CNRS Nantes University UFIP UFIP
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***  1w1d  ***

elNémo ID: 1901302327198361

Job options:

ID        	=	 1901302327198361
JOBID     	=	 1w1d
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 1w1d

HEADER    TRANSFERASE                             21-JUN-04   1W1D              
TITLE     CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN HOMOLOGY (PH)                
TITLE    2 DOMAIN BOUND TO INOSITOL (1,3,4,5)-TETRAKISPHOSPHATE                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE-1;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PLECKSTRIN HOMOLOGY DOMAIN, RESIDUES 409-556;              
COMPND   5 SYNONYM: HPDK1;                                                      
COMPND   6 EC: 2.7.1.37;                                                        
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    TRANSFERASE, PDK1, PHOSPHOINOSITIDE DEPENDENT PROTEIN                 
KEYWDS   2 KINASE 1, PKB, PLECKSTRIN HOMOLOGY DOMAIN, INOSITOL                  
KEYWDS   3 PHOSPHATE, PHOSPHOINOSITIDE, SIGNAL TRANSDUCTION,                    
KEYWDS   4 PI3-KINASE, SERINE/THREONINE PROTEIN KINASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.KOMANDER,M.DEAK,D.R.ALESSI,D.M.F.VAN AALTEN                         
REVDAT   2   24-FEB-09 1W1D    1       VERSN                                    
REVDAT   1   19-NOV-04 1W1D    0                                                
JRNL        AUTH   D.KOMANDER,A.FAIRSERVICE,M.DEAK,G.S.KULAR,                   
JRNL        AUTH 2 A.R.PRESCOTT,C.P.DOWNES,S.T.SAFRANY,D.R.ALESSI,              
JRNL        AUTH 3 D.M.F.VAN AALTEN                                             
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE REGULATION OF PDK1 BY           
JRNL        TITL 2 PHOSPHOINOSITIDES AND INOSITOL PHOSPHATES                    
JRNL        REF    EMBO J.                       V.  23  3918 2004              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   15457207                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7600379                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   D.KOMANDER,M.DEAK,N.MORRICE,D.M.F.VAN AALTEN                 
REMARK   1  TITL   PURIFICATION, CRYSTALLISATION AND PRELIMINARY X-             
REMARK   1  TITL 2 RAY DIFFFRACTION OF A PROTEOLYTIC FRAGMENT OF                
REMARK   1  TITL 3 PDK1, CONTAINING THE PLECKSTRIN HOMOLOGY DOMAIN              
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  60   314 2004              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   14747709                                                     
REMARK   1  DOI    10.1107/S0907444903028518                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.5  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 22641                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.145                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 617                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1673                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 43                           
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1220                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 217                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.57000                                              
REMARK   3    B22 (A**2) : -0.64000                                             
REMARK   3    B33 (A**2) : -0.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.44000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.088         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.078         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.332         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1287 ; 0.020 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1113 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1746 ; 1.785 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2604 ; 0.958 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   142 ; 6.717 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   184 ; 0.131 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1376 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   267 ; 0.009 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   241 ; 0.217 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1308 ; 0.264 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   707 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   142 ; 0.162 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     5 ; 0.148 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    57 ; 0.273 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    36 ; 0.202 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   721 ; 1.657 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1169 ; 2.383 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   566 ; 3.225 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   577 ; 4.620 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. THE SIDE CHAINS OF SOME DISORDERED RESIDUES       
