    326   1064       C  
ATOM   3099  C   ILE A 388      44.115  35.350  12.489  1.00 20.04           C  
ANISOU 3099  C   ILE A 388     2371   2876   2367   -492     47   1281       C  
ATOM   3100  O   ILE A 388      44.484  36.523  12.179  1.00 19.95           O  
ANISOU 3100  O   ILE A 388     2488   2854   2237   -585    105   1142       O  
ATOM   3101  CB  ILE A 388      45.874  33.514  12.752  1.00 18.48           C  
ANISOU 3101  CB  ILE A 388     2154   2904   1964   -444    409    762       C  
ATOM   3102  CG1 ILE A 388      46.922  32.914  13.676  1.00 19.56           C  
ANISOU 3102  CG1 ILE A 388     1858   3008   2566   -129    406    520       C  
ATOM   3103  CG2 ILE A 388      46.568  34.231  11.584  1.00 25.45           C  
ANISOU 3103  CG2 ILE A 388     3260   3774   2637   -680   1087   1067       C  
ATOM   3104  CD1 ILE A 388      47.691  31.720  13.252  1.00 21.72           C  
ANISOU 3104  CD1 ILE A 388     2394   3307   2551    125   1132    679       C  
ATOM   3105  N   HIS A 389      43.003  34.827  11.987  1.00 19.75           N  
ANISOU 3105  N   HIS A 389     2728   2582   2192   -510   -189   1097       N  
ATOM   3106  CA  HIS A 389      42.172  35.624  11.086  1.00 21.34           C  
ANISOU 3106  CA  HIS A 389     2558   3062   2487   -558   -158   1361       C  
ATOM   3107  C   HIS A 389      41.632  36.876  11.746  1.00 22.67           C  
ANISOU 3107  C   HIS A 389     2717   3206   2689    -76   -331   1407       C  
ATOM   3108  O   HIS A 389      41.577  38.012  11.212  1.00 25.11           O  
ANISOU 3108  O   HIS A 389     3128   3198   3213   -418   -396   1704       O  
ATOM   3109  CB  HIS A 389      41.051  34.703  10.535  1.00 23.95           C  
ANISOU 3109  CB  HIS A 389     2726   3487   2886   -854   -432   1471       C  
ATOM   3110  CG  HIS A 389      40.127  35.503   9.647  1.00 22.01           C  
ANISOU 3110  CG  HIS A 389     2870   3167   2326   -403   -208    874       C  
ATOM   3111  ND1 HIS A 389      40.483  36.010   8.407  1.00 28.48           N  
ANISOU 3111  ND1 HIS A 389     3359   4688   2774    -65    -65   1651       N  
ATOM   3112  CD2 HIS A 389      38.812  35.853   9.783  1.00 23.07           C  
ANISOU 3112  CD2 HIS A 389     3165   3171   2430      5   -202    289       C  
ATOM   3113  CE1 HIS A 389      39.478  36.658   7.841  1.00 26.28           C  
ANISOU 3113  CE1 HIS A 389     3736   3532   2719   -203   -540   1043       C  
ATOM   3114  NE2 HIS A 389      38.438  36.581   8.671  1.00 25.08           N  
ANISOU 3114  NE2 HIS A 389     3331   3423   2776   -216   -657    539       N  
ATOM   3115  N   LYS A 390      41.142  36.745  12.978  1.00 21.35           N  
ANISOU 3115  N   LYS A 390     2655   2798   2657      9   -356   1330       N  
ATOM   3116  CA  LYS A 390      40.531  37.833  13.698  1.00 21.81           C  
ANISOU 3116  CA  LYS A 390     2240   2817   3231      4   -253   1198       C  
ATOM   3117  C   LYS A 390      41.509  38.921  14.159  1.00 23.47           C  
ANISOU 3117  C   LYS A 390     2746   2542   3631   -127   -390   1337       C  
ATOM   3118  O   LYS A 390      41.249  40.113  13.991  1.00 25.46           O  
ANISOU 3118  O   LYS A 390     2795   2623   4254     47   -263   1431       O  
ATOM   3119  CB  LYS A 390      39.837  37.280  14.951  1.00 22.30           C  
ANISOU 3119  CB  LYS A 390     2481   2516   3475     40     96    928       C  
ATOM   3120  CG  LYS A 390      39.155  38.392  15.760  1.00 23.91           C  
ANISOU 3120  CG  LYS A 390     2560   2677   3846    522    236   1154       C  
ATOM   3121  CD  LYS A 390      38.158  37.783  16.743  1.00 27.81           C  
ANISOU 3121  CD  LYS A 390     2662   3632   4273    853    599   1688       C  
ATOM   3122  CE  LYS A 390      37.562  38.869  17.655  1.00 32.31           C  
ANISOU 3122  CE  LYS A 390     3091   4371   4813    571   1081   1016       C  
ATOM   3123  NZ  LYS A 390      36.272  39.424  17.105  1.00 46.73           N  
ANISOU 3123  NZ  LYS A 390     4496   5804   7454   2475   -749  -1959       N  
ATOM   3124  N   TYR A 391      42.610  38.497  14.741  1.00 19.97           N  
ANISOU 3124  N   TYR A 391     2236   2470   2880    -74     83   1022       N  
ATOM   3125  CA  TYR A 391      43.562  39.402  15.362  1.00 21.49           C  
ANISOU 3125  CA  TYR A 391     2543   2497   3127   -386     59   1218       C  
ATOM   3126  C   TYR A 391      44.808  39.719  14.540  1.00 21.82           C  
ANISOU 3126  C   TYR A 391     2558   2379   3353   -309    184   1096       C  
ATOM   3127  O   TYR A 391      45.509  40.694  14.857  1.00 24.72           O  
ANISOU 3127  O   TYR A 391     2898   2713   3780   -716    462    805       O  
ATOM   3128  CB  TYR A 391      44.021  38.840  16.730  1.00 21.53           C  
ANISOU 3128  CB  TYR A 391     2566   2608   3007   -140    -32    934       C  
ATOM   3129  CG  TYR A 391      42.896  38.751  17.723  1.00 20.52           C  
ANISOU 3129  CG  TYR A 391     2577   2416   2805    -58    -77    835       C  
ATOM   3130  CD1 TYR A 391      42.303  37.539  18.054  1.00 20.04           C  
ANISOU 3130  CD1 TYR A 391     2471   2461   2683     37   -188   1057       C  
ATOM   3131  CD2 TYR A 391      42.400  39.874  18.363  1.00 24.29           C  
ANISOU 3131  CD2 TYR A 391     2901   2584   3743   -216    226    445       C  
ATOM   3132  CE1 TYR A 391      41.274  37.461  18.972  1.00 22.64           C  
ANISOU 3132  CE1 TYR A 391     3106   2709   2789   -278    149    827       C  
ATOM   3133  CE2 TYR A 391      41.375  39.801  19.277  1.00 24.81           C  
ANISOU 3133  CE2 TYR A 391     3174   2659   3593    367    375    817       C  
ATOM   3134  CZ  TYR A 391      40.789  38.589  19.583  1.00 22.52           C  
ANISOU 3134  CZ  TYR A 391     2460   2974   3122    110    -45    785       C  
ATOM   3135  OH  TYR A 391      39.764  38.448  20.503  1.00 27.24           O  
ANISOU 3135  OH  TYR A 391     3155   3774   3420    426    497   1239       O  
ATOM   3136  N   GLY A 392      45.147  38.935  13.530  1.00 22.50           N  
ANISOU 3136  N   GLY A 392     2830   2778   2942   -468     79   1095       N  
ATOM   3137  CA  GLY A 392      46.394  39.103  12.791  1.00 22.35           C  
ANISOU 3137  CA  GLY A 392     3156   2533   2802   -627    274   1121       C  
ATOM   3138  C   GLY A 392      47.445  38.163  13.342  1.00 22.45           C  
ANISOU 3138  C   GLY A 392     2866   2941   2722   -467    453   1144       C  
ATOM   3139  O   GLY A 392      47.639  37.910  14.528  1.00 21.99           O  
ANISOU 3139  O   GLY A 392     2495   3184   2678   -521    366   1028       O  
ATOM   3140  N   ILE A 393      48.222  37.606  12.413  1.00 23.02           N  
ANISOU 3140  N   ILE A 393     3182   2916   2647   -538    423   1008       N  
ATOM   3141  CA  ILE A 393      49.247  36.607  12.797  1.00 24.06           C  
ANISOU 3141  CA  ILE A 393     2518   3445   3179   -497    898   1212       C  
ATOM   3142  C   ILE A 393      50.248  37.172  13.808  1.00 26.12           C  
ANISOU 3142  C   ILE A 393     2749   3715   3462   -673    537   1477       C  
ATOM   3143  O   ILE A 393      50.713  36.472  14.715  1.00 27.25           O  
ANISOU 3143  O   ILE A 393     3226   3996   3132   -578    726   1506       O  
ATOM   3144  CB  ILE A 393      49.934  36.037  11.552  1.00 28.05           C  
ANISOU 3144  CB  ILE A 393     2712   4887   3058    -14    975   1309       C  
ATOM   3145  CG1 ILE A 393      50.800  34.794  11.815  1.00 29.89           C  
ANISOU 3145  CG1 ILE A 393     2512   5554   3291    502   1101    941       C  
ATOM   3146  CG2 ILE A 393      50.702  37.124  10.770  1.00 31.60           C  
ANISOU 3146  CG2 ILE A 393     2756   6377   2875   -621    656   1870       C  
ATOM   3147  CD1 ILE A 393      51.344  34.174  10.546  1.00 38.33           C  
ANISOU 3147  CD1 ILE A 393     5158   5746   3660    763   1711    640       C  
ATOM   3148  N   GLU A 394      50.583  38.450  13.674  1.00 25.59           N  
ANISOU 3148  N   GLU A 394     2644   3602   3478   -671    791   1211       N  
ATOM   3149  CA  GLU A 394      51.618  39.011  14.558  1.00 26.09           C  
ANISOU 3149  CA  GLU A 394     2356   3881   3677   -831    517   1834       C  
ATOM   3150  C   GLU A 394      51.062  39.199  15.965  1.00 26.15           C  
ANISOU 3150  C   GLU A 394     2710   3695   3529   -927    296   1562       C  
ATOM   3151  O   GLU A 394      51.850  39.461  16.878  1.00 28.64           O  
ANISOU 3151  O   GLU A 394     2636   4262   3985  -1160    325   1098       O  
ATOM   3152  CB AGLU A 394      52.095  40.346  13.966  0.45 29.35           C  
ANISOU 3152  CB AGLU A 394     3467   3859   3826  -1202    614   1648       C  
ATOM   3153  CB BGLU A 394      52.249  40.273  13.960  0.55 27.72           C  
ANISOU 3153  CB BGLU A 394     3150   3534   3849   -891    728   1518       C  
ATOM   3154  CG AGLU A 394      50.990  41.383  13.899  0.45 32.26           C  
ANISOU 3154  CG AGLU A 394     4027   3730   4501   -986    596   1990       C  
ATOM   3155  CG BGLU A 394      53.038  40.051  12.680  0.55 30.80           C  
ANISOU 3155  CG BGLU A 394     3468   4801   3435  -1332    674   1892       C  
ATOM   3156  CD AGLU A 394      50.286  41.512  12.560  0.45 35.76           C  
ANISOU 3156  CD AGLU A 394     4039   4592   4957  -1325    263   2800       C  
ATOM   3157  CD BGLU A 394      53.949  38.839  12.636  0.55 36.29           C  
ANISOU 3157  CD BGLU A 394     2924   7145   3721    -70   1343   1540       C  
ATOM   3158  OE1AGLU A 394      49.599  40.577  12.073  0.45 29.30           O  
ANISOU 3158  OE1AGLU A 394     2902   4297   3935   -810    821   2748       O  
ATOM   3159  OE1BGLU A 394      54.393  38.361  13.710  0.55 64.44           O  
ANISOU 3159  OE1BGLU A 394     8167  10044   6274   2898  -1491   2145       O  
ATOM   3160  OE2AGLU A 394      50.412  42.619  11.986  0.45 62.00           O  
ANISOU 3160  OE2AGLU A 394    11128   4042   8388  -2312  -4413   3685       O  
ATOM   3161  OE2BGLU A 394      54.222  38.312  11.528  0.55 53.21           O  
ANISOU 3161  OE2BGLU A 394     4133   9602   6484   -547      5  -2642       O  
ATOM   3162  N   ASN A 395      49.735  39.064  16.165  1.00 22.78           N  
ANISOU 3162  N   ASN A 395     2650   3123   2881   -776    282   1486       N  
ATOM   3163  CA  ASN A 395      49.077  39.377  17.425  1.00 22.23           C  
ANISOU 3163  CA  ASN A 395     2958   2656   2831   -839    130   1090       C  
ATOM   3164  C   ASN A 395      48.505  38.144  18.119  1.00 20.16           C  
ANISOU 3164  C   ASN A 395     2564   2531   2566   -820    409    751       C  
ATOM   3165  O   ASN A 395      47.754  38.243  19.075  1.00 22.40           O  
ANISOU 3165  O   ASN A 395     3251   2390   2871   -795    808    555       O  
ATOM   3166  CB  ASN A 395      47.939  40.396  17.265  1.00 22.51           C  
ANISOU 3166  CB  ASN A 395     2901   2578   3075   -917     73   1019       C  
ATOM   3167  CG  ASN A 395      48.507  41.641  16.626  1.00 26.77           C  
ANISOU 3167  CG  ASN A 395     3081   2875   4213  -1223   -460   1716       C  
ATOM   3168  OD1 ASN A 395      49.386  42.240  17.272  1.00 28.10           O  
ANISOU 3168  OD1 ASN A 395     2955   3054   4667  -1172   -327   1331       O  
ATOM   3169  ND2 ASN A 395      48.015  41.976  15.440  1.00 30.66           N  
ANISOU 3169  ND2 ASN A 395     3436   3594   4617  -1192   -666   2335       N  
ATOM   3170  N   VAL A 396      48.902  36.961  17.654  1.00 18.35           N  
ANISOU 3170  N   VAL A 396     2129   2597   2247   -658    254    836       N  
ATOM   3171  CA  VAL A 396      48.490  35.697  18.298  1.00 16.52           C  
ANISOU 3171  CA  VAL A 396     1806   2569   1901   -364    453    819       C  
ATOM   3172  C   VAL A 396      49.702  34.888  18.685  1.00 18.52           C  
ANISOU 3172  C   VAL A 396     1549   3007   2482   -584    360   1127       C  
ATOM   3173  O   VAL A 396      50.669  34.744  17.927  1.00 19.98           O  
ANISOU 3173  O   VAL A 396     1666   3205   2722   -298    441   1179       O  
ATOM   3174  CB  VAL A 396      47.603  34.903  17.339  1.00 17.77           C  
ANISOU 3174  CB  VAL A 396     1800   2592   2358   -465    251    827       C  
ATOM   3175  CG1 VAL A 396      47.285  33.497  17.887  1.00 18.07           C  
ANISOU 3175  CG1 VAL A 396     2223   2562   2080   -354    604    733       C  
ATOM   3176  CG2 VAL A 396      46.343  35.663  17.002  1.00 20.45           C  
ANISOU 3176  CG2 VAL A 396     1872   3086   2813   -441    106   1229       C  
ATOM   3177  N   LYS A 397      49.695  34.378  19.908  1.00 17.18           N  
ANISOU 3177  N   LYS A 397     1676   2452   2401   -563    225    911       N  
ATOM   3178  CA  LYS A 397      50.736  33.505  20.449  1.00 18.41           C  
ANISOU 3178  CA  LYS A 397     1531   2680   2783   -594    158   1015       C  
ATOM   3179  C   LYS A 397      50.049  32.251  21.002  1.00 16.47           C  
ANISOU 3179  C   LYS A 397     1203   2515   2540   -345    252    891       C  
ATOM   3180  O   LYS A 397      49.091  32.394  21.755  1.00 17.29           O  
ANISOU 3180  O   LYS A 397     1591   2343   2633   -336    439    734       O  
ATOM   3181  CB  LYS A 397      51.610  34.161  21.496  1.00 20.61           C  
ANISOU 3181  CB  LYS A 397     2132   2704   2995   -824   -182   1177       C  
ATOM   3182  CG  LYS A 397      52.720  33.227  22.007  1.00 29.24           C  
ANISOU 3182  CG  LYS A 397     3168   3443   4500   -825  -1416   2091       C  
ATOM   3183  CD  LYS A 397      53.859  33.852  22.765  1.00 36.92           C  
ANISOU 3183  CD  LYS A 397     3256   5021   5753  -1371  -1791   2207       C  
ATOM   3184  CE  LYS A 397      54.859  32.777  23.149  1.00 40.81           C  
ANISOU 3184  CE  LYS A 397     2002   7086   6419   -600   -776   2676       C  
ATOM   3185  NZ  LYS A 397      55.783  33.187  24.257  1.00 46.40           N  
ANISOU 3185  NZ  LYS A 397     2670   9360   5600  -1146   -979   3691       N  
ATOM   3186  N   THR A 398      50.577  31.102  20.674  1.00 16.32           N  
ANISOU 3186  N   THR A 398     1345   2719   2139   -106    410   1139       N  
ATOM   3187  CA  THR A 398      50.030  29.855  21.231  1.00 15.52           C  
ANISOU 3187  CA  THR A 398     1332   2405   2161   -225    446    726       C  
ATOM   3188  C   THR A 398      51.060  29.234  22.166  1.00 14.84           C  
ANISOU 3188  C   THR A 398     1361   2137   2143    -73    579    732       C  
ATOM   3189  O   THR A 398      52.268  29.392  22.024  1.00 19.08           O  
ANISOU 3189  O   THR A 398     1287   3067   2897   -205    492   1320       O  
ATOM   3190  CB  THR A 398      49.608  28.815  20.157  1.00 19.35           C  
ANISOU 3190  CB  THR A 398     2140   3051   2163     10    350    228       C  
ATOM   3191  OG1 THR A 398      50.849  28.347  19.524  1.00 22.87           O  
ANISOU 3191  OG1 THR A 398     2385   3542   2763    369    410    179       O  
ATOM   3192  CG2 THR A 398      48.598  29.475  19.256  1.00 20.47           C  
ANISOU 3192  CG2 THR A 398     1579   4254   1943   -374    481    612       C  
ATOM   3193  N   TYR A 399      50.520  28.548  23.171  1.00 13.76           N  
ANISOU 3193  N   TYR A 399     1192   2095   1943   -328    342    500       N  
ATOM   3194  CA  TYR A 399      51.297  27.754  24.096  1.00 14.40           C  
ANISOU 3194  CA  TYR A 399     1317   2068   2087   -257    389    591       C  
ATOM   3195  C   TYR A 399      50.703  26.350  24.052  1.00 14.06           C  
ANISOU 3195  C   TYR A 399     1113   2030   2198   -201    283    543       C  
ATOM   3196  O   TYR A 399      49.494  26.195  24.099  1.00 15.83           O  
ANISOU 3196  O   TYR A 399     1098   2111   2806   -192    290    262       O  
ATOM   3197  CB  TYR A 399      51.246  28.309  25.535  1.00 14.76           C  
ANISOU 3197  CB  TYR A 399     1315   2204   2091   -241    205    499       C  
ATOM   3198  CG  TYR A 399      51.817  29.697  25.703  1.00 16.64           C  
ANISOU 3198  CG  TYR A 399     1627   2275   2420   -432      4    515       C  
ATOM   3199  CD1 TYR A 399      51.043  30.838  25.482  1.00 17.53           C  
ANISOU 3199  CD1 TYR A 399     1792   2221   2647   -381   -292    403       C  
ATOM   3200  CD2 TYR A 399      53.145  29.876  26.083  1.00 18.65           C  
ANISOU 3200  CD2 TYR A 399     1696   2376   3012   -463   -221    470       C  
ATOM   3201  CE1 TYR A 399      51.575  32.103  25.629  1.00 19.74           C  
ANISOU 3201  CE1 TYR A 399     2502   2228   2770   -469   -402    259       C  
ATOM   3202  CE2 TYR A 399      53.684  31.143  26.237  1.00 21.67           C  
ANISOU 3202  CE2 TYR A 399     2496   2379   3359   -712   -892    430       C  
ATOM   3203  CZ  TYR A 399      52.887  32.247  26.007  1.00 22.08           C  
ANISOU 3203  CZ  TYR A 399     2863   2229   3298   -807  -1129    578       C  
ATOM   3204  OH  TYR A 399      53.508  33.448  26.201  1.00 27.50           O  
ANISOU 3204  OH  TYR A 399     3308   2299   4842  -1053  -1180    717       O  
ATOM   3205  N   SER A 400      51.530  25.322  24.063  1.00 16.44           N  
ANISOU 3205  N   SER A 400     1035   2112   3101   -158    297    564       N  
ATOM   3206  CA  SER A 400      50.988  23.961  23.997  1.00 14.87           C  
ANISOU 3206  CA  SER A 400     1093   2023   2532    -89    449    338       C  
ATOM   3207  C   SER A 400      51.876  23.008  24.757  1.00 15.72           C  
ANISOU 3207  C   SER A 400     1045   1996   2934   -124    437    311       C  
ATOM   3208  O   SER A 400      53.065  23.300  24.999  1.00 19.28           O  
ANISOU 3208  O   SER A 400     1019   2291   4014   -217    175    522       O  
ATOM   3209  CB  SER A 400      50.788  23.576  22.549  1.00 19.24           C  
ANISOU 3209  CB  SER A 400     2339   2590   2383   -242    804    295       C  
ATOM   3210  OG  SER A 400      51.931  23.483  21.810  1.00 26.94           O  
ANISOU 3210  OG  SER A 400     3195   3823   3217   -218   1692    154       O  
ATOM   3211  N   THR A 401      51.315  21.855  25.085  1.00 14.26           N  
ANISOU 3211  N   THR A 401      976   1947   2496   -103    316    322       N  
ATOM   3212  CA  THR A 401      52.079  20.752  25.658  1.00 14.16           C  
ANISOU 3212  CA  THR A 401     1043   2014   2321    -51    290    185       C  
ATOM   3213  C   THR A 401      51.474  19.438  25.188  1.00 12.64           C  
ANISOU 3213  C   THR A 401      874   1965   1964    -79    399    376       C  
ATOM   3214  O   THR A 401      50.295  19.373  24.825  1.00 13.55           O  
ANISOU 3214  O   THR A 401     1002   2013   2132    -20    296    298       O  
ATOM   3215  CB  THR A 401      52.141  20.855  27.201  1.00 16.63           C  
ANISOU 3215  CB  THR A 401     1596   2387   2336     99     13     68       C  
ATOM   3216  OG1 THR A 401      53.131  19.928  27.696  1.00 20.79           O  
ANISOU 3216  OG1 THR A 401     2205   3072   2621    686   -284   -112       O  
ATOM   3217  CG2 THR A 401      50.816  20.594  27.890  1.00 19.16           C  
ANISOU 3217  CG2 THR A 401     2152   2897   2229    314    584    172       C  
ATOM   3218  N   SER A 402      52.287  18.396  25.290  1.00 13.77           N  
ANISOU 3218  N   SER A 402     1014   1998   2219     50    453    391       N  
ATOM   3219  CA  SER A 402      51.885  16.999  25.069  1.00 13.96           C  
ANISOU 3219  CA  SER A 402     1034   2026   2246     54    351    447       C  
ATOM   3220  C   SER A 402      52.560  16.137  26.094  1.00 14.19           C  
ANISOU 3220  C   SER A 402      951   2057   2384     48    384    478       C  
ATOM   3221  O   SER A 402      53.780  16.331  26.318  1.00 18.00           O  
ANISOU 3221  O   SER A 402      976   2495   3368   -145    -11    857       O  
ATOM   3222  CB  SER A 402      52.262  16.565  23.634  1.00 19.56           C  
ANISOU 3222  CB  SER A 402     2557   2632   2245    192    165     36       C  
ATOM   3223  OG  SER A 402      51.919  15.246  23.286  1.00 21.85           O  
ANISOU 3223  OG  SER A 402     2371   2963   2969     65    319   -354       O  
ATOM   3224  N   PHE A 403      51.848  15.251  26.780  1.00 12.83           N  
ANISOU 3224  N   PHE A 403      938   1815   2121    126    284    324       N  
ATOM   3225  CA  PHE A 403      52.423  14.425  27.818  1.00 13.39           C  
ANISOU 3225  CA  PHE A 403      905   2000   2184     83     90    361       C  
ATOM   3226  C   PHE A 403      51.599  13.160  27.945  1.00 12.58           C  
ANISOU 3226  C   PHE A 403      950   1961   1870    111    243    336       C  
ATOM   3227  O   PHE A 403      50.493  13.054  27.445  1.00 13.89           O  
ANISOU 3227  O   PHE A 403     1043   1909   2326     33     27    369       O  
ATOM   3228  CB  PHE A 403      52.513  15.165  29.166  1.00 14.81           C  
ANISOU 3228  CB  PHE A 403     1275   2144   2207   -113     97    269       C  
ATOM   3229  CG  PHE A 403      51.189  15.577  29.757  1.00 13.96           C  
ANISOU 3229  CG  PHE A 403     1139   2355   1809   -114    -89    260       C  
ATOM   3230  CD1 PHE A 403      50.600  16.749  29.370  1.00 14.24           C  
ANISOU 3230  CD1 PHE A 403     1269   2194   1947   -105     10    102       C  
ATOM   3231  CD2 PHE A 403      50.516  14.797  30.686  1.00 14.68           C  
ANISOU 3231  CD2 PHE A 403     1695   2179   1702     -7    261     22       C  
ATOM   3232  CE1 PHE A 403      49.393  17.186  29.908  1.00 14.97           C  
ANISOU 3232  CE1 PHE A 403     1631   2233   1823   -100    343   -258       C  
ATOM   3233  CE2 PHE A 403      49.349  15.246  31.273  1.00 15.57           C  
ANISOU 3233  CE2 PHE A 403     1750   2335   1832    -43    401   -115       C  
ATOM   3234  CZ  PHE A 403      48.745  16.398  30.847  1.00 14.92           C  
ANISOU 3234  CZ  PHE A 403     1614   2275   1782    -49    319   -106       C  
ATOM   3235  N   THR A 404      52.159  12.169  28.620  1.00 14.27           N  
ANISOU 3235  N   THR A 404     1003   2264   2154    163    360    602       N  
ATOM   3236  CA  THR A 404      51.444  10.943  28.973  1.00 13.87           C  
ANISOU 3236  CA  THR A 404     1095   2058   2117    151    400    538       C  
ATOM   3237  C   THR A 404      50.958  11.084  30.384  1.00 13.52           C  
ANISOU 3237  C   THR A 404     1148   2076   1912    120    148    554       C  
ATOM   3238  O   THR A 404      51.793  11.222  31.282  1.00 17.22           O  
ANISOU 3238  O   THR A 404     1303   2987   2255     43   -137    844       O  
ATOM   3239  CB  THR A 404      52.369   9.716  28.812  1.00 17.27           C  
ANISOU 3239  CB  THR A 404     1380   2386   2796    472    683    694       C  
ATOM   3240  OG1 THR A 404      52.827   9.598  27.467  1.00 19.93           O  
ANISOU 3240  OG1 THR A 404     1842   2610   3122    630   1176    618       O  
ATOM   3241  CG2 THR A 404      51.566   8.430  29.101  1.00 18.89           C  
ANISOU 3241  CG2 THR A 404     2010   2126   3042    476    860    679       C  
ATOM   3242  N   PRO A 405      49.651  11.042  30.647  1.00 12.64           N  
ANISOU 3242  N   PRO A 405     1139   1939   1724    111    206    242       N  
ATOM   3243  CA  PRO A 405      49.161  11.124  32.046  1.00 12.95           C  
ANISOU 3243  CA  PRO A 405     1537   1847   1536    -69    147     80       C  
ATOM   3244  C   PRO A 405      49.762  10.036  32.907  1.00 12.62           C  
ANISOU 3244  C   PRO A 405     1394   1815   1588    -46    316     21       C  
ATOM   3245  O   PRO A 405      49.978   8.915  32.497  1.00 13.34           O  
ANISOU 3245  O   PRO A 405     1479   1828   1760    131    316    137       O  
ATOM   3246  CB  PRO A 405      47.661  10.902  31.874  1.00 14.48           C  
ANISOU 3246  CB  PRO A 405     1409   2395   1698    171    440    292       C  
ATOM   3247  CG  PRO A 405      47.348  11.091  30.519  1.00 22.84           C  
ANISOU 3247  CG  PRO A 405     1253   5846   1578    -23    414   -540       C  
ATOM   3248  CD  PRO A 405      48.552  10.954  29.684  1.00 13.76           C  
ANISOU 3248  CD  PRO A 405     1023   2615   1588    239    305     28       C  
ATOM   3249  N   MET A 406      49.976  10.397  34.175  1.00 13.75           N  
ANISOU 3249  N   MET A 406     1800   1780   1645    -21     51    174       N  
ATOM   3250  CA  MET A 406      50.616   9.448  35.083  1.00 13.85           C  
ANISOU 3250  CA  MET A 406     1629   1762   1873     25    -64     85       C  
ATOM   3251  C   MET A 406      49.767   8.207  35.366  1.00 11.54           C  
ANISOU 3251  C   MET A 406     1415   1682   1289    121     77     83       C  
ATOM   3252  O   MET A 406      50.341   7.200  35.817  1.00 12.32           O  
ANISOU 3252  O   MET A 406     1609   1726   1345    266    164     58       O  
ATOM   3253  CB AMET A 406      51.364  10.094  36.253  0.46 13.51           C  
ANISOU 3253  CB AMET A 406     1647   1853   1634   -143    148     -7       C  
ATOM   3254  CB BMET A 406      50.661  10.148  36.429  0.54 14.95           C  
ANISOU 3254  CB BMET A 406     1758   1819   2104    -95   -463     67       C  
ATOM   3255  CG AMET A 406      50.333  10.556  37.220  0.46 12.98           C  
ANISOU 3255  CG AMET A 406     1037   1606   2288    327   -279   -346       C  
ATOM   3256  CG BMET A 406      51.349   9.527  37.597  0.54 15.48           C  
ANISOU 3256  CG BMET A 406     1748   1996   2135     49   -349    188       C  
ATOM   3257  SD AMET A 406      50.991  10.863  38.903  0.46 13.84           S  
ANISOU 3257  SD AMET A 406     1438   2100   1721   -167    594   -342       S  
ATOM   3258  SD BMET A 406      51.441  10.418  39.210  0.54 25.72           S  
ANISOU 3258  SD BMET A 406     2659   5481   1634   1834    452   -360       S  
ATOM   3259  CE AMET A 406      51.180   9.182  39.473  0.46 19.87           C  
ANISOU 3259  CE AMET A 406     2231   2887   2432   -259    580   1010       C  
ATOM   3260  CE BMET A 406      50.009  11.328  38.803  0.54 36.69           C  
ANISOU 3260  CE BMET A 406     2898   6129   4914   2521    176  -1187       C  
ATOM   3261  N   TYR A 407      48.460   8.210  35.080  1.00 11.48           N  
ANISOU 3261  N   TYR A 407     1393   1616   1354    184    193    -48       N  
ATOM   3262  CA  TYR A 407      47.680   6.979  35.099  1.00 11.04           C  
ANISOU 3262  CA  TYR A 407     1348   1560   1285    191    239    -19       C  
ATOM   3263  C   TYR A 407      48.404   5.867  34.305  1.00 10.93           C  
ANISOU 3263  C   TYR A 407     1163   1713   1277    195    153    -26       C  
ATOM   3264  O   TYR A 407      48.376   4.669  34.646  1.00 12.85           O  
ANISOU 3264  O   TYR A 407     1759   1715   1408    488    339    -10       O  
ATOM   3265  CB  TYR A 407      46.255   7.230  34.529  1.00 11.30           C  
ANISOU 3265  CB  TYR A 407     1340   1640   1314    327    273      4       C  
ATOM   3266  CG  TYR A 407      45.513   5.943  34.329  1.00 11.38           C  
ANISOU 3266  CG  TYR A 407     1280   1531   1513    352    179     74       C  
ATOM   3267  CD1 TYR A 407      44.938   5.292  35.402  1.00 12.90           C  
ANISOU 3267  CD1 TYR A 407     1852   1705   1343    208    366      3       C  
ATOM   3268  CD2 TYR A 407      45.510   5.314  33.086  1.00 11.48           C  
ANISOU 3268  CD2 TYR A 407     1268   1642   1451    236    294     68       C  
ATOM   3269  CE1 TYR A 407      44.315   4.089  35.230  1.00 13.83           C  
ANISOU 3269  CE1 TYR A 407     2068   1595   1592    178    537     42       C  
ATOM   3270  CE2 TYR A 407      44.933   4.083  32.905  1.00 12.34           C  
ANISOU 3270  CE2 TYR A 407     1528   1657   1502    252    185    -59       C  
ATOM   3271  CZ  TYR A 407      44.348   3.479  34.000  1.00 13.51           C  
ANISOU 3271  CZ  TYR A 407     1741   1786   1605    125    292     10       C  
ATOM   3272  OH  TYR A 407      43.726   2.234  33.815  1.00 16.11           O  
ANISOU 3272  OH  TYR A 407     2636   1723   1763    -38    693    -89       O  
ATOM   3273  N   HIS A 408      49.009   6.245  33.180  1.00 11.41           N  
ANISOU 3273  N   HIS A 408     1248   1657   1429    223    213   -162       N  
ATOM   3274  CA  HIS A 408      49.666   5.258  32.291  1.00 12.90           C  
ANISOU 3274  CA  HIS A 408     1362   2062   1477    233    299   -328       C  
ATOM   3275  C   HIS A 408      51.138   4.992  32.667  1.00 14.83           C  
ANISOU 3275  C   HIS A 408     1500   2234   1900    543    214   -591       C  
ATOM   3276  O   HIS A 408      51.788   4.237  31.957  1.00 17.02           O  
ANISOU 3276  O   HIS A 408     1559   2835   2071    633    244   -695       O  
ATOM   3277  CB  HIS A 408      49.578   5.743  30.867  1.00 13.01           C  
ANISOU 3277  CB  HIS A 408     1393   1991   1560    105    474   -213       C  
ATOM   3278  CG  HIS A 408      48.206   5.764  30.285  1.00 12.51           C  
ANISOU 3278  CG  HIS A 408     1549   1976   1227    204    353   -114       C  
ATOM   3279  ND1 HIS A 408      47.442   4.611  30.153  1.00 12.31           N  
ANISOU 3279  ND1 HIS A 408     1272   1935   1469    334    319   -185       N  
ATOM   3280  CD2 HIS A 408      47.434   6.785  29.750  1.00 13.83           C  
ANISOU 3280  CD2 HIS A 408     1822   2054   1381    260    276     60       C  
ATOM   3281  CE1 HIS A 408      46.276   4.960  29.561  1.00 12.58           C  
ANISOU 3281  CE1 HIS A 408     1362   1993   1426    447    396    -66       C  
ATOM   3282  NE2 HIS A 408      46.227   6.236  29.321  1.00 14.07           N  
ANISOU 3282  NE2 HIS A 408     1671   2077   1599    565    341    -81       N  
ATOM   3283  N   ALA A 409      51.638   5.538  33.755  1.00 16.61           N  
ANISOU 3283  N   ALA A 409     1358   2775   2176    504     52   -754       N  
ATOM   3284  CA  ALA A 409      53.031   5.218  34.146  1.00 20.06           C  
ANISOU 3284  CA  ALA A 409     1403   3184   3035    630   -132  -1331       C  
ATOM   3285  C   ALA A 409      53.288   3.744  34.349  1.00 21.37           C  
ANISOU 3285  C   ALA A 409     1614   3434   3070   1101   -477  -1240       C  
ATOM   3286  O   ALA A 409      54.383   3.254  34.179  1.00 24.99           O  
ANISOU 3286  O   ALA A 409     1987   4511   2998   1741    -39  -1074       O  
ATOM   3287  CB  ALA A 409      53.387   6.065  35.386  1.00 23.32           C  
ANISOU 3287  CB  ALA A 409     1738   3698   3426   1018   -615  -1682       C  
ATOM   3288  N   VAL A 410      52.258   2.986  34.692  1.00 19.30           N  
ANISOU 3288  N   VAL A 410     2093   3061   2180   1158   -344   -691       N  
ATOM   3289  CA  VAL A 410      52.347   1.587  35.052  1.00 21.75           C  
ANISOU 3289  CA  VAL A 410     2924   3108   2230   1760   -302   -713       C  
ATOM   3290  C   VAL A 410      51.640   0.675  34.066  1.00 18.40           C  
ANISOU 3290  C   VAL A 410     2037   2671   2284   1237     14   -159       C  
ATOM   3291  O   VAL A 410      51.575  -0.537  34.255  1.00 22.44           O  
ANISOU 3291  O   VAL A 410     3439   2641   2445   1612   -228   -111       O  
ATOM   3292  CB  VAL A 410      51.862   1.395  36.525  1.00 23.70           C  
ANISOU 3292  CB  VAL A 410     3783   2795   2427   1629    -98   -561       C  
ATOM   3293  CG1 VAL A 410      52.691   2.232  37.475  1.00 25.99           C  
ANISOU 3293  CG1 VAL A 410     4669   3099   2107   1985   -444   -752       C  
ATOM   3294  CG2 VAL A 410      50.376   1.638  36.595  1.00 25.12           C  
ANISOU 3294  CG2 VAL A 410     3909   3265   2372   1954    371    -55       C  
ATOM   3295  N   THR A 411      51.100   1.245  32.962  1.00 16.21           N  
ANISOU 3295  N   THR A 411     2035   2164   1960    871    176   -319       N  
ATOM   3296  CA  THR A 411      50.387   0.468  31.969  1.00 15.24           C  
ANISOU 3296  CA  THR A 411     2029   1910   1850    784    331   -218       C  
ATOM   3297  C   THR A 411      51.121   0.301  30.629  1.00 13.87           C  
ANISOU 3297  C   THR A 411     1650   1845   1775    537    105   -149       C  
ATOM   3298  O   THR A 411      51.893   1.155  30.185  1.00 16.54           O  
ANISOU 3298  O   THR A 411     1779   2125   2381    138    354   -540       O  
ATOM   3299  CB  THR A 411      48.997   1.082  31.657  1.00 14.72           C  
ANISOU 3299  CB  THR A 411     1988   1966   1640    673    399    -19       C  
ATOM   3300  OG1 THR A 411      49.047   2.328  31.009  1.00 14.00           O  
ANISOU 3300  OG1 THR A 411     1677   1946   1696    593    339    -36       O  
ATOM   3301  CG2 THR A 411      48.220   1.307  33.008  1.00 16.31           C  
ANISOU 3301  CG2 THR A 411     2100   2358   1739    820    496     47       C  
ATOM   3302  N   LYS A 412      50.858  -0.817  29.964  1.00 13.48           N  
ANISOU 3302  N   LYS A 412     1599   1819   1706    438    357    -89       N  
ATOM   3303  CA  LYS A 412      51.377  -1.063  28.613  1.00 13.24           C  
ANISOU 3303  CA  LYS A 412     1372   1874   1784    424    447   -165       C  
ATOM   3304  C   LYS A 412      50.556  -0.324  27.564  1.00 12.24           C  
ANISOU 3304  C   LYS A 412     1251   1711   1689    279    366   -251       C  
ATOM   3305  O   LYS A 412      51.111   0.048  26.516  1.00 15.41           O  
ANISOU 3305  O   LYS A 412     1470   2457   1928    453    548    170       O  
ATOM   3306  CB  LYS A 412      51.407  -2.567  28.358  1.00 14.96           C  
ANISOU 3306  CB  LYS A 412     2098   1899   1686    748    665     10       C  
ATOM   3307  CG  LYS A 412      52.396  -3.258  29.229  1.00 20.02           C  
ANISOU 3307  CG  LYS A 412     1791   2443   3371    942    280    231       C  
ATOM   3308  CD  LYS A 412      52.350  -4.779  29.035  1.00 26.00           C  
ANISOU 3308  CD  LYS A 412     3890   2394   3594   1690    788    444       C  
ATOM   3309  CE  LYS A 412      53.377  -5.304  30.020  1.00 30.75           C  
ANISOU 3309  CE  LYS A 412     4507   3625   3550   2615    950    785       C  
ATOM   3310  NZ  LYS A 412      52.892  -5.813  31.313  1.00 55.74           N  
ANISOU 3310  NZ  LYS A 412     6121   9752   5306   -510     21   4162       N  
ATOM   3311  N   ARG A 413      49.273  -0.116  27.748  1.00 12.59           N  
ANISOU 3311  N   ARG A 413     1323   1811   1649    375    427     27       N  
ATOM   3312  CA  ARG A 413      48.425   0.672  26.896  1.00 12.85           C  
ANISOU 3312  CA  ARG A 413     1346   1741   1794    373    364    -99       C  
ATOM   3313  C   ARG A 413      48.688   2.135  27.187  1.00 12.53           C  
ANISOU 3313  C   ARG A 413     1287   1796   1677    378    319   -134       C  
ATOM   3314  O   ARG A 413      48.884   2.509  28.362  1.00 14.82           O  
ANISOU 3314  O   ARG A 413     2097   1846   1687    380    211    -69       O  
ATOM   3315  CB  ARG A 413      46.961   0.290  27.144  1.00 14.99           C  
ANISOU 3315  CB  ARG A 413     1407   2210   2078    185    353     84       C  
ATOM   3316  CG  ARG A 413      45.928   0.952  26.279  1.00 16.57           C  
ANISOU 3316  CG  ARG A 413     1360   2825   2111    388    253   -170       C  
ATOM   3317  CD  ARG A 413      44.499   0.505  26.669  1.00 15.82           C  
ANISOU 3317  CD  ARG A 413     1577   2468   1965     50    143   -284       C  
ATOM   3318  NE  ARG A 413      44.126   1.130  27.942  1.00 14.64           N  
ANISOU 3318  NE  ARG A 413     1409   2223   1930    508    253     91       N  
ATOM   3319  CZ  ARG A 413      43.517   2.308  28.053  1.00 14.71           C  
ANISOU 3319  CZ  ARG A 413     1292   2224   2074    392    256    108       C  
ATOM   3320  NH1 ARG A 413      43.265   2.791  29.270  1.00 15.98           N  
ANISOU 3320  NH1 ARG A 413     1654   2318   2098    524    340    -58       N  
ATOM   3321  NH2 ARG A 413      43.201   3.031  27.017  1.00 17.89           N  
ANISOU 3321  NH2 ARG A 413     2151   2515   2132    866    162    259       N  
ATOM   3322  N   LYS A 414      48.640   3.005  26.204  1.00 12.73           N  