REMARK   3  WERE REFINED EITHER WITH THE OCCUPANCY SET TO 0.02, OR THE          
REMARK   3  RESIDUE WAS MUTATED TO ALA.                                         
REMARK   4                                                                      
REMARK   4 1W1D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-20190.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.861,1.040                        
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23341                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: RSPS,MLPHARE,DM                                       
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 0.41                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08 M MAGNESIUM ACETATE,                
REMARK 280  0.05M SODIUM CACODYLATE PH 6.5, 30 % PEG 4000                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.46100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   406                                                      
REMARK 465     PRO A   551                                                      
REMARK 465     ASP A   552                                                      
REMARK 465     ALA A   553                                                      
REMARK 465     ALA A   554                                                      
REMARK 465     VAL A   555                                                      
REMARK 465     GLN A   556                                                      
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     LEU A 408    CG   CD1  CD2                                       
REMARK 470     ASP A 420    CG   OD1  OD2                                       
REMARK 470     LYS A 509    CG   CD   CE   NZ                                   
REMARK 470     HIS A 550    CA   C    O    CB   CG   ND1  CD2  CE1  NE2         
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   CE1  HIS A   533  -  O    HOH A  2174              2.10            
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 433   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 464   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 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 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    ASN A 411       69.89     32.66                                   
REMARK 500    PHE A 470     -134.91   -127.46                                   
REMARK 500    ASN A 510     -160.73   -160.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  AU A1551                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4IP A1552                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1550                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1H1W   RELATED DB: PDB                                   
REMARK 900  HIGH RESOLUTION CRYSTAL STRUCTURE OF THE                            
REMARK 900  HUMAN PDK1 CATALYTIC DOMAIN                                         
REMARK 900 RELATED ID: 1OKY   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN                            
REMARK 900  COMPLEX WITH STAUROSPORINE                                          
REMARK 900 RELATED ID: 1OKZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN                            
REMARK 900  COMPLEX WITH UCN-01                                                 
REMARK 900 RELATED ID: 1UU3   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN                            
REMARK 900  COMPLEX WITH LY333531                                               
REMARK 900 RELATED ID: 1UU7   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN                            
REMARK 900  COMPLEX WITH BIM-2                                                  
REMARK 900 RELATED ID: 1UU8   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN                            
REMARK 900  COMPLEX WITH BIM-1                                                  
REMARK 900 RELATED ID: 1UU9   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN                            
REMARK 900  COMPLEX WITH BIM-3                                                  
REMARK 900 RELATED ID: 1UVR   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN                            