ANISOU 3322  N   LYS A 414     1498   1749   1591    318    374   -159       N  
ATOM   3323  CA  LYS A 414      48.881   4.432  26.398  1.00 12.99           C  
ANISOU 3323  CA  LYS A 414     1440   1784   1712    325    411   -145       C  
ATOM   3324  C   LYS A 414      47.858   5.277  25.719  1.00 13.29           C  
ANISOU 3324  C   LYS A 414     1606   1721   1723    268    271    -77       C  
ATOM   3325  O   LYS A 414      47.358   4.908  24.637  1.00 15.69           O  
ANISOU 3325  O   LYS A 414     1787   2079   2098    323    -28   -350       O  
ATOM   3326  CB  LYS A 414      50.271   4.804  25.771  1.00 13.86           C  
ANISOU 3326  CB  LYS A 414     1468   1864   1935    241    319    -90       C  
ATOM   3327  CG  LYS A 414      51.442   4.007  26.304  1.00 14.66           C  
ANISOU 3327  CG  LYS A 414     1462   2171   1935    441    421   -203       C  
ATOM   3328  CD  LYS A 414      51.747   4.195  27.768  1.00 14.56           C  
ANISOU 3328  CD  LYS A 414     1382   2249   1903    403    349   -228       C  
ATOM   3329  CE  LYS A 414      52.948   3.354  28.186  1.00 16.69           C  
ANISOU 3329  CE  LYS A 414     1734   2777   1831    593    428    -66       C  
ATOM   3330  NZ  LYS A 414      53.303   3.524  29.622  1.00 15.99           N  
ANISOU 3330  NZ  LYS A 414     1541   2508   2028    467    259   -122       N  
ATOM   3331  N   THR A 415      47.555   6.432  26.316  1.00 12.79           N  
ANISOU 3331  N   THR A 415     1345   1845   1670    306    297      6       N  
ATOM   3332  CA  THR A 415      46.883   7.521  25.692  1.00 12.31           C  
ANISOU 3332  CA  THR A 415     1408   1764   1503    324     97     61       C  
ATOM   3333  C   THR A 415      47.722   8.790  26.010  1.00 12.76           C  
ANISOU 3333  C   THR A 415     1392   1790   1667    427     52   -195       C  
ATOM   3334  O   THR A 415      48.434   8.808  26.988  1.00 14.68           O  
ANISOU 3334  O   THR A 415     1662   2027   1887    189    -45    -41       O  
ATOM   3335  CB  THR A 415      45.410   7.702  26.059  1.00 14.30           C  
ANISOU 3335  CB  THR A 415     1431   1927   2073    417    432   -131       C  
ATOM   3336  OG1 THR A 415      45.255   8.076  27.430  1.00 15.63           O  
ANISOU 3336  OG1 THR A 415     1760   2275   1903    690    382     89       O  
ATOM   3337  CG2 THR A 415      44.592   6.468  25.695  1.00 17.34           C  
ANISOU 3337  CG2 THR A 415     1532   2275   2782     77    210    -67       C  
ATOM   3338  N   LYS A 416      47.566   9.816  25.193  1.00 13.69           N  
ANISOU 3338  N   LYS A 416     1401   1894   1905    273    -60    -81       N  
ATOM   3339  CA  LYS A 416      48.241  11.072  25.364  1.00 14.74           C  
ANISOU 3339  CA  LYS A 416     1277   2051   2272     97    488   -109       C  
ATOM   3340  C   LYS A 416      47.298  12.166  25.880  1.00 11.47           C  
ANISOU 3340  C   LYS A 416      995   1801   1562     62    261    171       C  
ATOM   3341  O   LYS A 416      46.063  12.022  25.797  1.00 13.04           O  
ANISOU 3341  O   LYS A 416     1012   2029   1912    -35    201     70       O  
ATOM   3342  CB  LYS A 416      48.755  11.553  23.976  1.00 21.99           C  
ANISOU 3342  CB  LYS A 416     2260   2992   3103    383   1752     91       C  
ATOM   3343  CG  LYS A 416      49.560  12.795  23.794  1.00 38.08           C  
ANISOU 3343  CG  LYS A 416     5420   5509   3540  -2356   1352    896       C  
ATOM   3344  CD  LYS A 416      49.952  13.013  22.351  1.00 44.95           C  
ANISOU 3344  CD  LYS A 416     4829   8187   4064  -1864   1958   1826       C  
ATOM   3345  CE  LYS A 416      50.743  11.910  21.670  1.00 51.23           C  
ANISOU 3345  CE  LYS A 416     4839  10898   3726   -299   1632   1340       C  
ATOM   3346  NZ  LYS A 416      51.347  12.425  20.395  1.00 67.69           N  
ANISOU 3346  NZ  LYS A 416     6216  15962   3539    700   2062   2403       N  
ATOM   3347  N   CYS A 417      47.899  13.214  26.437  1.00 12.05           N  
ANISOU 3347  N   CYS A 417      906   1766   1908    -27    139    223       N  
ATOM   3348  CA  CYS A 417      47.153  14.438  26.669  1.00 11.88           C  
ANISOU 3348  CA  CYS A 417      990   1674   1849     22    298    247       C  
ATOM   3349  C   CYS A 417      47.842  15.535  25.845  1.00 11.37           C  
ANISOU 3349  C   CYS A 417      968   1665   1688     34    292    286       C  
ATOM   3350  O   CYS A 417      49.064  15.697  25.968  1.00 13.61           O  
ANISOU 3350  O   CYS A 417      815   2073   2284     11    210    503       O  
ATOM   3351  CB ACYS A 417      47.150  14.714  28.182  0.81 12.01           C  
ANISOU 3351  CB ACYS A 417     1104   1719   1741    131    292    657       C  
ATOM   3352  CB BCYS A 417      46.940  15.223  27.949  0.19 13.39           C  
ANISOU 3352  CB BCYS A 417     1230   1807   2049   -605    735     34       C  
ATOM   3353  SG ACYS A 417      46.221  16.278  28.502  0.81 13.91           S  
ANISOU 3353  SG ACYS A 417     1183   2085   2018      0    455    -54       S  
ATOM   3354  SG BCYS A 417      47.390  13.953  29.061  0.19 53.08           S  
ANISOU 3354  SG BCYS A 417    13239   4678   2251   3691  -2701   -352       S  
ATOM   3355  N   VAL A 418      47.055  16.275  25.111  1.00 11.02           N  
ANISOU 3355  N   VAL A 418      922   1721   1546     56    255    223       N  
ATOM   3356  CA  VAL A 418      47.509  17.448  24.376  1.00 11.21           C  
ANISOU 3356  CA  VAL A 418      963   1568   1728     29    199    280       C  
ATOM   3357  C   VAL A 418      46.688  18.624  24.827  1.00 11.08           C  
ANISOU 3357  C   VAL A 418      934   1673   1604    -73    112    141       C  
ATOM   3358  O   VAL A 418      45.447  18.539  25.002  1.00 11.37           O  
ANISOU 3358  O   VAL A 418      925   1653   1743   -114    278     98       O  
ATOM   3359  CB  VAL A 418      47.463  17.257  22.839  1.00 12.71           C  
ANISOU 3359  CB  VAL A 418     1153   2050   1627   -144    397     70       C  
ATOM   3360  CG1 VAL A 418      48.416  16.164  22.382  1.00 15.17           C  
ANISOU 3360  CG1 VAL A 418     1520   2292   1951    125    419     12       C  
ATOM   3361  CG2 VAL A 418      46.038  16.940  22.379  1.00 13.85           C  
ANISOU 3361  CG2 VAL A 418     1327   2107   1829    -98    189   -121       C  
ATOM   3362  N   MET A 419      47.347  19.785  24.978  1.00 11.05           N  
ANISOU 3362  N   MET A 419      931   1648   1619   -143    196     70       N  
ATOM   3363  CA  MET A 419      46.689  21.002  25.374  1.00 11.46           C  
ANISOU 3363  CA  MET A 419      813   1757   1784    -29    277     40       C  
ATOM   3364  C   MET A 419      47.247  22.176  24.573  1.00 11.37           C  
ANISOU 3364  C   MET A 419      967   1587   1767   -131    133    -40       C  
ATOM   3365  O   MET A 419      48.460  22.247  24.347  1.00 12.86           O  
ANISOU 3365  O   MET A 419      904   1858   2123    -80    202    158       O  
ATOM   3366  CB  MET A 419      46.880  21.304  26.836  1.00 12.82           C  
ANISOU 3366  CB  MET A 419     1202   1888   1781    -71    251   -125       C  
ATOM   3367  CG  MET A 419      46.263  20.288  27.758  1.00 13.04           C  
ANISOU 3367  CG  MET A 419     1213   2139   1604    115    368   -136       C  
ATOM   3368  SD  MET A 419      46.842  20.530  29.460  1.00 16.82           S  
ANISOU 3368  SD  MET A 419     1512   3092   1788     -4    260   -138       S  
ATOM   3369  CE  MET A 419      45.644  19.581  30.352  1.00 17.95           C  
ANISOU 3369  CE  MET A 419     2069   2984   1768    263    326    383       C  
ATOM   3370  N   LYS A 420      46.378  23.097  24.187  1.00 12.54           N  
ANISOU 3370  N   LYS A 420     1007   1638   2120    -52    220    182       N  
ATOM   3371  CA  LYS A 420      46.739  24.314  23.461  1.00 12.77           C  
ANISOU 3371  CA  LYS A 420     1090   1687   2076   -134    266    223       C  
ATOM   3372  C   LYS A 420      45.972  25.509  24.071  1.00 11.98           C  
ANISOU 3372  C   LYS A 420     1070   1605   1876   -190    149    263       C  
ATOM   3373  O   LYS A 420      44.741  25.446  24.148  1.00 13.54           O  
ANISOU 3373  O   LYS A 420     1013   1738   2394   -166    172     31       O  
ATOM   3374  CB  LYS A 420      46.508  24.217  21.970  1.00 14.32           C  
ANISOU 3374  CB  LYS A 420     1207   2203   2032   -238    309     75       C  
ATOM   3375  CG  LYS A 420      46.824  25.494  21.205  1.00 15.20           C  
ANISOU 3375  CG  LYS A 420     1695   2002   2078   -236    103    244       C  
ATOM   3376  CD  LYS A 420      46.496  25.477  19.702  1.00 16.83           C  
ANISOU 3376  CD  LYS A 420     1819   2602   1971   -308    351    -52       C  
ATOM   3377  CE  LYS A 420      47.321  24.506  18.939  1.00 18.46           C  
ANISOU 3377  CE  LYS A 420     1862   2725   2426    -55    170   -195       C  
ATOM   3378  NZ  LYS A 420      47.007  24.591  17.463  1.00 17.33           N  
ANISOU 3378  NZ  LYS A 420     1842   2519   2224   -335    451   -134       N  
ATOM   3379  N   MET A 421      46.689  26.551  24.375  1.00 11.59           N  
ANISOU 3379  N   MET A 421      949   1606   1847   -180    228    217       N  
ATOM   3380  CA  MET A 421      46.159  27.844  24.766  1.00 11.84           C  
ANISOU 3380  CA  MET A 421     1128   1559   1810   -113    250    264       C  
ATOM   3381  C   MET A 421      46.454  28.826  23.645  1.00 11.49           C  
ANISOU 3381  C   MET A 421     1065   1594   1706   -180    139    225       C  
ATOM   3382  O   MET A 421      47.610  28.983  23.262  1.00 13.95           O  
ANISOU 3382  O   MET A 421     1086   2090   2126    -61    301    604       O  
ATOM   3383  CB  MET A 421      46.810  28.296  26.077  1.00 12.90           C  
ANISOU 3383  CB  MET A 421     1424   1802   1675   -282    407    218       C  
ATOM   3384  CG  MET A 421      46.454  29.663  26.532  1.00 14.52           C  
ANISOU 3384  CG  MET A 421     1564   1694   2260   -231    190    111       C  
ATOM   3385  SD  MET A 421      47.445  30.291  27.878  1.00 16.27           S  
ANISOU 3385  SD  MET A 421     1904   2029   2248   -304    142    100       S  
ATOM   3386  CE  MET A 421      46.716  29.395  29.189  1.00 17.33           C  
ANISOU 3386  CE  MET A 421     1738   2636   2210   -233    344     86       C  
ATOM   3387  N   VAL A 422      45.440  29.538  23.185  1.00 11.84           N  
ANISOU 3387  N   VAL A 422     1038   1830   1631   -109    224    360       N  
ATOM   3388  CA  VAL A 422      45.532  30.550  22.119  1.00 12.22           C  
ANISOU 3388  CA  VAL A 422     1035   1876   1731    -70    248    400       C  
ATOM   3389  C   VAL A 422      45.370  31.900  22.761  1.00 13.45           C  
ANISOU 3389  C   VAL A 422     1338   1839   1932   -205    231    321       C  
ATOM   3390  O   VAL A 422      44.326  32.173  23.378  1.00 13.36           O  
ANISOU 3390  O   VAL A 422     1474   1665   1938   -150    301    358       O  
ATOM   3391  CB  VAL A 422      44.487  30.292  21.042  1.00 12.92           C  
ANISOU 3391  CB  VAL A 422     1300   1958   1653    -33    160    345       C  
ATOM   3392  CG1 VAL A 422      44.661  31.322  19.922  1.00 14.53           C  
ANISOU 3392  CG1 VAL A 422     1818   2012   1690    -70    211    396       C  
ATOM   3393  CG2 VAL A 422      44.555  28.890  20.474  1.00 14.58           C  
ANISOU 3393  CG2 VAL A 422     1622   2047   1871   -192    260    199       C  
ATOM   3394  N   CYS A 423      46.419  32.760  22.604  1.00 13.78           N  
ANISOU 3394  N   CYS A 423     1610   1845   1782   -329    347    418       N  
ATOM   3395  CA  CYS A 423      46.403  34.073  23.251  1.00 14.67           C  
ANISOU 3395  CA  CYS A 423     1698   1778   2097   -286    356    418       C  
ATOM   3396  C   CYS A 423      46.455  35.195  22.211  1.00 16.23           C  
ANISOU 3396  C   CYS A 423     1924   1926   2318   -425    326    553       C  
ATOM   3397  O   CYS A 423      47.159  35.063  21.207  1.00 18.77           O  
ANISOU 3397  O   CYS A 423     2297   2325   2510   -178    592    860       O  
ATOM   3398  CB  CYS A 423      47.631  34.190  24.165  1.00 16.48           C  
ANISOU 3398  CB  CYS A 423     1990   2252   2021   -669    205    345       C  
ATOM   3399  SG  CYS A 423      47.686  33.061  25.563  1.00 16.76           S  
ANISOU 3399  SG  CYS A 423     2086   2000   2283   -453    104    441       S  
ATOM   3400  N   ALA A 424      45.753  36.278  22.502  1.00 16.19           N  
ANISOU 3400  N   ALA A 424     1934   1867   2350   -363    263    779       N  
ATOM   3401  CA  ALA A 424      45.698  37.416  21.605  1.00 17.36           C  
ANISOU 3401  CA  ALA A 424     2420   1983   2191   -384     42    726       C  
ATOM   3402  C   ALA A 424      46.222  38.669  22.264  1.00 17.29           C  
ANISOU 3402  C   ALA A 424     2050   1936   2584   -466    343    654       C  
ATOM   3403  O   ALA A 424      45.926  38.976  23.423  1.00 18.15           O  
ANISOU 3403  O   ALA A 424     2353   1905   2638   -397    327    541       O  
ATOM   3404  CB  ALA A 424      44.260  37.637  21.135  1.00 19.36           C  
ANISOU 3404  CB  ALA A 424     2638   2137   2582   -282   -332    766       C  
ATOM   3405  N   ASN A 425      46.909  39.475  21.454  1.00 21.12           N  
ANISOU 3405  N   ASN A 425     3201   2277   2546   -903    315    706       N  
ATOM   3406  CA  ASN A 425      47.409  40.816  21.819  1.00 25.54           C  
ANISOU 3406  CA  ASN A 425     3304   2331   4068  -1184   -435   1110       C  
ATOM   3407  C   ASN A 425      48.454  40.880  22.900  1.00 25.09           C  
ANISOU 3407  C   ASN A 425     3753   2553   3225  -1691    -83   1091       C  
ATOM   3408  O   ASN A 425      48.892  39.823  23.388  1.00 23.00           O  
ANISOU 3408  O   ASN A 425     2733   2712   3293  -1319    -26    880       O  
ATOM   3409  CB  ASN A 425      46.200  41.717  22.096  1.00 27.01           C  
ANISOU 3409  CB  ASN A 425     4361   2136   3764   -818   -317    242       C  
ATOM   3410  CG  ASN A 425      45.323  41.866  20.845  1.00 29.99           C  
ANISOU 3410  CG  ASN A 425     3497   3329   4568   -628   -333   1611       C  
ATOM   3411  OD1 ASN A 425      44.099  41.870  21.003  1.00 34.83           O  
ANISOU 3411  OD1 ASN A 425     3486   3526   6221   -675    -45    623       O  
ATOM   3412  ND2 ASN A 425      45.826  41.936  19.631  1.00 30.69           N  
ANISOU 3412  ND2 ASN A 425     3548   3839   4273   -345   -790   2111       N  
ATOM   3413  N   LYS A 426      48.912  42.063  23.277  1.00 26.44           N  
ANISOU 3413  N   LYS A 426     3925   2710   3411  -1688    159    555       N  
ATOM   3414  CA  LYS A 426      50.068  42.161  24.142  1.00 28.81           C  
ANISOU 3414  CA  LYS A 426     3273   3404   4268  -2163    310    737       C  
ATOM   3415  C   LYS A 426      49.819  41.564  25.516  1.00 25.36           C  
ANISOU 3415  C   LYS A 426     2977   3236   3421  -1750    -47    -98       C  
ATOM   3416  O   LYS A 426      50.699  40.955  26.135  1.00 26.21           O  
ANISOU 3416  O   LYS A 426     2623   3632   3705  -1528    309     65       O  
ATOM   3417  CB  LYS A 426      50.455  43.658  24.221  1.00 38.50           C  
ANISOU 3417  CB  LYS A 426     5733   4023   4872  -3428    160    292       C  
ATOM   3418  CG  LYS A 426      51.068  44.039  25.537  1.00 57.55           C  
ANISOU 3418  CG  LYS A 426    10207   5013   6648  -4108  -2630    436       C  
ATOM   3419  CD  LYS A 426      51.233  45.531  25.789  1.00 68.81           C  
ANISOU 3419  CD  LYS A 426    12096   5466   8584  -3258  -3521  -1329       C  
ATOM   3420  CE  LYS A 426      52.539  45.799  26.523  1.00 76.35           C  
ANISOU 3420  CE  LYS A 426    13182   5951   9877  -3584  -4591  -2220       C  
ATOM   3421  NZ  LYS A 426      52.651  47.277  26.751  1.00 62.60           N  
ANISOU 3421  NZ  LYS A 426     5431   5397  12957  -1569  -2675  -1524       N  
ATOM   3422  N   GLU A 427      48.573  41.730  25.971  1.00 22.69           N  
ANISOU 3422  N   GLU A 427     3114   2187   3319  -1268    -43    414       N  
ATOM   3423  CA  GLU A 427      48.151  41.197  27.242  1.00 21.11           C  
ANISOU 3423  CA  GLU A 427     3057   1873   3093   -681    -85    370       C  
ATOM   3424  C   GLU A 427      47.934  39.694  27.208  1.00 17.41           C  
ANISOU 3424  C   GLU A 427     2004   1916   2695   -652     63    257       C  
ATOM   3425  O   GLU A 427      47.703  39.119  28.275  1.00 18.19           O  
ANISOU 3425  O   GLU A 427     2151   2173   2586   -633    -79    373       O  
ATOM   3426  CB  GLU A 427      46.846  41.850  27.759  1.00 23.80           C  
ANISOU 3426  CB  GLU A 427     3658   1850   3533   -263    175    148       C  
ATOM   3427  CG  GLU A 427      45.616  41.534  26.951  1.00 30.59           C  
ANISOU 3427  CG  GLU A 427     3057   2971   5592   -905   -121   1131       C  
ATOM   3428  CD  GLU A 427      44.266  41.957  27.484  1.00 46.64           C  
ANISOU 3428  CD  GLU A 427     3906   5605   8211   1265   -622  -1011       C  
ATOM   3429  OE1 GLU A 427      44.257  42.468  28.637  1.00 60.95           O  
ANISOU 3429  OE1 GLU A 427     6494   9821   6844   3148     52   -357       O  
ATOM   3430  OE2 GLU A 427      43.225  41.780  26.779  1.00 58.45           O  
ANISOU 3430  OE2 GLU A 427     3643   4313  14252   1003  -1875  -4176       O  
ATOM   3431  N   GLU A 428      48.014  39.009  26.083  1.00 18.29           N  
ANISOU 3431  N   GLU A 428     2173   2119   2656   -830    295    196       N  
ATOM   3432  CA  GLU A 428      47.804  37.562  25.997  1.00 16.71           C  
ANISOU 3432  CA  GLU A 428     1880   2011   2457   -667    117    237       C  
ATOM   3433  C   GLU A 428      46.467  37.155  26.604  1.00 14.82           C  
ANISOU 3433  C   GLU A 428     1711   1730   2190   -420    -51    189       C  
ATOM   3434  O   GLU A 428      46.363  36.248  27.442  1.00 15.98           O  
ANISOU 3434  O   GLU A 428     1666   1944   2461   -341     22    469       O  
ATOM   3435  CB  GLU A 428      48.991  36.806  26.622  1.00 18.31           C  
ANISOU 3435  CB  GLU A 428     1653   2392   2912   -700     75    296       C  
ATOM   3436  CG  GLU A 428      50.295  37.039  25.829  1.00 20.96           C  
ANISOU 3436  CG  GLU A 428     1941   2822   3202   -765    376    133       C  
ATOM   3437  CD  GLU A 428      51.426  36.097  26.206  1.00 23.88           C  
ANISOU 3437  CD  GLU A 428     1673   3961   3440   -501     76    -58       C  
ATOM   3438  OE1 GLU A 428      52.276  35.769  25.346  1.00 33.93           O  
ANISOU 3438  OE1 GLU A 428     2862   6292   3737   1001    448     -2       O  
ATOM   3439  OE2 GLU A 428      51.560  35.681  27.395  1.00 26.08           O  
ANISOU 3439  OE2 GLU A 428     2237   3732   3940   -207    462    703       O  
ATOM   3440  N   LYS A 429      45.413  37.832  26.161  1.00 15.92           N  
ANISOU 3440  N   LYS A 429     1884   1809   2357   -432     50    441       N  
ATOM   3441  CA  LYS A 429      44.060  37.395  26.453  1.00 16.11           C  
ANISOU 3441  CA  LYS A 429     1737   1583   2800   -396    -88    160       C  
ATOM   3442  C   LYS A 429      43.855  35.971  25.954  1.00 13.98           C  
ANISOU 3442  C   LYS A 429     1596   1587   2130   -175    101    192       C  
ATOM   3443  O   LYS A 429      44.214  35.629  24.821  1.00 14.90           O  
ANISOU 3443  O   LYS A 429     1687   1750   2225   -244    280    274       O  
ATOM   3444  CB  LYS A 429      43.066  38.341  25.777  1.00 17.55           C  
ANISOU 3444  CB  LYS A 429     2183   1567   2917    -70    -94    158       C  
ATOM   3445  CG  LYS A 429      41.644  37.995  26.116  1.00 21.36           C  
ANISOU 3445  CG  LYS A 429     2015   2022   4081    -64   -374    190       C  
ATOM   3446  CD  LYS A 429      40.676  39.037  25.559  1.00 28.11           C  
ANISOU 3446  CD  LYS A 429     2691   2634   5354    556  -1067    -70       C  
ATOM   3447  CE  LYS A 429      39.240  38.850  25.983  1.00 33.93           C  
ANISOU 3447  CE  LYS A 429     2599   3143   7152    807   -936    195       C  
ATOM   3448  NZ  LYS A 429      38.413  39.919  25.315  1.00 35.51           N  
ANISOU 3448  NZ  LYS A 429     2706   3392   7393    834     72   1211       N  
ATOM   3449  N   VAL A 430      43.331  35.107  26.845  1.00 13.42           N  
ANISOU 3449  N   VAL A 430     1579   1601   1918   -244    172     83       N  
ATOM   3450  CA  VAL A 430      43.093  33.707  26.429  1.00 13.23           C  
ANISOU 3450  CA  VAL A 430     1394   1702   1930   -215    238     99       C  
ATOM   3451  C   VAL A 430      41.814  33.627  25.644  1.00 13.87           C  
ANISOU 3451  C   VAL A 430     1308   1870   2092   -337    312    117       C  
ATOM   3452  O   VAL A 430      40.716  33.784  26.173  1.00 16.93           O  
ANISOU 3452  O   VAL A 430     1328   2633   2470   -316    524     49       O  
ATOM   3453  CB  VAL A 430      43.058  32.775  27.667  1.00 14.24           C  
ANISOU 3453  CB  VAL A 430     1685   1737   1987   -216    276     94       C  
ATOM   3454  CG1 VAL A 430      42.704  31.366  27.233  1.00 14.56           C  
ANISOU 3454  CG1 VAL A 430     1844   1708   1979   -240    344    -39       C  
ATOM   3455  CG2 VAL A 430      44.429  32.823  28.384  1.00 15.23           C  
ANISOU 3455  CG2 VAL A 430     2096   1798   1892   -269    -54    240       C  
ATOM   3456  N   VAL A 431      41.978  33.451  24.332  1.00 12.64           N  
ANISOU 3456  N   VAL A 431     1297   1531   1973    -81    176    259       N  
ATOM   3457  CA  VAL A 431      40.815  33.437  23.431  1.00 13.24           C  
ANISOU 3457  CA  VAL A 431     1328   1581   2120    -13    146    412       C  
ATOM   3458  C   VAL A 431      40.435  32.034  22.989  1.00 12.01           C  
ANISOU 3458  C   VAL A 431     1331   1648   1582    -96    253    269       C  
ATOM   3459  O   VAL A 431      39.358  31.873  22.366  1.00 13.87           O  
ANISOU 3459  O   VAL A 431     1191   1776   2304    -94    131    467       O  
ATOM   3460  CB  VAL A 431      41.014  34.379  22.224  1.00 13.73           C  
ANISOU 3460  CB  VAL A 431     1519   1705   1995   -216     77    326       C  
ATOM   3461  CG1 VAL A 431      41.171  35.800  22.729  1.00 16.63           C  
ANISOU 3461  CG1 VAL A 431     2440   1554   2324   -295    221    442       C  
ATOM   3462  CG2 VAL A 431      42.182  33.960  21.353  1.00 15.50           C  
ANISOU 3462  CG2 VAL A 431     1732   2047   2111   -102    279    594       C  
ATOM   3463  N   GLY A 432      41.233  31.010  23.291  1.00 12.43           N  
ANISOU 3463  N   GLY A 432     1272   1554   1897   -144    127    254       N  
ATOM   3464  CA  GLY A 432      40.881  29.642  23.004  1.00 12.08           C  
ANISOU 3464  CA  GLY A 432     1298   1619   1672   -287     87    175       C  
ATOM   3465  C   GLY A 432      41.626  28.688  23.897  1.00 11.72           C  
ANISOU 3465  C   GLY A 432     1232   1547   1675   -172    278    211       C  
ATOM   3466  O   GLY A 432      42.808  28.936  24.198  1.00 12.21           O  
ANISOU 3466  O   GLY A 432     1202   1643   1794   -170    242    263       O  
ATOM   3467  N   ILE A 433      40.994  27.613  24.311  1.00 11.62           N  
ANISOU 3467  N   ILE A 433     1073   1495   1849    -70    230    254       N  
ATOM   3468  CA  ILE A 433      41.568  26.487  25.002  1.00 11.31           C  
ANISOU 3468  CA  ILE A 433     1130   1489   1677   -125    131    169       C  
ATOM   3469  C   ILE A 433      41.102  25.227  24.331  1.00 11.15           C  
ANISOU 3469  C   ILE A 433      899   1503   1836   -126    181    258       C  
ATOM   3470  O   ILE A 433      39.917  25.048  24.163  1.00 12.03           O  
ANISOU 3470  O   ILE A 433      971   1513   2085    -71    170    145       O  
ATOM   3471  CB AILE A 433      41.162  26.502  26.498  0.32 12.45           C  
ANISOU 3471  CB AILE A 433     1247   1722   1760    121    215    238       C  
ATOM   3472  CB BILE A 433      41.169  26.438  26.490  0.68 13.33           C  
ANISOU 3472  CB BILE A 433     1483   1825   1759   -226    106    348       C  
ATOM   3473  CG1AILE A 433      41.711  27.712  27.236  0.32 12.19           C  
ANISOU 3473  CG1AILE A 433     1008   2101   1524   -249    817     38       C  
ATOM   3474  CG1BILE A 433      41.734  27.669  27.181  0.68 15.55           C  
ANISOU 3474  CG1BILE A 433     2422   1745   1742     74    -44     22       C  
ATOM   3475  CG2AILE A 433      41.548  25.187  27.173  0.32 13.75           C  
ANISOU 3475  CG2AILE A 433     1531   1990   1704    590    481    349       C  
ATOM   3476  CG2BILE A 433      41.616  25.153  27.196  0.68 18.61           C  
ANISOU 3476  CG2BILE A 433     3263   1795   2015   -449   -616    532       C  
ATOM   3477  CD1AILE A 433      43.169  27.646  27.629  0.32 11.57           C  
ANISOU 3477  CD1AILE A 433     1040   1401   1954   -146    739    156       C  
ATOM   3478  CD1BILE A 433      41.129  27.822  28.537  0.68 17.28           C  
ANISOU 3478  CD1BILE A 433     2598   2147   1821    186    151    290       C  
ATOM   3479  N   HIS A 434      42.032  24.313  24.003  1.00 11.29           N  
ANISOU 3479  N   HIS A 434      981   1516   1793   -103    208     90       N  
ATOM   3480  CA  HIS A 434      41.749  23.090  23.264  1.00 11.61           C  
ANISOU 3480  CA  HIS A 434      976   1602   1832   -136    102     73       C  
ATOM   3481  C   HIS A 434      42.533  21.940  23.886  1.00 11.25           C  
ANISOU 3481  C   HIS A 434      923   1501   1852   -133    266     36       C  
ATOM   3482  O   HIS A 434      43.731  22.078  24.089  1.00 13.57           O  
ANISOU 3482  O   HIS A 434      858   1681   2619   -117    135    204       O  
ATOM   3483  CB  HIS A 434      42.140  23.272  21.807  1.00 12.09           C  
ANISOU 3483  CB  HIS A 434     1124   1641   1829    -20    260      0       C  
ATOM   3484  CG  HIS A 434      41.608  24.532  21.195  1.00 12.79           C  
ANISOU 3484  CG  HIS A 434     1304   1698   1858     55    328     27       C  
ATOM   3485  ND1 HIS A 434      40.280  24.679  20.886  1.00 14.35           N  
ANISOU 3485  ND1 HIS A 434     1411   2014   2028    -55    199    534       N  
ATOM   3486  CD2 HIS A 434      42.209  25.718  20.963  1.00 13.74           C  
ANISOU 3486  CD2 HIS A 434     1540   1789   1893    -91    234    277       C  
ATOM   3487  CE1 HIS A 434      40.124  25.911  20.429  1.00 14.40           C  
ANISOU 3487  CE1 HIS A 434     1575   2041   1853   -177    135    753       C  
ATOM   3488  NE2 HIS A 434      41.272  26.578  20.482  1.00 13.44           N  
ANISOU 3488  NE2 HIS A 434     1530   1829   1746   -138    218    275       N  
ATOM   3489  N   MET A 435      41.892  20.814  24.188  1.00 10.98           N  
ANISOU 3489  N   MET A 435      844   1555   1774    -68    163    106       N  
ATOM   3490  CA  MET A 435      42.601  19.735  24.789  1.00 10.55           C  
ANISOU 3490  CA  MET A 435      936   1469   1603    -17    147     80       C  
ATOM   3491  C   MET A 435      41.935  18.390  24.486  1.00  9.53           C  
ANISOU 3491  C   MET A 435      770   1572   1281     40    195      7       C  
ATOM   3492  O   MET A 435      40.759  18.305  24.236  1.00 10.36           O  
ANISOU 3492  O   MET A 435      867   1515   1555      8    254     91       O  
ATOM   3493  CB  MET A 435      42.693  19.929  26.298  1.00 12.45           C  
ANISOU 3493  CB  MET A 435     1308   1698   1723    -86    170   -104       C  
ATOM   3494  CG  MET A 435      41.386  20.137  26.949  1.00 15.43           C  
ANISOU 3494  CG  MET A 435     1831   2443   1588    296    561    575       C  
ATOM   3495  SD  MET A 435      41.728  20.580  28.681  1.00 19.48           S  
ANISOU 3495  SD  MET A 435     1854   3423   2124    383    441   -119       S  
ATOM   3496  CE  MET A 435      40.109  21.061  29.104  1.00 24.51           C  
ANISOU 3496  CE  MET A 435     2330   5382   1603   1596    215    220       C  
ATOM   3497  N   GLN A 436      42.753  17.354  24.582  1.00  9.96           N  
ANISOU 3497  N   GLN A 436      807   1427   1550    -55    209     54       N  
ATOM   3498  CA  GLN A 436      42.254  15.986  24.568  1.00  9.88           C  
ANISOU 3498  CA  GLN A 436      894   1463   1397      1    255     63       C  
ATOM   3499  C   GLN A 436      43.077  15.197  25.560  1.00  9.51           C  
ANISOU 3499  C   GLN A 436      946   1346   1321    -86    160     16       C  
ATOM   3500  O   GLN A 436      44.295  15.277  25.561  1.00 11.30           O  
ANISOU 3500  O   GLN A 436      854   1696   1743     28    187    268       O  
ATOM   3501  CB  GLN A 436      42.311  15.351  23.185  1.00 10.16           C  
ANISOU 3501  CB  GLN A 436      898   1536   1427     58    239    -13       C  
ATOM   3502  CG  GLN A 436      41.827  13.949  23.111  1.00 10.98           C  
ANISOU 3502  CG  GLN A 436     1109   1630   1435     -8    277   -121       C  
ATOM   3503  CD  GLN A 436      41.570  13.359  21.771  1.00 10.89           C  
ANISOU 3503  CD  GLN A 436      997   1773   1367     82    229    -74       C  
ATOM   3504  OE1 GLN A 436      42.030  13.898  20.734  1.00 12.67           O  
ANISOU 3504  OE1 GLN A 436     1174   2306   1334   -220    376   -162       O  
ATOM   3505  NE2 GLN A 436      40.837  12.242  21.688  1.00 12.69           N  
ANISOU 3505  NE2 GLN A 436     1351   2057   1416   -247    366   -363       N  
ATOM   3506  N   GLY A 437      42.426  14.395  26.414  1.00 10.25           N  
ANISOU 3506  N   GLY A 437      886   1557   1451     73    243    136       N  
ATOM   3507  CA  GLY A 437      43.153  13.659  27.410  1.00 10.35           C  
ANISOU 3507  CA  GLY A 437     1087   1451   1393     64    241    167       C  
ATOM   3508  C   GLY A 437      42.235  13.167  28.522  1.00 10.50           C  
ANISOU 3508  C   GLY A 437      951   1637   1400     75    231    136       C  
ATOM   3509  O   GLY A 437      41.092  13.637  28.667  1.00 10.99           O  
ANISOU 3509  O   GLY A 437      978   1760   1438    206    231    148       O  
ATOM   3510  N   LEU A 438      42.722  12.226  29.337  1.00 10.76           N  
ANISOU 3510  N   LEU A 438      994   1681   1415    180    268    194       N  
ATOM   3511  CA  LEU A 438      41.990  11.774  30.515  1.00 11.85           C  
ANISOU 3511  CA  LEU A 438     1073   2014   1418    226    344    304       C  
ATOM   3512  C   LEU A 438      41.603  12.948  31.415  1.00 11.55           C  
ANISOU 3512  C   LEU A 438     1063   2154   1173    202    271    235       C  
ATOM   3513  O   LEU A 438      42.471  13.775  31.721  1.00 13.34           O  
ANISOU 3513  O   LEU A 438     1093   2251   1726    100    349     62       O  
ATOM   3514  CB  LEU A 438      42.835  10.789  31.281  1.00 13.93           C  
ANISOU 3514  CB  LEU A 438     1450   2193   1650    360    449    536       C  
ATOM   3515  CG  LEU A 438      43.017   9.412  30.659  1.00 16.70           C  
ANISOU 3515  CG  LEU A 438     1772   2179   2393    488    691    462       C  
ATOM   3516  CD1 LEU A 438      44.038   8.629  31.448  1.00 17.57           C  
ANISOU 3516  CD1 LEU A 438     1970   2384   2321    714    704    517       C  
ATOM   3517  CD2 LEU A 438      41.648   8.710  30.672  1.00 26.15           C  
ANISOU 3517  CD2 LEU A 438     2222   2435   5277    -84   -468    370       C  
ATOM   3518  N   GLY A 439      40.342  13.008  31.790  1.00 12.87           N  
ANISOU 3518  N   GLY A 439      997   2231   1662    272    338    285       N  
ATOM   3519  CA  GLY A 439      39.853  14.081  32.671  1.00 14.16           C  
ANISOU 3519  CA  GLY A 439     1235   2568   1578    444    617    227       C  
ATOM   3520  C   GLY A 439      39.367  15.306  31.960  1.00 12.29           C  
ANISOU 3520  C   GLY A 439      959   2171   1538    102    295    -73       C  
ATOM   3521  O   GLY A 439      38.789  16.169  32.621  1.00 13.79           O  
ANISOU 3521  O   GLY A 439     1365   2184   1691    149    485   -118       O  
ATOM   3522  N   CYS A 440      39.623  15.418  30.630  1.00 11.72           N  
ANISOU 3522  N   CYS A 440     1052   1875   1526    182    344    -33       N  
ATOM   3523  CA  CYS A 440      39.314  16.704  29.994  1.00 12.23           C  
ANISOU 3523  CA  CYS A 440     1120   1846   1680    118    307   -126       C  
ATOM   3524  C   CYS A 440      37.828  16.985  29.979  1.00 12.15           C  
ANISOU 3524  C   CYS A 440     1070   1772   1775    133    241    106       C  
ATOM   3525  O   CYS A 440      37.430  18.156  29.885  1.00 13.61           O  
ANISOU 3525  O   CYS A 440     1331   1843   1996    262    375    -55       O  
ATOM   3526  CB  CYS A 440      39.950  16.701  28.605  1.00 14.31           C  
ANISOU 3526  CB  CYS A 440     1529   1833   2074    183    766    340       C  
ATOM   3527  SG  CYS A 440      41.801  16.824  28.691  1.00 15.83           S  
ANISOU 3527  SG  CYS A 440     1565   2182   2266    -75    664   -138       S  
ATOM   3528  N   ASP A 441      36.979  15.964  30.037  1.00 12.09           N  
ANISOU 3528  N   ASP A 441     1058   1870   1667    127    264   -206       N  
ATOM   3529  CA  ASP A 441      35.538  16.131  30.142  1.00 11.48           C  
ANISOU 3529  CA  ASP A 441     1046   1910   1407     99     67   -139       C  
ATOM   3530  C   ASP A 441      35.085  16.932  31.338  1.00 11.50           C  
ANISOU 3530  C   ASP A 441     1055   1886   1428    176    282     -6       C  
ATOM   3531  O   ASP A 441      34.136  17.746  31.231  1.00 13.73           O  
ANISOU 3531  O   ASP A 441     1210   2297   1710    384    389     25       O  
ATOM   3532  CB  ASP A 441      34.836  14.785  30.117  1.00 12.57           C  
ANISOU 3532  CB  ASP A 441     1179   1927   1668     39    238   -251       C  
ATOM   3533  CG  ASP A 441      35.220  13.759  31.128  1.00 13.53           C  
ANISOU 3533  CG  ASP A 441     1369   1923   1850    -35    340   -137       C  
ATOM   3534  OD1 ASP A 441      36.451  13.599  31.346  1.00 15.66           O  
ANISOU 3534  OD1 ASP A 441     1371   2270   2309    118    302    254       O  
ATOM   3535  OD2 ASP A 441      34.334  13.071  31.722  1.00 15.32           O  
ANISOU 3535  OD2 ASP A 441     1522   1978   2321    -96    504    -39       O  
ATOM   3536  N   GLU A 442      35.717  16.729  32.507  1.00 11.04           N  
ANISOU 3536  N   GLU A 442     1184   1526   1487     39    210    -96       N  
ATOM   3537  CA  GLU A 442      35.352  17.426  33.737  1.00 10.86           C  
ANISOU 3537  CA  GLU A 442     1119   1649   1358    -78    160    -53       C  
ATOM   3538  C   GLU A 442      36.200  18.667  34.004  1.00 10.48           C  
ANISOU 3538  C   GLU A 442     1151   1630   1201    -64    328    -21       C  
ATOM   3539  O   GLU A 442      35.885  19.504  34.835  1.00 12.29           O  
ANISOU 3539  O   GLU A 442     1245   1750   1674   -145    464   -274       O  
ATOM   3540  CB  GLU A 442      35.328  16.472  34.910  1.00 12.00           C  
ANISOU 3540  CB  GLU A 442     1213   1819   1527    -81    177    117       C  
ATOM   3541  CG  GLU A 442      34.269  15.397  34.852  1.00 12.21           C  
ANISOU 3541  CG  GLU A 442     1155   1704   1780     67    221    160       C  
ATOM   3542  CD  GLU A 442      32.856  15.889  35.068  1.00 12.54           C  
ANISOU 3542  CD  GLU A 442     1164   1628   1973    -19    418     -7       C  
ATOM   3543  OE1 GLU A 442      31.932  15.013  35.018  1.00 13.39           O  
ANISOU 3543  OE1 GLU A 442     1100   1873   2114     -3    257    -45       O  
ATOM   3544  OE2 GLU A 442      32.620  17.084  35.304  1.00 12.85           O  
ANISOU 3544  OE2 GLU A 442     1141   1867   1876     -9    469    -82       O  
ATOM   3545  N   MET A 443      37.313  18.836  33.264  1.00 11.08           N  
ANISOU 3545  N   MET A 443     1288   1590   1331    -91    410   -177       N  