REMARK 900  COMPLEX WITH BIM-8                                                  
REMARK 900 RELATED ID: 1W1G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN                            
REMARK 900  HOMOLOGY (PH) DOMAIN BOUND TO                                       
REMARK 900  DIC4-PHOSPHATIDYLINOSITOL (3,4,5)-TRISPHOSPHATE                     
REMARK 900 RELATED ID: 1W1H   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN                            
REMARK 900  HOMOLOGY (PH) DOMAIN                                                
DBREF  1W1D A  406   408  PDB    1W1D     1W1D           406    408             
DBREF  1W1D A  409   556  UNP    O15530   PDPK_HUMAN     409    556             
SEQRES   1 A  151  GLY PRO LEU GLY SER ASN ILE GLU GLN TYR ILE HIS ASP          
SEQRES   2 A  151  LEU ASP SER ASN SER PHE GLU LEU ASP LEU GLN PHE SER          
SEQRES   3 A  151  GLU ASP GLU LYS ARG LEU LEU LEU GLU LYS GLN ALA GLY          
SEQRES   4 A  151  GLY ASN PRO TRP HIS GLN PHE VAL GLU ASN ASN LEU ILE          
SEQRES   5 A  151  LEU LYS MET GLY PRO VAL ASP LYS ARG LYS GLY LEU PHE          
SEQRES   6 A  151  ALA ARG ARG ARG GLN LEU LEU LEU THR GLU GLY PRO HIS          
SEQRES   7 A  151  LEU TYR TYR VAL ASP PRO VAL ASN LYS VAL LEU LYS GLY          
SEQRES   8 A  151  GLU ILE PRO TRP SER GLN GLU LEU ARG PRO GLU ALA LYS          
SEQRES   9 A  151  ASN PHE LYS THR PHE PHE VAL HIS THR PRO ASN ARG THR          
SEQRES  10 A  151  TYR TYR LEU MET ASP PRO SER GLY ASN ALA HIS LYS TRP          
SEQRES  11 A  151  CYS ARG LYS ILE GLN GLU VAL TRP ARG GLN ARG TYR GLN          
SEQRES  12 A  151  SER HIS PRO ASP ALA ALA VAL GLN                              
HET     AU  A1551       2                                                       
HET    4IP  A1552      28                                                       
HET    GOL  A1550       6                                                       
HETNAM      AU GOLD ION                                                         
HETNAM     4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE                             
HETNAM     GOL GLYCEROL                                                         
FORMUL   2   AU    AU 1+                                                        
FORMUL   3  4IP    C6 H16 O18 P4                                                
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HOH   *217(H2 O1)                                                   
HELIX    1   1 ASN A  411  GLN A  414  5                                   4    
HELIX    2   2 SER A  431  ASN A  446  1                                  16    
HELIX    3   3 TRP A  448  VAL A  452  5                                   5    
HELIX    4   4 ASN A  531  GLN A  548  1                                  18    
SHEET    1  AA 6 ILE A 416  ASP A 420  0                                        
SHEET    2  AA 6 SER A 423  LEU A 426 -1  O  SER A 423   N  LEU A 419           
SHEET    3  AA 6 ILE A 457  LYS A 467 -1  O  LEU A 458   N  LEU A 426           
SHEET    4  AA 6 PHE A 470  THR A 479 -1  O  PHE A 470   N  LYS A 467           
SHEET    5  AA 6 HIS A 483  ASP A 488 -1  O  HIS A 483   N  THR A 479           
SHEET    6  AA 6 VAL A 493  ILE A 498 -1  O  VAL A 493   N  ASP A 488           
SHEET    1  AB 6 ILE A 416  ASP A 420  0                                        
SHEET    2  AB 6 SER A 423  LEU A 426 -1  O  SER A 423   N  LEU A 419           
SHEET    3  AB 6 ILE A 457  LYS A 467 -1  O  LEU A 458   N  LEU A 426           
SHEET    4  AB 6 ARG A 521  MET A 526 -1  O  TYR A 524   N  ARG A 466           
SHEET    5  AB 6 THR A 513  THR A 518 -1  O  PHE A 514   N  LEU A 525           
SHEET    6  AB 6 ARG A 505  ASN A 510 -1  O  ARG A 505   N  HIS A 517           
CISPEP   1 GLY A  481    PRO A  482          0         1.03                     
SITE     1 AC1  5 ALA A 508  CYS A 536  ARG A 537  HOH A2025                    
SITE     2 AC1  5 HOH A2149                                                     
SITE     1 AC2 16 HIS A 417  LYS A 465  LYS A 467  ARG A 472                    
SITE     2 AC2 16 ARG A 474  TYR A 486  LYS A 495  ARG A 521                    
SITE     3 AC2 16 HOH A2100  HOH A2103  HOH A2205  HOH A2206                    
SITE     4 AC2 16 HOH A2207  HOH A2208  HOH A2209  HOH A2211                    
SITE     1 AC3  6 ARG A 466  LYS A 467  GLY A 468  HOH A2159                    
SITE     2 AC3  6 HOH A2203  HOH A2204                                          
CRYST1   35.399   58.922   36.578  90.00 101.48  90.00 P 1 21 1      2          
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      0.028249  0.000000  0.005737        0.00000                         