ATOM   3546  CA  MET A 443      38.262  19.899  33.456  1.00 10.83           C  
ANISOU 3546  CA  MET A 443      926   1735   1453     49     60     32       C  
ATOM   3547  C   MET A 443      37.826  21.207  32.823  1.00 10.43           C  
ANISOU 3547  C   MET A 443      825   1627   1511     49    288    -74       C  
ATOM   3548  O   MET A 443      38.230  22.299  33.286  1.00 12.35           O  
ANISOU 3548  O   MET A 443     1319   1736   1639   -252    313      4       O  
ATOM   3549  CB  MET A 443      39.612  19.489  32.829  1.00 14.85           C  
ANISOU 3549  CB  MET A 443      860   2102   2683    229    153     59       C  
ATOM   3550  CG  MET A 443      40.759  20.310  33.091  1.00 15.88           C  
ANISOU 3550  CG  MET A 443     1224   2262   2549    -25    456    -14       C  
ATOM   3551  SD  MET A 443      42.181  19.796  32.118  1.00 17.67           S  
ANISOU 3551  SD  MET A 443     1273   3259   2182    201    594    303       S  
ATOM   3552  CE  MET A 443      42.379  18.098  32.559  1.00 16.21           C  
ANISOU 3552  CE  MET A 443     1362   2834   1963    217    278   -552       C  
ATOM   3553  N   LEU A 444      37.055  21.156  31.748  1.00 10.93           N  
ANISOU 3553  N   LEU A 444      940   1565   1649     27    168     72       N  
ATOM   3554  CA  LEU A 444      36.842  22.309  30.916  1.00 11.48           C  
ANISOU 3554  CA  LEU A 444     1079   1488   1796     69    293    171       C  
ATOM   3555  C   LEU A 444      35.949  23.361  31.540  1.00 11.64           C  
ANISOU 3555  C   LEU A 444     1117   1478   1829     60    468    254       C  
ATOM   3556  O   LEU A 444      36.200  24.554  31.320  1.00 11.36           O  
ANISOU 3556  O   LEU A 444     1291   1481   1546    -38    396     91       O  
ATOM   3557  CB  LEU A 444      36.212  21.846  29.580  1.00 11.76           C  
ANISOU 3557  CB  LEU A 444     1127   1569   1772     88    250    172       C  
ATOM   3558  CG  LEU A 444      35.975  22.926  28.545  1.00 12.86           C  
ANISOU 3558  CG  LEU A 444     1179   1793   1914    203    128    227       C  
ATOM   3559  CD1 LEU A 444      37.289  23.578  28.063  1.00 15.29           C  
ANISOU 3559  CD1 LEU A 444     1492   2202   2117   -115    433    513       C  
ATOM   3560  CD2 LEU A 444      35.184  22.366  27.389  1.00 13.61           C  
ANISOU 3560  CD2 LEU A 444     1503   1999   1671    182    306     67       C  
ATOM   3561  N   GLN A 445      34.901  22.984  32.294  1.00 10.89           N  
ANISOU 3561  N   GLN A 445     1135   1355   1648     37    344    161       N  
ATOM   3562  CA  GLN A 445      33.902  23.973  32.693  1.00 10.45           C  
ANISOU 3562  CA  GLN A 445      966   1439   1566    128    211     98       C  
ATOM   3563  C   GLN A 445      34.469  25.201  33.387  1.00 10.48           C  
ANISOU 3563  C   GLN A 445      961   1522   1498    151    265    132       C  
ATOM   3564  O   GLN A 445      34.112  26.321  33.059  1.00 10.83           O  
ANISOU 3564  O   GLN A 445     1118   1390   1605     28     83     25       O  
ATOM   3565  CB  GLN A 445      32.827  23.296  33.566  1.00 10.88           C  
ANISOU 3565  CB  GLN A 445      998   1712   1424     89    187    139       C  
ATOM   3566  CG  GLN A 445      31.651  24.238  33.928  1.00 10.80           C  
ANISOU 3566  CG  GLN A 445      978   1619   1506     64    144    -17       C  
ATOM   3567  CD  GLN A 445      30.679  24.361  32.758  1.00 10.09           C  
ANISOU 3567  CD  GLN A 445      840   1596   1399    127    328     89       C  
ATOM   3568  OE1 GLN A 445      29.829  23.473  32.528  1.00 11.47           O  
ANISOU 3568  OE1 GLN A 445     1057   1693   1608    -46    122     39       O  
ATOM   3569  NE2 GLN A 445      30.813  25.457  32.023  1.00 11.67           N  
ANISOU 3569  NE2 GLN A 445     1176   1658   1599     84    305    171       N  
ATOM   3570  N   GLY A 446      35.369  24.959  34.342  1.00 11.25           N  
ANISOU 3570  N   GLY A 446      927   1721   1626    -31    189    150       N  
ATOM   3571  CA  GLY A 446      35.911  26.068  35.070  1.00 12.48           C  
ANISOU 3571  CA  GLY A 446     1123   1928   1690   -134    205     47       C  
ATOM   3572  C   GLY A 446      36.773  26.972  34.213  1.00 12.52           C  
ANISOU 3572  C   GLY A 446     1125   1828   1802   -193    222     93       C  
ATOM   3573  O   GLY A 446      36.786  28.190  34.370  1.00 12.47           O  
ANISOU 3573  O   GLY A 446     1189   1893   1656    -78    106     39       O  
ATOM   3574  N   PHE A 447      37.546  26.365  33.307  1.00 11.99           N  
ANISOU 3574  N   PHE A 447     1138   1590   1828   -106    251    166       N  
ATOM   3575  CA  PHE A 447      38.329  27.172  32.367  1.00 12.49           C  
ANISOU 3575  CA  PHE A 447     1136   1668   1942     -3    267    275       C  
ATOM   3576  C   PHE A 447      37.436  27.996  31.473  1.00 12.23           C  
ANISOU 3576  C   PHE A 447     1051   1726   1869     15    396    292       C  
ATOM   3577  O   PHE A 447      37.780  29.116  31.080  1.00 13.38           O  
ANISOU 3577  O   PHE A 447     1250   1711   2124    -93    265    378       O  
ATOM   3578  CB  PHE A 447      39.327  26.325  31.581  1.00 12.18           C  
ANISOU 3578  CB  PHE A 447     1153   1674   1802     19    274    332       C  
ATOM   3579  CG  PHE A 447      40.469  25.803  32.441  1.00 12.54           C  
ANISOU 3579  CG  PHE A 447      939   1801   2023    -85    318    420       C  
ATOM   3580  CD1 PHE A 447      40.555  24.524  32.864  1.00 12.93           C  
ANISOU 3580  CD1 PHE A 447     1187   1772   1952     41    325    422       C  
ATOM   3581  CD2 PHE A 447      41.468  26.675  32.863  1.00 13.32           C  
ANISOU 3581  CD2 PHE A 447     1214   1850   1999    -88    178    111       C  
ATOM   3582  CE1 PHE A 447      41.610  24.095  33.617  1.00 13.88           C  
ANISOU 3582  CE1 PHE A 447     1211   2003   2061     37    275    625       C  
ATOM   3583  CE2 PHE A 447      42.549  26.234  33.589  1.00 13.97           C  
ANISOU 3583  CE2 PHE A 447     1090   2041   2178     30    150    -89       C  
ATOM   3584  CZ  PHE A 447      42.595  24.953  34.021  1.00 13.37           C  
ANISOU 3584  CZ  PHE A 447     1343   2180   1557     65    354    103       C  
ATOM   3585  N   ALA A 448      36.270  27.450  31.090  1.00 11.86           N  
ANISOU 3585  N   ALA A 448     1149   1566   1792     -8    270    318       N  
ATOM   3586  CA  ALA A 448      35.309  28.225  30.278  1.00 11.75           C  
ANISOU 3586  CA  ALA A 448     1310   1545   1611      7    147    229       C  
ATOM   3587  C   ALA A 448      34.836  29.436  31.090  1.00 11.23           C  
ANISOU 3587  C   ALA A 448     1056   1604   1608    -66     71    144       C  
ATOM   3588  O   ALA A 448      34.608  30.499  30.453  1.00 12.72           O  
ANISOU 3588  O   ALA A 448     1381   1623   1827     51    105    243       O  
ATOM   3589  CB  ALA A 448      34.171  27.317  29.851  1.00 11.35           C  
ANISOU 3589  CB  ALA A 448     1246   1570   1495    132    218     19       C  
ATOM   3590  N   VAL A 449      34.607  29.338  32.383  1.00 11.30           N  
ANISOU 3590  N   VAL A 449     1109   1502   1682    -23    151    185       N  
ATOM   3591  CA  VAL A 449      34.216  30.519  33.147  1.00 12.35           C  
ANISOU 3591  CA  VAL A 449     1223   1709   1760    -36     40     15       C  
ATOM   3592  C   VAL A 449      35.311  31.571  33.084  1.00 12.59           C  
ANISOU 3592  C   VAL A 449     1233   1672   1878    -65     46    -28       C  
ATOM   3593  O   VAL A 449      35.023  32.762  32.838  1.00 13.73           O  
ANISOU 3593  O   VAL A 449     1552   1649   2018    -59    -20    -75       O  
ATOM   3594  CB  VAL A 449      33.960  30.156  34.643  1.00 12.46           C  
ANISOU 3594  CB  VAL A 449     1107   1906   1723    -40     21    -27       C  
ATOM   3595  CG1 VAL A 449      33.681  31.416  35.467  1.00 14.03           C  
ANISOU 3595  CG1 VAL A 449     1700   1734   1897   -181     62    -34       C  
ATOM   3596  CG2 VAL A 449      32.817  29.141  34.768  1.00 13.12           C  
ANISOU 3596  CG2 VAL A 449     1283   1649   2051      5    150     85       C  
ATOM   3597  N   ALA A 450      36.544  31.164  33.238  1.00 12.51           N  
ANISOU 3597  N   ALA A 450     1286   1510   1956   -102     58    -78       N  
ATOM   3598  CA  ALA A 450      37.664  32.140  33.145  1.00 13.35           C  
ANISOU 3598  CA  ALA A 450     1411   1600   2062   -308    -54     56       C  
ATOM   3599  C   ALA A 450      37.739  32.808  31.756  1.00 13.44           C  
ANISOU 3599  C   ALA A 450     1201   1597   2309   -246   -149    270       C  
ATOM   3600  O   ALA A 450      37.981  34.004  31.686  1.00 14.19           O  
ANISOU 3600  O   ALA A 450     1549   1668   2176   -306     -6    218       O  
ATOM   3601  CB  ALA A 450      38.966  31.427  33.458  1.00 15.36           C  
ANISOU 3601  CB  ALA A 450     1401   2073   2362   -262   -100    530       C  
ATOM   3602  N   VAL A 451      37.609  32.027  30.722  1.00 13.10           N  
ANISOU 3602  N   VAL A 451     1237   1589   2152   -231    -43    355       N  
ATOM   3603  CA  VAL A 451      37.655  32.575  29.369  1.00 14.09           C  
ANISOU 3603  CA  VAL A 451     1423   1655   2277   -326     55    344       C  
ATOM   3604  C   VAL A 451      36.519  33.571  29.184  1.00 14.62           C  
ANISOU 3604  C   VAL A 451     1568   1812   2177   -180     35    464       C  
ATOM   3605  O   VAL A 451      36.698  34.664  28.631  1.00 16.41           O  
ANISOU 3605  O   VAL A 451     2115   1778   2344   -105    208    457       O  
ATOM   3606  CB  VAL A 451      37.654  31.476  28.288  1.00 14.85           C  
ANISOU 3606  CB  VAL A 451     1603   1874   2166   -355    274    297       C  
ATOM   3607  CG1 VAL A 451      37.452  32.061  26.896  1.00 16.54           C  
ANISOU 3607  CG1 VAL A 451     1942   2168   2173   -473    174    452       C  
ATOM   3608  CG2 VAL A 451      38.954  30.672  28.353  1.00 16.06           C  
ANISOU 3608  CG2 VAL A 451     1637   2156   2311   -177    321    153       C  
ATOM   3609  N   LYS A 452      35.285  33.215  29.589  1.00 15.00           N  
ANISOU 3609  N   LYS A 452     1382   1892   2427   -106   -162    575       N  
ATOM   3610  CA  LYS A 452      34.156  34.116  29.477  1.00 16.40           C  
ANISOU 3610  CA  LYS A 452     1605   2114   2513     50   -176    519       C  
ATOM   3611  C   LYS A 452      34.398  35.429  30.227  1.00 16.43           C  
ANISOU 3611  C   LYS A 452     1396   2131   2716    189     -2    506       C  
ATOM   3612  O   LYS A 452      33.892  36.474  29.783  1.00 19.78           O  
ANISOU 3612  O   LYS A 452     1753   2192   3569    300    -92    682       O  
ATOM   3613  CB ALYS A 452      32.863  33.490  30.019  0.45 19.09           C  
ANISOU 3613  CB ALYS A 452     1423   2718   3113   -155   -135    142       C  
ATOM   3614  CB BLYS A 452      32.894  33.364  29.921  0.55 19.72           C  
ANISOU 3614  CB BLYS A 452     1464   2418   3611     -4     42    319       C  
ATOM   3615  CG ALYS A 452      32.150  32.523  29.110  0.45 21.45           C  
ANISOU 3615  CG ALYS A 452     2505   2352   3292   -502   -248    252       C  
ATOM   3616  CG BLYS A 452      31.613  34.142  29.691  0.55 21.43           C  
ANISOU 3616  CG BLYS A 452     1684   3122   3337    501     -3   -183       C  
ATOM   3617  CD ALYS A 452      31.610  33.187  27.868  0.45 23.03           C  
ANISOU 3617  CD ALYS A 452     2499   2842   3411   -152   -666      0       C  
ATOM   3618  CD BLYS A 452      31.112  33.960  28.272  0.55 25.42           C  
ANISOU 3618  CD BLYS A 452     3151   3045   3463    898   -595   -129       C  
ATOM   3619  CE ALYS A 452      30.409  34.053  28.131  0.45 22.38           C  
ANISOU 3619  CE ALYS A 452     2671   2949   2882   -107   -372    -57       C  
ATOM   3620  CE BLYS A 452      29.884  34.797  27.945  0.55 25.87           C  
ANISOU 3620  CE BLYS A 452     3666   2937   3225   1165   -604    -59       C  
ATOM   3621  NZ ALYS A 452      29.787  34.620  26.906  0.45 26.04           N  
ANISOU 3621  NZ ALYS A 452     2194   5827   1873   1445   -215  -1146       N  
ATOM   3622  NZ BLYS A 452      28.636  34.009  28.115  0.55 25.90           N  
ANISOU 3622  NZ BLYS A 452     3121   4348   2370   1304   -115    205       N  
ATOM   3623  N   MET A 453      35.118  35.403  31.309  1.00 15.85           N  
ANISOU 3623  N   MET A 453     1702   1948   2375    215    172    216       N  
ATOM   3624  CA  MET A 453      35.506  36.582  32.093  1.00 17.73           C  
ANISOU 3624  CA  MET A 453     2021   1932   2783    118    332     22       C  
ATOM   3625  C   MET A 453      36.637  37.399  31.491  1.00 18.12           C  
ANISOU 3625  C   MET A 453     2327   1881   2677      9    181    186       C  
ATOM   3626  O   MET A 453      37.039  38.424  31.998  1.00 23.57           O  
ANISOU 3626  O   MET A 453     3659   1920   3376   -496   1155   -293       O  
ATOM   3627  CB  MET A 453      35.986  36.192  33.502  1.00 19.72           C  
ANISOU 3627  CB  MET A 453     2453   2422   2617   -615    301    -61       C  
ATOM   3628  CG  MET A 453      34.894  35.740  34.416  1.00 20.10           C  
ANISOU 3628  CG  MET A 453     1931   2627   3078   -208    296    345       C  
ATOM   3629  SD  MET A 453      35.561  35.128  35.983  1.00 21.81           S  
ANISOU 3629  SD  MET A 453     2380   3397   2510   -154    406    -70       S  
ATOM   3630  CE  MET A 453      35.996  36.687  36.630  1.00 19.68           C  
ANISOU 3630  CE  MET A 453     2356   2782   2338    238    836    185       C  
ATOM   3631  N   GLY A 454      37.232  36.933  30.402  1.00 15.86           N  
ANISOU 3631  N   GLY A 454     1612   1718   2696   -170     62    141       N  
ATOM   3632  CA  GLY A 454      38.336  37.658  29.782  1.00 16.88           C  
ANISOU 3632  CA  GLY A 454     1746   1658   3008   -269    -16    389       C  
ATOM   3633  C   GLY A 454      39.687  37.382  30.383  1.00 16.28           C  
ANISOU 3633  C   GLY A 454     1644   1864   2677   -191    113    384       C  
ATOM   3634  O   GLY A 454      40.588  38.270  30.346  1.00 17.07           O  
ANISOU 3634  O   GLY A 454     1730   1849   2906   -210    257    213       O  
ATOM   3635  N   ALA A 455      39.935  36.217  30.916  1.00 14.40           N  
ANISOU 3635  N   ALA A 455     1486   1690   2295    -82    178     35       N  
ATOM   3636  CA  ALA A 455      41.211  35.861  31.519  1.00 14.42           C  
ANISOU 3636  CA  ALA A 455     1427   1810   2241    -61    271     97       C  
ATOM   3637  C   ALA A 455      42.335  36.082  30.535  1.00 14.11           C  
ANISOU 3637  C   ALA A 455     1492   1710   2161   -215    200     57       C  
ATOM   3638  O   ALA A 455      42.216  35.801  29.349  1.00 15.98           O  
ANISOU 3638  O   ALA A 455     1652   2258   2162   -157    252    -61       O  
ATOM   3639  CB  ALA A 455      41.200  34.389  31.901  1.00 16.65           C  
ANISOU 3639  CB  ALA A 455     1459   1823   3045    -63    304    403       C  
ATOM   3640  N   THR A 456      43.470  36.502  31.119  1.00 15.12           N  
ANISOU 3640  N   THR A 456     1481   1817   2449   -287    175     74       N  
ATOM   3641  CA  THR A 456      44.711  36.572  30.375  1.00 14.83           C  
ANISOU 3641  CA  THR A 456     1469   1824   2340   -314    151    353       C  
ATOM   3642  C   THR A 456      45.589  35.431  30.818  1.00 13.57           C  
ANISOU 3642  C   THR A 456     1543   1716   1896   -342    176    149       C  
ATOM   3643  O   THR A 456      45.361  34.725  31.815  1.00 13.98           O  
ANISOU 3643  O   THR A 456     1811   1613   1886   -335    305    172       O  
ATOM   3644  CB  THR A 456      45.485  37.867  30.680  1.00 16.14           C  
ANISOU 3644  CB  THR A 456     1701   1792   2640   -315    239    252       C  
ATOM   3645  OG1 THR A 456      45.813  37.829  32.100  1.00 18.46           O  
ANISOU 3645  OG1 THR A 456     2042   2278   2695   -459     88     15       O  
ATOM   3646  CG2 THR A 456      44.610  39.062  30.332  1.00 19.73           C  
ANISOU 3646  CG2 THR A 456     2629   1706   3161    -11    402    280       C  
ATOM   3647  N   LYS A 457      46.703  35.215  30.095  1.00 14.14           N  
ANISOU 3647  N   LYS A 457     1570   1791   2010   -235    257    293       N  
ATOM   3648  CA  LYS A 457      47.612  34.161  30.473  1.00 14.85           C  
ANISOU 3648  CA  LYS A 457     1743   1729   2169   -250    145    127       C  
ATOM   3649  C   LYS A 457      48.141  34.443  31.869  1.00 15.15           C  
ANISOU 3649  C   LYS A 457     1628   1784   2346    -26    -50    -28       C  
ATOM   3650  O   LYS A 457      48.357  33.495  32.667  1.00 16.24           O  
ANISOU 3650  O   LYS A 457     1928   1905   2338   -109    -79    171       O  
ATOM   3651  CB ALYS A 457      48.773  34.001  29.500  0.66 18.26           C  
ANISOU 3651  CB ALYS A 457     1864   2790   2283    515    218    609       C  
ATOM   3652  CB BLYS A 457      48.713  34.066  29.427  0.34 17.44           C  
ANISOU 3652  CB BLYS A 457     1892   2487   2248    417    244    752       C  
ATOM   3653  CG ALYS A 457      49.436  32.672  29.818  0.66 15.24           C  
ANISOU 3653  CG ALYS A 457     1422   2165   2202   -218    217    488       C  
ATOM   3654  CG BLYS A 457      50.046  33.428  29.718  0.34 15.11           C  
ANISOU 3654  CG BLYS A 457     1546   1870   2325   -217    130    850       C  
ATOM   3655  CD ALYS A 457      50.406  32.249  28.753  0.66 16.80           C  
ANISOU 3655  CD ALYS A 457     1791   2258   2334    230    328    625       C  
ATOM   3656  CD BLYS A 457      49.907  31.915  29.831  0.34 14.40           C  
ANISOU 3656  CD BLYS A 457     1327   1809   2336   -235    219    399       C  
ATOM   3657  CE ALYS A 457      51.026  30.918  29.188  0.66 20.95           C  
ANISOU 3657  CE ALYS A 457     3342   1894   2725    470   -120     65       C  
ATOM   3658  CE BLYS A 457      51.140  31.187  29.343  0.34 15.57           C  
ANISOU 3658  CE BLYS A 457     1306   2163   2447   -272    194      5       C  
ATOM   3659  NZ ALYS A 457      52.070  31.131  30.212  0.66 30.13           N  
ANISOU 3659  NZ ALYS A 457     3814   3003   4629    671  -1527    925       N  
ATOM   3660  NZ BLYS A 457      52.281  31.268  30.278  0.34 14.16           N  
ANISOU 3660  NZ BLYS A 457      999   2513   1868   -370    639   -341       N  
ATOM   3661  N   ALA A 458      48.397  35.706  32.249  1.00 15.66           N  
ANISOU 3661  N   ALA A 458     1646   1833   2471   -275   -181    -51       N  
ATOM   3662  CA  ALA A 458      48.817  36.022  33.596  1.00 16.87           C  
ANISOU 3662  CA  ALA A 458     1736   2248   2427   -562     63   -169       C  
ATOM   3663  C   ALA A 458      47.822  35.554  34.645  1.00 16.86           C  
ANISOU 3663  C   ALA A 458     1786   2035   2585   -175    126    146       C  
ATOM   3664  O   ALA A 458      48.209  35.118  35.711  1.00 16.72           O  
ANISOU 3664  O   ALA A 458     1706   2074   2573     21     51    184       O  
ATOM   3665  CB  ALA A 458      49.050  37.527  33.783  1.00 19.50           C  
ANISOU 3665  CB  ALA A 458     2426   2513   2471  -1192     43   -270       C  
ATOM   3666  N   ASP A 459      46.541  35.617  34.379  1.00 14.83           N  
ANISOU 3666  N   ASP A 459     1709   1870   2056   -160    216     94       N  
ATOM   3667  CA  ASP A 459      45.535  35.128  35.351  1.00 14.57           C  
ANISOU 3667  CA  ASP A 459     1863   1781   1893     59    328    -88       C  
ATOM   3668  C   ASP A 459      45.685  33.649  35.556  1.00 13.25           C  
ANISOU 3668  C   ASP A 459     1550   1718   1764   -144    143    -48       C  
ATOM   3669  O   ASP A 459      45.532  33.145  36.677  1.00 14.80           O  
ANISOU 3669  O   ASP A 459     2095   1754   1774     -5    188   -136       O  
ATOM   3670  CB  ASP A 459      44.113  35.456  34.862  1.00 15.14           C  
ANISOU 3670  CB  ASP A 459     1670   1752   2328     43    301    -30       C  
ATOM   3671  CG  ASP A 459      43.770  36.945  34.873  1.00 16.10           C  
ANISOU 3671  CG  ASP A 459     1907   1664   2546    -44    -91   -105       C  
ATOM   3672  OD1 ASP A 459      44.091  37.596  35.879  1.00 18.87           O  
ANISOU 3672  OD1 ASP A 459     2564   1852   2755     66   -168   -304       O  
ATOM   3673  OD2 ASP A 459      43.135  37.434  33.897  1.00 18.59           O  
ANISOU 3673  OD2 ASP A 459     2383   2000   2679    140   -205    -13       O  
ATOM   3674  N   PHE A 460      45.969  32.876  34.513  1.00 13.31           N  
ANISOU 3674  N   PHE A 460     1663   1688   1706    -12     20     45       N  
ATOM   3675  CA  PHE A 460      46.207  31.455  34.658  1.00 13.09           C  
ANISOU 3675  CA  PHE A 460     1579   1683   1712     88    249    121       C  
ATOM   3676  C   PHE A 460      47.462  31.192  35.453  1.00 13.64           C  
ANISOU 3676  C   PHE A 460     1667   1572   1943    -51    130    113       C  
ATOM   3677  O   PHE A 460      47.486  30.403  36.403  1.00 14.69           O  
ANISOU 3677  O   PHE A 460     2071   1657   1856   -179    -45    257       O  
ATOM   3678  CB  PHE A 460      46.326  30.768  33.265  1.00 13.23           C  
ANISOU 3678  CB  PHE A 460     1606   1630   1792   -105    266     89       C  
ATOM   3679  CG  PHE A 460      45.036  30.473  32.565  1.00 13.57           C  
ANISOU 3679  CG  PHE A 460     1674   1706   1775   -159    182    240       C  
ATOM   3680  CD1 PHE A 460      44.063  31.429  32.294  1.00 16.75           C  
ANISOU 3680  CD1 PHE A 460     1898   1581   2887   -190   -296     37       C  
ATOM   3681  CD2 PHE A 460      44.802  29.170  32.110  1.00 14.54           C  
ANISOU 3681  CD2 PHE A 460     1706   1740   2078   -180    231     79       C  
ATOM   3682  CE1 PHE A 460      42.880  31.113  31.636  1.00 16.49           C  
ANISOU 3682  CE1 PHE A 460     1792   1815   2661   -110   -149    255       C  
ATOM   3683  CE2 PHE A 460      43.641  28.851  31.437  1.00 16.92           C  
ANISOU 3683  CE2 PHE A 460     1789   1756   2884   -323    -71    336       C  
ATOM   3684  CZ  PHE A 460      42.714  29.832  31.186  1.00 14.87           C  
ANISOU 3684  CZ  PHE A 460     1640   1954   2056   -247     97     78       C  
ATOM   3685  N  AASP A 461      48.527  31.899  35.050  0.20 13.34           N  
ANISOU 3685  N  AASP A 461     1267   2087   1716    453    610    259       N  
ATOM   3686  N  BASP A 461      48.541  31.893  35.073  0.80 14.46           N  
ANISOU 3686  N  BASP A 461     1625   1909   1960    -60     73    377       N  
ATOM   3687  CA AASP A 461      49.846  31.887  35.647  0.20 16.30           C  
ANISOU 3687  CA AASP A 461     1337   2597   2258    189    443    347       C  
ATOM   3688  CA BASP A 461      49.828  31.615  35.710  0.80 15.94           C  
ANISOU 3688  CA BASP A 461     1443   2316   2298     26    266    193       C  
ATOM   3689  C  AASP A 461      49.707  32.016  37.178  0.20 14.91           C  
ANISOU 3689  C  AASP A 461      888   2519   2260   -622    304    233       C  
ATOM   3690  C  BASP A 461      49.828  32.106  37.172  0.80 16.04           C  
ANISOU 3690  C  BASP A 461     1759   2198   2139   -365      8    378       C  
ATOM   3691  O  AASP A 461      50.262  31.235  37.941  0.20 13.74           O  
ANISOU 3691  O  AASP A 461     1330   1775   2114   -968    113     -7       O  
ATOM   3692  O  BASP A 461      50.642  31.611  37.962  0.80 18.26           O  
ANISOU 3692  O  BASP A 461     1587   2708   2641   -701   -282    585       O  
ATOM   3693  CB AASP A 461      50.767  33.025  35.212  0.20 17.58           C  
ANISOU 3693  CB AASP A 461     1235   3000   2445    240    427    912       C  
ATOM   3694  CB BASP A 461      50.940  32.236  34.870  0.80 17.41           C  
ANISOU 3694  CB BASP A 461     1734   2479   2401   -319    233    404       C  
ATOM   3695  CG AASP A 461      51.512  32.934  33.906  0.20 18.71           C  
ANISOU 3695  CG AASP A 461     1802   3103   2203   -295    344    542       C  
ATOM   3696  CG BASP A 461      51.097  31.711  33.458  0.80 17.09           C  
ANISOU 3696  CG BASP A 461     1097   2780   2616   -157    351     93       C  
ATOM   3697  OD1AASP A 461      51.569  31.853  33.278  0.20 21.17           O  
ANISOU 3697  OD1AASP A 461     2138   3081   2823   -687    905    382       O  
ATOM   3698  OD1BASP A 461      50.623  30.595  33.126  0.80 23.72           O  
ANISOU 3698  OD1BASP A 461     1934   3119   3958   -270    608   -828       O  
ATOM   3699  OD2AASP A 461      52.082  33.972  33.472  0.20 18.80           O  
ANISOU 3699  OD2AASP A 461     2317   2999   1827   -442    515    253       O  
ATOM   3700  OD2BASP A 461      51.708  32.400  32.607  0.80 22.36           O  
ANISOU 3700  OD2BASP A 461     2519   3289   2687    249    785    634       O  
ATOM   3701  N   ASN A 462      48.964  33.047  37.554  1.00 15.81           N  
ANISOU 3701  N   ASN A 462     1903   2205   1897   -507     72     81       N  
ATOM   3702  CA  ASN A 462      48.825  33.514  38.926  1.00 18.43           C  
ANISOU 3702  CA  ASN A 462     2637   2419   1947   -948     77    -68       C  
ATOM   3703  C   ASN A 462      48.012  32.535  39.780  1.00 16.23           C  
ANISOU 3703  C   ASN A 462     2217   2032   1919   -682     68   -150       C  
ATOM   3704  O   ASN A 462      47.875  32.786  40.984  1.00 18.49           O  
ANISOU 3704  O   ASN A 462     2685   2362   1979  -1062    135   -262       O  
ATOM   3705  CB AASN A 462      48.013  34.820  38.830  0.42 21.30           C  
ANISOU 3705  CB AASN A 462     3873   2152   2069   -695    890    -43       C  
ATOM   3706  CB BASN A 462      48.284  34.931  39.019  0.58 23.95           C  
ANISOU 3706  CB BASN A 462     4663   1968   2471  -1240    206   -525       C  
ATOM   3707  CG AASN A 462      47.883  35.715  40.033  0.42 20.99           C  
ANISOU 3707  CG AASN A 462     2221   3551   2204   -444    191   -672       C  
ATOM   3708  CG BASN A 462      49.036  36.105  38.452  0.58 29.12           C  
ANISOU 3708  CG BASN A 462     5313   2658   3091  -1217     89    601       C  
ATOM   3709  OD1AASN A 462      48.891  35.853  40.746  0.42 21.34           O  
ANISOU 3709  OD1AASN A 462     2596   2733   2778  -1120   -422    678       O  
ATOM   3710  OD1BASN A 462      50.245  36.124  38.236  0.58 38.23           O  
ANISOU 3710  OD1BASN A 462     5359   5666   3502  -3267     74   -675       O  
ATOM   3711  ND2AASN A 462      46.767  36.401  40.335  0.42 22.49           N  
ANISOU 3711  ND2AASN A 462     2336   3762   2447   -508    502   -761       N  
ATOM   3712  ND2BASN A 462      48.310  37.211  38.209  0.58 47.64           N  
ANISOU 3712  ND2BASN A 462     8719   2541   6841  -1269  -4914   1051       N  
ATOM   3713  N   THR A 463      47.425  31.508  39.190  1.00 13.17           N  
ANISOU 3713  N   THR A 463     1588   1774   1641   -239    120    -12       N  
ATOM   3714  CA  THR A 463      46.641  30.548  39.961  1.00 12.23           C  
ANISOU 3714  CA  THR A 463     1402   1645   1599    -74    167     86       C  
ATOM   3715  C   THR A 463      47.547  29.372  40.314  1.00 12.14           C  
ANISOU 3715  C   THR A 463     1099   1816   1697   -140    142     14       C  
ATOM   3716  O   THR A 463      48.140  28.753  39.476  1.00 13.82           O  
ANISOU 3716  O   THR A 463     1600   1961   1690    232    298    130       O  
ATOM   3717  CB  THR A 463      45.461  30.067  39.119  1.00 12.13           C  
ANISOU 3717  CB  THR A 463     1445   1641   1524    -44     77     22       C  
ATOM   3718  OG1 THR A 463      44.684  31.173  38.661  1.00 14.43           O  
ANISOU 3718  OG1 THR A 463     1527   1650   2306    -59     -3    131       O  
ATOM   3719  CG2 THR A 463      44.600  29.160  39.986  1.00 13.95           C  
ANISOU 3719  CG2 THR A 463     1458   1725   2117   -186    335     57       C  
ATOM   3720  N   VAL A 464      47.630  29.036  41.613  1.00 11.69           N  
ANISOU 3720  N   VAL A 464     1190   1518   1735   -185    186     74       N  
ATOM   3721  CA  VAL A 464      48.468  27.946  42.057  1.00 11.75           C  
ANISOU 3721  CA  VAL A 464     1082   1700   1684    -47     19   -100       C  
ATOM   3722  C   VAL A 464      47.914  26.644  41.550  1.00 10.87           C  
ANISOU 3722  C   VAL A 464     1127   1563   1440   -209    142     61       C  
ATOM   3723  O   VAL A 464      46.719  26.391  41.508  1.00 12.03           O  
ANISOU 3723  O   VAL A 464     1058   1700   1813   -128    209   -123       O  
ATOM   3724  CB  VAL A 464      48.638  27.986  43.586  1.00 12.20           C  
ANISOU 3724  CB  VAL A 464     1223   1752   1661   -126    -13   -222       C  
ATOM   3725  CG1 VAL A 464      49.377  26.760  44.085  1.00 12.24           C  
ANISOU 3725  CG1 VAL A 464     1347   1928   1375      8     87   -179       C  
ATOM   3726  CG2 VAL A 464      49.374  29.268  43.971  1.00 14.73           C  
ANISOU 3726  CG2 VAL A 464     1527   1815   2256   -149   -232   -393       C  
ATOM   3727  N   ALA A 465      48.840  25.802  41.052  1.00 11.40           N  
ANISOU 3727  N   ALA A 465     1013   1637   1684   -251    126    -68       N  
ATOM   3728  CA  ALA A 465      48.557  24.501  40.482  1.00 11.00           C  
ANISOU 3728  CA  ALA A 465     1058   1614   1508   -191     92      2       C  
ATOM   3729  C   ALA A 465      48.046  23.543  41.566  1.00 10.50           C  
ANISOU 3729  C   ALA A 465     1144   1466   1379      1    206   -143       C  
ATOM   3730  O   ALA A 465      48.300  23.703  42.750  1.00 11.84           O  
ANISOU 3730  O   ALA A 465     1245   1856   1397   -224    167    -83       O  
ATOM   3731  CB  ALA A 465      49.796  23.927  39.819  1.00 12.94           C  
ANISOU 3731  CB  ALA A 465     1332   2030   1556    -24    382   -168       C  
ATOM   3732  N   ILE A 466      47.341  22.509  41.072  1.00 11.00           N  
ANISOU 3732  N   ILE A 466     1288   1566   1327   -210    100     82       N  
ATOM   3733  CA  ILE A 466      46.924  21.354  41.867  1.00 11.27           C  
ANISOU 3733  CA  ILE A 466     1138   1685   1460    -64    266    128       C  
ATOM   3734  C   ILE A 466      47.694  20.159  41.407  1.00 10.67           C  
ANISOU 3734  C   ILE A 466     1114   1575   1365    -92    148     40       C  
ATOM   3735  O   ILE A 466      47.626  19.786  40.220  1.00 11.96           O  
ANISOU 3735  O   ILE A 466     1300   1745   1498    -52    152     -2       O  
ATOM   3736  CB  ILE A 466      45.430  21.087  41.706  1.00 11.83           C  
ANISOU 3736  CB  ILE A 466     1163   1777   1555   -238    311   -208       C  
ATOM   3737  CG1 ILE A 466      44.620  22.332  42.062  1.00 13.38           C  
ANISOU 3737  CG1 ILE A 466     1260   1991   1834    191    375     62       C  
ATOM   3738  CG2 ILE A 466      45.034  19.868  42.529  1.00 14.26           C  
ANISOU 3738  CG2 ILE A 466     1538   1708   2172   -298    532   -168       C  
ATOM   3739  CD1 ILE A 466      43.228  22.265  41.498  1.00 15.26           C  
ANISOU 3739  CD1 ILE A 466     1478   2715   1604    112    248   -148       C  
ATOM   3740  N   HIS A 467      48.456  19.497  42.262  1.00 11.22           N  
ANISOU 3740  N   HIS A 467     1276   1641   1346    -70    232    130       N  
ATOM   3741  CA  HIS A 467      49.361  18.413  41.945  1.00 11.05           C  
ANISOU 3741  CA  HIS A 467     1190   1503   1504   -105    244    136       C  
ATOM   3742  C   HIS A 467      49.002  17.163  42.730  1.00 10.88           C  
ANISOU 3742  C   HIS A 467     1146   1682   1307   -206     19     71       C  
ATOM   3743  O   HIS A 467      48.679  17.262  43.913  1.00 12.21           O  
ANISOU 3743  O   HIS A 467     1409   1799   1431   -167    140    215       O  
ATOM   3744  CB  HIS A 467      50.797  18.802  42.291  1.00 12.16           C  
ANISOU 3744  CB  HIS A 467     1267   1693   1662   -193    105    151       C  
ATOM   3745  CG  HIS A 467      51.868  17.840  41.850  1.00 12.53           C  
ANISOU 3745  CG  HIS A 467     1104   1629   2028   -177     23    196       C  
ATOM   3746  ND1 HIS A 467      52.180  17.608  40.532  1.00 14.32           N  
ANISOU 3746  ND1 HIS A 467     1014   2184   2242    -80    341    106       N  
ATOM   3747  CD2 HIS A 467      52.702  17.064  42.607  1.00 14.68           C  
ANISOU 3747  CD2 HIS A 467     1374   1510   2695   -204   -365    189       C  
ATOM   3748  CE1 HIS A 467      53.152  16.715  40.494  1.00 16.60           C  
ANISOU 3748  CE1 HIS A 467      797   2385   3126    -62    473     53       C  
ATOM   3749  NE2 HIS A 467      53.491  16.383  41.709  1.00 18.41           N  
ANISOU 3749  NE2 HIS A 467     1598   1999   3400    240   -211    -32       N  
ATOM   3750  N   PRO A 468      49.134  15.976  42.115  1.00 11.01           N  
ANISOU 3750  N   PRO A 468     1135   1506   1542   -154     93    182       N  
ATOM   3751  CA  PRO A 468      49.385  15.666  40.707  1.00 11.08           C  
ANISOU 3751  CA  PRO A 468      937   1641   1633     30    212     11       C  
ATOM   3752  C   PRO A 468      48.052  15.541  39.997  1.00 10.54           C  
ANISOU 3752  C   PRO A 468     1040   1320   1646   -133    126     62       C  
ATOM   3753  O   PRO A 468      47.187  14.733  40.382  1.00 11.71           O  
ANISOU 3753  O   PRO A 468     1161   1639   1648   -211    193     95       O  
ATOM   3754  CB  PRO A 468      50.148  14.406  40.771  1.00 13.16           C  
ANISOU 3754  CB  PRO A 468     1126   1700   2172     93    322    325       C  
ATOM   3755  CG  PRO A 468      50.162  13.863  42.107  1.00 18.58           C  
ANISOU 3755  CG  PRO A 468     3416   1782   1861    680     -7    -50       C  
ATOM   3756  CD  PRO A 468      49.216  14.720  42.938  1.00 13.89           C  
ANISOU 3756  CD  PRO A 468     1504   1836   1937    -23     84    439       C  
ATOM   3757  N   THR A 469      47.870  16.361  38.951  1.00 10.76           N  
ANISOU 3757  N   THR A 469     1042   1464   1582   -142    199     58       N  
ATOM   3758  CA  THR A 469      46.686  16.288  38.108  1.00 10.84           C  
ANISOU 3758  CA  THR A 469      990   1599   1531    -20    227     10       C  
ATOM   3759  C   THR A 469      47.111  16.559  36.646  1.00 11.18           C  
ANISOU 3759  C   THR A 469     1009   1630   1609      0    279    141       C  
ATOM   3760  O   THR A 469      48.169  17.135  36.435  1.00 12.55           O  
ANISOU 3760  O   THR A 469     1158   2016   1595   -194    235     67       O  
ATOM   3761  CB  THR A 469      45.556  17.290  38.477  1.00 11.45           C  
ANISOU 3761  CB  THR A 469     1117   1715   1521     42    316    -45       C  
ATOM   3762  OG1 THR A 469      46.017  18.635  38.244  1.00 12.52           O  
ANISOU 3762  OG1 THR A 469     1373   1650   1734    159    233    -17       O  
ATOM   3763  CG2 THR A 469      45.094  17.147  39.894  1.00 13.14           C  
ANISOU 3763  CG2 THR A 469     1285   2099   1607     58    464   -148       C  
ATOM   3764  N   SER A 470      46.248  16.245  35.689  1.00 10.87           N  
ANISOU 3764  N   SER A 470     1125   1439   1567      2    222    -46       N  
ATOM   3765  CA  SER A 470      46.456  16.755  34.328  1.00 11.44           C  
ANISOU 3765  CA  SER A 470     1041   1727   1581    105    340    -44       C  
ATOM   3766  C   SER A 470      46.151  18.243  34.229  1.00 11.04           C  
ANISOU 3766  C   SER A 470     1131   1620   1444    -85    281    -31       C  
ATOM   3767  O   SER A 470      46.816  18.992  33.493  1.00 11.74           O  
ANISOU 3767  O   SER A 470     1172   1806   1484    -48    356    -29       O  
ATOM   3768  CB  SER A 470      45.607  16.011  33.306  1.00 12.15           C  
ANISOU 3768  CB  SER A 470     1631   1515   1469     -1    355    -80       C  
ATOM   3769  OG  SER A 470      46.156  14.722  33.135  1.00 15.38           O  