SCALE2      0.000000  0.016972  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027897        0.00000                         
ATOM      1  N   PRO A 407      -5.503  14.445  41.552  1.00 38.81           N  
ANISOU    1  N   PRO A 407     4895   4970   4882     -9     34     15       N  
ATOM      2  CA  PRO A 407      -5.533  13.749  42.881  1.00 38.00           C  
ANISOU    2  CA  PRO A 407     4783   4840   4814     -4     16      5       C  
ATOM      3  C   PRO A 407      -5.415  14.792  43.959  1.00 37.37           C  
ANISOU    3  C   PRO A 407     4681   4778   4739    -18     17     18       C  
ATOM      4  O   PRO A 407      -4.679  15.769  43.755  1.00 37.26           O  
ANISOU    4  O   PRO A 407     4629   4729   4797    -33    -10     84       O  
ATOM      5  CB  PRO A 407      -4.293  12.829  42.859  1.00 38.07           C  
ANISOU    5  CB  PRO A 407     4813   4848   4803     -3     -9     33       C  
ATOM      6  CG  PRO A 407      -3.866  12.747  41.421  1.00 39.13           C  
ANISOU    6  CG  PRO A 407     4894   5029   4941     11     59     12       C  
ATOM      7  CD  PRO A 407      -4.677  13.722  40.576  1.00 38.81           C  
ANISOU    7  CD  PRO A 407     4876   4971   4896     29     51      7       C  
ATOM      8  N   LEU A 408      -6.146  14.625  45.062  1.00 36.47           N  
ANISOU    8  N   LEU A 408     4624   4622   4611    -22     -4     26       N  
ATOM      9  CA  LEU A 408      -6.079  15.585  46.141  1.00 35.25           C  
ANISOU    9  CA  LEU A 408     4412   4506   4476      1      5      3       C  
ATOM     10  C   LEU A 408      -4.639  15.703  46.641  1.00 34.14           C  
ANISOU   10  C   LEU A 408     4280   4314   4375    -12     51      0       C  
ATOM     11  O   LEU A 408      -3.964  14.697  46.924  1.00 32.51           O  
ANISOU   11  O   LEU A 408     3902   4234   4213     50     49    -68       O  
ATOM     12  CB  LEU A 408      -7.041  15.184  47.310  1.00 35.91           C  
ANISOU   12  CB  LEU A 408     4540   4569   4535    -45     13     22       C  
ATOM     13  N   GLY A 409      -4.185  16.943  46.757  1.00 32.96           N  
ANISOU   13  N   GLY A 409     4129   4166   4228      6     31     -7       N  
ATOM     14  CA  GLY A 409      -2.868  17.237  47.291  1.00 32.59           C  
ANISOU   14  CA  GLY A 409     4080   4146   4156     22     89     -6       C  
ATOM     15  C   GLY A 409      -1.760  17.261  46.235  1.00 31.50           C  
ANISOU   15  C   GLY A 409     3952   4018   3997     -3     66    -13       C  
ATOM     16  O   GLY A 409      -0.603  17.497  46.615  1.00 32.50           O  
ANISOU   16  O   GLY A 409     4051   4070   4225     35     84     46       O  
ATOM     17  N   SER A 410      -2.100  17.052  44.952  1.00 29.97           N  
ANISOU   17  N   SER A 410     3718   3802   3866     26     60     36       N  
ATOM     18  CA  SER A 410      -1.083  16.935  43.878  1.00 28.59           C  
ANISOU   18  CA  SER A 410     3594   3568   3699      9      8     23       C  
ATOM     19  C   SER A 410      -0.559  18.296  43.421  1.00 27.44           C  
ANISOU   19  C   SER A 410     3421   3419   3584     32     61     36       C  
ATOM     20  O   SER A 410       0.624  18.424  43.125  1.00 26.66           O  
ANISOU   20  O   SER A 410     3236   3222   3670    -55    -61    -17       O  
ATOM     21  CB  SER A 410      -1.598  16.137  42.672  1.00 28.81           C  
ANISOU   21  CB  SER A 410     3622   3643   3680     51     36     -9       C  
ATOM     22  OG  SER A 410      -2.629  16.838  41.997  1.00 29.31           O  
ANISOU   22  OG  SER A 410     3720   3654   3762     16     41     62       O  
ATOM     23  N   ASN A 411      -1.441  19.296  43.354  1.00 26.10           N  
ANISOU   23  N   ASN A 411     3260   3235   3418    -26     75     33       N  
ATOM     24  CA  ASN A 411      -1.069  20.670  42.919  1.00 24.72           C  
ANISOU   24  CA  ASN A 411     3132   3113   3148    -65     68      8       C  
ATOM     25  C   ASN A 411       0.038  20.698  41.879  1.00 23.66           C  
ANISOU   25  C   ASN A 411     2915   2997   3076    -25      9    -20       C  
ATOM     26  O   ASN A 411       1.147  21.181  42.146  1.00 24.33           O  
ANISOU   26  O   ASN A 411     2932   3016   3296   -124    140     30       O  
ATOM     27  CB  ASN A 411      -0.581  21.459  44.118  1.00 24.40           C  
ANISOU   27  CB  ASN A 411     3067   3051   3151   -138     64     -8       C  
ATOM     28  CG  ASN A 411      -0.360  22.956  43.818  1.00 25.13           C  
ANISOU   28  CG  ASN A 411     3206   3155   3185     -6   -181    100       C  
ATOM     29  OD1 ASN A 411      -1.098  23.600  43.048  1.00 26.86           O  