ANISOU 3769  OG  SER A 470     1901   1974   1971    227    389   -381       O  
ATOM   3770  N   SER A 471      45.135  18.708  34.983  1.00 11.29           N  
ANISOU 3770  N   SER A 471     1123   1597   1570    -10    343     16       N  
ATOM   3771  CA  SER A 471      44.643  20.075  34.882  1.00 11.48           C  
ANISOU 3771  CA  SER A 471     1043   1674   1643     10    301     99       C  
ATOM   3772  C   SER A 471      45.714  21.125  35.184  1.00 10.74           C  
ANISOU 3772  C   SER A 471     1230   1530   1320     75    409     47       C  
ATOM   3773  O   SER A 471      45.679  22.219  34.611  1.00 12.29           O  
ANISOU 3773  O   SER A 471     1401   1572   1698     -6    328    118       O  
ATOM   3774  CB  SER A 471      43.465  20.238  35.849  1.00 14.05           C  
ANISOU 3774  CB  SER A 471     1533   1727   2077    -52    712   -226       C  
ATOM   3775  OG  SER A 471      43.819  20.226  37.206  1.00 14.30           O  
ANISOU 3775  OG  SER A 471     1464   1937   2032    198    696     90       O  
ATOM   3776  N   GLU A 472      46.670  20.782  36.037  1.00 11.41           N  
ANISOU 3776  N   GLU A 472     1155   1629   1552    -12    237     -3       N  
ATOM   3777  CA  GLU A 472      47.696  21.794  36.354  1.00 11.68           C  
ANISOU 3777  CA  GLU A 472     1314   1649   1475    -78    261     13       C  
ATOM   3778  C   GLU A 472      48.517  22.180  35.159  1.00 11.24           C  
ANISOU 3778  C   GLU A 472     1168   1620   1481      9    233    -33       C  
ATOM   3779  O   GLU A 472      49.168  23.242  35.165  1.00 12.52           O  
ANISOU 3779  O   GLU A 472     1461   1703   1591   -242    238     20       O  
ATOM   3780  CB  GLU A 472      48.623  21.275  37.415  1.00 13.24           C  
ANISOU 3780  CB  GLU A 472     1572   1724   1734   -190    -24     67       C  
ATOM   3781  CG  GLU A 472      49.358  20.002  37.178  1.00 13.63           C  
ANISOU 3781  CG  GLU A 472     1347   1995   1835      8    125    244       C  
ATOM   3782  CD  GLU A 472      50.325  19.607  38.256  1.00 14.99           C  
ANISOU 3782  CD  GLU A 472     1398   2250   2047    -26     -8    160       C  
ATOM   3783  OE1 GLU A 472      51.022  20.492  38.815  1.00 19.71           O  
ANISOU 3783  OE1 GLU A 472     1870   2690   2931   -419   -569    122       O  
ATOM   3784  OE2 GLU A 472      50.436  18.379  38.600  1.00 15.60           O  
ANISOU 3784  OE2 GLU A 472     1620   2290   2017    321     90    285       O  
ATOM   3785  N   GLU A 473      48.579  21.309  34.145  1.00 11.31           N  
ANISOU 3785  N   GLU A 473     1189   1609   1497    -30    257     50       N  
ATOM   3786  CA  GLU A 473      49.397  21.621  32.962  1.00 11.67           C  
ANISOU 3786  CA  GLU A 473     1067   2035   1333    -73    208    121       C  
ATOM   3787  C   GLU A 473      48.901  22.873  32.274  1.00 12.66           C  
ANISOU 3787  C   GLU A 473      986   2350   1474    -58    301    352       C  
ATOM   3788  O   GLU A 473      49.693  23.581  31.645  1.00 14.74           O  
ANISOU 3788  O   GLU A 473     1177   2380   2045    -20    385    676       O  
ATOM   3789  CB  GLU A 473      49.465  20.396  32.079  1.00 13.11           C  
ANISOU 3789  CB  GLU A 473     1257   2328   1395   -290    206    -30       C  
ATOM   3790  CG  GLU A 473      50.170  19.189  32.733  1.00 14.89           C  
ANISOU 3790  CG  GLU A 473     1471   1987   2198     23    385   -352       C  
ATOM   3791  CD  GLU A 473      51.563  19.405  33.217  1.00 19.01           C  
ANISOU 3791  CD  GLU A 473     1325   2643   3254    127    262    518       C  
ATOM   3792  OE1 GLU A 473      52.357  20.159  32.613  1.00 19.15           O  
ANISOU 3792  OE1 GLU A 473     1368   2791   3118      8    483    246       O  
ATOM   3793  OE2 GLU A 473      51.902  18.799  34.277  1.00 23.45           O  
ANISOU 3793  OE2 GLU A 473     1651   3458   3800   -235   -177   1037       O  
ATOM   3794  N   LEU A 474      47.614  23.237  32.398  1.00 12.63           N  
ANISOU 3794  N   LEU A 474     1095   2080   1625      3    267    172       N  
ATOM   3795  CA  LEU A 474      47.103  24.423  31.736  1.00 13.94           C  
ANISOU 3795  CA  LEU A 474     1260   2398   1641     -6    132    338       C  
ATOM   3796  C   LEU A 474      47.515  25.700  32.433  1.00 13.10           C  
ANISOU 3796  C   LEU A 474     1234   2123   1618    -73    358    518       C  
ATOM   3797  O   LEU A 474      47.400  26.793  31.853  1.00 16.53           O  
ANISOU 3797  O   LEU A 474     1652   2429   2201    -75     70    857       O  
ATOM   3798  CB ALEU A 474      45.580  24.457  31.655  0.51 15.05           C  
ANISOU 3798  CB ALEU A 474     1248   2516   1953    119     37     36       C  
ATOM   3799  CB BLEU A 474      45.587  24.269  31.573  0.49 14.56           C  
ANISOU 3799  CB BLEU A 474     1194   2252   2085    -12    220    436       C  
ATOM   3800  CG ALEU A 474      45.019  23.662  30.489  0.51 15.04           C  
ANISOU 3800  CG ALEU A 474     1117   2061   2537    -67    206   -309       C  
ATOM   3801  CG BLEU A 474      44.848  25.076  30.509  0.49 15.40           C  
ANISOU 3801  CG BLEU A 474     1704   2342   1805     61   -171     71       C  
ATOM   3802  CD1ALEU A 474      43.494  23.607  30.587  0.51 19.35           C  
ANISOU 3802  CD1ALEU A 474     1090   4060   2204    232    175  -1066       C  
ATOM   3803  CD1BLEU A 474      45.532  25.008  29.148  0.49 17.19           C  
ANISOU 3803  CD1BLEU A 474     1987   2648   1897    142     14    120       C  
ATOM   3804  CD2ALEU A 474      45.425  24.228  29.123  0.51 17.43           C  
ANISOU 3804  CD2ALEU A 474     1423   3112   2087   -220    -14   -529       C  
ATOM   3805  CD2BLEU A 474      43.390  24.654  30.391  0.49 18.11           C  
ANISOU 3805  CD2BLEU A 474     1527   3088   2268    367   -187   -191       C  
ATOM   3806  N   VAL A 475      47.860  25.650  33.713  1.00 12.59           N  
ANISOU 3806  N   VAL A 475     1207   1906   1671    -89    226    376       N  
ATOM   3807  CA  VAL A 475      48.291  26.827  34.463  1.00 12.53           C  
ANISOU 3807  CA  VAL A 475     1203   1733   1824     33    283    388       C  
ATOM   3808  C   VAL A 475      49.814  26.913  34.603  1.00 12.79           C  
ANISOU 3808  C   VAL A 475     1354   1937   1568   -151    273     97       C  
ATOM   3809  O   VAL A 475      50.306  27.791  35.304  1.00 14.73           O  
ANISOU 3809  O   VAL A 475     1440   2017   2138   -312    449    -45       O  
ATOM   3810  CB  VAL A 475      47.573  26.996  35.836  1.00 13.39           C  
ANISOU 3810  CB  VAL A 475     1325   1885   1878    364    284    288       C  
ATOM   3811  CG1 VAL A 475      46.070  27.141  35.613  1.00 14.51           C  
ANISOU 3811  CG1 VAL A 475     1228   1925   2360    152    410    228       C  
ATOM   3812  CG2 VAL A 475      47.859  25.855  36.796  1.00 13.15           C  
ANISOU 3812  CG2 VAL A 475     1405   1930   1662    -29    367    258       C  
ATOM   3813  N   THR A 476      50.551  26.019  33.899  1.00 13.28           N  
ANISOU 3813  N   THR A 476     1096   2116   1834    -99    231     37       N  
ATOM   3814  CA  THR A 476      52.039  26.004  34.005  1.00 14.31           C  
ANISOU 3814  CA  THR A 476     1110   2421   1907    -78     86    166       C  
ATOM   3815  C   THR A 476      52.675  25.982  32.619  1.00 13.99           C  
ANISOU 3815  C   THR A 476     1111   2213   1993    -51    279    345       C  
ATOM   3816  O   THR A 476      53.841  25.620  32.508  1.00 16.32           O  
ANISOU 3816  O   THR A 476     1168   2669   2366    120    351    465       O  
ATOM   3817  CB ATHR A 476      52.569  24.921  34.966  0.70 13.47           C  
ANISOU 3817  CB ATHR A 476     1138   2088   1894   -215    326    144       C  
ATOM   3818  CB BTHR A 476      52.477  24.774  34.810  0.30 15.76           C  
ANISOU 3818  CB BTHR A 476     1593   2572   1822   -173   -216    296       C  
ATOM   3819  OG1ATHR A 476      52.078  23.688  34.460  0.70 14.95           O  
ANISOU 3819  OG1ATHR A 476     1072   2163   2445    -83    193   -197       O  
ATOM   3820  OG1BTHR A 476      53.877  24.498  34.687  0.30 30.97           O  
ANISOU 3820  OG1BTHR A 476     2175   4809   4785   1492   -175    580       O  
ATOM   3821  CG2ATHR A 476      52.096  25.109  36.407  0.70 14.67           C  
ANISOU 3821  CG2ATHR A 476     1383   2354   1837   -184    190    196       C  
ATOM   3822  CG2BTHR A 476      51.784  23.549  34.235  0.30 25.70           C  
ANISOU 3822  CG2BTHR A 476     5428   2569   1769   -793  -1480    427       C  
ATOM   3823  N   LEU A 477      51.963  26.400  31.588  1.00 14.55           N  
ANISOU 3823  N   LEU A 477     1223   2347   1960    -13    416    409       N  
ATOM   3824  CA  LEU A 477      52.551  26.496  30.239  1.00 14.53           C  
ANISOU 3824  CA  LEU A 477     1324   2391   1805    -23    428    214       C  
ATOM   3825  C   LEU A 477      53.569  27.631  30.163  1.00 15.52           C  
ANISOU 3825  C   LEU A 477     1311   2611   1973   -151    543    259       C  
ATOM   3826  O   LEU A 477      53.330  28.698  30.742  1.00 17.34           O  
ANISOU 3826  O   LEU A 477     1687   2389   2511   -138    506    211       O  
ATOM   3827  CB  LEU A 477      51.459  26.788  29.188  1.00 15.10           C  
ANISOU 3827  CB  LEU A 477     1330   2308   2100    -48    280    385       C  
ATOM   3828  CG  LEU A 477      50.418  25.708  29.007  1.00 15.47           C  
ANISOU 3828  CG  LEU A 477     1607   2404   1868    -91    201    318       C  
ATOM   3829  CD1 LEU A 477      49.205  26.174  28.223  1.00 18.10           C  
ANISOU 3829  CD1 LEU A 477     1483   3092   2304   -240    -29    500       C  
ATOM   3830  CD2 LEU A 477      51.005  24.462  28.329  1.00 25.34           C  
ANISOU 3830  CD2 LEU A 477     2893   2474   4261    279    -10   -468       C  
ATOM   3831  N   ARG A 478      54.667  27.417  29.444  1.00 18.79           N  
ANISOU 3831  N   ARG A 478     1393   3279   2468    -54    689    138       N  
ATOM   3832  CA  ARG A 478      55.655  28.435  29.216  1.00 22.23           C  
ANISOU 3832  CA  ARG A 478     1339   4082   3025   -296    568   1130       C  
ATOM   3833  C   ARG A 478      56.111  28.437  27.738  1.00 25.65           C  
ANISOU 3833  C   ARG A 478     1275   5458   3012   -483    614   1014       C  
ATOM   3834  O   ARG A 478      56.799  29.435  27.395  1.00 36.63           O  
ANISOU 3834  O   ARG A 478     2305   7618   3994  -1795    169   2666       O  
ATOM   3835  CB  ARG A 478      56.870  28.227  30.117  1.00 24.75           C  
ANISOU 3835  CB  ARG A 478     1400   4986   3016   -569    527   1207       C  
ATOM   3836  CG  ARG A 478      56.506  28.364  31.599  1.00 21.75           C  
ANISOU 3836  CG  ARG A 478     1371   3869   3026   -682    348    705       C  
ATOM   3837  CD  ARG A 478      57.725  28.289  32.454  1.00 22.63           C  
ANISOU 3837  CD  ARG A 478     1491   3779   3329   -606    128    425       C  
ATOM   3838  NE  ARG A 478      58.518  29.534  32.406  1.00 23.33           N  
ANISOU 3838  NE  ARG A 478     1512   3832   3520   -690   -102   1124       N  
ATOM   3839  CZ  ARG A 478      59.836  29.627  32.608  1.00 24.09           C  
ANISOU 3839  CZ  ARG A 478     1698   4383   3072   -912   -332   1336       C  
ATOM   3840  NH1 ARG A 478      60.553  28.559  32.874  1.00 24.25           N  
ANISOU 3840  NH1 ARG A 478     1857   4965   2393     47     17    369       N  
ATOM   3841  NH2 ARG A 478      60.383  30.823  32.529  1.00 31.06           N  
ANISOU 3841  NH2 ARG A 478     2040   5099   4664  -1639   -267   1805       N  
ATOM   3842  OXT ARG A 478      55.786  27.402  27.072  1.00 32.30           O  
ANISOU 3842  OXT ARG A 478     3618   5056   3598   1286   -294    332       O  
TER    3843      ARG A 478                                                      
HETATM 3844  S   SO4 A 580      34.274  16.494   6.722  1.00 29.00           S  
ANISOU 3844  S   SO4 A 580     2864   5814   2342    -42    361    850       S  
HETATM 3845  O1  SO4 A 580      33.184  16.457   7.618  1.00 31.02           O  
ANISOU 3845  O1  SO4 A 580     2476   5058   4251    813    896   1622       O  
HETATM 3846  O2  SO4 A 580      35.517  16.285   7.462  1.00 25.71           O  
ANISOU 3846  O2  SO4 A 580     2378   5044   2346    -41    468    659       O  
HETATM 3847  O3  SO4 A 580      34.222  17.403   5.638  1.00 44.47           O  
ANISOU 3847  O3  SO4 A 580     3348   9261   4289    566    343   3396       O  
HETATM 3848  O4  SO4 A 580      34.286  15.034   6.269  1.00 38.77           O  
ANISOU 3848  O4  SO4 A 580     5436   6920   2375  -1176    818  -1082       O  
HETATM 3849  S   SO4 A 582      33.770  18.391   0.834  1.00 21.23           S  
ANISOU 3849  S   SO4 A 582     2819   2448   2801    463    248    604       S  
HETATM 3850  O1  SO4 A 582      35.143  19.015   0.746  1.00 23.38           O  
ANISOU 3850  O1  SO4 A 582     2937   2866   3079    164    391    715       O  
HETATM 3851  O2  SO4 A 582      33.362  17.876  -0.493  1.00 29.05           O  
ANISOU 3851  O2  SO4 A 582     4366   3881   2791   -229   -541    950       O  
HETATM 3852  O3  SO4 A 582      32.888  19.431   1.272  1.00 31.34           O  
ANISOU 3852  O3  SO4 A 582     3329   2996   5584   1080    693    485       O  
HETATM 3853  O4  SO4 A 582      33.818  17.267   1.819  1.00 22.18           O  
ANISOU 3853  O4  SO4 A 582     3769   2267   2393    -11    297    369       O  
HETATM 3854  PA  FAD A 479      14.787  18.211  20.847  1.00 12.21           P  
ANISOU 3854  PA  FAD A 479     1136   1490   2012    164    427    132       P  
HETATM 3855  O1A FAD A 479      15.082  17.419  19.639  1.00 14.54           O  
ANISOU 3855  O1A FAD A 479     1603   1764   2158    297    216   -115       O  
HETATM 3856  O2A FAD A 479      15.310  17.734  22.144  1.00 14.62           O  
ANISOU 3856  O2A FAD A 479     1873   1573   2110    268    515    639       O  
HETATM 3857  O5B FAD A 479      13.258  18.365  21.217  1.00 13.55           O  
ANISOU 3857  O5B FAD A 479     1280   1914   1956    -26    287    124       O  
HETATM 3858  C5B FAD A 479      12.292  18.625  20.191  1.00 13.49           C  
ANISOU 3858  C5B FAD A 479     1455   1575   2096   -261   -142    192       C  
HETATM 3859  C4B FAD A 479      11.011  17.952  20.666  1.00 12.20           C  
ANISOU 3859  C4B FAD A 479     1091   1613   1931    156    178    -83       C  
HETATM 3860  O4B FAD A 479       9.968  18.431  19.740  1.00 11.71           O  
ANISOU 3860  O4B FAD A 479     1226   1638   1585    113    217    -37       O  
HETATM 3861  C3B FAD A 479      11.019  16.429  20.553  1.00 12.60           C  
ANISOU 3861  C3B FAD A 479     1130   1605   2052      0    196    171       C  
HETATM 3862  O3B FAD A 479      10.719  15.818  21.791  1.00 13.77           O  
ANISOU 3862  O3B FAD A 479     1207   1925   2102    -32    257    252       O  
HETATM 3863  C2B FAD A 479       9.981  16.115  19.408  1.00 12.47           C  
ANISOU 3863  C2B FAD A 479     1138   1550   2049     40    245   -134       C  
HETATM 3864  O2B FAD A 479       9.284  14.899  19.595  1.00 14.67           O  
ANISOU 3864  O2B FAD A 479     1348   1692   2534   -187    431   -290       O  
HETATM 3865  C1B FAD A 479       9.069  17.290  19.537  1.00 12.68           C  
ANISOU 3865  C1B FAD A 479     1106   1777   1936    109    148     98       C  
HETATM 3866  N9A FAD A 479       8.316  17.651  18.314  1.00 11.57           N  
ANISOU 3866  N9A FAD A 479     1151   1794   1450    134    354    -90       N  
HETATM 3867  C8A FAD A 479       8.879  17.892  17.080  1.00 12.90           C  
ANISOU 3867  C8A FAD A 479     1201   2127   1572    -23    204   -198       C  
HETATM 3868  N7A FAD A 479       7.988  18.431  16.235  1.00 13.01           N  
ANISOU 3868  N7A FAD A 479     1228   2084   1630     87    352    -23       N  
HETATM 3869  C5A FAD A 479       6.813  18.539  16.976  1.00 11.94           C  
ANISOU 3869  C5A FAD A 479     1132   1845   1559    -12    236   -169       C  
HETATM 3870  C6A FAD A 479       5.518  19.037  16.621  1.00 12.29           C  
ANISOU 3870  C6A FAD A 479     1141   1951   1577      3    190    -73       C  
HETATM 3871  N6A FAD A 479       5.217  19.635  15.511  1.00 13.74           N  
ANISOU 3871  N6A FAD A 479     1334   2370   1515    120    211      6       N  
HETATM 3872  N1A FAD A 479       4.580  18.971  17.624  1.00 12.73           N  
ANISOU 3872  N1A FAD A 479     1120   2096   1620     30    224     56       N  
HETATM 3873  C2A FAD A 479       4.898  18.439  18.854  1.00 12.35           C  
ANISOU 3873  C2A FAD A 479     1294   1696   1702    235    125     88       C  
HETATM 3874  N3A FAD A 479       6.074  17.974  19.235  1.00 12.08           N  
ANISOU 3874  N3A FAD A 479     1113   1890   1587    184    245    -94       N  
HETATM 3875  C4A FAD A 479       6.975  18.007  18.257  1.00 11.21           C  
ANISOU 3875  C4A FAD A 479     1129   1662   1469    -55    171   -183       C  
HETATM 3876  N1  FAD A 479      24.366  17.878  23.175  1.00 10.42           N  
ANISOU 3876  N1  FAD A 479     1057   1517   1383     -6    181   -170       N  
HETATM 3877  C2  FAD A 479      25.105  18.171  24.241  1.00  9.82           C  
ANISOU 3877  C2  FAD A 479      951   1370   1411    -14    175   -145       C  
HETATM 3878  O2  FAD A 479      25.055  19.236  24.861  1.00 10.19           O  
ANISOU 3878  O2  FAD A 479     1043   1434   1395     56    114   -160       O  
HETATM 3879  N3  FAD A 479      25.958  17.158  24.790  1.00 10.62           N  
ANISOU 3879  N3  FAD A 479     1144   1424   1466    128    183   -188       N  
HETATM 3880  C4  FAD A 479      26.084  15.944  24.186  1.00 12.28           C  
ANISOU 3880  C4  FAD A 479     1417   1595   1654    329   -120   -367       C  
HETATM 3881  O4  FAD A 479      26.870  15.093  24.735  1.00 16.71           O  
ANISOU 3881  O4  FAD A 479     2160   1862   2326    855   -738   -531       O  
HETATM 3882  C4X FAD A 479      25.284  15.644  23.092  1.00 11.51           C  
ANISOU 3882  C4X FAD A 479     1383   1607   1383    244     11   -199       C  
HETATM 3883  N5  FAD A 479      25.408  14.432  22.452  1.00 13.67           N  
ANISOU 3883  N5  FAD A 479     1528   1671   1994    259   -159   -562       N  
HETATM 3884  C5X FAD A 479      24.476  14.111  21.494  1.00 10.91           C  
ANISOU 3884  C5X FAD A 479     1083   1535   1527    -59    377   -218       C  
HETATM 3885  C6  FAD A 479      24.440  12.841  20.942  1.00 11.53           C  
ANISOU 3885  C6  FAD A 479     1141   1569   1672    -11    221   -308       C  
HETATM 3886  C7  FAD A 479      23.524  12.470  19.909  1.00 11.48           C  
ANISOU 3886  C7  FAD A 479     1234   1546   1584    -44    387   -238       C  
HETATM 3887  C7M FAD A 479      23.538  11.049  19.352  1.00 13.38           C  
ANISOU 3887  C7M FAD A 479     1627   1600   1858    -65    311   -492       C  
HETATM 3888  C8  FAD A 479      22.575  13.404  19.494  1.00 10.69           C  
ANISOU 3888  C8  FAD A 479     1086   1661   1314    -14    393   -195       C  
HETATM 3889  C8M FAD A 479      21.551  13.038  18.473  1.00 12.99           C  
ANISOU 3889  C8M FAD A 479     1443   1818   1676   -119    122   -354       C  
HETATM 3890  C9  FAD A 479      22.577  14.676  20.100  1.00 11.17           C  
ANISOU 3890  C9  FAD A 479     1305   1671   1267    -87    302   -204       C  
HETATM 3891  C9A FAD A 479      23.504  15.051  21.023  1.00 10.19           C  
ANISOU 3891  C9A FAD A 479     1106   1580   1185    -22    407   -255       C  
HETATM 3892  N10 FAD A 479      23.574  16.378  21.591  1.00 10.42           N  
ANISOU 3892  N10 FAD A 479     1105   1577   1278     76    169   -109       N  
HETATM 3893  C10 FAD A 479      24.451  16.651  22.598  1.00 10.16           C  
ANISOU 3893  C10 FAD A 479     1071   1578   1213     98    196   -234       C  
HETATM 3894  C1' FAD A 479      22.731  17.466  21.092  1.00 10.98           C  
ANISOU 3894  C1' FAD A 479     1248   1607   1318    266    264    -11       C  
HETATM 3895  C2' FAD A 479      21.479  17.681  21.965  1.00 11.53           C  
ANISOU 3895  C2' FAD A 479     1217   1508   1655    205    288     65       C  
HETATM 3896  O2' FAD A 479      20.836  16.431  22.195  1.00 12.49           O  
ANISOU 3896  O2' FAD A 479     1295   1610   1842    235    491     88       O  
HETATM 3897  C3' FAD A 479      20.478  18.583  21.186  1.00 10.34           C  
ANISOU 3897  C3' FAD A 479     1080   1440   1408    136    353    -20       C  
HETATM 3898  O3' FAD A 479      21.252  19.796  20.871  1.00 12.29           O  
ANISOU 3898  O3' FAD A 479     1047   1627   1995    103    366    144       O  
HETATM 3899  C4' FAD A 479      19.297  19.031  22.015  1.00 10.97           C  
ANISOU 3899  C4' FAD A 479     1091   1509   1566    206    355    151       C  
HETATM 3900  O4' FAD A 479      18.551  17.822  22.420  1.00 13.96           O  
ANISOU 3900  O4' FAD A 479     1634   1741   1929     17    664    285       O  
HETATM 3901  C5' FAD A 479      18.355  19.813  21.176  1.00 11.44           C  
ANISOU 3901  C5' FAD A 479     1056   1874   1416    377    445    195       C  
HETATM 3902  O5' FAD A 479      17.204  20.225  22.012  1.00 10.82           O  
ANISOU 3902  O5' FAD A 479     1013   1752   1346    262    320    247       O  
HETATM 3903  P   FAD A 479      15.954  20.885  21.315  1.00  9.92           P  
ANISOU 3903  P   FAD A 479     1023   1529   1217     99    276     54       P  
HETATM 3904  O1P FAD A 479      15.067  21.325  22.411  1.00 12.14           O  
ANISOU 3904  O1P FAD A 479     1213   2196   1205    340    417   -147       O  
HETATM 3905  O2P FAD A 479      16.360  21.824  20.234  1.00 10.34           O  
ANISOU 3905  O2P FAD A 479     1017   1583   1329     88    185    179       O  
HETATM 3906  O3P FAD A 479      15.270  19.698  20.507  1.00 10.70           O  
ANISOU 3906  O3P FAD A 479     1303   1558   1204    106    242    209       O  
HETATM 3907  N1  GSH A 481      20.031  20.936  35.443  1.00 18.26           N  
ANISOU 3907  N1  GSH A 481     2714   2599   1624    257    307    262       N  
HETATM 3908  CA1 GSH A 481      20.553  21.590  34.227  1.00 15.44           C  
ANISOU 3908  CA1 GSH A 481     1943   2256   1668    386    260    129       C  
HETATM 3909  C1  GSH A 481      20.159  23.092  34.290  1.00 15.37           C  
ANISOU 3909  C1  GSH A 481     1866   2257   1717    525    128    -52       C  
HETATM 3910  O11 GSH A 481      19.398  23.457  35.223  1.00 19.64           O  
ANISOU 3910  O11 GSH A 481     2710   2842   1908   1067    295     41       O  
HETATM 3911  O12 GSH A 481      20.562  23.866  33.418  1.00 15.59           O  
ANISOU 3911  O12 GSH A 481     1525   2191   2208    370     37     49       O  
HETATM 3912  CB1 GSH A 481      20.021  20.967  33.006  1.00 14.80           C  
ANISOU 3912  CB1 GSH A 481     1782   2124   1716    315    351     55       C  
HETATM 3913  CG1 GSH A 481      20.390  19.478  32.824  1.00 16.50           C  
ANISOU 3913  CG1 GSH A 481     1999   2271   1999    569    195    -99       C  
HETATM 3914  CD1 GSH A 481      19.986  19.098  31.458  1.00 13.69           C  
ANISOU 3914  CD1 GSH A 481     1278   2146   1777    316    457     70       C  
HETATM 3915  OE1 GSH A 481      20.542  19.481  30.441  1.00 14.57           O  
ANISOU 3915  OE1 GSH A 481     1354   2108   2072    113    416    225       O  
HETATM 3916  N2  GSH A 481      18.861  18.285  31.390  1.00 15.54           N  
ANISOU 3916  N2  GSH A 481     1756   1983   2165    -35    512    156       N  
HETATM 3917  CA2 GSH A 481      18.208  17.997  30.090  1.00 15.99           C  
ANISOU 3917  CA2 GSH A 481     1851   1837   2390    -91    417    -73       C  
HETATM 3918  C2  GSH A 481      17.037  18.970  29.845  1.00 16.78           C  
ANISOU 3918  C2  GSH A 481     2254   2013   2108    281    201   -247       C  
HETATM 3919  O2  GSH A 481      16.523  18.877  28.708  1.00 26.93           O  
ANISOU 3919  O2  GSH A 481     4754   3195   2283   1737   -589   -712       O  
HETATM 3920  CB2AGSH A 481      17.774  16.553  30.032  0.41 19.06           C  
ANISOU 3920  CB2AGSH A 481     2088   1783   3369   -114    120     -3       C  
HETATM 3921  CB2BGSH A 481      17.633  16.610  29.881  0.59 15.64           C  
ANISOU 3921  CB2BGSH A 481     1085   1805   3054    -24    582    -50       C  
HETATM 3922  SG2AGSH A 481      18.916  15.299  30.868  0.41 16.59           S  
ANISOU 3922  SG2AGSH A 481     2453   1933   1918    107    625      0       S  
HETATM 3923  SG2BGSH A 481      18.875  15.412  29.154  0.59 17.99           S  
ANISOU 3923  SG2BGSH A 481     1200   1796   3838    164   1006    303       S  
HETATM 3924  N3  GSH A 481      16.647  19.777  30.736  1.00 14.35           N  
ANISOU 3924  N3  GSH A 481     1653   1732   2067   -221    532   -151       N  
HETATM 3925  CA3 GSH A 481      15.492  20.723  30.555  1.00 17.35           C  
ANISOU 3925  CA3 GSH A 481     1523   2530   2539    129    314   -644       C  
HETATM 3926  C3  GSH A 481      15.220  21.381  31.991  1.00 16.11           C  
ANISOU 3926  C3  GSH A 481     1597   2438   2087    234    533    -26       C  
HETATM 3927  O31 GSH A 481      14.149  22.032  32.073  1.00 16.13           O  
ANISOU 3927  O31 GSH A 481     1661   2286   2183    381    392    156       O  
HETATM 3928  O32 GSH A 481      16.130  21.198  32.814  1.00 20.46           O  
ANISOU 3928  O32 GSH A 481     2118   3297   2361   1023     97   -500       O  
HETATM 3929  N1  GSH A 482      24.735  16.626  35.502  0.51 12.82           N  
ANISOU 3929  N1  GSH A 482     1063   2004   1805    -48    396    -34       N  
HETATM 3930  CA1 GSH A 482      25.034  15.472  36.420  0.51 15.06           C  
ANISOU 3930  CA1 GSH A 482     1093   1947   2681    113    174    157       C  
HETATM 3931  C1  GSH A 482      25.647  14.244  35.751  0.51 14.87           C  
ANISOU 3931  C1  GSH A 482     1987   1661   2003   -405    390    233       C  
HETATM 3932  O11 GSH A 482      25.797  14.311  34.490  0.51 19.75           O  
ANISOU 3932  O11 GSH A 482     3176   2278   2048   -652    622    209       O  
HETATM 3933  O12 GSH A 482      25.829  13.284  36.554  0.51 24.27           O  
ANISOU 3933  O12 GSH A 482     5936   1564   1723    627  -1170   -301       O  
HETATM 3934  CB1 GSH A 482      23.737  15.006  37.173  0.51 16.54           C  
ANISOU 3934  CB1 GSH A 482     1792   2152   2342   -354    351    262       C  
HETATM 3935  CG1 GSH A 482      22.861  14.174  36.235  0.51 18.61           C  
ANISOU 3935  CG1 GSH A 482     1832   2144   3096   -651    -23    565       C  
HETATM 3936  CD1 GSH A 482      21.750  14.986  35.638  0.51 19.54           C  
ANISOU 3936  CD1 GSH A 482     1677   2524   3222   -456     91    552       C  
HETATM 3937  OE1 GSH A 482      21.865  16.067  35.016  0.51 27.86           O  
ANISOU 3937  OE1 GSH A 482     4042   1808   4735     -7   -431    505       O  
HETATM 3938  N2  GSH A 482      20.613  14.279  35.567  0.51 22.89           N  
ANISOU 3938  N2  GSH A 482     1737   3066   3896   -601    -21  -1059       N  
HETATM 3939  C1  GOL A 602      50.199  22.165  14.734  0.00 25.54           C  
ANISOU 3939  C1  GOL A 602     1144   4624   3935  -1086     50   1127       C  
HETATM 3940  O1  GOL A 602      51.267  21.654  15.542  0.00 25.57           O  
ANISOU 3940  O1  GOL A 602     1156   4623   3936  -1085     43   1127       O  
HETATM 3941  C2  GOL A 602      48.849  21.829  15.370  0.00 24.64           C  
ANISOU 3941  C2  GOL A 602     1152   4306   3905  -1087     71    958       C  
HETATM 3942  O2  GOL A 602      47.828  21.782  14.366  0.00 23.24           O  
ANISOU 3942  O2  GOL A 602     1036   3827   3968   -673     91    768       O  
HETATM 3943  C3  GOL A 602      48.672  23.072  16.245  0.00 25.33           C  
ANISOU 3943  C3  GOL A 602     1341   4410   3872  -1059    -80    882       C  
HETATM 3944  O3  GOL A 602      49.023  24.249  15.506  0.00 25.19           O  
ANISOU 3944  O3  GOL A 602     1371   4313   3889  -1031   -107    832       O  
HETATM 3945  C1  GOL A 603       7.695  40.134  20.906  1.00 54.47           C  
ANISOU 3945  C1  GOL A 603     8974   5612   6111   5475  -3801  -3279       C  
HETATM 3946  O1  GOL A 603       9.237  40.096  21.001  1.00 51.33           O  
ANISOU 3946  O1  GOL A 603     9064   3777   6664   3630  -4703  -1456       O  
HETATM 3947  C2  GOL A 603       7.252  39.466  19.628  1.00 39.64           C  
ANISOU 3947  C2  GOL A 603     5946   4753   4362   3603  -1440  -1990       C  
HETATM 3948  O2  GOL A 603       7.797  39.362  18.435  1.00 44.77           O  
ANISOU 3948  O2  GOL A 603     7450   4602   4959   1448    -19   -923       O  
HETATM 3949  C3  GOL A 603       5.889  39.642  19.958  1.00 46.31           C  
ANISOU 3949  C3  GOL A 603     6148   5341   6107   3044   -570   -693       C  
HETATM 3950  O3  GOL A 603       5.068  40.697  20.327  1.00 36.94           O  
ANISOU 3950  O3  GOL A 603     4732   4051   5254   1526   1942   1033       O  
HETATM 3951  C1  GOL A 604      32.286  28.036  20.425  0.00 15.95           C  
ANISOU 3951  C1  GOL A 604     1603   2255   2201    -76    378    220       C  
HETATM 3952  O1  GOL A 604      33.478  28.047  21.219  0.00 16.31           O  
ANISOU 3952  O1  GOL A 604     1664   2225   2308   -125    297    250       O  
HETATM 3953  C2  GOL A 604      31.716  29.452  20.310  0.00 15.98           C  
ANISOU 3953  C2  GOL A 604     1641   2260   2172    -59    406    215       C  
HETATM 3954  O2  GOL A 604      30.473  29.543  21.017  0.00 16.04           O  
ANISOU 3954  O2  GOL A 604     1661   2267   2166    -60    422    205       O  
HETATM 3955  C3  GOL A 604      31.478  29.587  18.805  0.00 15.93           C  
ANISOU 3955  C3  GOL A 604     1626   2256   2169    -56    417    217       C  
HETATM 3956  O3  GOL A 604      31.041  28.336  18.260  0.00 15.92           O  
ANISOU 3956  O3  GOL A 604     1627   2257   2166    -54    417    214       O  
HETATM 3957  C1  GOL A 605      17.646  -1.978  35.463  1.00 71.90           C  
ANISOU 3957  C1  GOL A 605    15268   5328   6725  -1398  -5151   1987       C  
HETATM 3958  O1  GOL A 605      16.259  -1.609  35.264  1.00 73.37           O  
ANISOU 3958  O1  GOL A 605    16639   6713   4527   3033  -2055   1962       O  
HETATM 3959  C2  GOL A 605      17.688  -2.653  36.922  1.00 39.90           C  
ANISOU 3959  C2  GOL A 605     5076   4098   5986  -1859   -919   1151       C  
HETATM 3960  O2  GOL A 605      19.187  -2.352  37.246  1.00 33.01           O  
ANISOU 3960  O2  GOL A 605     4369   3786   4388  -1523    561    670       O  
HETATM 3961  C3  GOL A 605      17.464  -4.018  36.331  1.00 42.08           C  
ANISOU 3961  C3  GOL A 605     5532   4943   5513  -2778    740    359       C  
HETATM 3962  O3  GOL A 605      18.627  -4.404  35.466  1.00 44.37           O  
ANISOU 3962  O3  GOL A 605     5039   5245   6575  -3052   1012    475       O  
HETATM 3963  O   HOH A1001      14.723  23.156  18.500  1.00 10.31           O  
ANISOU 3963  O   HOH A1001     1175   1555   1188    130    262    -41       O  
HETATM 3964  O   HOH A1002      12.409  21.436  22.886  1.00 10.55           O  
ANISOU 3964  O   HOH A1002     1248   1504   1256    174    310    107       O  
HETATM 3965  O   HOH A1003      20.394  23.148  20.629  1.00 12.06           O  
ANISOU 3965  O   HOH A1003     1110   1940   1532     57    451    120       O  
HETATM 3966  O   HOH A1004      47.880  23.016  45.386  1.00 12.42           O  
ANISOU 3966  O   HOH A1004     1140   1858   1719     95    244     11       O  
HETATM 3967  O   HOH A1005      19.431  27.736  20.641  1.00 13.34           O  
ANISOU 3967  O   HOH A1005     1166   1864   2038     69    398   -219       O  
HETATM 3968  O   HOH A1006      19.304  34.623  22.223  1.00 11.94           O  
ANISOU 3968  O   HOH A1006     1179   1823   1533      7    321     12       O  
HETATM 3969  O   HOH A1007      27.253  20.303  26.157  1.00 11.01           O  
ANISOU 3969  O   HOH A1007      973   1794   1417    151    240    -22       O  
HETATM 3970  O   HOH A1008      20.213  27.073  17.014  1.00 13.12           O  
ANISOU 3970  O   HOH A1008     1329   1974   1683    216    402    193       O  
HETATM 3971  O   HOH A1009      44.981  14.169  30.752  1.00 16.58           O  
ANISOU 3971  O   HOH A1009     1368   2753   2178    -93    495   -595       O  
HETATM 3972  O   HOH A1010      18.755   1.825  35.220  1.00 15.44           O  
ANISOU 3972  O   HOH A1010     1564   2398   1903    420    435    -30       O  
HETATM 3973  O   HOH A1011      17.130  34.278  24.066  1.00 12.24           O  
ANISOU 3973  O   HOH A1011     1501   1720   1428     93    348    110       O  
HETATM 3974  O   HOH A1012      49.426   5.659  38.140  1.00 13.12           O  
ANISOU 3974  O   HOH A1012     1415   2057   1512    323    208     81       O  
HETATM 3975  O   HOH A1013      45.008  10.775  28.069  1.00 13.57           O  
ANISOU 3975  O   HOH A1013     1148   2201   1808    337    270    -50       O  
HETATM 3976  O   HOH A1014      18.992  32.131  12.017  1.00 13.69           O  
ANISOU 3976  O   HOH A1014     1544   2173   1483    313    438    352       O  
HETATM 3977  O   HOH A1015      33.901  20.303  32.226  1.00 13.34           O  
ANISOU 3977  O   HOH A1015     1268   1674   2128   -148    415    -39       O  
HETATM 3978  O   HOH A1016      20.940  25.645  19.637  1.00 12.43           O  
ANISOU 3978  O   HOH A1016     1190   1849   1682    187    343    129       O  
HETATM 3979  O   HOH A1017      46.788  10.516  35.053  1.00 17.83           O  
ANISOU 3979  O   HOH A1017     2796   2223   1755    802    725    227       O  
HETATM 3980  O   HOH A1018      32.549  12.948  36.825  1.00 15.66           O  
ANISOU 3980  O   HOH A1018     1388   2130   2433   -142    316    235       O  
HETATM 3981  O   HOH A1019      47.542  13.134  34.825  1.00 29.87           O  
ANISOU 3981  O   HOH A1019     7332   1887   2132    795   -683   -189       O  
HETATM 3982  O   HOH A1020      11.786  33.008  10.767  1.00 13.23           O  
ANISOU 3982  O   HOH A1020     1526   2192   1310    297    363    105       O  
HETATM 3983  O   HOH A1021       5.349  37.639  33.722  1.00 13.05           O  
ANISOU 3983  O   HOH A1021     1364   1741   1852    147    665   -118       O  
HETATM 3984  O   HOH A1022      14.164  26.671  33.043  1.00 11.23           O  
ANISOU 3984  O   HOH A1022     1215   1598   1455      7    225    -65       O  
HETATM 3985  O   HOH A1023      37.318  14.065   6.876  1.00 14.49           O  
ANISOU 3985  O   HOH A1023     2033   2025   1448     -4    234   -176       O  
HETATM 3986  O   HOH A1024      17.300  17.634  17.819  1.00 13.11           O  
ANISOU 3986  O   HOH A1024     1561   1806   1614    194    270    -23       O  
HETATM 3987  O   HOH A1025      23.317  11.078   9.872  1.00 14.46           O  
ANISOU 3987  O   HOH A1025     1329   2222   1943     88    264   -236       O  
HETATM 3988  O   HOH A1026      18.518  29.470  11.365  1.00 14.73           O  
ANISOU 3988  O   HOH A1026     1725   1913   1958     52    509    280       O  
HETATM 3989  O   HOH A1027      23.813  12.171  12.569  1.00 13.93           O  
ANISOU 3989  O   HOH A1027     1726   2101   1464    114    401   -213       O  
HETATM 3990  O   HOH A1028      15.755  36.779  24.002  1.00 13.03           O  
ANISOU 3990  O   HOH A1028     1449   1777   1723    186    305     61       O  
HETATM 3991  O   HOH A1029       3.797  39.846  33.423  1.00 13.15           O  
ANISOU 3991  O   HOH A1029     1358   1847   1792    -39    640     75       O  
HETATM 3992  O   HOH A1030      31.793  13.527  32.661  1.00 17.88           O  
ANISOU 3992  O   HOH A1030     1231   2947   2614   -304    239   -857       O  
HETATM 3993  O   HOH A1031      18.713  20.404  13.433  1.00 15.00           O  
ANISOU 3993  O   HOH A1031     1921   2135   1644    213    659      2       O  
HETATM 3994  O   HOH A1032       8.619  26.501  36.777  1.00 18.96           O  
ANISOU 3994  O   HOH A1032     2448   2427   2331   -150    775    649       O  
HETATM 3995  O   HOH A1033      21.080   0.214  21.779  1.00 14.59           O  
ANISOU 3995  O   HOH A1033     1648   2023   1873    135    455    -95       O  
HETATM 3996  O   HOH A1034      29.441  19.221  24.795  1.00 15.11           O  
ANISOU 3996  O   HOH A1034     1085   2122   2533    280    395   -127       O  
HETATM 3997  O   HOH A1035      33.537  28.444  21.993  1.00 15.37           O  
ANISOU 3997  O   HOH A1035     1287   2140   2414     24    217    267       O  
HETATM 3998  O   HOH A1036      20.608  20.951  11.401  1.00 16.88           O  
ANISOU 3998  O   HOH A1036     2387   2321   1706    799    591    -33       O  
HETATM 3999  O   HOH A1037      39.714   2.361 -10.019  1.00 16.08           O  
ANISOU 3999  O   HOH A1037     2208   2349   1551    -93    705   -397       O  
HETATM 4000  O   HOH A1038      35.816  22.286  35.516  1.00 15.34           O  
ANISOU 4000  O   HOH A1038     1778   2213   1839    426    479    242       O  
HETATM 4001  O   HOH A1039      19.202  18.335  15.225  1.00 15.32           O  
ANISOU 4001  O   HOH A1039     2090   1910   1823    438    372   -157       O  
HETATM 4002  O   HOH A1040      22.246  12.220  14.855  1.00 15.44           O  
ANISOU 4002  O   HOH A1040     2158   1787   1920    127    858    -20       O  
HETATM 4003  O   HOH A1041      35.847  25.912  20.827  1.00 15.86           O  
ANISOU 4003  O   HOH A1041     1553   2147   2328   -111    244     50       O  
HETATM 4004  O   HOH A1042      13.187  27.749  35.467  1.00 14.70           O  
ANISOU 4004  O   HOH A1042     1726   2122   1736   -205    214     64       O  
HETATM 4005  O   HOH A1043      37.617  -1.838  15.762  1.00 16.25           O  
ANISOU 4005  O   HOH A1043     1805   2173   2196     16    112     16       O  
HETATM 4006  O   HOH A1044      47.535  -1.671  29.715  1.00 15.84           O  
ANISOU 4006  O   HOH A1044     1879   2080   2058    429    502     11       O  
HETATM 4007  O   HOH A1045      34.352  10.902  33.187  1.00 20.91           O  
ANISOU 4007  O   HOH A1045     2159   3391   2397   -161    555   -194       O  
HETATM 4008  O   HOH A1046      33.330   7.276  22.174  1.00 18.52           O  
ANISOU 4008  O   HOH A1046     2691   2395   1952    533   -332   -351       O  
HETATM 4009  O   HOH A1047      18.877  36.607  11.169  1.00 16.62           O  
ANISOU 4009  O   HOH A1047     2457   2093   1765     47    700    441       O  
HETATM 4010  O   HOH A1048      50.424  28.287  38.019  1.00 21.22           O  
ANISOU 4010  O   HOH A1048     1341   4038   2682   -294    273   -550       O  
HETATM 4011  O   HOH A1049      46.041  30.435  43.605  1.00 15.11           O  
ANISOU 4011  O   HOH A1049     1646   2017   2078   -240    350   -260       O  
HETATM 4012  O   HOH A1050      44.772  12.008  23.398  1.00 18.60           O  
ANISOU 4012  O   HOH A1050     1464   3505   2097    252    114    585       O  
HETATM 4013  O   HOH A1051      30.910  29.519  20.856  1.00 16.19           O  
ANISOU 4013  O   HOH A1051     1722   2278   2152    -89    422    209       O  
HETATM 4014  O   HOH A1052      40.151  10.077  19.621  1.00 17.76           O  
ANISOU 4014  O   HOH A1052     1896   2725   2126   -252    346   -573       O  
HETATM 4015  O   HOH A1053      37.484   3.182  21.144  1.00 18.71           O  
ANISOU 4015  O   HOH A1053     1655   2812   2643    -36    163     15       O  
HETATM 4016  O   HOH A1054      13.161   3.714  27.699  1.00 14.93           O  
ANISOU 4016  O   HOH A1054     1758   2082   1830     56     83    -80       O  
HETATM 4017  O   HOH A1055      34.848  11.764  35.855  1.00 21.75           O  
ANISOU 4017  O   HOH A1055     2587   3329   2350    887    152   -397       O  
HETATM 4018  O   HOH A1056      43.020   6.617  -3.802  1.00 15.94           O  
ANISOU 4018  O   HOH A1056     1961   2327   1768    -49    585   -502       O  
HETATM 4019  O   HOH A1057      24.309  17.959  17.950  1.00 16.94           O  
ANISOU 4019  O   HOH A1057     1805   2323   2310    127    761   -375       O  
HETATM 4020  O   HOH A1058      52.917  21.166  40.683  1.00 14.30           O  
ANISOU 4020  O   HOH A1058     1379   2076   1977   -204    540     55       O  
HETATM 4021  O   HOH A1059      35.745   7.951  19.948  1.00 16.85           O  
ANISOU 4021  O   HOH A1059     2692   2102   1610   -464   -103    -52       O  
HETATM 4022  O   HOH A1060      53.478  10.174  33.035  1.00 46.20           O  
ANISOU 4022  O   HOH A1060     5087   6130   6337   1099  -2680  -1162       O  
HETATM 4023  O   HOH A1061      47.999  13.094  37.673  1.00 24.98           O  
ANISOU 4023  O   HOH A1061     3159   3566   2767   1100    982   -384       O  
HETATM 4024  O   HOH A1062      19.835   9.843  17.829  1.00 23.34           O  
ANISOU 4024  O   HOH A1062     3005   4202   1661  -1557   1088  -1065       O  
HETATM 4025  O   HOH A1063       7.853  19.825  13.786  1.00 16.76           O  
ANISOU 4025  O   HOH A1063     1550   2852   1965    365    424     -2       O  
HETATM 4026  O   HOH A1064      38.659   0.288  -8.585  1.00 16.91           O  
ANISOU 4026  O   HOH A1064     2310   2323   1794   -125    749   -457       O  
HETATM 4027  O   HOH A1065      19.554  29.762  17.846  1.00 16.74           O  
ANISOU 4027  O   HOH A1065     1955   2258   2147    129    493   -265       O  
HETATM 4028  O   HOH A1066      21.609  17.306  17.772  1.00 17.61           O  
ANISOU 4028  O   HOH A1066     1818   2530   2343    526    218   -225       O  
HETATM 4029  O   HOH A1067      28.873  10.032  33.578  1.00 17.86           O  
ANISOU 4029  O   HOH A1067     3255   1824   1706   -485    781    -80       O  
HETATM 4030  O   HOH A1068      55.315   0.063  34.765  1.00 19.99           O  
ANISOU 4030  O   HOH A1068     1596   2993   3009     82    451    -81       O  
HETATM 4031  O   HOH A1069       9.052  37.480  17.238  1.00 16.20           O  
ANISOU 4031  O   HOH A1069     1857   2131   2168    179    384    269       O  
HETATM 4032  O   HOH A1070      36.010   9.285  -2.174  1.00 18.41           O  
ANISOU 4032  O   HOH A1070     2191   2669   2134     83    417    160       O  
HETATM 4033  O   HOH A1071      31.738   9.886  33.514  1.00 22.64           O  
ANISOU 4033  O   HOH A1071     1967   3575   3059   -430    698   -564       O  
HETATM 4034  O   HOH A1072      18.073   4.308  12.293  1.00 18.04           O  
ANISOU 4034  O   HOH A1072     2091   2601   2162   -106    880     10       O  
HETATM 4035  O   HOH A1073      22.230  36.103  20.526  1.00 18.22           O  
ANISOU 4035  O   HOH A1073     1587   2966   2369    436    496    970       O  
HETATM 4036  O   HOH A1074      36.756  11.626  -0.474  1.00 19.73           O  
ANISOU 4036  O   HOH A1074     3707   1853   1936    351   -387    -91       O  
HETATM 4037  O   HOH A1076      13.010  16.588  16.454  1.00 20.11           O  
ANISOU 4037  O   HOH A1076     2307   2309   3024   -178    827   -557       O  
HETATM 4038  O   HOH A1077      53.883   6.063  30.488  1.00 23.82           O  
ANISOU 4038  O   HOH A1077     2715   2966   3372   1074   -655   -702       O  
HETATM 4039  O   HOH A1078      46.667  -5.104  32.002  1.00 19.29           O  
ANISOU 4039  O   HOH A1078     2282   2682   2365    803    281    -42       O  
HETATM 4040  O   HOH A1079      49.732  28.432  31.542  1.00 17.10           O  
ANISOU 4040  O   HOH A1079     1715   2585   2200    160    470    654       O  
HETATM 4041  O   HOH A1080      29.340  15.309  23.104  1.00 18.66           O  
ANISOU 4041  O   HOH A1080     1681   2503   2904     -7    423   -417       O  
HETATM 4042  O   HOH A1081      25.866  13.853  12.487  1.00 20.10           O  
ANISOU 4042  O   HOH A1081     1889   3730   2020   -320    288     74       O  
HETATM 4043  O   HOH A1082      38.170  11.260  31.255  1.00 20.47           O  
ANISOU 4043  O   HOH A1082     1806   2894   3078   -551    197    100       O  
HETATM 4044  O   HOH A1083      37.284  33.626  22.718  1.00 19.12           O  
ANISOU 4044  O   HOH A1083     1784   2165   3317    307   -340   -162       O  
HETATM 4045  O   HOH A1084      10.694  12.916  22.000  1.00 16.06           O  
ANISOU 4045  O   HOH A1084     1806   1996   2301     19    377   -152       O  
HETATM 4046  O   HOH A1085      29.775   8.367   2.144  1.00 19.21           O  
ANISOU 4046  O   HOH A1085     2770   2405   2123    -14   1066   -574       O  
HETATM 4047  O   HOH A1086      33.113   4.492  33.221  1.00 20.72           O  
ANISOU 4047  O   HOH A1086     2225   3666   1982   -220    559   -146       O  
HETATM 4048  O   HOH A1087      20.084  29.069   8.991  1.00 19.81           O  
ANISOU 4048  O   HOH A1087     2521   2763   2244   -275    761    126       O  
HETATM 4049  O   HOH A1088      24.769  34.810  27.378  1.00 20.06           O  
ANISOU 4049  O   HOH A1088     2427   3156   2041     59    312     42       O  
HETATM 4050  O   HOH A1089      20.917  31.679  16.441  1.00 18.87           O  
ANISOU 4050  O   HOH A1089     2137   2688   2346    352    266    309       O  
HETATM 4051  O   HOH A1090      18.098   3.726  25.534  1.00 17.81           O  
ANISOU 4051  O   HOH A1090     1583   2348   2837   -123    156    471       O  
HETATM 4052  O   HOH A1091      16.201  26.519  36.482  1.00 19.52           O  
ANISOU 4052  O   HOH A1091     2640   2431   2347     90    164   -101       O  
HETATM 4053  O   HOH A1092       1.911  34.652  18.777  1.00 18.21           O  
ANISOU 4053  O   HOH A1092     1930   2978   2014    449    149     79       O  
HETATM 4054  O   HOH A1093      11.707  42.304  23.907  1.00 23.09           O  
ANISOU 4054  O   HOH A1093     4320   2070   2383   1437    151    -24       O  
HETATM 4055  O   HOH A1094      35.582  10.277  -4.677  1.00 19.84           O  
ANISOU 4055  O   HOH A1094     2654   2784   2100    286    487    -70       O  
HETATM 4056  O   HOH A1096       6.462  23.892   7.529  1.00 20.60           O  
ANISOU 4056  O   HOH A1096     2438   3222   2167    327    363   -554       O  
HETATM 4057  O   HOH A1097      31.347  17.872  15.000  1.00 20.46           O  
ANISOU 4057  O   HOH A1097     2877   2182   2716    374    881    129       O  
HETATM 4058  O   HOH A1098      44.034  10.254  34.932  1.00 29.72           O  
ANISOU 4058  O   HOH A1098     3042   3907   4345   1551   -230   -550       O  
HETATM 4059  O   HOH A1099      17.711  12.139  16.757  1.00 27.79           O  
ANISOU 4059  O   HOH A1099     5262   3046   2249   -977    934     30       O  
HETATM 4060  O   HOH A1100      -4.370  32.988  29.410  1.00 30.42           O  
ANISOU 4060  O   HOH A1100     1999   5560   3999   1540   -269  -2113       O  
HETATM 4061  O   HOH A1101      12.700   6.779  24.717  1.00 18.11           O  
ANISOU 4061  O   HOH A1101     2473   2034   2375   -104    163    -92       O  
HETATM 4062  O   HOH A1102      37.985   2.097  -1.979  1.00 20.55           O  
ANISOU 4062  O   HOH A1102     3053   2390   2365   -232   1024   -138       O  
HETATM 4063  O   HOH A1103      28.431  32.360  25.974  1.00 19.82           O  
ANISOU 4063  O   HOH A1103     1971   2811   2750   -143   -204    952       O  
HETATM 4064  O   HOH A1104       1.997  27.653  33.323  1.00 21.51           O  
ANISOU 4064  O   HOH A1104     3623   2375   2175    445    -57   -431       O  
HETATM 4065  O   HOH A1105      26.562  22.806  16.153  1.00 24.26           O  
ANISOU 4065  O   HOH A1105     2308   3604   3307    -55   1735   -330       O  
HETATM 4066  O   HOH A1106      13.635  41.856  20.176  1.00 20.57           O  
ANISOU 4066  O   HOH A1106     2853   2248   2716   -233    580   -365       O  
HETATM 4067  O   HOH A1107       3.454  12.879  23.745  1.00 19.00           O  
ANISOU 4067  O   HOH A1107     1643   2285   3291     -2    533    291       O  
HETATM 4068  O   HOH A1108      38.617  23.205  18.672  1.00 24.14           O  
ANISOU 4068  O   HOH A1108     3320   3703   2148  -1740   1364   -944       O  
HETATM 4069  O   HOH A1109      26.274  35.927  20.073  1.00 21.10           O  
ANISOU 4069  O   HOH A1109     2328   2619   3070    105    234    896       O  
HETATM 4070  O   HOH A1110      52.225  22.444  31.045  1.00 21.04           O  
ANISOU 4070  O   HOH A1110     1484   3497   3015    327    689    663       O  
HETATM 4071  O   HOH A1111      28.332  15.128  14.333  1.00 21.03           O  
ANISOU 4071  O   HOH A1111     1599   3766   2627    -68    -12   1132       O  
HETATM 4072  O   HOH A1112      -4.427  30.237  30.051  1.00 27.72           O  
ANISOU 4072  O   HOH A1112     1494   6408   2629    324    272   -283       O  
HETATM 4073  O   HOH A1113      33.478  12.887   6.295  1.00 20.58           O  
ANISOU 4073  O   HOH A1113     2341   3677   1803    730    220   -687       O  
HETATM 4074  O   HOH A1114      31.993  35.795  25.523  1.00 26.26           O  
ANISOU 4074  O   HOH A1114     3479   2738   3762    176    455   -778       O  
HETATM 4075  O   HOH A1115      38.612   0.655  20.273  1.00 20.76           O  
ANISOU 4075  O   HOH A1115     1912   3220   2755    280    135    122       O  
HETATM 4076  O   HOH A1116      35.690   8.551  32.551  1.00 22.87           O  
ANISOU 4076  O   HOH A1116     1638   2980   4071   -333     98   -433       O  
HETATM 4077  O   HOH A1117      54.107  -0.104  32.078  1.00 25.07           O  
ANISOU 4077  O   HOH A1117     2168   4454   2903    425    534     56       O  
HETATM 4078  O   HOH A1118       6.909  27.648  38.534  1.00 27.21           O  
ANISOU 4078  O   HOH A1118     3380   3998   2960     59   1423   -528       O  
HETATM 4079  O   HOH A1119      29.227  13.111  12.858  1.00 20.95           O  
ANISOU 4079  O   HOH A1119     3027   2353   2582   -829   -981    545       O  
HETATM 4080  O   HOH A1120      11.360  42.605  26.629  1.00 22.22           O  
ANISOU 4080  O   HOH A1120     3506   2055   2880    149   1136     60       O  
HETATM 4081  O   HOH A1121      38.873  12.539  -2.333  1.00 27.47           O  
ANISOU 4081  O   HOH A1121     5479   3199   1760   1555    405   -166       O  
HETATM 4082  O   HOH A1122      11.473  31.182   3.940  1.00 24.75           O  
ANISOU 4082  O   HOH A1122     3454   4323   1628   1311    124    165       O  
HETATM 4083  O   HOH A1123      32.438  -7.723  23.199  1.00 21.72           O  
ANISOU 4083  O   HOH A1123     3001   2137   3115    396    964    268       O  
HETATM 4084  O   HOH A1124      20.105  33.891  17.870  1.00 19.20           O  
ANISOU 4084  O   HOH A1124     2287   2152   2858    249   -225    290       O  
HETATM 4085  O   HOH A1126      18.542  -0.572  15.054  1.00 22.90           O  
ANISOU 4085  O   HOH A1126     2858   2517   3325   -585    419   -958       O  
HETATM 4086  O   HOH A1127      22.840  -1.306   9.417  1.00 22.21           O  
ANISOU 4086  O   HOH A1127     1862   3407   3172   -355    713  -1170       O  
HETATM 4087  O   HOH A1128      38.623  35.606  26.746  1.00 26.10           O  
ANISOU 4087  O   HOH A1128     3904   2735   3276  -1191   1041    199       O  
HETATM 4088  O   HOH A1129      -2.159  31.036  12.780  1.00 23.62           O  
ANISOU 4088  O   HOH A1129     2413   4296   2266    450    242    299       O  
HETATM 4089  O   HOH A1130      14.064   4.500  25.266  1.00 19.52           O  
ANISOU 4089  O   HOH A1130     2302   2919   2197   -269    816   -141       O  
HETATM 4090  O   HOH A1131      43.154   3.246  10.264  1.00 24.70           O  
ANISOU 4090  O   HOH A1131     1958   3747   3679    749    552   -419       O  
HETATM 4091  O   HOH A1132      10.590  25.874  39.148  1.00 58.77           O  
ANISOU 4091  O   HOH A1132     6296   7369   8667   1146   -603   -526       O  
HETATM 4092  O   HOH A1133      33.263  25.055  21.651  1.00 21.19           O  
ANISOU 4092  O   HOH A1133     2581   2888   2583   -504    528   -110       O  
HETATM 4093  O   HOH A1134      23.442  -5.536  16.223  1.00 22.57           O  
ANISOU 4093  O   HOH A1134     2466   3195   2916   -116    258   -626       O  
HETATM 4094  O   HOH A1135       6.494  11.729  27.580  1.00 21.65           O  
ANISOU 4094  O   HOH A1135     2638   3045   2542   -790    451   -121       O  
HETATM 4095  O   HOH A1136      43.278   2.434  24.068  1.00 23.02           O  
ANISOU 4095  O   HOH A1136     2420   3773   2552    518    321    377       O  
HETATM 4096  O   HOH A1137      11.167   5.657  27.345  1.00 21.08           O  
ANISOU 4096  O   HOH A1137     2300   2278   3431    450   -366   -554       O  
HETATM 4097  O   HOH A1138      27.388  -2.762  -2.427  1.00 26.23           O  
ANISOU 4097  O   HOH A1138     4167   3351   2447  -1327    578   -231       O  
HETATM 4098  O   HOH A1139      48.986  38.023  30.414  1.00 21.64           O  
ANISOU 4098  O   HOH A1139     2124   2483   3614   -673    211    695       O  
HETATM 4099  O   HOH A1140      19.710  -2.221  13.140  1.00 21.93           O  
ANISOU 4099  O   HOH A1140     2696   2475   3162   -666    788   -547       O  
HETATM 4100  O   HOH A1141      -2.333  16.709  15.525  1.00 23.06           O  
ANISOU 4100  O   HOH A1141     1569   3267   3925    -95     -3  -1522       O  
HETATM 4101  O   HOH A1143      26.415  -8.961  14.440  1.00 24.49           O  
ANISOU 4101  O   HOH A1143     3446   2847   3011  -1047    891   -544       O  
HETATM 4102  O   HOH A1144      42.622   6.175   2.226  1.00 23.74           O  
ANISOU 4102  O   HOH A1144     3345   3574   2100    864    811    -73       O  
HETATM 4103  O   HOH A1145      27.149  10.313  19.695  1.00 33.01           O  
ANISOU 4103  O   HOH A1145     2242   6917   3384   -567    830  -1126       O  
HETATM 4104  O   HOH A1146       8.138  35.381  39.626  1.00 23.56           O  
ANISOU 4104  O   HOH A1146     3551   2958   2443    539    195   -324       O  
HETATM 4105  O   HOH A1147      -5.372  18.755  21.517  1.00 22.87           O  
ANISOU 4105  O   HOH A1147     1986   3182   3522   -121    409    274       O  
HETATM 4106  O   HOH A1148       5.507  11.746  35.940  1.00 18.89           O  
ANISOU 4106  O   HOH A1148     1499   3346   2331   -381    158    828       O  
HETATM 4107  O   HOH A1149      22.104  23.780  31.108  1.00 14.84           O  
ANISOU 4107  O   HOH A1149     1411   1884   2342    138    175    151       O  
HETATM 4108  O   HOH A1150      37.739   8.724  30.388  1.00 26.51           O  
ANISOU 4108  O   HOH A1150     2145   3303   4623   -210    -33   -391       O  
HETATM 4109  O   HOH A1151      16.425   5.256  24.021  1.00 18.78           O  
ANISOU 4109  O   HOH A1151     1674   2219   3242   -212    198    235       O  
HETATM 4110  O   HOH A1152       2.326  29.873  35.856  1.00 34.22           O  
ANISOU 4110  O   HOH A1152     4575   4771   3657   2109   1914    746       O  
HETATM 4111  O   HOH A1153      15.337  32.569   4.093  1.00 23.88           O  
ANISOU 4111  O   HOH A1153     3171   3427   2475   -359    780    -44       O  
HETATM 4112  O   HOH A1154      54.845  12.430  29.606  1.00 25.18           O  
ANISOU 4112  O   HOH A1154     1553   3625   4390   -176   -574   1089       O  
HETATM 4113  O   HOH A1155      15.864   1.356  23.262  1.00 21.57           O  
ANISOU 4113  O   HOH A1155     2061   3360   2775   -410    630    289       O  
HETATM 4114  O   HOH A1156      -1.285  18.685  31.599  1.00 24.95           O  
ANISOU 4114  O   HOH A1156     3237   3438   2805  -1224   1325    183       O  
HETATM 4115  O   HOH A1157      45.388  11.476   8.927  1.00 22.76           O  
ANISOU 4115  O   HOH A1157     1850   3806   2991    402     60     34       O  
HETATM 4116  O   HOH A1159      36.062  27.606  17.595  1.00 24.52           O  
ANISOU 4116  O   HOH A1159     2556   3997   2764  -1153    461     78       O  
HETATM 4117  O   HOH A1160      25.588  -8.781  21.690  1.00 23.98           O  
ANISOU 4117  O   HOH A1160     2984   2592   3538    -49     41    931       O  
HETATM 4118  O   HOH A1161      53.269  29.193  33.419  1.00 20.23           O  
ANISOU 4118  O   HOH A1161     2604   2610   2471     11    521    200       O  
HETATM 4119  O   HOH A1162      36.916   9.677  -7.080  1.00 26.11           O  
ANISOU 4119  O   HOH A1162     3443   4003   2474    538    232   -717       O  
HETATM 4120  O   HOH A1163      27.158  20.404  18.417  1.00 22.31           O  
ANISOU 4120  O   HOH A1163     2169   2948   3360    496   1069     54       O  
HETATM 4121  O   HOH A1164      38.596  -2.367  12.383  1.00 26.48           O  
ANISOU 4121  O   HOH A1164     3079   3228   3753   1300   1371    725       O  
HETATM 4122  O   HOH A1165      23.341  21.150  11.346  1.00 27.28           O  
ANISOU 4122  O   HOH A1165     2962   4156   3247    784    705    149       O  
HETATM 4123  O   HOH A1166      22.658  -2.671  38.339  1.00 22.55           O  
ANISOU 4123  O   HOH A1166     2911   2973   2684   -612    217    176       O  
HETATM 4124  O   HOH A1167      17.545  12.879   5.662  1.00 34.08           O  
ANISOU 4124  O   HOH A1167     3999   5378   3574   2365  -1321  -1197       O  
HETATM 4125  O   HOH A1168      52.812   7.939  32.307  1.00 26.07           O  
ANISOU 4125  O   HOH A1168     3205   3169   3531   1031   -218   -187       O  
HETATM 4126  O   HOH A1169      37.093  -3.594  18.651  1.00 25.19           O  
ANISOU 4126  O   HOH A1169     3486   3208   2877   1254    230   -602       O  
HETATM 4127  O   HOH A1170       1.379  39.536  31.940  1.00 22.40           O  
ANISOU 4127  O   HOH A1170     2521   2793   3198   -301    453    211       O  
HETATM 4128  O   HOH A1172       3.932  21.802   6.592  1.00 26.84           O  
ANISOU 4128  O   HOH A1172     3751   4239   2208    864   -353  -1036       O  
HETATM 4129  O   HOH A1173      42.575  10.098  -6.038  1.00 26.43           O  
ANISOU 4129  O   HOH A1173     2988   4309   2747   -715   1247   -519       O  
HETATM 4130  O   HOH A1174      14.556  42.980  22.628  1.00 21.19           O  
ANISOU 4130  O   HOH A1174     2982   2363   2708    225     74    442       O  
HETATM 4131  O   HOH A1175      13.061  11.626  21.100  1.00 23.82           O  
ANISOU 4131  O   HOH A1175     2939   3302   2810    398   -375   -305       O  
HETATM 4132  O   HOH A1176      44.229  36.648  38.542  1.00 24.44           O  
ANISOU 4132  O   HOH A1176     3097   3008   3182   -432     65     16       O  
HETATM 4133  O   HOH A1177      41.175   5.273  26.384  1.00 30.18           O  
ANISOU 4133  O   HOH A1177     2295   5034   4140    390     -4   -181       O  
HETATM 4134  O   HOH A1178      22.447  -2.145  12.466  1.00 24.11           O  
ANISOU 4134  O   HOH A1178     2540   3152   3470   -361   1101   -393       O  
HETATM 4135  O   HOH A1179       4.270  27.629  38.139  1.00 24.55           O  
ANISOU 4135  O   HOH A1179     2611   3028   3688   -291   1241   -620       O  
HETATM 4136  O   HOH A1180      42.310  18.916  10.178  1.00 22.77           O  
ANISOU 4136  O   HOH A1180     2768   3100   2783     17   1103    728       O  
HETATM 4137  O   HOH A1181      -1.404  14.518  16.823  1.00 27.64           O  
ANISOU 4137  O   HOH A1181     2402   4827   3274   -941   -560   -279       O  
HETATM 4138  O   HOH A1183      52.381  31.230  18.394  1.00 25.27           O  
ANISOU 4138  O   HOH A1183     2740   4025   2837   -709   1132    569       O  
HETATM 4139  O   HOH A1184       8.999   4.086  29.247  1.00 28.88           O  
ANISOU 4139  O   HOH A1184     3345   3939   3690   -976   -438   1215       O  
HETATM 4140  O   HOH A1185      44.999  19.090  11.319  1.00 22.93           O  
ANISOU 4140  O   HOH A1185     2546   3557   2610   -457    269    131       O  
HETATM 4141  O   HOH A1186      15.656   5.300  18.852  1.00 22.83           O  
ANISOU 4141  O   HOH A1186     3190   2788   2697   -186   1443   -599       O  
HETATM 4142  O   HOH A1188      33.946  31.926  20.677  1.00 25.30           O  
ANISOU 4142  O   HOH A1188     2239   3941   3433    490   1079   1341       O  
HETATM 4143  O   HOH A1189      15.212   4.662  21.508  1.00 24.04           O  
ANISOU 4143  O   HOH A1189     2887   3850   2397   -959    724   -514       O  
HETATM 4144  O   HOH A1190      11.935  25.979  37.297  1.00 37.22           O  
ANISOU 4144  O   HOH A1190     5211   5530   3401  -1879    413   1089       O  
HETATM 4145  O  AHOH A1191      13.375  20.639  34.500  0.45 28.00           O  
ANISOU 4145  O  AHOH A1191     2807   3522   4311   1202   1717    369       O  
HETATM 4146  O   HOH A1192      19.160  25.750  36.683  1.00 22.86           O  
ANISOU 4146  O   HOH A1192     3362   3288   2036   1089   -106   -344       O  
HETATM 4147  O   HOH A1193      10.227  15.553  39.085  1.00 25.30           O  
ANISOU 4147  O   HOH A1193     3511   3492   2611      4    607    176       O  
HETATM 4148  O   HOH A1194      25.397  18.105  15.343  1.00 28.18           O  
ANISOU 4148  O   HOH A1194     3375   5148   2186  -1075    754   -819       O  
HETATM 4149  O   HOH A1195      42.451   4.990   4.649  1.00 29.58           O  
ANISOU 4149  O   HOH A1195     2764   4169   4307   1040   1520    573       O  
HETATM 4150  O   HOH A1196      54.130  33.081  29.403  1.00 39.35           O  
ANISOU 4150  O   HOH A1196     3860   5643   5449  -2971    676   -777       O  
HETATM 4151  O   HOH A1197      43.878   5.580  21.644  1.00 27.18           O  
ANISOU 4151  O   HOH A1197     3055   3717   3557   -183   -616    749       O  
HETATM 4152  O   HOH A1198      41.067  -1.705  -2.282  1.00 34.48           O  
ANISOU 4152  O   HOH A1198     5415   4150   3537    683   2172    408       O  
HETATM 4153  O   HOH A1199      53.293  12.460  32.933  1.00 43.68           O  
ANISOU 4153  O   HOH A1199     6115   4734   5748    176  -2854  -1223       O  
HETATM 4154  O   HOH A1200      43.312  33.993  38.193  1.00 21.59           O  
ANISOU 4154  O   HOH A1200     2503   2455   3247   -227    380   -359       O  
HETATM 4155  O   HOH A1201      14.429  -1.784  30.658  1.00 26.18           O  
ANISOU 4155  O   HOH A1201     1943   3515   4488   -548    536    -51       O  
HETATM 4156  O   HOH A1202      -2.408  19.724  13.542  1.00 23.27           O  
ANISOU 4156  O   HOH A1202     2432   3869   2540    -48     75  -1008       O  
HETATM 4157  O   HOH A1204      20.265  11.450  36.869  1.00 24.20           O  
ANISOU 4157  O   HOH A1204     2738   3116   3340  -1033    102   -567       O  
HETATM 4158  O   HOH A1205      48.972  14.601  18.742  1.00 27.10           O  
ANISOU 4158  O   HOH A1205     2062   4397   3840    -78   1084    -31       O  
HETATM 4159  O   HOH A1206       4.612  39.149  29.229  1.00 24.65           O  
ANISOU 4159  O   HOH A1206     2386   2583   4398    378    851   -242       O  
HETATM 4160  O   HOH A1207       6.812  11.534  30.270  1.00 20.46           O  
ANISOU 4160  O   HOH A1207     1846   3428   2501     65    179   -529       O  
HETATM 4161  O   HOH A1208       6.929  40.750  26.344  1.00 26.86           O  
ANISOU 4161  O   HOH A1208     3680   3800   2725   1837    602    676       O  
HETATM 4162  O   HOH A1209      13.813  41.043  14.428  1.00 25.00           O  
ANISOU 4162  O   HOH A1209     4098   2719   2681    643   -147    502       O  
HETATM 4163  O   HOH A1210       4.834  39.992  11.924  1.00 29.26           O  
ANISOU 4163  O   HOH A1210     5192   3425   2500   1818    191   1086       O  
HETATM 4164  O   HOH A1211       2.284  36.155   9.491  1.00 23.71           O  
ANISOU 4164  O   HOH A1211     2555   3442   3012    762    146    -38       O  
HETATM 4165  O   HOH A1213      48.545   2.025  23.476  1.00 26.92           O  
ANISOU 4165  O   HOH A1213     5321   2976   1929    107    662   -365       O  
HETATM 4166  O   HOH A1214      34.226  -6.637   6.589  1.00 27.90           O  
ANISOU 4166  O   HOH A1214     3285   3771   3546    810     59  -1828       O  
HETATM 4167  O   HOH A1216      36.987  13.111  34.285  1.00 29.40           O  
ANISOU 4167  O   HOH A1216     2425   5229   3514   -132    775    871       O  
HETATM 4168  O   HOH A1217      37.315  35.789  24.445  1.00 24.64           O  
ANISOU 4168  O   HOH A1217     3051   2573   3737    -68   -314     11       O  
HETATM 4169  O   HOH A1218      23.631  -4.326  13.626  1.00 24.91           O  
ANISOU 4169  O   HOH A1218     2707   3736   3020   -750    367   -751       O  
HETATM 4170  O   HOH A1219      26.787  26.112  14.777  1.00 32.96           O  
ANISOU 4170  O   HOH A1219     3296   6282   2944    264   2066    540       O  
HETATM 4171  O   HOH A1220      24.228  18.853  10.249  1.00 31.20           O  
ANISOU 4171  O   HOH A1220     2446   3264   6143    -50   1185   -327       O  
HETATM 4172  O   HOH A1221      20.341  30.918  30.737  1.00 24.69           O  
ANISOU 4172  O   HOH A1221     2348   3663   3372   -339    811  -1182       O  
HETATM 4173  O   HOH A1222      30.324  22.411  19.312  1.00 35.33           O  
ANISOU 4173  O   HOH A1222     4763   4971   3691    930    -23     -5       O  
HETATM 4174  O   HOH A1223      25.790  16.367  13.463  1.00 30.86           O  
ANISOU 4174  O   HOH A1223     2772   3835   5117    551    200  -1478       O  
HETATM 4175  O   HOH A1224      20.274  39.597  15.055  1.00 28.98           O  
ANISOU 4175  O   HOH A1224     2926   4541   3544  -1526   -402   2054       O  
HETATM 4176  O   HOH A1225      -0.920  26.341  32.099  1.00 26.44           O  
ANISOU 4176  O   HOH A1225     2441   4720   2884   -136   1220   -864       O  
HETATM 4177  O   HOH A1226      20.038  -5.052  -1.572  1.00 28.73           O  
ANISOU 4177  O   HOH A1226     3979   2964   3975   -554  -1439   -683       O  
HETATM 4178  O   HOH A1227      13.153   6.724  22.026  1.00 25.31           O  
ANISOU 4178  O   HOH A1227     2984   3520   3113   -542    193   -719       O  
HETATM 4179  O   HOH A1228      43.912  32.011   9.845  1.00 28.88           O  
ANISOU 4179  O   HOH A1228     3456   5161   2358   -737   1019    479       O  
HETATM 4180  O   HOH A1229      19.965  -5.603  32.714  1.00 26.41           O  
ANISOU 4180  O   HOH A1229     3179   3048   3807   -434    685    892       O  
HETATM 4181  O   HOH A1230      24.117  -8.662  10.185  1.00 31.68           O  
ANISOU 4181  O   HOH A1230     4712   4016   3310  -1788    662   -537       O  
HETATM 4182  O   HOH A1231      21.452  38.700  28.569  1.00 28.13           O  
ANISOU 4182  O   HOH A1231     2282   3311   5095    217   -926   -637       O  
HETATM 4183  O   HOH A1232       1.668  12.435  18.844  1.00 28.59           O  
ANISOU 4183  O   HOH A1232     2452   3206   5204    404   -938  -1254       O  
HETATM 4184  O   HOH A1233      -0.693  17.853  12.475  1.00 32.15           O  
ANISOU 4184  O   HOH A1233     3115   4680   4419   1090    103   -781       O  
HETATM 4185  O   HOH A1234      37.428  -1.873   5.687  1.00 34.93           O  
ANISOU 4185  O   HOH A1234     3556   4620   5095   -923    685    847       O  
HETATM 4186  O   HOH A1235      20.902  27.919  35.981  1.00 25.78           O  
ANISOU 4186  O   HOH A1235     2786   3719   3290   1442   -647  -1075       O  
HETATM 4187  O   HOH A1236      54.313  26.245  24.251  1.00 34.71           O  
ANISOU 4187  O   HOH A1236     1580   3516   8092   -263   -135   2142       O  
HETATM 4188  O   HOH A1237      47.532  -3.751  27.912  1.00 33.22           O  
ANISOU 4188  O   HOH A1237     3767   4359   4495   -617   1731  -1745       O  
HETATM 4189  O   HOH A1238      46.085  11.822  11.630  1.00 34.12           O  
ANISOU 4189  O   HOH A1238     2118   5926   4919     -7    314   1380       O  
HETATM 4190  O   HOH A1239      19.133   7.096  38.025  1.00 37.08           O  
ANISOU 4190  O   HOH A1239     8206   2711   3171  -1768  -1539    423       O  
HETATM 4191  O   HOH A1240       1.995  38.019  14.181  1.00 27.59           O  
ANISOU 4191  O   HOH A1240     2847   3981   3654   1493   -266    491       O  
HETATM 4192  O   HOH A1241      43.934   4.545   0.481  1.00 27.40           O  
ANISOU 4192  O   HOH A1241     4033   3700   2678   1130    861   -118       O  
HETATM 4193  O   HOH A1242      45.399   3.660  22.794  1.00 30.12           O  
ANISOU 4193  O   HOH A1242     2686   4844   3913    278    519    171       O  
HETATM 4194  O   HOH A1243      46.413  16.724  45.583  1.00 28.62           O  
ANISOU 4194  O   HOH A1243     1850   5197   3829   -373    410   -470       O  
HETATM 4195  O   HOH A1244      41.213  17.406   1.802  1.00 30.14           O  
ANISOU 4195  O   HOH A1244     3801   3222   4430   -257   1668    700       O  
HETATM 4196  O   HOH A1245      44.364   4.856  -2.167  1.00 29.85           O  
ANISOU 4196  O   HOH A1245     4728   4316   2298   1984    436   -661       O  
HETATM 4197  O   HOH A1246      54.506  22.927  29.699  1.00 30.18           O  
ANISOU 4197  O   HOH A1246     2066   5720   3681    -14   1195    516       O  
HETATM 4198  O   HOH A1247      34.430   1.760  36.026  1.00 35.04           O  
ANISOU 4198  O   HOH A1247     3109   6271   3934   1331    717   -568       O  
HETATM 4199  O   HOH A1248      33.344   7.054  32.966  1.00 29.60           O  
ANISOU 4199  O   HOH A1248     1965   4546   4735  -1142    781  -1101       O  
HETATM 4200  O   HOH A1249       0.434  19.542  33.526  1.00 34.07           O  
ANISOU 4200  O   HOH A1249     4232   5184   3529  -2441   -539   1711       O  
HETATM 4201  O   HOH A1250      -9.389  31.787  23.696  1.00 34.56           O  
ANISOU 4201  O   HOH A1250     2242   6939   3952    981   -434    -63       O  
HETATM 4202  O   HOH A1251      38.400  -3.486  -5.380  1.00 27.22           O  
ANISOU 4202  O   HOH A1251     3145   2920   4279    110   1882   -463       O  
HETATM 4203  O   HOH A1253      48.664  12.810  11.562  1.00 32.67           O  
ANISOU 4203  O   HOH A1253     2001   5181   5230   -211    274  -1620       O  
HETATM 4204  O   HOH A1254      28.987  -9.220  18.181  1.00 31.34           O  
ANISOU 4204  O   HOH A1254     4048   3471   4389   1127   1257    562       O  
HETATM 4205  O   HOH A1255      37.960  34.438  13.084  1.00 26.21           O  
ANISOU 4205  O   HOH A1255     2256   3231   4472      8   -287    981       O  
HETATM 4206  O   HOH A1256      38.430   5.646  20.151  1.00 29.85           O  
ANISOU 4206  O   HOH A1256     6048   2790   2504  -1073   1279   -346       O  
HETATM 4207  O   HOH A1257      30.470  11.291   2.131  1.00 30.88           O  
ANISOU 4207  O   HOH A1257     3348   3947   4438   -598    742  -1081       O  
HETATM 4208  O   HOH A1258       9.411  39.022  15.158  1.00 30.27           O  
ANISOU 4208  O   HOH A1258     2268   4804   4430    608    577   1599       O  
HETATM 4209  O   HOH A1259      41.310   4.272  23.870  1.00 32.62           O  
ANISOU 4209  O   HOH A1259     3431   6068   2894   1971   -157   -366       O  
HETATM 4210  O   HOH A1260      18.554  33.158  31.841  1.00 36.19           O  
ANISOU 4210  O   HOH A1260     3863   4678   5209   -209    440  -1907       O  
HETATM 4211  O   HOH A1261       6.317  15.254  15.606  1.00 29.29           O  
ANISOU 4211  O   HOH A1261     5255   3330   2544   -347    877    -27       O  
HETATM 4212  O   HOH A1262      49.388  37.402  22.246  1.00 30.62           O  
ANISOU 4212  O   HOH A1262     3623   3073   4937   -832   -265   -102       O  
HETATM 4213  O   HOH A1263      -3.310  16.203  25.226  1.00 30.97           O  
ANISOU 4213  O   HOH A1263     2340   4798   4631  -1589    963   -359       O  
HETATM 4214  O   HOH A1264     -10.627  24.034  18.766  1.00 32.33           O  
ANISOU 4214  O   HOH A1264     1472   5367   5445    332    522   -488       O  
HETATM 4215  O   HOH A1266      48.137  16.920  17.600  1.00 25.49           O  
ANISOU 4215  O   HOH A1266     2040   3477   4170    -46    691   -406       O  
HETATM 4216  O   HOH A1267      16.780   8.383  38.150  1.00 28.94           O  
ANISOU 4216  O   HOH A1267     2089   4747   4159   -343    439  -1767       O  