ANISOU   29  OD1 ASN A 411     3635   3589   2979     62   -342     47       O  
ATOM     30  ND2 ASN A 411       0.660  23.521  44.476  1.00 20.97           N  
ANISOU   30  ND2 ASN A 411     2733   2647   2586    -31    142    -72       N  
ATOM     31  N   ILE A 412      -0.303  20.247  40.688  1.00 22.79           N  
ANISOU   31  N   ILE A 412     2827   2841   2989    -37     61     20       N  
ATOM     32  CA  ILE A 412       0.605  20.142  39.589  1.00 21.28           C  
ANISOU   32  CA  ILE A 412     2644   2637   2804     54     -1    -30       C  
ATOM     33  C   ILE A 412       1.156  21.511  39.145  1.00 20.76           C  
ANISOU   33  C   ILE A 412     2561   2562   2761     49    126    -47       C  
ATOM     34  O   ILE A 412       2.259  21.634  38.587  1.00 19.58           O  
ANISOU   34  O   ILE A 412     2294   2429   2716     37    146   -265       O  
ATOM     35  CB  ILE A 412      -0.127  19.356  38.475  1.00 22.86           C  
ANISOU   35  CB  ILE A 412     2878   2806   2998    -48    -41     19       C  
ATOM     36  CG1 ILE A 412       0.863  18.648  37.635  1.00 22.29           C  
ANISOU   36  CG1 ILE A 412     2812   2779   2876   -117    -48    -61       C  
ATOM     37  CG2 ILE A 412      -1.058  20.215  37.660  1.00 23.79           C  
ANISOU   37  CG2 ILE A 412     2762   2955   3322     49   -177    -15       C  
ATOM     38  CD1 ILE A 412       1.497  17.520  38.363  1.00 20.89           C  
ANISOU   38  CD1 ILE A 412     2684   2575   2675   -230   -139    -24       C  
ATOM     39  N   GLU A 413       0.409  22.565  39.462  1.00 20.72           N  
ANISOU   39  N   GLU A 413     2625   2537   2710     46    184    -68       N  
ATOM     40  CA  GLU A 413       0.783  23.921  39.117  1.00 20.63           C  
ANISOU   40  CA  GLU A 413     2609   2591   2636      6    121    -52       C  
ATOM     41  C   GLU A 413       2.079  24.367  39.795  1.00 17.95           C  
ANISOU   41  C   GLU A 413     2364   2201   2253     71    208   -174       C  
ATOM     42  O   GLU A 413       2.663  25.377  39.368  1.00 18.30           O  
ANISOU   42  O   GLU A 413     2588   2073   2291     45    344   -105       O  
ATOM     43  CB  GLU A 413      -0.357  24.896  39.489  1.00 20.98           C  
ANISOU   43  CB  GLU A 413     2740   2544   2686     60    135    -21       C  
ATOM     44  CG  GLU A 413      -1.527  24.860  38.517  1.00 26.11           C  
ANISOU   44  CG  GLU A 413     3225   3435   3257     37    -32    -55       C  
ATOM     45  CD  GLU A 413      -2.516  23.729  38.759  1.00 31.35           C  
ANISOU   45  CD  GLU A 413     3957   3874   4078   -110     51     28       C  
ATOM     46  OE1 GLU A 413      -2.542  23.162  39.890  1.00 32.59           O  
ANISOU   46  OE1 GLU A 413     4200   4076   4103     77      1     17       O  
ATOM     47  OE2 GLU A 413      -3.303  23.409  37.788  1.00 36.50           O  
ANISOU   47  OE2 GLU A 413     4559   4818   4492      3   -142    -13       O  
ATOM     48  N   GLN A 414       2.537  23.642  40.808  1.00 16.42           N  
ANISOU   48  N   GLN A 414     2243   1890   2105     97    252   -254       N  
ATOM     49  CA  GLN A 414       3.812  23.896  41.453  1.00 16.19           C  
ANISOU   49  CA  GLN A 414     2195   1960   1998      1    107   -161       C  
ATOM     50  C   GLN A 414       5.016  23.897  40.521  1.00 16.87           C  
ANISOU   50  C   GLN A 414     2235   2055   2118    -25     73   -178       C  
ATOM     51  O   GLN A 414       6.045  24.537  40.795  1.00 18.56           O  
ANISOU   51  O   GLN A 414     2501   2502   2048    -70      8   -267       O  
ATOM     52  CB  GLN A 414       4.089  22.897  42.563  1.00 17.30           C  
ANISOU   52  CB  GLN A 414     2453   2027   2090      0    150   -217       C  
ATOM     53  CG  GLN A 414       4.321  21.450  42.112  1.00 17.05           C  
ANISOU   53  CG  GLN A 414     2377   1951   2147     60    -18    -70       C  
ATOM     54  CD  GLN A 414       4.405  20.480  43.253  1.00 18.60           C  
ANISOU   54  CD  GLN A 414     2757   2176   2132    -69     38   -208       C  
ATOM     55  OE1 GLN A 414       3.466  19.701  43.476  1.00 19.54           O  
ANISOU   55  OE1 GLN A 414     2931   2420   2070   -230    226   -126       O  
ATOM     56  NE2 GLN A 414       5.548  20.454  43.915  1.00 17.74           N  
ANISOU   56  NE2 GLN A 414     2593   2295   1851    100     45    -75       N  
ATOM     57  N   TYR A 415       4.908  23.144  39.429  1.00 15.13           N  
ANISOU   57  N   TYR A 415     2021   1865   1862    -24    -22   -121       N  
ATOM     58  CA  TYR A 415       5.995  23.024  38.498  1.00 14.42           C  