HETATM 4217  O   HOH A1269      10.055  13.099  17.639  1.00 31.37           O  
ANISOU 4217  O   HOH A1269     3669   3773   4479  -1136   1103  -1194       O  
HETATM 4218  O   HOH A1270      22.732  35.083  17.865  1.00 33.20           O  
ANISOU 4218  O   HOH A1270     4812   4601   3202   1621    590   1648       O  
HETATM 4219  O   HOH A1271      20.906  32.629  13.948  1.00 27.58           O  
ANISOU 4219  O   HOH A1271     2274   5827   2377   -918    161    980       O  
HETATM 4220  O   HOH A1272      50.144  32.578  42.607  1.00 37.10           O  
ANISOU 4220  O   HOH A1272     6053   4238   3805   -576  -1898    109       O  
HETATM 4221  O   HOH A1273      12.911  28.574   2.569  1.00 32.41           O  
ANISOU 4221  O   HOH A1273     4251   5123   2939   -748    256   -298       O  
HETATM 4222  O   HOH A1274      17.326  43.785  29.678  1.00 32.13           O  
ANISOU 4222  O   HOH A1274     3531   5004   3672  -1379    326    -45       O  
HETATM 4223  O   HOH A1275      20.495  -2.261  -2.359  1.00 34.30           O  
ANISOU 4223  O   HOH A1275     4226   4661   4144   -704   -814  -1478       O  
HETATM 4224  O   HOH A1276      40.309   7.763 -12.335  1.00 31.60           O  
ANISOU 4224  O   HOH A1276     5191   4039   2775   1268   -440   -719       O  
HETATM 4225  O   HOH A1277      33.425  -8.333  16.496  1.00 26.98           O  
ANISOU 4225  O   HOH A1277     3305   3640   3306    179    244    650       O  
HETATM 4226  O   HOH A1278      47.752   6.523  22.200  1.00 37.83           O  
ANISOU 4226  O   HOH A1278     5879   5453   3044   1905   1407   -341       O  
HETATM 4227  O   HOH A1279      42.245   7.925  35.148  1.00 44.27           O  
ANISOU 4227  O   HOH A1279     3721   7749   5350   2485   -379   -158       O  
HETATM 4228  O   HOH A1280      -2.530  23.285   9.871  1.00 34.40           O  
ANISOU 4228  O   HOH A1280     3898   5314   3861   -522  -1077   -348       O  
HETATM 4229  O   HOH A1281      12.836   9.091  20.511  1.00 26.56           O  
ANISOU 4229  O   HOH A1281     3011   3632   3447   -165    277   -173       O  
HETATM 4230  O   HOH A1282      -3.748  39.993  29.754  1.00 40.81           O  
ANISOU 4230  O   HOH A1282     2031   8582   4895    512   -362   1328       O  
HETATM 4231  O   HOH A1283      50.957   7.653  -6.678  1.00 24.67           O  
ANISOU 4231  O   HOH A1283     2936   3048   3389   -515    318  -1188       O  
HETATM 4232  O   HOH A1284      56.677  31.996  28.691  1.00 42.92           O  
ANISOU 4232  O   HOH A1284     4324   5372   6611  -2627   -433   1583       O  
HETATM 4233  O   HOH A1285       2.580  39.076  20.329  1.00 28.32           O  
ANISOU 4233  O   HOH A1285     3578   2831   4352   1025   1411    973       O  
HETATM 4234  O   HOH A1286      24.059  -1.891  25.103  1.00 31.84           O  
ANISOU 4234  O   HOH A1286     4445   3852   3800   -975   1332   -518       O  
HETATM 4235  O   HOH A1288      30.030  -8.973  23.239  1.00 28.33           O  
ANISOU 4235  O   HOH A1288     3566   3586   3611    276    636   -234       O  
HETATM 4236  O   HOH A1289      17.544   6.582   1.611  1.00 28.69           O  
ANISOU 4236  O   HOH A1289     2775   4764   3364   -501    232   -179       O  
HETATM 4237  O   HOH A1290      27.270  -8.117  23.575  1.00 26.86           O  
ANISOU 4237  O   HOH A1290     3313   4156   2739   1140    337   -843       O  
HETATM 4238  O   HOH A1291      38.596   5.219  27.388  1.00 32.56           O  
ANISOU 4238  O   HOH A1291     1898   6083   4389     35    768   -167       O  
HETATM 4239  O   HOH A1292      14.750  -2.543  27.700  1.00 30.33           O  
ANISOU 4239  O   HOH A1292     4625   3244   3653  -1788   -691    317       O  
HETATM 4240  O   HOH A1293      49.562  15.029  10.855  1.00 53.62           O  
ANISOU 4240  O   HOH A1293     5745   9344   5286   -641   4050   -508       O  
HETATM 4241  O   HOH A1294      39.677  26.818  12.469  1.00 26.56           O  
ANISOU 4241  O   HOH A1294     4505   3340   2245   -354   -203    303       O  
HETATM 4242  O   HOH A1295      21.459  12.219  -0.750  1.00 30.71           O  
ANISOU 4242  O   HOH A1295     5232   3002   3434    262    643     65       O  
HETATM 4243  O   HOH A1296      31.078  14.512   8.579  1.00 31.35           O  
ANISOU 4243  O   HOH A1296     4597   2859   4455   1003  -1441    350       O  
HETATM 4244  O   HOH A1297      53.468  18.842  30.215  1.00 30.65           O  
ANISOU 4244  O   HOH A1297     2717   4958   3970    534    207      2       O  
HETATM 4245  O   HOH A1298      48.388  19.022  13.582  1.00 28.09           O  
ANISOU 4245  O   HOH A1298     2690   4132   3849   -797    645     13       O  
HETATM 4246  O   HOH A1299      -7.074  32.061  17.009  1.00 36.92           O  
ANISOU 4246  O   HOH A1299     3041   5210   5777   1725    425   -792       O  
HETATM 4247  O   HOH A1300      29.406  19.110  19.651  1.00 40.46           O  
ANISOU 4247  O   HOH A1300     3349   7255   4768   1475    -74  -2922       O  
HETATM 4248  O   HOH A1301       5.429   9.451  26.637  1.00 30.42           O  
ANISOU 4248  O   HOH A1301     2940   3651   4967   -672   1297   -586       O  
HETATM 4249  O   HOH A1302      47.482  37.733   9.583  1.00 34.33           O  
ANISOU 4249  O   HOH A1302     4526   5827   2689   -699    551   1139       O  
HETATM 4250  O   HOH A1303      52.168  21.381  35.959  1.00 49.23           O  
ANISOU 4250  O   HOH A1303     4210   6654   7842  -1094    -68   2064       O  
HETATM 4251  O   HOH A1304      18.149  19.820   6.107  1.00 33.70           O  
ANISOU 4251  O   HOH A1304     5306   4079   3419   1205   1737    172       O  
HETATM 4252  O   HOH A1305      38.346   7.566  27.642  1.00 30.97           O  
ANISOU 4252  O   HOH A1305     4056   4300   3412    392   1696    661       O  
HETATM 4253  O   HOH A1306      43.846  -6.997  32.279  1.00 33.82           O  
ANISOU 4253  O   HOH A1306     5071   4849   2928    456   -652    -59       O  
HETATM 4254  O   HOH A1307      38.960   3.047  23.576  1.00 33.50           O  
ANISOU 4254  O   HOH A1307     3754   5203   3770   1647   -674   -394       O  
HETATM 4255  O   HOH A1309      -4.100  24.473  31.495  1.00 45.27           O  
ANISOU 4255  O   HOH A1309     4490   7563   5146   2337    946   -465       O  
HETATM 4256  O   HOH A1310      -4.125  16.501  22.611  1.00 30.94           O  
ANISOU 4256  O   HOH A1310     2021   4177   5558    119    510   -907       O  
HETATM 4257  O   HOH A1311      32.940  37.271  27.593  1.00 41.35           O  
ANISOU 4257  O   HOH A1311     6616   4025   5070  -1134  -1749    537       O  
HETATM 4258  O   HOH A1312      46.391  25.323  14.214  1.00 30.85           O  
ANISOU 4258  O   HOH A1312     3045   3864   4812     89    299   -283       O  
HETATM 4259  O   HOH A1313      38.020  36.258  20.805  1.00 34.25           O  
ANISOU 4259  O   HOH A1313     3702   4653   4660   1118    378   -793       O  
HETATM 4260  O   HOH A1314      55.200  18.874  24.840  1.00 36.00           O  
ANISOU 4260  O   HOH A1314     1795   5430   6452   -473    310    538       O  
HETATM 4261  O   HOH A1315      18.047  37.300  31.531  1.00 28.04           O  
ANISOU 4261  O   HOH A1315     2524   5497   2631   -622     57    130       O  
HETATM 4262  O   HOH A1316       8.365   6.559  32.806  1.00 27.24           O  
ANISOU 4262  O   HOH A1316     1446   3023   5882   -191    404  -1512       O  
HETATM 4263  O   HOH A1317      28.649  -9.697   2.754  1.00 38.72           O  
ANISOU 4263  O   HOH A1317     4982   5439   4291   -213    247  -2944       O  
HETATM 4264  O   HOH A1318      51.391  36.701  29.987  1.00 32.57           O  
ANISOU 4264  O   HOH A1318     2944   4271   5160   -403    121    199       O  
HETATM 4265  O   HOH A1319      30.825  13.023   6.202  1.00 33.70           O  
ANISOU 4265  O   HOH A1319     3755   5311   3736    336   1686    566       O  
HETATM 4266  O   HOH A1320      44.321  34.171   8.391  1.00 34.84           O  
ANISOU 4266  O   HOH A1320     5464   5007   2769   -911   -200   1130       O  
HETATM 4267  O   HOH A1321      27.405 -12.420   2.871  1.00 31.67           O  
ANISOU 4267  O   HOH A1321     4549   4113   3369   -309   -115   -391       O  
HETATM 4268  O   HOH A1322       8.040  28.994  40.844  1.00 46.66           O  
ANISOU 4268  O   HOH A1322     7469   7166   3092   -996   1670   -379       O  
HETATM 4269  O   HOH A1326      -5.078  18.545  14.034  1.00 31.15           O  
ANISOU 4269  O   HOH A1326     1921   5017   4896    223     14  -1111       O  
HETATM 4270  O   HOH A1328      23.638  -9.091  24.484  1.00 32.49           O  
ANISOU 4270  O   HOH A1328     4778   2952   4614    361   1016   -916       O  
HETATM 4271  O   HOH A1329      41.833  17.291  -0.848  1.00 38.07           O  
ANISOU 4271  O   HOH A1329     6057   4024   4383    930   1426    627       O  
HETATM 4272  O   HOH A1330      23.836  -8.221  -2.948  1.00 39.53           O  
ANISOU 4272  O   HOH A1330     7208   3191   4620     83    759   -853       O  
HETATM 4273  O   HOH A1331       6.254  18.817  11.812  1.00 32.44           O  
ANISOU 4273  O   HOH A1331     3925   5372   3030   -934   -277    339       O  
HETATM 4274  O   HOH A1332      19.127  29.824  35.280  1.00 27.71           O  
ANISOU 4274  O   HOH A1332     2295   4632   3603   1300   -571   -473       O  
HETATM 4275  O   HOH A1333      36.969  -4.847  -3.395  1.00 31.51           O  
ANISOU 4275  O   HOH A1333     4671   3179   4123    912   2229   -113       O  
HETATM 4276  O   HOH A1334      53.602  13.223  24.099  1.00 41.50           O  
ANISOU 4276  O   HOH A1334     3910   5588   6271    923   -412  -1276       O  
HETATM 4277  O   HOH A1335      50.430  33.678  15.288  1.00 26.83           O  
ANISOU 4277  O   HOH A1335     2993   3729   3472   -752    763    655       O  
HETATM 4278  O   HOH A1336       4.347  13.211  14.765  1.00 37.85           O  
ANISOU 4278  O   HOH A1336     5725   4624   4034   1389  -1014   -419       O  
HETATM 4279  O   HOH A1337      55.141   6.757  27.702  1.00 42.53           O  
ANISOU 4279  O   HOH A1337     2747   7199   6215   -202   1340   1036       O  
HETATM 4280  O   HOH A1338      41.315   5.738  22.099  1.00 40.58           O  
ANISOU 4280  O   HOH A1338     3368   6551   5499    563    216  -1918       O  
HETATM 4281  O   HOH A1339      11.657   1.583  27.309  1.00 37.55           O  
ANISOU 4281  O   HOH A1339     5838   3148   5282  -1197  -1089   -277       O  
HETATM 4282  O   HOH A1340       4.082  15.752  41.834  1.00 37.84           O  
ANISOU 4282  O   HOH A1340     5867   3917   4595  -1022   3266   -713       O  
HETATM 4283  O   HOH A1342       8.951  14.260  15.130  1.00 33.24           O  
ANISOU 4283  O   HOH A1342     3731   4805   4094  -1263    -83   -263       O  
HETATM 4284  O   HOH A1343       9.500  28.714   5.433  1.00 28.67           O  
ANISOU 4284  O   HOH A1343     2992   4538   3363    611     -9   -858       O  
HETATM 4285  O   HOH A1344      53.032  29.091  37.579  1.00 37.57           O  
ANISOU 4285  O   HOH A1344     2510   4249   7518  -1246    881  -1013       O  
HETATM 4286  O   HOH A1345      24.126  -7.928  15.218  1.00 35.24           O  
ANISOU 4286  O   HOH A1345     3648   3664   6076     61    572  -1809       O  
HETATM 4287  O   HOH A1346      20.815  35.251  14.166  1.00 35.06           O  
ANISOU 4287  O   HOH A1346     2373   4876   6073    194   -140    278       O  
HETATM 4288  O   HOH A1347      56.096  20.616  25.989  1.00 48.06           O  
ANISOU 4288  O   HOH A1347     2991   6636   8635   -393  -1719   1437       O  
HETATM 4289  O   HOH A1348      37.255  -4.227   2.339  1.00 39.26           O  
ANISOU 4289  O   HOH A1348     3361   5832   5725    455    873   1059       O  
HETATM 4290  O   HOH A1349      40.696  40.548  29.086  1.00 38.59           O  
ANISOU 4290  O   HOH A1349     5286   2625   6750   -109    674   1343       O  
HETATM 4291  O   HOH A1350      -3.820  19.095  27.569  1.00 29.84           O  
ANISOU 4291  O   HOH A1350     1496   5048   4795   -208    556   -405       O  
HETATM 4292  O   HOH A1351      46.487  40.266  33.126  1.00 35.86           O  
ANISOU 4292  O   HOH A1351     5366   2551   5706   -479  -1832   -146       O  
HETATM 4293  O   HOH A1352      54.816  28.652  22.896  1.00 33.81           O  
ANISOU 4293  O   HOH A1352     1851   6381   4614   -771    149   1904       O  
HETATM 4294  O   HOH A1353     -11.069  27.836  25.537  1.00 39.76           O  
ANISOU 4294  O   HOH A1353     2797   7208   5103  -1009   1160  -3007       O  
HETATM 4295  O   HOH A1354      12.392  14.152  17.633  1.00 31.19           O  
ANISOU 4295  O   HOH A1354     3251   3638   4962   -493    917    -23       O  
HETATM 4296  O   HOH A1355      24.242  37.882  20.704  1.00 32.40           O  
ANISOU 4296  O   HOH A1355     2859   4157   5294   -758    173   1227       O  
HETATM 4297  O   HOH A1356      48.922  -8.530  37.667  1.00 32.51           O  
ANISOU 4297  O   HOH A1356     4598   2673   5080    965   -938    559       O  
HETATM 4298  O   HOH A1357      15.281   9.277  -3.072  1.00 41.54           O  
ANISOU 4298  O   HOH A1357     5628   4711   5443    888  -3390   -787       O  
HETATM 4299  O   HOH A1358      56.736  32.057  31.949  1.00 54.10           O  
ANISOU 4299  O   HOH A1358     7341   6656   6557  -2015   1447   1550       O  
HETATM 4300  O   HOH A1359      49.940  31.237  16.756  1.00 27.50           O  
ANISOU 4300  O   HOH A1359     2748   3688   4014   -559    802    754       O  
HETATM 4301  O   HOH A1360      35.823  20.319   2.968  1.00 33.64           O  
ANISOU 4301  O   HOH A1360     4422   3919   4441    313    -94    252       O  
HETATM 4302  O   HOH A1361      10.661  22.914   6.201  1.00 35.74           O  
ANISOU 4302  O   HOH A1361     4812   6767   1998  -2190    190    -92       O  
HETATM 4303  O   HOH A1362      -5.662  26.910   8.540  1.00 37.36           O  
ANISOU 4303  O   HOH A1362     4080   6020   4096   -455    341     96       O  
HETATM 4304  O   HOH A1363      49.561  10.326  18.550  1.00 56.93           O  
ANISOU 4304  O   HOH A1363     6940   7400   7292  -1637   -111    353       O  
HETATM 4305  O   HOH A1364      35.916   8.009  -8.896  1.00 39.90           O  
ANISOU 4305  O   HOH A1364     7080   4986   3094   -952   -168    940       O  
HETATM 4306  O   HOH A1365      45.417  10.572   3.998  1.00 43.68           O  
ANISOU 4306  O   HOH A1365     4788   5718   6092   -593    147    864       O  
HETATM 4307  O   HOH A1366      21.110 -10.969  -0.631  1.00 42.48           O  
ANISOU 4307  O   HOH A1366     4975   4693   6472  -1676    562  -2394       O  
HETATM 4308  O   HOH A1367      27.962  -9.984   8.809  1.00 39.89           O  
ANISOU 4308  O   HOH A1367     4520   5798   4839   -274   1075  -2562       O  
HETATM 4309  O   HOH A1368       3.358  22.288  42.688  1.00 46.67           O  
ANISOU 4309  O   HOH A1368     7628   6969   3135   2249    944    486       O  
HETATM 4310  O   HOH A1369      19.721  -4.870  13.516  1.00 35.06           O  
ANISOU 4310  O   HOH A1369     6176   3183   3964   -549     26   -329       O  
HETATM 4311  O   HOH A1370      16.201  13.781  17.318  1.00 25.86           O  
ANISOU 4311  O   HOH A1370     3651   3764   2410   1027   1089    -58       O  
HETATM 4312  O   HOH A1371      45.169   7.619   3.062  1.00 40.06           O  
ANISOU 4312  O   HOH A1371     5312   6765   3143   1585   1766    601       O  
HETATM 4313  O   HOH A1372      18.760  -5.006  17.272  1.00 31.99           O  
ANISOU 4313  O   HOH A1372     4593   3880   3682  -1648    101   -464       O  
HETATM 4314  O   HOH A1373      -9.987  24.307  26.247  1.00 40.65           O  
ANISOU 4314  O   HOH A1373     5594   5378   4471   -218   1366   -930       O  
HETATM 4315  O   HOH A1374      40.097  39.718   9.706  1.00 39.66           O  
ANISOU 4315  O   HOH A1374     7274   4413   3380    437  -1354    286       O  
HETATM 4316  O   HOH A1375      37.176  13.063  -4.593  1.00 42.14           O  
ANISOU 4316  O   HOH A1375     9290   3923   2799   3003   -849   -295       O  
HETATM 4317  O   HOH A1376      45.755  17.899   7.654  1.00 33.30           O  
ANISOU 4317  O   HOH A1376     3290   5627   3736  -1706    702    259       O  
HETATM 4318  O   HOH A1377      29.090  17.532  13.663  1.00 35.86           O  
ANISOU 4318  O   HOH A1377     3714   3359   6554   -137  -1943    412       O  
HETATM 4319  O   HOH A1380      -3.183  20.928  11.162  1.00 38.34           O  
ANISOU 4319  O   HOH A1380     5017   5017   4535   -600  -1810   -821       O  
HETATM 4320  O   HOH A1382      30.227  19.889  16.072  1.00 31.88           O  
ANISOU 4320  O   HOH A1382     4063   3703   4348    547   1873    217       O  
HETATM 4321  O   HOH A1383      42.948   0.213  -2.205  1.00 27.30           O  
ANISOU 4321  O   HOH A1383     3343   4033   2997   -539    769    347       O  
HETATM 4322  O   HOH A1385      35.183  34.461  21.032  1.00 33.19           O  
ANISOU 4322  O   HOH A1385     2725   5094   4792    261     38   1276       O  
HETATM 4323  O   HOH A1386       6.909  30.550   4.816  1.00 40.57           O  
ANISOU 4323  O   HOH A1386     3038   7552   4826   1615    826   -707       O  
HETATM 4324  O   HOH A1387      28.577   8.905  -2.852  1.00 36.57           O  
ANISOU 4324  O   HOH A1387     4045   4045   5806   -526    626   1586       O  
HETATM 4325  O   HOH A1388      31.631  -9.272  18.172  1.00 39.30           O  
ANISOU 4325  O   HOH A1388     4192   6550   4188   1288    994   1331       O  
HETATM 4326  O   HOH A1389      54.826  24.902  27.791  1.00 47.68           O  
ANISOU 4326  O   HOH A1389     4463   6456   7198    381   2504  -2650       O  
HETATM 4327  O   HOH A1390      17.195  -2.899  16.065  1.00 36.48           O  
ANISOU 4327  O   HOH A1390     4420   4711   4729   -991    941   -541       O  
HETATM 4328  O   HOH A1391       7.350  16.328  13.225  1.00 33.69           O  
ANISOU 4328  O   HOH A1391     3510   5280   4011   -963   1101   -311       O  
HETATM 4329  O   HOH A1392      42.001  39.764  33.410  1.00 38.85           O  
ANISOU 4329  O   HOH A1392     4958   3225   6576   1503   1374    917       O  
HETATM 4330  O   HOH A1393      46.221  30.484  10.049  1.00 33.28           O  
ANISOU 4330  O   HOH A1393     3622   4691   4331   -579    919    900       O  
HETATM 4331  O   HOH A1394      20.747  20.332   7.608  1.00 44.19           O  
ANISOU 4331  O   HOH A1394     4539   7412   4839   1684   1474   2609       O  
HETATM 4332  O   HOH A1395      41.940  10.165 -12.068  1.00 37.53           O  
ANISOU 4332  O   HOH A1395     6011   3274   4976    492   -433    436       O  
HETATM 4333  O   HOH A1396       2.612  43.089  29.979  1.00 43.75           O  
ANISOU 4333  O   HOH A1396     4709   8247   3668   2877   -153   -313       O  
HETATM 4334  O   HOH A1397      48.010   1.164  19.189  1.00 49.00           O  
ANISOU 4334  O   HOH A1397     5942   6618   6058   2853   -196  -1418       O  
HETATM 4335  O   HOH A1398      18.539  -2.138  10.512  1.00 40.48           O  
ANISOU 4335  O   HOH A1398     5096   4038   6245  -1050  -1651   -403       O  
HETATM 4336  O   HOH A1399      33.792  -8.501  25.100  1.00 45.92           O  
ANISOU 4336  O   HOH A1399     4456   8166   4826    760   2512    882       O  
HETATM 4337  O   HOH A1400      15.266  29.335   0.954  1.00 50.15           O  
ANISOU 4337  O   HOH A1400     5385   7956   5716  -2041   -642    771       O  
HETATM 4338  O   HOH A1401      51.176  30.402  40.614  1.00 27.24           O  
ANISOU 4338  O   HOH A1401     2746   4261   3344   -480     67    629       O  
HETATM 4339  O   HOH A1402      26.345   6.438  -5.620  1.00 35.52           O  
ANISOU 4339  O   HOH A1402     3874   4783   4838    839    748   1260       O  
HETATM 4340  O   HOH A1403      46.852   7.211   6.767  1.00 44.37           O  
ANISOU 4340  O   HOH A1403     2992   7941   5926   1856    582  -1845       O  
HETATM 4341  O   HOH A1404      25.903 -10.277  12.614  1.00 56.98           O  
ANISOU 4341  O   HOH A1404     7131   8392   6126  -2512    309    943       O  
HETATM 4342  O   HOH A1405       3.755  38.453   9.533  1.00 34.16           O  
ANISOU 4342  O   HOH A1405     4708   4293   3980   1412   -521    435       O  
HETATM 4343  O   HOH A1406      15.010   8.430  13.231  1.00 38.69           O  
ANISOU 4343  O   HOH A1406     2581   6905   5213   1363     -1    137       O  
HETATM 4344  O   HOH A1407      30.684  20.720  -0.280  1.00 46.41           O  
ANISOU 4344  O   HOH A1407     4797   8412   4424  -1737    356   2781       O  
HETATM 4345  O   HOH A1409       1.027  37.246  18.204  1.00 36.81           O  
ANISOU 4345  O   HOH A1409     4414   4338   5233    503   -802   1678       O  
HETATM 4346  O   HOH A1410      48.534  -6.214  30.257  1.00 45.10           O  
ANISOU 4346  O   HOH A1410     3825   7567   5742   3058    334  -2199       O  
HETATM 4347  O   HOH A1411      28.423  38.217  26.943  1.00 39.17           O  
ANISOU 4347  O   HOH A1411     3332   6935   4614   -936    425   -695       O  
HETATM 4348  O   HOH A1412       0.079  21.618  37.458  1.00156.43           O  
ANISOU 4348  O   HOH A1412    20651  19143  19644    -42   -439      3       O  
HETATM 4349  O   HOH A1413      50.452  19.797  21.686  1.00 31.01           O  
ANISOU 4349  O   HOH A1413     3482   4479   3819   -134   -223   -427       O  
HETATM 4350  O   HOH A1414      43.516   1.246  13.520  1.00 35.26           O  
ANISOU 4350  O   HOH A1414     3382   3895   6120    855    227  -1569       O  
HETATM 4351  O   HOH A1415      55.263   9.184  31.785  1.00 56.46           O  
ANISOU 4351  O   HOH A1415     3397   9383   8675   3085   -134  -1873       O  
HETATM 4352  O   HOH A1416      15.542   8.286  -0.569  1.00 37.87           O  
ANISOU 4352  O   HOH A1416     3434   5621   5333    594    339  -1766       O  
HETATM 4353  O   HOH A1417      19.636 -11.271   3.929  1.00 40.00           O  
ANISOU 4353  O   HOH A1417     4959   4314   5924   -612  -2001   -834       O  
HETATM 4354  O   HOH A1418       1.491  11.019  22.908  1.00 33.52           O  
ANISOU 4354  O   HOH A1418     3333   3572   5833  -1311    703   -772       O  
HETATM 4355  O   HOH A1419      12.470  21.802  40.233  1.00 54.72           O  
ANISOU 4355  O   HOH A1419     9077   6587   5128  -1668  -1340   2215       O  
HETATM 4356  O   HOH A1420      31.163  37.708  23.745  1.00 44.41           O  
ANISOU 4356  O   HOH A1420     3673   6568   6634  -1994    563    393       O  
HETATM 4357  O   HOH A1421       5.250  36.506   6.899  1.00 31.55           O  
ANISOU 4357  O   HOH A1421     3998   3901   4088    986    -36    519       O  
HETATM 4358  O   HOH A1422      56.815  29.564  24.928  1.00 47.80           O  
ANISOU 4358  O   HOH A1422     3549   8846   5767   -579   1650    751       O  
HETATM 4359  O   HOH A1423      38.119  -1.389   3.555  1.00 36.97           O  
ANISOU 4359  O   HOH A1423     3795   3456   6797    585   -206   -265       O  
HETATM 4360  O   HOH A1424      -6.313  23.450  26.896  1.00 43.30           O  
ANISOU 4360  O   HOH A1424     7144   5783   3524   -145   2157   -378       O  
HETATM 4361  O   HOH A1425      16.559  17.663  24.136  1.00 16.68           O  
ANISOU 4361  O   HOH A1425     2204   2098   2035    175    613   -134       O  
HETATM 4362  O   HOH A1428       6.920  16.073  42.944  1.00 41.54           O  
ANISOU 4362  O   HOH A1428     6603   6305   2874    127    203   -979       O  
HETATM 4363  O   HOH A1429       3.248  39.361  26.981  1.00 65.44           O  
ANISOU 4363  O   HOH A1429     9543   9093   6229   4063   1012  -4009       O  
HETATM 4364  O   HOH A1430       4.727  25.088   5.203  1.00 37.50           O  
ANISOU 4364  O   HOH A1430     7059   4221   2968   -121    492   -641       O  
HETATM 4365  O   HOH A1431       0.972  36.684  12.017  1.00 33.38           O  
ANISOU 4365  O   HOH A1431     2460   5240   4981    679    499   -377       O  
HETATM 4366  O   HOH A1432      42.597  35.031   6.672  1.00 38.47           O  
ANISOU 4366  O   HOH A1432     4004   5557   5056   1168    953    -25       O  
HETATM 4367  O   HOH A1433      53.652  31.896  37.572  1.00 39.92           O  
ANISOU 4367  O   HOH A1433     4158   4455   6555   -965  -2135   1675       O  
HETATM 4368  O   HOH A1435      30.106 -10.040  11.769  1.00 45.66           O  
ANISOU 4368  O   HOH A1435     6918   3046   7385    900    107  -1884       O  
HETATM 4369  O   HOH A1436      10.253  44.886  27.375  1.00 41.87           O  
ANISOU 4369  O   HOH A1436     7907   3555   4448   2404   1481   -351       O  
HETATM 4370  O   HOH A1437      27.367  19.917  15.848  1.00 33.20           O  
ANISOU 4370  O   HOH A1437     3627   3878   5108   -695   -251   1425       O  
HETATM 4371  O   HOH A1438      -6.101  35.149  22.875  1.00 45.57           O  
ANISOU 4371  O   HOH A1438     9565   4322   3427    108   1122   -860       O  
HETATM 4372  O   HOH A1440      20.398 -12.018   1.275  1.00 46.17           O  
ANISOU 4372  O   HOH A1440     7485   4564   5494  -2211   -851   -133       O  
HETATM 4373  O   HOH A1441      17.018   8.077  11.563  1.00 33.00           O  
ANISOU 4373  O   HOH A1441     3349   4621   4569  -1109   -839   1119       O  
HETATM 4374  O   HOH A1442      -1.736  15.730  28.895  1.00 37.27           O  
ANISOU 4374  O   HOH A1442     4525   3893   5744  -1510    228   1526       O  
HETATM 4375  O   HOH A1444      37.840   4.478 -11.759  1.00 46.04           O  
ANISOU 4375  O   HOH A1444     2749   7447   7295   1132   -599  -1738       O  
HETATM 4376  O   HOH A1445       7.776  41.064  23.844  1.00 33.80           O  
ANISOU 4376  O   HOH A1445     5869   3525   3449   1547    806    470       O  
HETATM 4377  O   HOH A1446      25.133  -2.645  -8.747  1.00 61.70           O  
ANISOU 4377  O   HOH A1446    10595   7434   5415   1524   -124    174       O  
HETATM 4378  O   HOH A1447      48.183   3.161  21.516  1.00 49.27           O  
ANISOU 4378  O   HOH A1447     7621   6546   4553   2890   -716     51       O  
HETATM 4379  O   HOH A1448      19.127  35.129  32.848  1.00 44.57           O  
ANISOU 4379  O   HOH A1448     5825   6316   4795    240  -1452  -1720       O  
HETATM 4380  O   HOH A1449      24.631  39.203  18.126  1.00 41.56           O  
ANISOU 4380  O   HOH A1449     3591   5672   6528   -611   -579   2772       O  
HETATM 4381  O   HOH A1450      20.912  44.011  23.701  1.00 44.79           O  
ANISOU 4381  O   HOH A1450     4396   5663   6961     98   -207   -634       O  
HETATM 4382  O   HOH A1451      47.839  12.516  -0.182  1.00 34.89           O  
ANISOU 4382  O   HOH A1451     4109   5398   3748  -1937    286  -1572       O  
HETATM 4383  O   HOH A1453      -1.402  34.825  18.651  1.00 37.30           O  
ANISOU 4383  O   HOH A1453     5864   3945   4365   1520   -371  -1071       O  
HETATM 4384  O   HOH A1454      28.304  23.322  18.517  1.00 39.31           O  
ANISOU 4384  O   HOH A1454     4041   7536   3356    152    637   1142       O  
HETATM 4385  O   HOH A1455      36.820  36.974  12.696  1.00 36.39           O  
ANISOU 4385  O   HOH A1455     3380   5788   4659    814    282    346       O  
HETATM 4386  O   HOH A1456      23.912  38.296  26.059  1.00 37.88           O  
ANISOU 4386  O   HOH A1456     2873   5791   5731    253   -295   -950       O  
HETATM 4387  O   HOH A1457      55.916  16.020  28.151  1.00 53.25           O  
ANISOU 4387  O   HOH A1457     2343   9195   8694  -1240  -1050   -630       O  
HETATM 4388  O   HOH A1458      13.760  36.827  38.264  1.00 60.65           O  
ANISOU 4388  O   HOH A1458     9289   8695   5058   -407  -2119   -258       O  
HETATM 4389  O   HOH A1459      17.755   0.425   8.063  1.00 42.03           O  
ANISOU 4389  O   HOH A1459     3015   7979   4977   -260    765   -728       O  
HETATM 4390  O   HOH A1460      44.653  38.116   9.669  1.00 36.26           O  
ANISOU 4390  O   HOH A1460     4978   5908   2893  -1694    866   1106       O  
HETATM 4391  O   HOH A1461      27.202 -12.255  26.681  1.00 46.41           O  
ANISOU 4391  O   HOH A1461     4874   7699   5060   -318    944   -764       O  
HETATM 4392  O   HOH A1462      11.655  39.664  13.235  1.00 33.98           O  
ANISOU 4392  O   HOH A1462     5620   2562   4730    693  -1362    547       O  
HETATM 4393  O   HOH A1463      22.158  36.914  15.304  1.00 44.45           O  
ANISOU 4393  O   HOH A1463     3617   6406   6866   -519    780   -686       O  
HETATM 4394  O   HOH A1466      21.440  -1.204  -4.580  1.00 43.96           O  
ANISOU 4394  O   HOH A1466     4975   4878   6851    609   1359    784       O  
HETATM 4395  O   HOH A1467      28.965  -1.538  -6.337  1.00 50.55           O  
ANISOU 4395  O   HOH A1467     8999   6795   3412    909  -1211  -1280       O  
HETATM 4396  O   HOH A1468      15.602  -0.625   3.774  1.00 51.22           O  
ANISOU 4396  O   HOH A1468     7131   4921   7410  -2775   -992   -600       O  
HETATM 4397  O   HOH A1469      22.691  -6.891  12.260  1.00 48.90           O  
ANISOU 4397  O   HOH A1469     5783   7271   5526   -252   1916   -900       O  
HETATM 4398  O   HOH A1470      49.822  44.219  28.303  1.00 49.60           O  
ANISOU 4398  O   HOH A1470     5627   4463   8754  -1278   -358     47       O  
HETATM 4399  O   HOH A1471      21.787  -4.377   9.602  1.00 42.48           O  
ANISOU 4399  O   HOH A1471     5677   4630   5835    336   -832    631       O  
HETATM 4400  O   HOH A1473      46.869  43.977  25.059  1.00 43.10           O  
ANISOU 4400  O   HOH A1473     6472   4175   5730    553   -960  -1084       O  
HETATM 4401  O   HOH A1474      53.942   6.554  23.632  1.00 57.54           O  
ANISOU 4401  O   HOH A1474     8278   5819   7767   1909    -91  -1897       O  
HETATM 4402  O   HOH A1475      38.236  -3.119   9.833  1.00 37.69           O  
ANISOU 4402  O   HOH A1475     5002   4125   5193   -559   -900    764       O  
HETATM 4403  O   HOH A1476       0.523  38.919  16.031  1.00 42.77           O  
ANISOU 4403  O   HOH A1476     3865   6280   6105   1676    583   -705       O  
HETATM 4404  O   HOH A1478      52.236  26.189  20.681  1.00 33.39           O  
ANISOU 4404  O   HOH A1478     4160   4427   4099    314   1439   1174       O  
HETATM 4405  O   HOH A1479      48.183   7.024  14.861  1.00 57.08           O  
ANISOU 4405  O   HOH A1479     5660   7288   8739   2740    261  -2247       O  
HETATM 4406  O   HOH A1480      28.950  12.647   3.995  1.00 45.88           O  
ANISOU 4406  O   HOH A1480     4243   8811   4377    156   1911   1579       O  
HETATM 4407  O   HOH A1481      45.417   5.505   5.780  1.00 44.86           O  
ANISOU 4407  O   HOH A1481     4349   5987   6708   -212    717   -926       O  
HETATM 4408  O   HOH A1482      23.494  -6.391   8.476  1.00 38.44           O  
ANISOU 4408  O   HOH A1482     6366   4630   3609  -1318   -134  -1100       O  
HETATM 4409  O   HOH A1483      13.300  17.609  39.160  1.00 61.42           O  
ANISOU 4409  O   HOH A1483    10032   8122   5182    -61  -1016      3       O  
HETATM 4410  O   HOH A1484      46.489  39.274  36.341  1.00 44.05           O  
ANISOU 4410  O   HOH A1484     4513   5978   6247  -2220    768   -515       O  
HETATM 4411  O   HOH A1485      33.580  13.799  -3.831  1.00 41.48           O  
ANISOU 4411  O   HOH A1485     7823   4492   3447    963   -243    870       O  
HETATM 4412  O   HOH A1486      33.458  -9.320  -0.835  1.00 65.77           O  
ANISOU 4412  O   HOH A1486     6226  10028   8736    520   2802   -728       O  
HETATM 4413  O   HOH A1487      28.143  29.611  18.050  1.00 39.42           O  
ANISOU 4413  O   HOH A1487     3058   4964   6955   -507    235    513       O  
HETATM 4414  O   HOH A1488      37.253  38.005  23.055  1.00 49.73           O  
ANISOU 4414  O   HOH A1488     8729   5043   5123  -2252   -399   1726       O  
HETATM 4415  O   HOH A1489       1.121  20.212   8.581  1.00 36.68           O  
ANISOU 4415  O   HOH A1489     4143   5487   4306    -25   -543   -412       O  
HETATM 4416  O   HOH A1491      32.228  38.663  31.206  1.00 45.09           O  
ANISOU 4416  O   HOH A1491     5451   6578   5103   1550   1949   2543       O  
HETATM 4417  O   HOH A1492      35.505  36.166  19.120  1.00 35.60           O  
ANISOU 4417  O   HOH A1492     4858   4534   4135    300    346    758       O  
HETATM 4418  O   HOH A1493      39.839  24.447  12.164  1.00 41.26           O  
ANISOU 4418  O   HOH A1493     6164   6144   3369   -285   1178    776       O  
HETATM 4419  O   HOH A1494      50.668  17.983  19.931  1.00 43.21           O  
ANISOU 4419  O   HOH A1494     6331   6626   3459   -372   1030   1292       O  
HETATM 4420  O   HOH A1495      39.198  40.802  21.928  1.00 45.85           O  
ANISOU 4420  O   HOH A1495     5338   6418   5663     31   1478    232       O  
HETATM 4421  O   HOH A1496      51.142  14.400  14.994  1.00 53.89           O  
ANISOU 4421  O   HOH A1496     3421   7132   9924   -943  -2061   -305       O  
HETATM 4422  O   HOH A1497      36.964  39.636  34.803  1.00 52.35           O  
ANISOU 4422  O   HOH A1497     9165   4687   6037    361    585  -1478       O  
HETATM 4423  O   HOH A1498      38.560  11.887  -7.341  1.00 46.83           O  
ANISOU 4423  O   HOH A1498     6716   4545   6531   2119    562    880       O  
HETATM 4424  O   HOH A1499      14.882  -1.657  20.795  1.00 57.51           O  
ANISOU 4424  O   HOH A1499     5026   7764   9060  -2744   1169   3995       O  
HETATM 4425  O   HOH A1500      19.213  40.966  30.550  1.00 48.40           O  
ANISOU 4425  O   HOH A1500     7827   5085   5479    -31   -270   -414       O  
HETATM 4426  O   HOH A1501      49.148  40.426  31.660  1.00 48.93           O  
ANISOU 4426  O   HOH A1501     9127   3743   5719  -2436    142    683       O  
HETATM 4427  O   HOH A1502      17.278   0.827  -0.138  1.00 41.53           O  
ANISOU 4427  O   HOH A1502     4543   5609   5629  -1241   1817  -1357       O  
HETATM 4428  O   HOH A1503      25.310  38.540  23.729  1.00 43.60           O  
ANISOU 4428  O   HOH A1503     6136   3579   6853   1330   1594   1268       O  
HETATM 4429  O   HOH A1504      48.826  31.641   9.851  1.00 34.94           O  
ANISOU 4429  O   HOH A1504     4720   4828   3730   -148   1129    648       O  
HETATM 4430  O   HOH A1506       3.575   9.249  30.217  1.00 53.22           O  
ANISOU 4430  O   HOH A1506     8610   7058   4553  -2605   -477   1105       O  
HETATM 4431  O   HOH A1507      19.986  -3.280   7.449  1.00 37.23           O  
ANISOU 4431  O   HOH A1507     4537   5513   4096  -1439    296   -106       O  
HETATM 4432  O   HOH A1508      48.157  36.220  43.061  1.00 59.14           O  
ANISOU 4432  O   HOH A1508     2868   9987   9616   -818    390   -236       O  
HETATM 4433  O   HOH A1510       3.990   9.275  20.165  1.00 43.81           O  
ANISOU 4433  O   HOH A1510     5656   3563   7428    392   -402   -809       O  
HETATM 4434  O   HOH A1511      47.413 -10.424  40.436  1.00 37.82           O  
ANISOU 4434  O   HOH A1511     5346   4098   4925   -164  -1672    720       O  
HETATM 4435  O   HOH A1512      10.883  23.566  39.977  1.00 82.02           O  
ANISOU 4435  O   HOH A1512     9732  10594  10837   1106   -713     12       O  
HETATM 4436  O   HOH A1514      44.818  42.441  17.231  1.00 40.76           O  
ANISOU 4436  O   HOH A1514     5126   4591   5770   -287   -422   1972       O  
HETATM 4437  O   HOH A1515      39.149   4.428  29.719  1.00 47.73           O  
ANISOU 4437  O   HOH A1515     5695   6027   6414   2201   1542   -140       O  
HETATM 4438  O   HOH A1517      46.319   9.231  11.774  1.00 45.56           O  
ANISOU 4438  O   HOH A1517     5114   4268   7930   -498   -654   1025       O  
HETATM 4439  O   HOH A1518       8.557   6.613  29.222  1.00 33.00           O  
ANISOU 4439  O   HOH A1518     3831   3623   5084  -1401    817   -342       O  
HETATM 4440  O   HOH A1519      50.666  41.668  20.308  1.00 53.91           O  