ANISOU   58  CA  TYR A 415     2004   1656   1819     29     26    -64       C  
ATOM     59  C   TYR A 415       5.987  24.113  37.454  1.00 13.70           C  
ANISOU   59  C   TYR A 415     1828   1606   1771     -7    -13    -55       C  
ATOM     60  O   TYR A 415       6.915  24.185  36.675  1.00 14.71           O  
ANISOU   60  O   TYR A 415     2087   1662   1839    191    262   -150       O  
ATOM     61  CB  TYR A 415       5.998  21.638  37.821  1.00 12.63           C  
ANISOU   61  CB  TYR A 415     1781   1485   1531     82     82   -192       C  
ATOM     62  CG  TYR A 415       6.056  20.508  38.841  1.00 11.60           C  
ANISOU   62  CG  TYR A 415     1732   1511   1161     80    103   -213       C  
ATOM     63  CD1 TYR A 415       7.168  20.325  39.636  1.00 12.99           C  
ANISOU   63  CD1 TYR A 415     1777   1386   1770     -5      4    -98       C  
ATOM     64  CD2 TYR A 415       4.984  19.630  39.026  1.00 13.10           C  
ANISOU   64  CD2 TYR A 415     1978   1480   1519    164    114   -124       C  
ATOM     65  CE1 TYR A 415       7.193  19.358  40.617  1.00 12.70           C  
ANISOU   65  CE1 TYR A 415     1821   1897   1106   -130   -123   -109       C  
ATOM     66  CE2 TYR A 415       5.036  18.652  39.974  1.00 11.17           C  
ANISOU   66  CE2 TYR A 415     1614   1462   1165     15    226   -175       C  
ATOM     67  CZ  TYR A 415       6.160  18.496  40.728  1.00 11.59           C  
ANISOU   67  CZ  TYR A 415     1987   1398   1016     -6     29   -328       C  
ATOM     68  OH  TYR A 415       6.250  17.531  41.725  1.00 15.91           O  
ANISOU   68  OH  TYR A 415     2833   1617   1594   -227   -158     44       O  
ATOM     69  N   ILE A 416       4.959  24.957  37.438  1.00 14.63           N  
ANISOU   69  N   ILE A 416     1899   1838   1822     81     46   -145       N  
ATOM     70  CA  ILE A 416       4.786  25.935  36.396  1.00 15.57           C  
ANISOU   70  CA  ILE A 416     1999   1965   1952     63    146    -72       C  
ATOM     71  C   ILE A 416       5.079  27.302  36.942  1.00 15.19           C  
ANISOU   71  C   ILE A 416     2114   1862   1794    147    235    -86       C  
ATOM     72  O   ILE A 416       4.538  27.695  37.996  1.00 16.07           O  
ANISOU   72  O   ILE A 416     2449   1772   1882    364    463   -219       O  
ATOM     73  CB  ILE A 416       3.321  25.916  35.878  1.00 16.73           C  
ANISOU   73  CB  ILE A 416     2039   2241   2077     54     99    -76       C  
ATOM     74  CG1 ILE A 416       2.916  24.492  35.438  1.00 18.20           C  
ANISOU   74  CG1 ILE A 416     2273   2246   2396     69     53    -69       C  
ATOM     75  CG2 ILE A 416       3.135  26.976  34.784  1.00 19.02           C  
ANISOU   75  CG2 ILE A 416     2418   2329   2478    175     38    -26       C  
ATOM     76  CD1 ILE A 416       1.427  24.317  35.136  1.00 20.58           C  
ANISOU   76  CD1 ILE A 416     2545   2753   2520     29     43    -23       C  
ATOM     77  N   HIS A 417       5.877  28.050  36.210  1.00 15.55           N  
ANISOU   77  N   HIS A 417     2181   1840   1887    137    220    -72       N  
ATOM     78  CA  HIS A 417       6.295  29.380  36.582  1.00 15.56           C  
ANISOU   78  CA  HIS A 417     2278   1866   1767    159    139    -65       C  
ATOM     79  C   HIS A 417       6.001  30.367  35.475  1.00 17.65           C  
ANISOU   79  C   HIS A 417     2506   2092   2107    206    144     84       C  
ATOM     80  O   HIS A 417       6.634  30.385  34.420  1.00 16.22           O  
ANISOU   80  O   HIS A 417     2456   1888   1816    328    163    -71       O  
ATOM     81  CB  HIS A 417       7.711  29.341  36.978  1.00 15.76           C  
ANISOU   81  CB  HIS A 417     2384   1886   1716     50    137   -125       C  
ATOM     82  CG  HIS A 417       7.936  28.336  38.054  1.00 16.64           C  
ANISOU   82  CG  HIS A 417     2583   1990   1748    194    138     20       C  
ATOM     83  ND1 HIS A 417       7.470  28.539  39.333  1.00 21.17           N  
ANISOU   83  ND1 HIS A 417     3475   2550   2019    310    162   -304       N  
ATOM     84  CD2 HIS A 417       8.498  27.102  38.047  1.00 19.67           C  
ANISOU   84  CD2 HIS A 417     2972   2194   2306    138    100    -35       C  
ATOM     85  CE1 HIS A 417       7.738  27.484  40.072  1.00 20.72           C  
ANISOU   85  CE1 HIS A 417     3209   2434   2230    312    194    -61       C  
ATOM     86  NE2 HIS A 417       8.372  26.596  39.318  1.00 20.70           N  
ANISOU   86  NE2 HIS A 417     3321   2273   2268    192     59   -204       N  
ATOM     87  N   ASP A 418       4.978  31.177  35.722  1.00 19.65           N  