ANISOU 4440  O   HOH A1519     7720   7213   5551  -3502   2174     67       O  
HETATM 4441  O   HOH A1520      15.139  23.261  38.278  0.50 41.65           O  
ANISOU 4441  O   HOH A1520     5912   5731   4181  -2533  -1889    961       O  
HETATM 4442  O   HOH A1521      41.614   7.169  27.601  1.00 38.55           O  
ANISOU 4442  O   HOH A1521     6185   3334   5128    496   2628    352       O  
HETATM 4443  O   HOH A1522      45.485  38.742  42.757  1.00 58.23           O  
ANISOU 4443  O   HOH A1522     8390   6396   7338   1353  -1062    707       O  
HETATM 4444  O   HOH A1523      -3.261  34.984  21.498  1.00 37.73           O  
ANISOU 4444  O   HOH A1523     2545   4634   7157     28  -1070   1130       O  
HETATM 4445  O   HOH A1524       2.562  37.874  29.436  1.00 52.33           O  
ANISOU 4445  O   HOH A1524     4608   6990   8285   3467   -273  -1711       O  
HETATM 4446  O   HOH A1525      18.596   5.201   7.655  1.00 35.32           O  
ANISOU 4446  O   HOH A1525     4165   3596   5659   -664  -1213    980       O  
HETATM 4447  O   HOH A1526      46.767  12.298   2.372  1.00 48.02           O  
ANISOU 4447  O   HOH A1526     3705   7552   6990   -751    642  -1301       O  
HETATM 4448  O   HOH A1527      56.472  11.916  28.077  1.00112.22           O  
ANISOU 4448  O   HOH A1527    13363  14475  14801  -1586    189    131       O  
HETATM 4449  O   HOH A1528      15.828   3.232   6.569  1.00 43.87           O  
ANISOU 4449  O   HOH A1528     4350   7764   4555   1850   1246  -1764       O  
HETATM 4450  O   HOH A1529      55.750  13.204  26.313  1.00 56.91           O  
ANISOU 4450  O   HOH A1529     5003   8721   7899   2053    935    -28       O  
HETATM 4451  O   HOH A1530      41.032  -5.205  45.753  1.00 43.73           O  
ANISOU 4451  O   HOH A1530     7803   5515   3298     30   -182  -1107       O  
HETATM 4452  O   HOH A1531       1.983  24.408  43.790  1.00 56.81           O  
ANISOU 4452  O   HOH A1531    10021   7827   3735   2104   -595  -1812       O  
HETATM 4453  O   HOH A1533      46.950  20.585  10.168  1.00 45.47           O  
ANISOU 4453  O   HOH A1533     5948   6441   4887   -281   2545    185       O  
HETATM 4454  O   HOH A1534       8.681   7.899  20.910  1.00 42.07           O  
ANISOU 4454  O   HOH A1534     7692   4103   4191   1993   -710   -342       O  
HETATM 4455  O  AHOH A1535      12.482  45.191  34.969  0.70 27.03           O  
ANISOU 4455  O  AHOH A1535     3514   3062   3694     87   1356    500       O  
HETATM 4456  O  BHOH A1535      12.269  44.794  32.937  0.30 14.09           O  
ANISOU 4456  O  BHOH A1535     1142   2518   1695     33    -25   -583       O  
HETATM 4457  O   HOH A1536      17.548  -5.015  -0.618  1.00 54.17           O  
ANISOU 4457  O   HOH A1536     5318   8863   6399  -1583  -1481   -213       O  
HETATM 4458  O   HOH A1537      12.656   0.017  25.127  1.00 43.58           O  
ANISOU 4458  O   HOH A1537     4024   5334   7200   -560    258   -861       O  
HETATM 4459  O   HOH A1538      30.736  26.321  19.225  1.00 72.08           O  
ANISOU 4459  O   HOH A1538     9467   9262   8656  -2545   -419     46       O  
HETATM 4460  O   HOH A1539      22.279  41.847  25.680  1.00 48.34           O  
ANISOU 4460  O   HOH A1539     3195   8902   6269  -2175   1793   -596       O  
HETATM 4461  O   HOH A1540      -1.221  36.630  27.463  1.00 38.22           O  
ANISOU 4461  O   HOH A1540     4055   5594   4875   1581   1069   1114       O  
HETATM 4462  O   HOH A1541      27.737  -5.140  -6.227  1.00 47.92           O  
ANISOU 4462  O   HOH A1541     6427   7169   4611    182   2496   -524       O  
HETATM 4463  O   HOH A1542      34.876  38.015  14.954  1.00 47.13           O  
ANISOU 4463  O   HOH A1542     6490   5797   5621   -619   -854   1508       O  
HETATM 4464  O   HOH A1543      26.597  -7.807  -3.531  1.00 39.98           O  
ANISOU 4464  O   HOH A1543     5328   3794   6069   -219    302    933       O  
HETATM 4465  O   HOH A1544      39.634  -2.786  18.850  1.00 45.48           O  
ANISOU 4465  O   HOH A1544     5848   5755   5677   1253  -1537    347       O  
HETATM 4466  O   HOH A1546      20.666  -5.867  16.188  1.00 38.28           O  
ANISOU 4466  O   HOH A1546     2868   4789   6887   -631   -733    884       O  
HETATM 4467  O   HOH A1547      43.541  37.761   7.184  1.00 45.39           O  
ANISOU 4467  O   HOH A1547     5363   5800   6084    180  -1752    192       O  
HETATM 4468  O   HOH A1548      17.732  -1.389  -1.304  1.00 46.33           O  
ANISOU 4468  O   HOH A1548     4221   5433   7951  -1309   -945  -1018       O  
HETATM 4469  O   HOH A1549      29.226  14.778   6.944  1.00 50.01           O  
ANISOU 4469  O   HOH A1549     4695   7861   6447  -2416   1480   2221       O  
HETATM 4470  O   HOH A1550      42.087  39.739  36.896  1.00 43.13           O  
ANISOU 4470  O   HOH A1550     5492   3727   7166   -376   -372   -746       O  
HETATM 4471  O   HOH A1551       6.189   8.561  22.015  1.00 49.26           O  
ANISOU 4471  O   HOH A1551     8910   2843   6964   -842  -3264    176       O  
HETATM 4472  O   HOH A1553      48.466  44.217  21.221  1.00 48.22           O  
ANISOU 4472  O   HOH A1553     5571   6049   6702  -1767    373   1601       O  
HETATM 4473  O   HOH A1554       3.413  17.242  43.447  1.00 61.23           O  
ANISOU 4473  O   HOH A1554     8268   7735   7263   -455   -968   -756       O  
HETATM 4474  O   HOH A1555      38.615  -2.365  23.500  1.00 58.26           O  
ANISOU 4474  O   HOH A1555     5731   7042   9364   1727  -1049   -203       O  
HETATM 4475  O   HOH A1556      -2.988  12.725  21.436  1.00 50.20           O  
ANISOU 4475  O   HOH A1556     3233   7117   8724   -238   -187  -3257       O  
HETATM 4476  O   HOH A1557      17.277  44.755  34.291  0.50 52.99           O  
ANISOU 4476  O   HOH A1557     7055   6015   7062  -4354   -388   1928       O  
HETATM 4477  O   HOH A1558      14.096  13.218  19.340  1.00 42.33           O  
ANISOU 4477  O   HOH A1558     5533   4988   5563  -1120  -2653   2068       O  
HETATM 4478  O   HOH A1559      33.115  10.439  -5.610  1.00 48.62           O  
ANISOU 4478  O   HOH A1559     5475   6520   6478     77  -2499     63       O  
HETATM 4479  O   HOH A1560       0.231  13.960  29.811  1.00 33.42           O  
ANISOU 4479  O   HOH A1560     3354   4134   5211  -1033   1432  -1141       O  
HETATM 4480  O   HOH A1561      11.282  42.934  20.127  1.00 51.56           O  
ANISOU 4480  O   HOH A1561     8450   5406   5734    460  -1336    826       O  
HETATM 4481  O   HOH A1562      31.528  21.771  17.469  1.00 87.65           O  
ANISOU 4481  O   HOH A1562     9327  11316  12661   -996   -348     99       O  
HETATM 4482  O   HOH A1563       2.179  12.433  16.032  1.00 40.07           O  
ANISOU 4482  O   HOH A1563     5759   4853   4614  -1736   -771      6       O  
HETATM 4483  O   HOH A1564       6.512  38.846   8.672  1.00 43.51           O  
ANISOU 4483  O   HOH A1564     5944   5384   5203   1906  -1048   2333       O  
HETATM 4484  O   HOH A1565      28.450 -12.101  29.184  1.00 56.95           O  
ANISOU 4484  O   HOH A1565     6577   7255   7805    111   -558    292       O  
HETATM 4485  O   HOH A1566      27.205  22.088  13.870  1.00 70.90           O  
ANISOU 4485  O   HOH A1566     6125  10391  10422   -437     45    339       O  
HETATM 4486  O   HOH A1567      36.061  37.539   7.959  1.00 39.69           O  
ANISOU 4486  O   HOH A1567     3723   7249   4108   1189    -26   -224       O  
HETATM 4487  O   HOH A1568      25.184  12.315   1.605  1.00 58.11           O  
ANISOU 4487  O   HOH A1568     9849   7604   4625  -2708   -479   2792       O  
HETATM 4488  O   HOH A1570      42.447  43.213  19.463  1.00 45.87           O  
ANISOU 4488  O   HOH A1570     6903   3921   6605   1109    962   -671       O  
HETATM 4489  O   HOH A1571      40.264   3.901   2.810  1.00 46.58           O  
ANISOU 4489  O   HOH A1571     8211   5374   4112   1442   2723   -151       O  
HETATM 4490  O   HOH A1572      45.385  -5.798  28.060  1.00 49.07           O  
ANISOU 4490  O   HOH A1572     5339   7342   5963   1948    924  -1578       O  
HETATM 4491  O   HOH A1573      30.005  13.861  -2.712  1.00 55.53           O  
ANISOU 4491  O   HOH A1573     9673   6008   5418   -164  -3227  -1055       O  
HETATM 4492  O   HOH A1574      54.660  31.714  33.132  1.00 44.05           O  
ANISOU 4492  O   HOH A1574     2854   6276   7606   -576    816    145       O  
HETATM 4493  O   HOH A1575      14.909  42.875  18.035  1.00 40.53           O  
ANISOU 4493  O   HOH A1575     4099   7390   3909  -1177    172    689       O  
HETATM 4494  O   HOH A1576      -0.802  20.683  35.555  1.00 60.47           O  
ANISOU 4494  O   HOH A1576     4888   8950   9137   2259    712  -1533       O  
HETATM 4495  O   HOH A1577      12.027  25.498   4.367  1.00 54.08           O  
ANISOU 4495  O   HOH A1577     6508   6787   7251   1440  -2936  -1710       O  
HETATM 4496  O   HOH A1578      54.644  36.145  27.654  0.50 44.29           O  
ANISOU 4496  O   HOH A1578     6402   5200   5226    655  -1059  -2370       O  
HETATM 4497  O   HOH A1579      33.532  -8.901  20.639  1.00 46.83           O  
ANISOU 4497  O   HOH A1579     8330   5333   4129   1786    692  -1207       O  
HETATM 4498  O   HOH A1580      25.226  20.582  13.102  1.00 54.04           O  
ANISOU 4498  O   HOH A1580     4475   7708   8351    610    394   -650       O  
HETATM 4499  O   HOH A1581      51.345  15.452  20.314  1.00 42.99           O  
ANISOU 4499  O   HOH A1581     3503   5738   7092   1146   1061  -1051       O  
HETATM 4500  O   HOH A1582      52.728  20.244  22.048  1.00 46.83           O  
ANISOU 4500  O   HOH A1582     6289   5566   5937    840   1836    260       O  
HETATM 4501  O   HOH A1583      47.850  45.923  27.541  1.00 55.17           O  
ANISOU 4501  O   HOH A1583     6606   6363   7994  -1284  -1466   -109       O  
HETATM 4502  O   HOH A1584      15.885  24.453  -0.540  0.50 38.29           O  
ANISOU 4502  O   HOH A1584     6291   5339   2920   -150   -534   -538       O  
HETATM 4503  O   HOH A1585      50.543  25.698  17.329  1.00 49.12           O  
ANISOU 4503  O   HOH A1585     5084   6342   7239  -1590   1116   1263       O  
HETATM 4504  O   HOH A1586      23.773  34.755  32.220  1.00 51.89           O  
ANISOU 4504  O   HOH A1586     6396   5665   7654   3950  -2450  -1895       O  
HETATM 4505  O   HOH A1587      31.919  -9.457   9.446  1.00 49.22           O  
ANISOU 4505  O   HOH A1587     9327   3901   5471   2622   -991  -1778       O  
HETATM 4506  O   HOH A1588      23.585  22.731   8.714  0.50 36.45           O  
ANISOU 4506  O   HOH A1588     3965   4842   5043   1505   1718   1207       O  
HETATM 4507  O   HOH A1589       9.474  40.563   9.479  1.00 47.54           O  
ANISOU 4507  O   HOH A1589     8069   3604   6390   -484  -1457   1506       O  
HETATM 4508  O   HOH A1590      13.440   9.714  18.301  1.00 48.22           O  
ANISOU 4508  O   HOH A1590     4061   7378   6881     69  -1216   2022       O  
HETATM 4509  O   HOH A1591      52.028  39.986  28.671  1.00 50.20           O  
ANISOU 4509  O   HOH A1591     6076   6547   6449  -1577  -1287    793       O  
HETATM 4510  O   HOH A1592      42.707   0.314   6.089  1.00 49.82           O  
ANISOU 4510  O   HOH A1592     4230   8063   6637   1054   2612    -48       O  
HETATM 4511  O   HOH A1593      28.688 -10.942  16.247  1.00 41.97           O  
ANISOU 4511  O   HOH A1593     6503   4757   4687    257   1030   -326       O  
HETATM 4512  O   HOH A1595      53.278   7.085  26.263  1.00 39.56           O  
ANISOU 4512  O   HOH A1595     4843   4567   5622   -961   1277     94       O  
HETATM 4513  O   HOH A1596      11.731   2.745  24.457  1.00 72.68           O  
ANISOU 4513  O   HOH A1596    10797   9217   7600    949  -1298   -473       O  
HETATM 4514  O   HOH A1597      54.855  14.237  32.322  1.00 42.43           O  
ANISOU 4514  O   HOH A1597     3847   7939   4335   1144    446   -286       O  
HETATM 4515  O   HOH A1598      54.953  11.077  26.577  1.00 53.55           O  
ANISOU 4515  O   HOH A1598     3918  10114   6315  -1718   2974     25       O  
HETATM 4516  O   HOH A1601      36.978   6.822 -10.956  0.50 34.98           O  
ANISOU 4516  O   HOH A1601     4071   5261   3960    489   -964  -1294       O  
HETATM 4517  O   HOH A1603      21.907  27.341  10.463  1.00 43.88           O  
ANISOU 4517  O   HOH A1603     4583   6384   5703    106   -363    205       O  
HETATM 4518  O   HOH A1604      36.358  39.954  28.172  1.00 62.50           O  
ANISOU 4518  O   HOH A1604     6334   8494   8918    544  -1348   2548       O  
HETATM 4519  O   HOH A1605      61.473  33.765  33.597  1.00 55.52           O  
ANISOU 4519  O   HOH A1605    10731   6218   4147   -483    535  -2042       O  
HETATM 4520  O   HOH A1606      27.329  11.587   2.725  1.00 63.15           O  
ANISOU 4520  O   HOH A1606     7676   7254   9064   1742   -194  -1088       O  
HETATM 4521  O   HOH A1607      35.928  -8.282  19.846  1.00 45.95           O  
ANISOU 4521  O   HOH A1607     5155   5051   7252   1492    325  -1078       O  
HETATM 4522  O   HOH A1608       7.883  18.230  10.322  1.00 63.50           O  
ANISOU 4522  O   HOH A1608     8021   8954   7151  -3885   2135   2418       O  
HETATM 4523  O   HOH A1609      49.778  28.455  12.920  1.00 44.54           O  
ANISOU 4523  O   HOH A1609     6167   6161   4596   -356   1941   -535       O  
HETATM 4524  O   HOH A1610      49.610  18.150  15.871  1.00 42.73           O  
ANISOU 4524  O   HOH A1610     5318   6391   4528   -942   1712   1220       O  
HETATM 4525  O   HOH A1611       5.106   9.319  24.309  1.00 52.67           O  
ANISOU 4525  O   HOH A1611     5661   6832   7518    350    166    126       O  
HETATM 4526  O   HOH A1612      20.731 -14.449   4.844  1.00 43.56           O  
ANISOU 4526  O   HOH A1612     6323   6490   3739  -1934   2408  -1545       O  
HETATM 4527  O   HOH A1613      35.420  -9.105  31.415  1.00 48.65           O  
ANISOU 4527  O   HOH A1613     4461   7738   6286    330  -1764  -2472       O  
HETATM 4528  O   HOH A1614      26.888  19.109  10.554  1.00 67.15           O  
ANISOU 4528  O   HOH A1614     6733   8946   9835   3474    863  -1420       O  
HETATM 4529  O   HOH A1615      36.824  -5.241   5.813  1.00 37.61           O  
ANISOU 4529  O   HOH A1615     4816   4395   5079   -607   -181   -261       O  
HETATM 4530  O   HOH A1616      48.718  44.671  14.492  1.00 59.70           O  
ANISOU 4530  O   HOH A1616     9124   6015   7545  -3073   -252   3400       O  
HETATM 4531  O   HOH A1617      43.111  41.397  24.079  1.00 48.78           O  
ANISOU 4531  O   HOH A1617     4252   7371   6913   -964    341    892       O  
HETATM 4532  O   HOH A1618       7.067  31.785  40.873  1.00 45.42           O  
ANISOU 4532  O   HOH A1618    10302   3999   2955   -466    217    665       O  
HETATM 4533  O   HOH A1619      18.059  45.222  23.544  1.00 42.02           O  
ANISOU 4533  O   HOH A1619     6099   4820   5047   -979   1780    995       O  
HETATM 4534  O   HOH A1620      -2.076  12.321  17.926  1.00 54.76           O  
ANISOU 4534  O   HOH A1620     6133   7326   7348   -530   -141   -750       O  
HETATM 4535  O   HOH A1621      25.556  15.574   4.852  1.00 51.45           O  
ANISOU 4535  O   HOH A1621     7207   5037   7304  -1729   -697    831       O  
HETATM 4536  O   HOH A1622      16.980   5.407  10.603  1.00 53.44           O  
ANISOU 4536  O   HOH A1622     2522   8120   9662    362    414   -708       O  
HETATM 4537  O   HOH A1623      28.904 -10.386  20.597  1.00 44.74           O  
ANISOU 4537  O   HOH A1623     7143   3906   5950    542   -276  -1174       O  
HETATM 4538  O   HOH A1624      34.778  35.368  17.094  1.00 46.97           O  
ANISOU 4538  O   HOH A1624     4945   5893   7010   1010   -355   1146       O  
HETATM 4539  O   HOH A1625     -14.781  32.216  22.703  1.00 59.14           O  
ANISOU 4539  O   HOH A1625     8189   7371   6912  -1623   -834   1541       O  
HETATM 4540  O   HOH A1627      -2.019  16.028  11.951  1.00 60.85           O  
ANISOU 4540  O   HOH A1627     8390   6467   8262    135  -1165  -1663       O  
HETATM 4541  O   HOH A1628      53.258  39.827  25.309  1.00 47.72           O  
ANISOU 4541  O   HOH A1628     3646   7924   6563    255   1314   1342       O  
HETATM 4542  O   HOH A1630      42.333   0.309  23.340  1.00 46.37           O  
ANISOU 4542  O   HOH A1630     5450   6786   5384  -1231   1524   1560       O  
HETATM 4543  O   HOH A1631      18.145  -5.757  26.556  1.00 43.23           O  
ANISOU 4543  O   HOH A1631     5648   5512   5265  -1526   2517  -1145       O  
HETATM 4544  O   HOH A1632      -3.685  20.876  34.386  1.00 61.56           O  
ANISOU 4544  O   HOH A1632     7083   8245   8061   -609   -194    490       O  
HETATM 4545  O   HOH A1633     -12.318  29.389  24.399  1.00 51.82           O  
ANISOU 4545  O   HOH A1633     8868   5505   5317   2402    759  -2199       O  
HETATM 4546  O   HOH A1636       6.132   8.100  33.095  1.00 32.58           O  
ANISOU 4546  O   HOH A1636     3251   4483   4643    139     60  -1092       O  
HETATM 4547  O   HOH A1637      28.780  17.892  22.165  1.00 34.18           O  
ANISOU 4547  O   HOH A1637     6283   3332   3372   1194   -214   -367       O  
HETATM 4548  O   HOH A1638      51.096  40.414  33.954  0.50 40.38           O  
ANISOU 4548  O   HOH A1638     4636   4167   6539  -2698  -1517    157       O  
HETATM 4549  O   HOH A1639       1.699  28.785  37.782  1.00 57.42           O  
ANISOU 4549  O   HOH A1639     8516   4767   8535   -170   -888    749       O  
HETATM 4550  O   HOH A1640      31.666  21.535   2.555  1.00 48.61           O  
ANISOU 4550  O   HOH A1640     5063   6140   7264   1317   1471   1307       O  
HETATM 4551  O   HOH A1641      45.496  -8.070  30.424  1.00 52.66           O  
ANISOU 4551  O   HOH A1641     8215   5558   6238   1186  -1780    -72       O  
HETATM 4552  O   HOH A1642      45.656  13.663  -6.879  1.00 41.12           O  
ANISOU 4552  O   HOH A1642     4887   6499   4238   -530    282   1521       O  
HETATM 4553  O   HOH A1643      21.227 -10.452   7.750  1.00 51.70           O  
ANISOU 4553  O   HOH A1643     5548   7401   6693  -2494   -982   1677       O  
HETATM 4554  O   HOH A1644      45.658  38.097   5.328  1.00 51.18           O  
ANISOU 4554  O   HOH A1644     4888   8079   6478  -1235  -1950   1884       O  
HETATM 4555  O   HOH A1645      52.110  -6.687  34.599  1.00 55.95           O  
ANISOU 4555  O   HOH A1645     6180   7454   7624    923   1522    379       O  
HETATM 4556  O   HOH A1646      14.734  11.475  15.792  1.00 46.91           O  
ANISOU 4556  O   HOH A1646     3266   5965   8593    508   -321    389       O  
HETATM 4557  O   HOH A1647      15.952  12.865   8.156  1.00 37.02           O  
ANISOU 4557  O   HOH A1647     4398   5201   4466    322    543   -224       O  
HETATM 4558  O   HOH A1648      47.541  28.812  12.608  1.00 56.85           O  
ANISOU 4558  O   HOH A1648     5003   9570   7026    443   1322   -175       O  
HETATM 4559  O   HOH A1649      26.722  17.907   8.557  0.50 38.42           O  
ANISOU 4559  O   HOH A1649     3892   4795   5910  -1982     26   1435       O  
HETATM 4560  O   HOH A1650      39.054 -12.386  35.686  1.00 68.21           O  
ANISOU 4560  O   HOH A1650     9555   6736   9626    644   -959   -440       O  
HETATM 4561  O   HOH A1651       4.658  26.233  40.837  1.00 45.06           O  
ANISOU 4561  O   HOH A1651     5762   5997   5363  -1199    106    854       O  
HETATM 4562  O   HOH A1652      41.373  11.752  -7.134  1.00 41.63           O  
ANISOU 4562  O   HOH A1652     5991   5006   4822  -1006    840   1524       O  
HETATM 4563  O   HOH A1653      60.094  28.048  28.395  0.50 38.83           O  
ANISOU 4563  O   HOH A1653     2632   6503   5618   1304    995   -788       O  
HETATM 4564  O   HOH A1654      16.867  10.757   2.971  1.00 42.57           O  
ANISOU 4564  O   HOH A1654     3749   7161   5267   1247    109      5       O  
HETATM 4565  O   HOH A1655      54.308  18.499  35.359  1.00 30.71           O  
ANISOU 4565  O   HOH A1655     3477   3907   4285  -1459   -787    426       O  
HETATM 4566  O   HOH A1656      18.980 -15.562   2.955  1.00 46.34           O  
ANISOU 4566  O   HOH A1656     4946   6072   6587  -2780    -33    453       O  
HETATM 4567  O   HOH A1657       2.603  40.784  23.223  1.00 56.44           O  
ANISOU 4567  O   HOH A1657    10223   4906   6314   2940  -1647   -887       O  
HETATM 4568  O   HOH A1658      28.742  24.309  16.488  1.00 49.03           O  
ANISOU 4568  O   HOH A1658     2436   7898   8296    363    811    691       O  
HETATM 4569  O   HOH A1659      -0.055  39.079  30.194  1.00 58.82           O  
ANISOU 4569  O   HOH A1659     7001   7538   7811  -1741    509    413       O  
HETATM 4570  O   HOH A1660      51.591  38.042  20.135  1.00 51.62           O  
ANISOU 4570  O   HOH A1660     6694   5056   7864   -660  -1085   -159       O  
HETATM 4571  O   HOH A1661      13.844   2.449  22.579  1.00 58.17           O  
ANISOU 4571  O   HOH A1661     4170   8840   9092   1024    -46   -594       O  
HETATM 4572  O   HOH A1662      53.893  33.594  17.705  1.00 49.45           O  
ANISOU 4572  O   HOH A1662     4058   9211   5518  -2888   1527    513       O  
HETATM 4573  O   HOH A1663      22.208  22.870  -1.876  1.00 54.16           O  
ANISOU 4573  O   HOH A1663     6733   5685   8161  -1057   -101  -1011       O  
HETATM 4574  O   HOH A1664      21.037  44.141  20.208  1.00 42.71           O  
ANISOU 4574  O   HOH A1664     4603   6544   5080  -1014     82    114       O  
HETATM 4575  O   HOH A1665      52.547  37.106  23.148  1.00 37.42           O  
ANISOU 4575  O   HOH A1665     4595   4797   4827   -549    876    461       O  
HETATM 4576  O   HOH A1666      19.040  42.381  15.810  1.00 51.45           O  
ANISOU 4576  O   HOH A1666     6249   4969   8332  -1078   -409   3048       O  
HETATM 4577  O   HOH A1667      46.786  10.918   5.866  1.00 45.59           O  
ANISOU 4577  O   HOH A1667     2752   8471   6099  -1038    845   1037       O  
HETATM 4578  O   HOH A1668      16.296   0.541  14.011  1.00 40.96           O  
ANISOU 4578  O   HOH A1668     4869   4865   5828  -1961  -1910   -365       O  
HETATM 4579  O   HOH A1670      18.446   0.128  -3.872  0.50 40.13           O  
ANISOU 4579  O   HOH A1670     4790   5080   5377  -1028    553    602       O  
HETATM 4580  O   HOH A1671       3.804  31.719   2.747  1.00 47.90           O  
ANISOU 4580  O   HOH A1671     4877   7360   5964  -1117  -1607   1474       O  
HETATM 4581  O   HOH A1673      26.787 -11.274  24.649  1.00 48.25           O  
ANISOU 4581  O   HOH A1673    10071   4232   4031   -791     61     98       O  
HETATM 4582  O   HOH A1674      27.833   9.535   1.853  1.00 65.86           O  
ANISOU 4582  O   HOH A1674    10611   6093   8320  -2667  -2192   2744       O  
HETATM 4583  O   HOH A1675      -0.076  12.720  14.922  1.00 44.59           O  
ANISOU 4583  O   HOH A1675     7917   4407   4618    -61  -2053  -1404       O  
HETATM 4584  O   HOH A1676      51.669  28.042  16.764  1.00 48.58           O  
ANISOU 4584  O   HOH A1676     6801   5940   5718    653   -327   -294       O  
HETATM 4585  O   HOH A1677      40.372 -13.678  39.296  1.00 69.06           O  
ANISOU 4585  O   HOH A1677     6323  10286   9631  -4110   -251    947       O  
HETATM 4586  O   HOH A1678      13.354  10.724  12.567  1.00 60.34           O  
ANISOU 4586  O   HOH A1678     6427   7602   8896  -1372  -1699   1099       O  
HETATM 4587  O   HOH A1679      29.418  10.586  -1.103  1.00 66.85           O  
ANISOU 4587  O   HOH A1679     8730   8436   8236   1186    -84   -781       O  
HETATM 4588  O   HOH A1680      43.911  11.359 -12.939  1.00 43.68           O  
ANISOU 4588  O   HOH A1680     6249   4842   5507   -483    964    295       O  
HETATM 4589  O   HOH A1681      10.745  35.346  40.093  0.50 30.53           O  
ANISOU 4589  O   HOH A1681     2333   5141   4127    634   -750  -1111       O  
HETATM 4590  O   HOH A1684      43.602   2.379   7.831  1.00 54.21           O  
ANISOU 4590  O   HOH A1684     6669   8789   5140  -1696   2944  -1479       O  
HETATM 4591  O   HOH A1685      36.540   4.620  -8.776  1.00 45.71           O  
ANISOU 4591  O   HOH A1685     5956   6760   4650    -10   1532      6       O  
HETATM 4592  O   HOH A1686      23.194 -10.600   9.199  1.00 52.22           O  
ANISOU 4592  O   HOH A1686     6541   6346   6954    944   -266   -182       O  
HETATM 4593  O   HOH A1688      41.660  -1.718  12.866  1.00 54.65           O  
ANISOU 4593  O   HOH A1688     7426   7602   5735   3696  -1674  -3160       O  
HETATM 4594  O   HOH A1689      25.808  24.840  12.965  1.00 61.20           O  
ANISOU 4594  O   HOH A1689     4541  10081   8632   3478   1086  -1524       O  
HETATM 4595  O   HOH A1690      48.512  42.886  30.771  1.00 48.56           O  
ANISOU 4595  O   HOH A1690     8662   4426   5360   1997   -767   -724       O  
HETATM 4596  O   HOH A1691       1.104  34.622   5.430  1.00 53.60           O  
ANISOU 4596  O   HOH A1691     7197   6537   6629   2214  -1748    703       O  
HETATM 4597  O   HOH A1692      37.229  39.126  11.969  1.00 46.20           O  
ANISOU 4597  O   HOH A1692     5761   4555   7239   -405  -2478    277       O  
HETATM 4598  O   HOH A1694      12.970  20.599   6.072  0.50 44.50           O  
ANISOU 4598  O   HOH A1694     5505   4635   6768  -2306   -671   -540       O  
HETATM 4599  O   HOH A1695      34.131  29.892  18.924  1.00 53.85           O  
ANISOU 4599  O   HOH A1695     6788   8655   5020    978  -1253   -522       O  
HETATM 4600  O   HOH A1696      -0.136  36.176   8.378  0.50 34.34           O  
ANISOU 4600  O   HOH A1696     3662   3955   5430    986  -1370   -255       O  
HETATM 4601  O   HOH A1697      55.942  16.351  23.887  1.00 63.50           O  
ANISOU 4601  O   HOH A1697     3943  10757   9426   1427   2857  -2509       O  
HETATM 4602  O   HOH A1698      56.368  38.420  25.685  0.50 54.55           O  
ANISOU 4602  O   HOH A1698     6548   6771   7409    205   -242     49       O  
HETATM 4603  O   HOH A1699       1.481  36.963  27.519  1.00 41.07           O  
ANISOU 4603  O   HOH A1699     4233   6705   4666   1387   1238     54       O  
HETATM 4604  O   HOH A1700      39.178  41.679  13.788  1.00 46.43           O  
ANISOU 4604  O   HOH A1700     5134   5313   7194   2337   1288   1717       O  
HETATM 4605  O   HOH A1701      42.463  -6.538  27.717  0.50 45.16           O  
ANISOU 4605  O   HOH A1701     5336   6123   5699   1854    567  -2066       O  
HETATM 4606  O   HOH A1702      15.733  12.008  -4.468  0.50 31.02           O  
ANISOU 4606  O   HOH A1702     2601   4244   4941    187    101    804       O  
HETATM 4607  O   HOH A1703      51.805   8.452  -3.737  1.00 51.09           O  
ANISOU 4607  O   HOH A1703     6263   7614   5535    764     84   1365       O  
HETATM 4608  O   HOH A1704      25.993 -11.472  30.983  1.00 50.55           O  
ANISOU 4608  O   HOH A1704     6842   5481   6884   -765   -916   -176       O  
HETATM 4609  O   HOH A1705      14.924  40.779  38.259  1.00 57.06           O  
ANISOU 4609  O   HOH A1705     7975   7927   5777   2439    375  -2848       O  
HETATM 4610  O   HOH A1706      34.914  -7.644  26.950  0.50 49.90           O  
ANISOU 4610  O   HOH A1706     6468   6011   6481    832   -709   -812       O  
HETATM 4611  O   HOH A1709      47.116  13.803   6.768  1.00 46.27           O  
ANISOU 4611  O   HOH A1709     2528   8404   6649    131    272  -3033       O  
HETATM 4612  O   HOH A1710       7.562  35.306   4.386  1.00 48.26           O  
ANISOU 4612  O   HOH A1710     6300   6802   5235  -1912     92   2831       O  
HETATM 4613  O   HOH A1711       8.363  24.761   5.420  1.00 46.65           O  
ANISOU 4613  O   HOH A1711     2994   9680   5052    127   1327   -226       O  
HETATM 4614  O   HOH A1712      48.009   6.669   9.632  1.00 66.88           O  
ANISOU 4614  O   HOH A1712     7126   9464   8821    143   -296    554       O  
HETATM 4615  O   HOH A1715      41.971  42.015  11.327  1.00 83.53           O  
ANISOU 4615  O   HOH A1715    10368  10392  10978  -2006    446   1723       O  
HETATM 4616  O   HOH A1716      19.027  31.714  33.531  1.00 31.33           O  
ANISOU 4616  O   HOH A1716     2478   4096   5331   -401    991  -1209       O  
HETATM 4617  O   HOH A1717      11.934  32.231  41.074  1.00 78.38           O  
ANISOU 4617  O   HOH A1717    11778   8706   9296   1813    208  -1665       O  
HETATM 4618  O   HOH A1718      51.594   1.985  -4.263  0.50 41.73           O  
ANISOU 4618  O   HOH A1718     5773   5574   4510   -837   1156     80       O  
HETATM 4619  O   HOH A1719      55.552  23.388  23.095  1.00 62.84           O  
ANISOU 4619  O   HOH A1719     6568   8664   8647  -1608   1159   1324       O  
HETATM 4620  O   HOH A1720      40.746 -14.287  41.817  1.00 69.64           O  
ANISOU 4620  O   HOH A1720     9251   8518   8692    417    224   -717       O  
HETATM 4621  O   HOH A1722      53.208  36.346  18.765  1.00 59.19           O  
ANISOU 4621  O   HOH A1722     6196   9204   7089  -2596   1026   2566       O  
HETATM 4622  O   HOH A1723       6.467  14.735   6.099  0.50 47.82           O  
ANISOU 4622  O   HOH A1723     7089   5103   5978   1091    910  -3027       O  
HETATM 4623  O   HOH A1724      -1.288  21.545   8.608  0.50 40.38           O  
ANISOU 4623  O   HOH A1724     6609   4355   4377    105   -986   -191       O  
HETATM 4624  O   HOH A1725      43.972  17.981  -1.307  1.00 63.46           O  
ANISOU 4624  O   HOH A1725     5993   9727   8391  -1999   2024   1475       O  
HETATM 4625  O   HOH A1727      -2.949  37.432  21.857  1.00 47.45           O  
ANISOU 4625  O   HOH A1727     5363   6313   6352   -752   -669    689       O  
HETATM 4626  O   HOH A1728      35.459  33.114  14.439  0.50 35.86           O  
ANISOU 4626  O   HOH A1728     3094   7043   3487   1882    914   1042       O  
HETATM 4627  O   HOH A1729      48.343  39.530   8.444  1.00 61.61           O  
ANISOU 4627  O   HOH A1729     7908   7452   8049    145  -1435   1670       O  
HETATM 4628  O   HOH A1732      57.790  25.046  26.269  1.00 64.86           O  
ANISOU 4628  O   HOH A1732     5445   8847  10351   1942  -1311   -542       O  
HETATM 4629  O   HOH A1733      44.052   4.928   8.253  1.00 48.26           O  
ANISOU 4629  O   HOH A1733     4001   7146   7192    989   1046    176       O  
HETATM 4630  O   HOH A1735      37.998   8.844 -11.341  1.00 47.63           O  
ANISOU 4630  O   HOH A1735     5968   8142   3988   1710    997   -550       O  
HETATM 4631  O   HOH A1736      16.651   2.307  11.602  1.00 50.80           O  
ANISOU 4631  O   HOH A1736     2659   8025   8617   -153   -525   1002       O  
HETATM 4632  O   HOH A1737      16.832  14.751   4.541  1.00 67.78           O  
ANISOU 4632  O   HOH A1737    11438   6792   7524   -588  -1780    184       O  
HETATM 4633  O   HOH A1739      42.528  -3.132   3.133  0.50 50.21           O  
ANISOU 4633  O   HOH A1739     5849   6258   6970   -416   -159    -64       O  
HETATM 4634  O   HOH A1740      14.810  14.475  40.460  0.50 35.51           O  
ANISOU 4634  O   HOH A1740     3967   5651   3874    478   1084    -15       O  
HETATM 4635  O   HOH A1741      27.467  39.959  19.231  0.50 47.08           O  
ANISOU 4635  O   HOH A1741     5076   7091   5721  -2474   1084   1934       O  
HETATM 4636  O   HOH A1742      27.865  34.437  17.429  0.50 48.72           O  
ANISOU 4636  O   HOH A1742     6817   7225   4469  -2950    955   3149       O  
HETATM 4637  O   HOH A1743      34.241  36.844  22.130  1.00 44.71           O  
ANISOU 4637  O   HOH A1743     6954   4217   5819   -699   -881   -116       O  
HETATM 4638  O   HOH A1744      54.113  22.011  33.702  1.00 26.48           O  
ANISOU 4638  O   HOH A1744     2665   4532   2866    750   -274   -674       O  
HETATM 4639  O   HOH A1745      24.986  43.193  22.965  1.00 57.56           O  
ANISOU 4639  O   HOH A1745     6745   8503   6623  -2243    858   1751       O  
HETATM 4640  O   HOH A1746      30.438  22.079  15.415  0.50 39.48           O  
ANISOU 4640  O   HOH A1746     3106   6756   5138   2231    479     -9       O  
HETATM 4641  O   HOH A1747      21.190  -7.022  35.129  0.50 34.09           O  
ANISOU 4641  O   HOH A1747     4398   3351   5202   -900    955    556       O  
HETATM 4642  O   HOH A1749      37.300  -5.399   0.363  0.50 38.24           O  
ANISOU 4642  O   HOH A1749     2271   7017   5243   1029   1983   1009       O  
HETATM 4643  O   HOH A1750      -3.578  14.874  27.077  1.00 61.51           O  
ANISOU 4643  O   HOH A1750     7574   7663   8134   3557   -247  -2217       O  
HETATM 4644  O   HOH A1751      -7.978  17.837  25.028  0.50 42.96           O  
ANISOU 4644  O   HOH A1751     6052   5291   4978  -2937     52   1968       O  
HETATM 4645  O   HOH A1752      26.781  31.905  12.928  1.00 68.90           O  
ANISOU 4645  O   HOH A1752     8965   8045   9170   2511   -438  -1026       O  
HETATM 4646  O   HOH A1753       6.430  15.379  11.345  1.00 54.05           O  
ANISOU 4646  O   HOH A1753     5837   7169   7531   1767  -1219    159       O  
HETATM 4647  O   HOH A1754      34.638  -9.460  -3.428  1.00 73.32           O  
ANISOU 4647  O   HOH A1754     7696  10988   9176  -1988    122    752       O  
HETATM 4648  O   HOH A1756      51.700  21.154  19.267  1.00 63.28           O  
ANISOU 4648  O   HOH A1756     8798   8436   6811   -906    153  -1233       O  
HETATM 4649  O   HOH A1757      25.665  -9.368  17.000  1.00 47.60           O  
ANISOU 4649  O   HOH A1757     6796   4410   6878     75   -410  -1247       O  
HETATM 4650  O   HOH A1759      15.100   4.291  14.953  0.50 38.39           O  
ANISOU 4650  O   HOH A1759     4395   4408   5785  -1501   -955    815       O  
HETATM 4651  O   HOH A1760      33.456  25.249  19.402  1.00 34.88           O  
ANISOU 4651  O   HOH A1760     3633   4738   4882   -313    111    168       O  
HETATM 4652  O   HOH A1764      56.049   8.809  23.161  0.50 42.07           O  
ANISOU 4652  O   HOH A1764     3702   6680   5601  -1786   1269  -1686       O  
HETATM 4653  O   HOH A1766      48.043  35.617   8.407  0.50 36.58           O  
ANISOU 4653  O   HOH A1766     5241   4319   4337    894    511  -1385       O  
HETATM 4654  O   HOH A1767      30.118 -12.742   2.779  1.00 60.30           O  
ANISOU 4654  O   HOH A1767     7870   7532   7511  -1998  -1570   -392       O  
HETATM 4655  O   HOH A1768      -1.022  10.504  24.436  1.00 51.77           O  
ANISOU 4655  O   HOH A1768     7339   4537   7794  -2321    682   -222       O  
HETATM 4656  O   HOH A1770      23.702  24.695  10.760  1.00 62.06           O  
ANISOU 4656  O   HOH A1770     6484  10491   6603    182   3311  -3918       O  
HETATM 4657  O   HOH A1772      33.674  31.986  18.094  0.50 37.55           O  
ANISOU 4657  O   HOH A1772     2324   6481   5461    146    358   -772       O  
HETATM 4658  O   HOH A1773      36.876 -10.254  23.768  1.00 66.78           O  
ANISOU 4658  O   HOH A1773     7380   8620   9373  -3882    -61   1183       O  
HETATM 4659  O   HOH A1774       4.960  29.019  41.908  1.00 53.24           O  
ANISOU 4659  O   HOH A1774     4836   9901   5493   -997   1979   -646       O  
HETATM 4660  O   HOH A1775      43.080  11.365 -10.187  1.00 39.87           O  
ANISOU 4660  O   HOH A1775     4955   5318   4874   -626     18    476       O  
HETATM 4661  O   HOH A1777      31.193  -8.635  -4.446  1.00 63.57           O  
ANISOU 4661  O   HOH A1777     9527   8665   5962   1661     44  -2403       O  
HETATM 4662  O   HOH A1778      50.411   8.236  17.963  0.50 29.55           O  
ANISOU 4662  O   HOH A1778     3099   5031   3098    367    666     17       O  
HETATM 4663  O   HOH A1779      49.821   7.901  22.344  1.00 60.87           O  
ANISOU 4663  O   HOH A1779     7086   7300   8742  -3202     75   1457       O  
HETATM 4664  O   HOH A1780      19.373  47.068  37.543  0.50 37.82           O  