ANISOU   87  N   ASP A 418     2627   2506   2332    166    179    -10       N  
ATOM     88  CA  ASP A 418       4.538  32.124  34.699  1.00 20.34           C  
ANISOU   88  CA  ASP A 418     2651   2647   2427     92      6     15       C  
ATOM     89  C   ASP A 418       5.396  33.367  34.664  1.00 20.94           C  
ANISOU   89  C   ASP A 418     2771   2694   2491     10     51    -28       C  
ATOM     90  O   ASP A 418       5.737  33.953  35.702  1.00 20.00           O  
ANISOU   90  O   ASP A 418     2821   2821   1956   -114    171     61       O  
ATOM     91  CB  ASP A 418       3.079  32.491  34.922  1.00 20.14           C  
ANISOU   91  CB  ASP A 418     2610   2656   2385    113     11   -109       C  
ATOM     92  CG  ASP A 418       2.171  31.298  34.821  1.00 23.24           C  
ANISOU   92  CG  ASP A 418     2973   2968   2887    -61     81     49       C  
ATOM     93  OD1 ASP A 418       2.144  30.574  33.764  1.00 24.52           O  
ANISOU   93  OD1 ASP A 418     2864   3498   2953    134    241    -51       O  
ATOM     94  OD2 ASP A 418       1.430  30.980  35.783  1.00 29.11           O  
ANISOU   94  OD2 ASP A 418     3585   4062   3414    -94    343     30       O  
ATOM     95  N   LEU A 419       5.758  33.821  33.474  1.00 21.19           N  
ANISOU   95  N   LEU A 419     2704   2843   2501     40     11    -15       N  
ATOM     96  CA  LEU A 419       6.391  35.137  33.342  1.00 24.18           C  
ANISOU   96  CA  LEU A 419     3082   3020   3083     20      0    -25       C  
ATOM     97  C   LEU A 419       5.445  36.221  32.839  1.00 25.65           C  
ANISOU   97  C   LEU A 419     3238   3196   3311     64      6    -54       C  
ATOM     98  O   LEU A 419       5.663  37.410  33.132  1.00 27.57           O  
ANISOU   98  O   LEU A 419     3496   3213   3764    -25     -6    -25       O  
ATOM     99  CB  LEU A 419       7.600  35.082  32.389  1.00 24.29           C  
ANISOU   99  CB  LEU A 419     3103   3109   3014    -36     41    -32       C  
ATOM    100  CG  LEU A 419       8.923  34.494  32.852  1.00 25.92           C  
ANISOU  100  CG  LEU A 419     3322   3309   3215     24    -39     22       C  
ATOM    101  CD1 LEU A 419       9.685  33.910  31.677  1.00 27.65           C  
ANISOU  101  CD1 LEU A 419     3443   3604   3458     67     99    -58       C  
ATOM    102  CD2 LEU A 419       9.819  35.512  33.550  1.00 26.90           C  
ANISOU  102  CD2 LEU A 419     3426   3481   3313    -42    -16   -166       C  
ATOM    103  N   ASP A 420       4.439  35.797  32.079  1.00 25.76           N  
ANISOU  103  N   ASP A 420     3187   3246   3354     60     -1    -37       N  
ATOM    104  CA  ASP A 420       3.436  36.675  31.459  1.00 26.79           C  
ANISOU  104  CA  ASP A 420     3369   3363   3446     60    -20      0       C  
ATOM    105  C   ASP A 420       2.300  35.762  30.979  1.00 27.33           C  
ANISOU  105  C   ASP A 420     3372   3416   3596     58    -67     -9       C  
ATOM    106  O   ASP A 420       2.342  34.542  31.208  1.00 27.19           O  
ANISOU  106  O   ASP A 420     3239   3354   3737    122      7    -72       O  
ATOM    107  CB  ASP A 420       4.054  37.463  30.285  1.00 27.09           C  
ANISOU  107  CB  ASP A 420     3459   3297   3536     46     -8     15       C  
ATOM    108  N   SER A 421       1.253  36.341  30.382  1.00 27.04           N  
ANISOU  108  N   SER A 421     3425   3353   3493    111    -47      7       N  
ATOM    109  CA  SER A 421       0.068  35.580  29.951  1.00 25.95           C  
ANISOU  109  CA  SER A 421     3231   3270   3355     52     40    -16       C  
ATOM    110  C   SER A 421       0.348  34.515  28.870  1.00 25.32           C  
ANISOU  110  C   SER A 421     3128   3186   3306     26      1     50       C  
ATOM    111  O   SER A 421      -0.390  33.524  28.770  1.00 27.32           O  
ANISOU  111  O   SER A 421     3316   3377   3686    -26     -2      9       O  
ATOM    112  CB  SER A 421      -0.997  36.539  29.399  1.00 26.78           C  
ANISOU  112  CB  SER A 421     3304   3398   3470     -5    -14     11       C  
ATOM    113  OG  SER A 421      -0.526  37.264  28.291  1.00 28.85           O  
ANISOU  113  OG  SER A 421     3634   3681   3646    223     29     65       O  
ATOM    114  N   ASN A 422       1.386  34.738  28.063  1.00 22.44           N  
ANISOU  114  N   ASN A 422     2738   2895   2893    170     34     33       N  
ATOM    115  CA  ASN A 422       1.740  33.831  26.954  1.00 20.84           C  
ANISOU  115  CA  ASN A 422     2539   2682   2695     67    -35     51       C  
ATOM    116  C   ASN A 422       3.143  33.229  27.149  1.00 16.88           C  
ANISOU  116  C   ASN A 422     2101   2207   2103     98      2     11       C  