ANISOU 4664  O   HOH A1780     5043   4509   4818   -988    738    371       O  
HETATM 4665  O   HOH A1783      24.748  34.353  16.845  0.50 34.86           O  
ANISOU 4665  O   HOH A1783     3438   4617   5189   1954    858    345       O  
HETATM 4666  O   HOH A1784      -5.831  27.113   4.592  0.50 35.05           O  
ANISOU 4666  O   HOH A1784     3125   5384   4809    205    131  -1076       O  
HETATM 4667  O   HOH A1785      55.786  23.802  32.165  0.50 36.04           O  
ANISOU 4667  O   HOH A1785     4692   4252   4752   2898   -480  -1106       O  
HETATM 4668  O   HOH A1788      38.694  -2.754  21.236  0.50 32.26           O  
ANISOU 4668  O   HOH A1788     3667   4492   4098    821    273   -254       O  
HETATM 4669  O   HOH A1790      35.446  36.956  27.025  0.50 31.88           O  
ANISOU 4669  O   HOH A1790     3727   3019   5365   -566   -452   1099       O  
HETATM 4670  O   HOH A1793      22.251  42.866  29.539  0.50 38.68           O  
ANISOU 4670  O   HOH A1793     5044   4922   4729   -707  -1065    898       O  
HETATM 4671  O   HOH A1794      43.021   5.863  29.125  1.00 32.84           O  
ANISOU 4671  O   HOH A1794     2486   4079   5913    588    945    223       O  
HETATM 4672  O   HOH A1796      10.510   5.910  22.070  0.50 31.89           O  
ANISOU 4672  O   HOH A1796     3521   3202   5395   1020   -393    -67       O  
HETATM 4673  O   HOH A1797      15.572   5.267   5.212  1.00 48.88           O  
ANISOU 4673  O   HOH A1797     4077   6438   8059   -446   1717   -679       O  
HETATM 4674  O   HOH A1798      -3.821  28.049  31.522  0.50 34.34           O  
ANISOU 4674  O   HOH A1798     5153   4973   2923  -1396   -793   -116       O  
HETATM 4675  O   HOH A1799      37.806  -5.921  19.599  0.50 29.66           O  
ANISOU 4675  O   HOH A1799     2530   4161   4580    771     17    127       O  
HETATM 4676  O   HOH A1800      36.787  -7.075  17.402  0.50 33.25           O  
ANISOU 4676  O   HOH A1800     4850   4329   3454   1306    456   -102       O  
HETATM 4677  O   HOH A1802      46.389  11.241  -9.065  0.50 35.91           O  
ANISOU 4677  O   HOH A1802     4341   3275   6030   -368   -723   1507       O  
HETATM 4678  O   HOH A1803      -5.608  24.755   9.309  1.00 52.05           O  
ANISOU 4678  O   HOH A1803     4898   8179   6699    433    426  -2329       O  
HETATM 4679  O   HOH A1807      38.143 -12.532  32.502  0.50 44.54           O  
ANISOU 4679  O   HOH A1807     5731   6022   5169    541   -278    349       O  
HETATM 4680  O   HOH A1808      42.570  38.942   9.191  0.50 42.80           O  
ANISOU 4680  O   HOH A1808     7143   4469   4651   -876  -1575    393       O  
HETATM 4681  O   HOH A1816      19.723  -7.308  10.666  0.50 60.81           O  
ANISOU 4681  O   HOH A1816     8115   7113   7876    -51   -648    556       O  
HETATM 4682  O   HOH A1817      56.342  35.224  26.536  0.50 48.23           O  
ANISOU 4682  O   HOH A1817     3933   8525   5868  -1690   2131   1199       O  
HETATM 4683  O   HOH A1821      39.179  40.499  33.803  0.50 45.46           O  
ANISOU 4683  O   HOH A1821     4904   5527   6843   2278   1202  -1202       O  
HETATM 4684  O   HOH A1823       5.608  24.318  41.872  0.50 44.69           O  
ANISOU 4684  O   HOH A1823     7040   5668   4272   -481    600    650       O  
HETATM 4685  O   HOH A1827      34.753 -12.225  28.485  0.50 45.60           O  
ANISOU 4685  O   HOH A1827     3655   7722   5949   1015  -1025  -1211       O  
HETATM 4686  O   HOH A1828      49.550  20.678  17.257  0.50 38.87           O  
ANISOU 4686  O   HOH A1828     3137   5103   6530   1022    927  -1539       O  
HETATM 4687  O   HOH A2095      23.521   9.401  13.130  1.00 14.53           O  
ANISOU 4687  O   HOH A2095     2064   1854   1604   -222    579   -345       O  
HETATM 4688  O  AHOH A2125      35.497  16.598  10.160  0.44 21.59           O  
ANISOU 4688  O  AHOH A2125     4201   1959   2044   -544   -665    401       O  
HETATM 4689  O  BHOH A2125      35.230  16.937  10.002  0.56 16.44           O  
ANISOU 4689  O  BHOH A2125     1615   2435   2198     53    298    193       O  
HETATM 4690  O   HOH A2182      32.176  10.580   5.737  1.00 20.86           O  
ANISOU 4690  O   HOH A2182     2486   3175   2264    109    742    -52       O  
HETATM 4691  O  AHOH A2212      31.983   9.515   3.177  0.46 11.66           O  
ANISOU 4691  O  AHOH A2212     1319   1563   1548    230    283      9       O  
HETATM 4692  O  BHOH A2212      32.550   9.213   4.075  0.54 16.22           O  
ANISOU 4692  O  BHOH A2212     1846   2613   1702    441    718      8       O  
HETATM 4693  O  AHOH A2252      43.622  25.923  14.238  0.79 23.44           O  
ANISOU 4693  O  AHOH A2252     3229   3453   2223   1166    920    518       O  
HETATM 4694  O  BHOH A2252      42.511  24.755  12.613  0.21 15.28           O  
ANISOU 4694  O  BHOH A2252     1454   2338   2014   -319    237    184       O  
HETATM 4695  O  AHOH A2325      49.052  22.366  15.748  0.74 26.78           O  
ANISOU 4695  O  AHOH A2325     1207   4957   4012  -1300    -36   1435       O  
HETATM 4696  O  BHOH A2325      48.088  21.284  14.542  0.26 20.48           O  
ANISOU 4696  O  BHOH A2325     1144   2983   3656   -471    194   -150       O  
HETATM 4697  O  AHOH A2378      20.866  28.063  31.371  0.37  9.56           O  
ANISOU 4697  O  AHOH A2378      863   1785    984    124    306     -9       O  
HETATM 4698  O  BHOH A2378      20.907  28.383  31.930  0.63 23.44           O  
ANISOU 4698  O  BHOH A2378     1432   3877   3598     97    219    -91       O  
HETATM 4699  O  AHOH A2379      23.451  26.070  29.819  0.37 13.69           O  
ANISOU 4699  O  AHOH A2379     1453   2228   1520    427    270    166       O  
HETATM 4700  O  BHOH A2379      22.117  26.145  29.892  0.63 10.94           O  
ANISOU 4700  O  BHOH A2379      992   1793   1371    273    193   -137       O  
HETATM 4701  O  AHOH A2464      39.966   9.372  34.212  0.62 29.19           O  
ANISOU 4701  O  AHOH A2464     3843   3688   3559    216   -246   -834       O  
HETATM 4702  O  BHOH A2464      38.655  10.836  34.252  0.38 21.22           O  
ANISOU 4702  O  BHOH A2464     1701   3236   3125   -977   -365    558       O  
HETATM 4703  O  AHOH A2505      33.718  18.696  13.165  0.44 19.61           O  
ANISOU 4703  O  AHOH A2505     2040   2447   2962    430    255   -306       O  
HETATM 4704  O  BHOH A2505      30.101  18.053  11.677  0.56 38.89           O  
ANISOU 4704  O  BHOH A2505     6257   4934   3586   -119    430    512       O  
HETATM 4705  O   HOH A2513      33.178  17.559  10.831  1.00 60.70           O  
ANISOU 4705  O   HOH A2513    10027   7307   5728  -2343      6   3057       O  
HETATM 4706  O  AHOH A2516      41.166  21.425  11.763  0.55 20.15           O  
ANISOU 4706  O  AHOH A2516     2438   3466   1753   -278    718   -218       O  
HETATM 4707  O  BHOH A2516      41.177  21.260   9.949  0.45 23.36           O  
ANISOU 4707  O  BHOH A2516     3105   2150   3621    -70    436     47       O  
HETATM 4708  O  AHOH A2545      49.160  29.551  33.465  0.20 52.79           O  
ANISOU 4708  O  AHOH A2545     4456   1665  13935    739  -5104    865       O  
HETATM 4709  O  BHOH A2545      52.007  35.064  32.311  0.80 29.20           O  
ANISOU 4709  O  BHOH A2545     2586   3497   5010     45    232     69       O  
HETATM 4710  O  AHOH A2552      11.023   0.880  31.881  0.72 27.90           O  
ANISOU 4710  O  AHOH A2552     3779   3424   3398   -530    994    393       O  
HETATM 4711  O  BHOH A2552      12.593   0.640  30.749  0.28 22.40           O  
ANISOU 4711  O  BHOH A2552     1242   4013   3258   -564    623  -1094       O  
HETATM 4712  O  AHOH A2569      38.176   8.156  20.414  0.62 20.37           O  
ANISOU 4712  O  AHOH A2569     2276   3132   2330    826   -316  -1012       O  
HETATM 4713  O  BHOH A2569      40.147   7.249  20.358  0.38 16.80           O  
ANISOU 4713  O  BHOH A2569     1405   3840   1138   -644    824   -509       O  
HETATM 4714  O  AHOH A2594      16.302  10.361  10.240  0.44 19.44           O  
ANISOU 4714  O  AHOH A2594     2652   2726   2010   -787   -194   -272       O  
HETATM 4715  O  BHOH A2594      17.307   9.680   8.946  0.56 26.52           O  
ANISOU 4715  O  BHOH A2594     2038   4301   3736    -37     87   -408       O  
HETATM 4716  O  AHOH A2600      17.229   2.320  -3.810  0.56 35.03           O  
ANISOU 4716  O  AHOH A2600     4821   5258   3231   -496    119  -2119       O  
HETATM 4717  O  BHOH A2600      18.044   4.218   0.146  0.44 24.77           O  
ANISOU 4717  O  BHOH A2600     1462   4928   3023    -85     80    511       O  
HETATM 4718  O  AHOH A2629      27.928  15.080  10.648  0.42 19.64           O  
ANISOU 4718  O  AHOH A2629     2019   2843   2602    -81    328   -229       O  
HETATM 4719  O  BHOH A2629      29.605  13.892  10.729  0.58 19.25           O  
ANISOU 4719  O  BHOH A2629     1987   2232   3095   -250    228   -650       O  
HETATM 4720  O  AHOH A2635      23.469  28.406  31.195  0.37 20.41           O  
ANISOU 4720  O  AHOH A2635     1938   2685   3134    360   -590   -578       O  
HETATM 4721  O  BHOH A2635      24.381  27.421  30.829  0.63 13.87           O  
ANISOU 4721  O  BHOH A2635      985   2148   2138     68    300   -477       O  
HETATM 4722  O  AHOH A2669      35.325   3.447  34.749  0.52 37.14           O  
ANISOU 4722  O  AHOH A2669     1053   7438   5621   -272   -344   -609       O  
HETATM 4723  O  AHOH A2683      20.050  26.476  -1.618  0.70 44.37           O  
ANISOU 4723  O  AHOH A2683     7868   4802   4190  -2101   3375  -1318       O  
HETATM 4724  O  BHOH A2683      19.819  27.520  -2.376  0.29 46.66           O  
ANISOU 4724  O  BHOH A2683     8848   4187   4696  -2851   2628  -1384       O  
HETATM 4725  O  AHOH A2707      10.645  17.670   9.521  0.54 40.12           O  
ANISOU 4725  O  AHOH A2707     5416   4433   5393   2338  -3404  -2772       O  
HETATM 4726  O  BHOH A2707      11.485  18.696   8.472  0.46 29.34           O  
ANISOU 4726  O  BHOH A2707     3012   5714   2422   1480   -123  -2268       O  
HETATM 4727  O  AHOH A2713      50.926  35.771  36.552  0.42 24.59           O  
ANISOU 4727  O  AHOH A2713     2352   3388   3603   -789    595    911       O  
HETATM 4728  O  BHOH A2713      52.665  36.348  34.454  0.58 31.82           O  
ANISOU 4728  O  BHOH A2713     3302   4269   4520    -96    411  -1577       O  
HETATM 4729  O   HOH A2714      14.543  46.183  29.667  0.65 26.69           O  
ANISOU 4729  O   HOH A2714     4202   2002   3938   -654   1050   -486       O  
HETATM 4730  O   HOH A2730      37.531  -2.053  25.500  0.52 32.17           O  
ANISOU 4730  O   HOH A2730     4414   3340   4469   1203  -2292  -1511       O  
HETATM 4731  O  AHOH A2734      -3.670  34.816  25.212  0.61 32.72           O  
ANISOU 4731  O  AHOH A2734     1367   3548   7517   -118    -45   -524       O  
HETATM 4732  O  BHOH A2734      -3.574  34.582  26.975  0.39 21.53           O  
ANISOU 4732  O  BHOH A2734     1433   2741   4005    522    551  -1010       O  
HETATM 4733  O   HOH A2748      18.730  29.005  -0.798  0.70 32.48           O  
ANISOU 4733  O   HOH A2748     3658   5518   3165  -2020    436    547       O  
HETATM 4734  O   HOH A2755      22.623  32.022  30.041  0.67 32.26           O  
ANISOU 4734  O   HOH A2755     2744   3309   6203   -168   1113  -1498       O  
HETATM 4735  O  AHOH A2758       2.667  23.453   4.435  0.38 55.75           O  
ANISOU 4735  O  AHOH A2758    10737   9402   1043  -5778  -1703    974       O  
HETATM 4736  O  BHOH A2758       0.676  23.380   5.087  0.62 34.40           O  
ANISOU 4736  O  BHOH A2758     3063   6983   3024     42   -463  -1099       O  
HETATM 4737  O  AHOH A2763      35.429  26.087  14.771  0.37 25.26           O  
ANISOU 4737  O  AHOH A2763     3046   2570   3982    406    605    -82       O  
HETATM 4738  O  BHOH A2763      36.988  26.169  12.696  0.63 33.43           O  
ANISOU 4738  O  BHOH A2763     5490   3076   4137   -751   -448    921       O  
HETATM 4739  O  AHOH A2781      42.396  18.084   7.465  0.44 23.49           O  
ANISOU 4739  O  AHOH A2781     3815   3163   1947    328   1182   -330       O  
HETATM 4740  O  BHOH A2781      41.838  18.109   5.436  0.56 35.78           O  
ANISOU 4740  O  BHOH A2781     3512   5501   4582   -915    349    691       O  
HETATM 4741  O  AHOH A2792      16.005  -4.825  26.540  0.57 26.11           O  
ANISOU 4741  O  AHOH A2792     2691   2643   4585    440   -343   -682       O  
HETATM 4742  O  BHOH A2792      18.730  -6.135  24.059  0.43 22.21           O  
ANISOU 4742  O  BHOH A2792     2743   3629   2065    765   1103   -303       O  
HETATM 4743  O  AHOH A2795      17.282  19.348  34.577  0.33 36.60           O  
ANISOU 4743  O  AHOH A2795     1403   9327   3176  -1289      8   3896       O  
HETATM 4744  O  BHOH A2795      15.099  19.902  36.250  0.67 23.92           O  
ANISOU 4744  O  BHOH A2795     2362   3587   3139   -230     22    415       O  
HETATM 4745  O  BHOH A2800      19.700  14.704  32.805  0.59 67.10           O  
ANISOU 4745  O  BHOH A2800    10749   6685   8062  -2776  -4550   -852       O  
HETATM 4746  O  AHOH A2824      36.982   0.892  34.872  0.52 33.26           O  
ANISOU 4746  O  AHOH A2824     5020   3968   3651  -1019    448   -203       O  
HETATM 4747  O  BHOH A3004      32.099  17.556   4.077  1.00 33.91           O  
ANISOU 4747  O  BHOH A3004     3994   5477   3412    350    865     56       O  
HETATM 4748  O  BHOH A3010      17.704  11.052  37.939  1.00 37.93           O  
ANISOU 4748  O  BHOH A3010     2589   6997   4823   1163    469   -866       O  
HETATM 4749  O  BHOH A3013      16.431  42.281  16.185  1.00 35.47           O  
ANISOU 4749  O  BHOH A3013     5147   3185   5146  -1168     89    918       O  
HETATM 4750  O  BHOH A3015      12.366  40.598   9.779  1.00 47.58           O  
ANISOU 4750  O  BHOH A3015     8057   4916   5105   -498   -946    640       O  
HETATM 4751  O  BHOH A3023      50.795  30.838  11.782  1.00 41.98           O  
ANISOU 4751  O  BHOH A3023     2947   7727   5275   -219    754    846       O  
HETATM 4752  O  BHOH A3026      13.940   6.572  17.725  1.00 47.42           O  
ANISOU 4752  O  BHOH A3026     2638   8905   6473  -1139    -75   1063       O  
HETATM 4753  O  BHOH A3032      28.773  26.018  20.367  1.00 48.69           O  
ANISOU 4753  O  BHOH A3032     6805   7107   4586  -1161  -1535    979       O  
HETATM 4754  O  BHOH A3036      31.075  19.633  18.184  1.00 37.04           O  
ANISOU 4754  O  BHOH A3036     2987   5993   5092    189    522    951       O  
HETATM 4755  O  BHOH A3101      14.527  24.109  33.673  1.00 15.71           O  
ANISOU 4755  O  BHOH A3101     1590   2030   2348    118    300    276       O  
HETATM 4756  O  BHOH A3103      14.791  17.547  37.232  1.00 34.31           O  
ANISOU 4756  O  BHOH A3103     2817   4566   5653   -660  -1157    737       O  
HETATM 4757  O  BHOH A3107      14.311  24.248  36.348  1.00 32.09           O  
ANISOU 4757  O  BHOH A3107     5479   3566   3148  -1981   -115    711       O  
HETATM 4758  O  BHOH A3209      47.585  11.054  20.535  1.00 45.98           O  
ANISOU 4758  O  BHOH A3209     4659   5149   7663   1345   -382   1278       O  
HETATM 4759  O  BHOH A3211      49.968  10.257  -2.462  1.00 49.02           O  
ANISOU 4759  O  BHOH A3211     7849   5829   4947  -1495  -1550    414       O  
HETATM 4760  O  BHOH A3230      21.100  13.639  -3.196  1.00 54.08           O  
ANISOU 4760  O  BHOH A3230     5887   6543   8118   -396   -606    -50       O  
HETATM 4761  O  BHOH A3231      51.905  31.773  14.000  1.00 43.59           O  
ANISOU 4761  O  BHOH A3231     6012   5589   4962    861   1218   -484       O  
HETATM 4762  O  BHOH A3239      15.749  -4.511  24.355  0.43 29.50           O  
ANISOU 4762  O  BHOH A3239     4349   3506   3353  -2114    173    755       O  
HETATM 4763  O   HOH A3301      16.927  22.173  35.415  1.00 58.09           O  
ANISOU 4763  O   HOH A3301     7711   7740   6622    736   -966    800       O  
HETATM 4764  O   HOH A3302      22.179  12.439  33.056  1.00 62.31           O  
ANISOU 4764  O   HOH A3302    10526   7137   6013  -2113  -2372   -670       O  
HETATM 4765  O   HOH A3303      34.590  -8.566   8.182  1.00 65.18           O  
ANISOU 4765  O   HOH A3303    11326   6116   7323    177   -728    535       O  
HETATM 4766  O   HOH A3304      14.554  20.492  38.398  1.00 67.82           O  
ANISOU 4766  O   HOH A3304     8564   9214   7990   -884  -1387   1127       O  
HETATM 4767  O   HOH A3305      18.270  14.827  36.225  1.00 68.56           O  
ANISOU 4767  O   HOH A3305     9670   7119   9260    619  -1324  -1796       O  
HETATM 4768  O   HOH A3306      10.702  10.562  17.834  1.00 55.24           O  
ANISOU 4768  O   HOH A3306     4280   8787   7922    920    878   -466       O  
HETATM 4769  O   HOH A3307      -6.225  38.945  20.022  1.00 65.77           O  
ANISOU 4769  O   HOH A3307     7818   8231   8941   2915   -339  -1317       O  
HETATM 4770  O   HOH A3308      12.553  42.870  16.080  1.00 58.18           O  
ANISOU 4770  O   HOH A3308     9217   6338   6550   3767   -846  -1000       O  
HETATM 4771  O   HOH A3309      16.684  12.248  40.127  1.00 50.47           O  
ANISOU 4771  O   HOH A3309     4985   8352   5840    656   -294   -809       O  
HETATM 4772  O   HOH A3310       2.129  40.270  12.697  1.00 66.21           O  
ANISOU 4772  O   HOH A3310     7902   8667   8587    624  -1941   -362       O  
HETATM 4773  O   HOH A3311      27.939   6.681  -7.923  1.00 66.40           O  
ANISOU 4773  O   HOH A3311     8193  10231   6806  -1504    476   1104       O  
HETATM 4774  O   HOH A3312      18.084  34.648  35.964  1.00 61.11           O  
ANISOU 4774  O   HOH A3312     6286   8973   7962    918  -1386    278       O  
HETATM 4775  O   HOH A3313      55.360  17.048  30.877  1.00 60.26           O  
ANISOU 4775  O   HOH A3313     8563   6894   7439    568  -1269   -386       O  
HETATM 4776  O   HOH A3314      16.215  38.381  35.775  1.00 73.60           O  
ANISOU 4776  O   HOH A3314     9725   9013   9227   -765   -531    364       O  
HETATM 4777  O   HOH A3315      38.836  24.147   9.540  1.00 53.30           O  
ANISOU 4777  O   HOH A3315     6535   6416   7301   -207     -7   1709       O  
HETATM 4778  O   HOH A3316      -9.562  25.136  21.769  1.00 45.96           O  
ANISOU 4778  O   HOH A3316     4409   7353   5701  -1084    -13  -1400       O  
HETATM 4779  O   HOH A3317      52.241  11.115  -6.352  1.00105.39           O  
ANISOU 4779  O   HOH A3317    12507  14374  13161  -1089    907   -114       O  
HETATM 4780  O   HOH A3318       3.688  14.272  11.854  1.00 58.72           O  
ANISOU 4780  O   HOH A3318     9060   7667   5584   -524    480  -1607       O  
HETATM 4781  O   HOH A3319      37.555   7.724  34.537  1.00 85.12           O  
ANISOU 4781  O   HOH A3319    12426   9760  10155   1013  -1179   -435       O  
HETATM 4782  O   HOH A3320      -5.677  20.686  25.420  1.00 81.20           O  
ANISOU 4782  O   HOH A3320    11134   9422  10295  -1552  -1179    759       O  
HETATM 4783  O   HOH A3321       6.265   7.946  28.418  1.00 82.73           O  
ANISOU 4783  O   HOH A3321    11133   9012  11287    175  -2987     54       O  
HETATM 4784  O   HOH A3322      46.964  42.573  11.694  1.00 60.09           O  
ANISOU 4784  O   HOH A3322     7413   7189   8228  -1068   -467   2085       O  
HETATM 4785  O   HOH A3323      35.304  25.891  10.347  1.00 66.22           O  
ANISOU 4785  O   HOH A3323     7840   7959   9361   1846   -527   -253       O  
HETATM 4786  O   HOH A3324      22.561  -9.945  16.727  1.00 56.00           O  
ANISOU 4786  O   HOH A3324     6766   6915   7595   -677    802   -939       O  
HETATM 4787  O   HOH A3325      16.553  -1.576   6.253  1.00 59.52           O  
ANISOU 4787  O   HOH A3325     7297   7649   7670   -366   1503   -144       O  
HETATM 4788  O   HOH A3326       0.783  40.686  20.946  1.00 70.73           O  
ANISOU 4788  O   HOH A3326    10816   7469   8589   -683  -1886   -230       O  
HETATM 4789  O   HOH A3327      -1.725  37.180  19.211  1.00 57.16           O  
ANISOU 4789  O   HOH A3327     5255   6415  10047   2376   -915     15       O  
HETATM 4790  O   HOH A3328      39.891  28.591  10.294  1.00 46.12           O  
ANISOU 4790  O   HOH A3328     5212   7027   5283   -154    -56    849       O  
HETATM 4791  O   HOH A3329      22.923  43.600  17.072  1.00 66.10           O  
ANISOU 4791  O   HOH A3329     8309   8509   8299  -2979    993   1788       O  
HETATM 4792  O   HOH A3330      29.772 -12.418   9.202  1.00 72.36           O  
ANISOU 4792  O   HOH A3330    11715   7130   8650    739  -1965  -1125       O  
HETATM 4793  O   HOH A3331      -2.254  31.243   5.056  1.00 52.37           O  
ANISOU 4793  O   HOH A3331     3927   8062   7911    501  -1092   1220       O  
HETATM 4794  O   HOH A3332      43.399  45.475  20.325  1.00 77.15           O  
ANISOU 4794  O   HOH A3332     9022   9861  10430    343   -782   -433       O  
HETATM 4795  O   HOH A3333      40.386  -3.506   4.754  1.00108.01           O  
ANISOU 4795  O   HOH A3333    14018  13590  13432    222   -887    220       O  
HETATM 4796  O   HOH A3334      17.754  47.028  35.499  1.00 68.20           O  
ANISOU 4796  O   HOH A3334     9398   7174   9340     88  -1057   -431       O  
HETATM 4797  O   HOH A3335      26.486  28.986  12.899  1.00 66.69           O  
ANISOU 4797  O   HOH A3335     8647   8354   8338   1391    539    -73       O  
HETATM 4798  O   HOH A3336      40.661  32.062   8.115  1.00 78.48           O  
ANISOU 4798  O   HOH A3336    11084  10194   8539   -773   -521    565       O  
HETATM 4799  O   HOH A3440      50.192  13.819  -0.208  1.00 77.37           O  
ANISOU 4799  O   HOH A3440    10702   9571   9123  -1208   -247    306       O  
HETATM 4800  O   HOH A3441      47.984  15.682  -4.300  1.00 84.80           O  
ANISOU 4800  O   HOH A3441    11217  10678  10323  -2010   -390    406       O  
HETATM 4801  O   HOH A3442      39.155  -5.438  47.622  1.00 65.21           O  
ANISOU 4801  O   HOH A3442     7899   9083   7795   1570   -232   -416       O  
HETATM 4802  O   HOH A3443      -1.633  39.227  14.256  1.00 62.26           O  
ANISOU 4802  O   HOH A3443     6581   9352   7721   2635    274  -1411       O  
HETATM 4803  O   HOH A3444      23.833  42.680  19.135  1.00 63.35           O  
ANISOU 4803  O   HOH A3444     7580   8513   7979  -2069    368    937       O  
HETATM 4804  O   HOH A3445       1.988   9.765  27.540  1.00 90.62           O  
ANISOU 4804  O   HOH A3445    12590  10860  10981    205   -641   -196       O  
HETATM 4805  O   HOH A3446      43.729  17.727  -4.437  1.00 81.20           O  
ANISOU 4805  O   HOH A3446    11564   8834  10455    795  -1179   -215       O  
HETATM 4806  O   HOH A3447      40.357  47.370  19.214  1.00 77.70           O  
ANISOU 4806  O   HOH A3447    10681   7957  10886   -221  -1468   -758       O  
HETATM 4807  O   HOH A3448       7.538  24.965  40.283  1.00 71.10           O  
ANISOU 4807  O   HOH A3448    10604   8082   8330   -718  -1145    -14       O  
HETATM 4808  O   HOH A3449      33.767 -12.045   2.784  1.00 65.58           O  
ANISOU 4808  O   HOH A3449     9953   5688   9276   3322  -1179  -1634       O  
HETATM 4809  O   HOH A3540      47.422  16.884  -0.209  1.00 94.50           O  
ANISOU 4809  O   HOH A3540    12488  12006  11411    250   -628   -749       O  
HETATM 4810  O   HOH A3541      55.018  36.648  21.962  1.00 62.13           O  
ANISOU 4810  O   HOH A3541     7552   7913   8142  -2829    720   1194       O  
HETATM 4811  O   HOH A3542       2.854  18.075  41.259  1.00 75.57           O  
ANISOU 4811  O   HOH A3542     9513  10084   9115  -1686    783   1481       O  
HETATM 4812  O   HOH A3543      13.880  -2.133  17.434  1.00 80.64           O  
ANISOU 4812  O   HOH A3543    10335   9968  10338  -3486   -990    809       O  
HETATM 4813  O   HOH A3544      46.213   0.155  16.038  1.00 73.22           O  
ANISOU 4813  O   HOH A3544     8925   8779  10115   1808   -800  -1534       O  
HETATM 4814  O   HOH A3545      25.413   2.440  -8.472  1.00 68.70           O  
ANISOU 4814  O   HOH A3545     8428  10665   7011   -524   1979    691       O  
HETATM 4815  O   HOH A3600      52.944  39.640   9.396  1.00 74.11           O  
ANISOU 4815  O   HOH A3600     9947   9220   8993    726    317    863       O  
HETATM 4816  O   HOH A3621      -2.184  34.340   7.945  1.00 84.92           O  
ANISOU 4816  O   HOH A3621    11407  10800  10060    -32   -511    -33       O  
HETATM 4817  O   HOH A3667      44.896  22.408   9.222  1.00 78.16           O  
ANISOU 4817  O   HOH A3667    11485   9505   8707    723  -1231   -304       O  
HETATM 4818  O   HOH A3676      44.449  -2.704  16.712  1.00 74.58           O  
ANISOU 4818  O   HOH A3676    10212   8085  10038   2623  -1689  -1150       O  
HETATM 4819  O   HOH A3696      22.903  40.436  15.492  1.00 71.74           O  
ANISOU 4819  O   HOH A3696     8080  10796   8383  -1187   1140    782       O  
HETATM 4820  O  AHOH A9039      18.071   6.326   4.582  0.44 30.65           O  
ANISOU 4820  O  AHOH A9039     4690   3928   3028    635   1464   -872       O  
HETATM 4821  O   HOH A9040     -12.154  27.563  16.891  1.00 50.00           O  
HETATM 4822  O   HOH A9041      45.886  43.099  30.680  1.00 50.00           O  
HETATM 4823  O   HOH A9042      33.061  23.465  15.172  1.00 66.53           O  
ANISOU 4823  O   HOH A9042     9885   8392   7001   1244  -1842   -545       O  
HETATM 4824  O   HOH A9043      33.888  22.987  18.022  1.00 65.14           O  
ANISOU 4824  O   HOH A9043     9189   8251   7310    555  -1866   -902       O  
HETATM 4825  O   HOH A9044      36.396  24.717  17.621  1.00 46.44           O  
ANISOU 4825  O   HOH A9044     6898   4971   5776    303   -322   -965       O  
HETATM 4826  O   HOH A9045      40.194   0.044   2.175  1.00 53.11           O  
ANISOU 4826  O   HOH A9045     5608   9137   5435   1645   -174  -1146       O  
HETATM 4827  O   HOH A9046      42.097   2.121  -0.133  1.00 65.92           O  
ANISOU 4827  O   HOH A9046    11418   5582   8049    215  -2590   -486       O  
CONECT  305 3923                                                                
CONECT 3844 3845 3846 3847 3848                                                 
CONECT 3845 3844                                                                
CONECT 3846 3844                                                                
CONECT 3847 3844                                                                
CONECT 3848 3844                                                                
CONECT 3849 3850 3851 3852 3853                                                 
CONECT 3850 3849                                                                
CONECT 3851 3849                                                                
CONECT 3852 3849                                                                
CONECT 3853 3849                                                                
CONECT 3854 3855 3856 3857 3906                                                 
CONECT 3855 3854                                                                
CONECT 3856 3854                                                                
CONECT 3857 3854 3858                                                           
CONECT 3858 3857 3859                                                           
CONECT 3859 3858 3860 3861                                                      
CONECT 3860 3859 3865                                                           
CONECT 3861 3859 3862 3863                                                      
CONECT 3862 3861                                                                
CONECT 3863 3861 3864 3865                                                      
CONECT 3864 3863                                                                
CONECT 3865 3860 3863 3866                                                      
CONECT 3866 3865 3867 3875                                                      
CONECT 3867 3866 3868                                                           
CONECT 3868 3867 3869                                                           
CONECT 3869 3868 3870 3875                                                      
CONECT 3870 3869 3871 3872                                                      
CONECT 3871 3870                                                                
CONECT 3872 3870 3873                                                           
CONECT 3873 3872 3874                                                           
CONECT 3874 3873 3875                                                           
CONECT 3875 3866 3869 3874                                                      
CONECT 3876 3877 3893                                                           
CONECT 3877 3876 3878 3879                                                      
CONECT 3878 3877                                                                
CONECT 3879 3877 3880                                                           
CONECT 3880 3879 3881 3882                                                      
CONECT 3881 3880                                                                
CONECT 3882 3880 3883 3893                                                      
CONECT 3883 3882 3884                                                           
CONECT 3884 3883 3885 3891                                                      
CONECT 3885 3884 3886                                                           
CONECT 3886 3885 3887 3888                                                      
CONECT 3887 3886                                                                
CONECT 3888 3886 3889 3890                                                      
CONECT 3889 3888                                                                
CONECT 3890 3888 3891                                                           
CONECT 3891 3884 3890 3892                                                      
CONECT 3892 3891 3893 3894                                                      
CONECT 3893 3876 3882 3892                                                      
CONECT 3894 3892 3895                                                           
CONECT 3895 3894 3896 3897                                                      
CONECT 3896 3895                                                                
CONECT 3897 3895 3898 3899                                                      
CONECT 3898 3897                                                                
CONECT 3899 3897 3900 3901                                                      
CONECT 3900 3899                                                                
CONECT 3901 3899 3902                                                           
CONECT 3902 3901 3903                                                           
CONECT 3903 3902 3904 3905 3906                                                 
CONECT 3904 3903                                                                
CONECT 3905 3903                                                                
CONECT 3906 3854 3903                                                           
CONECT 3907 3908                                                                
CONECT 3908 3907 3909 3912                                                      
CONECT 3909 3908 3910 3911                                                      
CONECT 3910 3909                                                                
CONECT 3911 3909                                                                
CONECT 3912 3908 3913                                                           
CONECT 3913 3912 3914                                                           
CONECT 3914 3913 3915 3916                                                      
CONECT 3915 3914                                                                
CONECT 3916 3914 3917                                                           
CONECT 3917 3916 3918 3920 3921                                                 
CONECT 3918 3917 3919 3924                                                      
CONECT 3919 3918                                                                
CONECT 3920 3917 3922                                                           
CONECT 3921 3917 3923                                                           
CONECT 3922 3920                                                                
CONECT 3923  305 3921                                                           
CONECT 3924 3918 3925                                                           
CONECT 3925 3924 3926                                                           
CONECT 3926 3925 3927 3928                                                      
CONECT 3927 3926                                                                
CONECT 3928 3926                                                                
CONECT 3929 3930                                                                
CONECT 3930 3929 3931 3934                                                      
CONECT 3931 3930 3932 3933                                                      
CONECT 3932 3931                                                                
CONECT 3933 3931                                                                
CONECT 3934 3930 3935                                                           
CONECT 3935 3934 3936                                                           
CONECT 3936 3935 3937 3938                                                      
CONECT 3937 3936                                                                
CONECT 3938 3936                                                                
CONECT 3939 3940 3941                                                           
CONECT 3940 3939                                                                
CONECT 3941 3939 3942 3943                                                      
CONECT 3942 3941                                                                
CONECT 3943 3941 3944                                                           
CONECT 3944 3943                                                                
CONECT 3945 3946 3947                                                           
CONECT 3946 3945                                                                
CONECT 3947 3945 3948 3949                                                      
CONECT 3948 3947                                                                
CONECT 3949 3947 3950                                                           
CONECT 3950 3949                                                                
CONECT 3951 3952 3953                                                           
CONECT 3952 3951                                                                
CONECT 3953 3951 3954 3955                                                      
CONECT 3954 3953                                                                
CONECT 3955 3953 3956                                                           
CONECT 3956 3955                                                                
CONECT 3957 3958 3959                                                           
CONECT 3958 3957                                                                
CONECT 3959 3957 3960 3961                                                      
CONECT 3960 3959                                                                
CONECT 3961 3959 3962                                                           
CONECT 3962 3961                                                                
MASTER      352    0    9   16   23    0   29    6 4452    1  120   37          
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.