ATOM    117  O   ASN A 422       3.825  32.798  26.200  1.00 14.56           O  
ANISOU  117  O   ASN A 422     1846   1958   1724     33    -55    209       O  
ATOM    118  CB  ASN A 422       1.631  34.548  25.608  1.00 22.02           C  
ANISOU  118  CB  ASN A 422     2717   2883   2764     39    -27     94       C  
ATOM    119  CG  ASN A 422       2.491  35.829  25.527  1.00 24.82           C  
ANISOU  119  CG  ASN A 422     3136   3054   3241     57     41     14       C  
ATOM    120  OD1 ASN A 422       3.239  36.167  26.468  1.00 30.74           O  
ANISOU  120  OD1 ASN A 422     4064   3888   3726    112   -241     48       O  
ATOM    121  ND2 ASN A 422       2.426  36.527  24.364  1.00 27.93           N  
ANISOU  121  ND2 ASN A 422     3731   3505   3375      7    -28    196       N  
ATOM    122  N   SER A 423       3.598  33.268  28.378  1.00 14.74           N  
ANISOU  122  N   SER A 423     1868   1929   1803    166    165     49       N  
ATOM    123  CA  SER A 423       4.983  32.920  28.706  1.00 12.99           C  
ANISOU  123  CA  SER A 423     1722   1738   1475    145    101    -11       C  
ATOM    124  C   SER A 423       5.066  32.192  30.018  1.00 13.65           C  
ANISOU  124  C   SER A 423     1962   1648   1576    269    108     41       C  
ATOM    125  O   SER A 423       4.609  32.712  31.023  1.00 15.78           O  
ANISOU  125  O   SER A 423     2622   2012   1360    514    175    144       O  
ATOM    126  CB ASER A 423       5.799  34.168  28.801  0.50 13.97           C  
ANISOU  126  CB ASER A 423     1722   1850   1734    110      2    -14       C  
ATOM    127  OG ASER A 423       5.707  34.820  27.587  0.50 14.27           O  
ANISOU  127  OG ASER A 423     1911   1707   1801    121    151     66       O  
ATOM    128  CB BSER A 423       5.798  34.235  28.725  0.50 13.99           C  
ANISOU  128  CB BSER A 423     1717   1870   1727     98     -4    -17       C  
ATOM    129  OG BSER A 423       7.210  34.081  28.936  0.50 14.76           O  
ANISOU  129  OG BSER A 423     1651   2125   1832     14    117    -12       O  
ATOM    130  N   PHE A 424       5.667  31.023  30.025  1.00 12.07           N  
ANISOU  130  N   PHE A 424     1748   1444   1392    252    125    -21       N  
ATOM    131  CA  PHE A 424       5.964  30.293  31.285  1.00 10.80           C  
ANISOU  131  CA  PHE A 424     1481   1259   1362     97     25     29       C  
ATOM    132  C   PHE A 424       7.144  29.355  31.066  1.00 10.02           C  
ANISOU  132  C   PHE A 424     1484   1119   1202     44    112     -9       C  
ATOM    133  O   PHE A 424       7.557  29.099  29.928  1.00 11.43           O  
ANISOU  133  O   PHE A 424     1673   1322   1345   -122      6     32       O  
ATOM    134  CB  PHE A 424       4.742  29.470  31.769  1.00 11.50           C  
ANISOU  134  CB  PHE A 424     1385   1451   1532    151     23     25       C  
ATOM    135  CG  PHE A 424       4.364  28.346  30.849  1.00 11.45           C  
ANISOU  135  CG  PHE A 424     1392   1522   1436     68    134     60       C  
ATOM    136  CD1 PHE A 424       4.996  27.103  30.942  1.00 14.28           C  
ANISOU  136  CD1 PHE A 424     2031   1675   1716    145   -102   -241       C  
ATOM    137  CD2 PHE A 424       3.386  28.501  29.876  1.00 14.04           C  
ANISOU  137  CD2 PHE A 424     1906   1582   1846    185   -101   -102       C  
ATOM    138  CE1 PHE A 424       4.646  26.078  30.002  1.00 13.81           C  
ANISOU  138  CE1 PHE A 424     1686   1597   1962     31    237   -285       C  
ATOM    139  CE2 PHE A 424       3.022  27.430  29.024  1.00 14.27           C  
ANISOU  139  CE2 PHE A 424     1703   1774   1944    -29   -135    -19       C  
ATOM    140  CZ  PHE A 424       3.702  26.269  29.095  1.00 13.63           C  
ANISOU  140  CZ  PHE A 424     1824   1679   1675     69    274   -271       C  
ATOM    141  N   GLU A 425       7.661  28.808  32.163  1.00 10.47           N  
ANISOU  141  N   GLU A 425     1430   1247   1299    127     31   -128       N  
ATOM    142  CA  GLU A 425       8.609  27.704  32.100  1.00 11.63           C  
ANISOU  142  CA  GLU A 425     1509   1430   1479     98    -20      3       C  
ATOM    143  C   GLU A 425       8.300  26.714  33.196  1.00 10.39           C  
ANISOU  143  C   GLU A 425     1453   1345   1147    115     71    -66       C  
ATOM    144  O   GLU A 425       7.697  27.077  34.235  1.00 11.20           O  
ANISOU  144  O   GLU A 425     1662   1397   1195    274    304    -91       O  
ATOM    145  CB  GLU A 425      10.033  28.205  32.095  1.00 14.25           C  
ANISOU  145  CB  GLU A 425     1800   1684   1927    114      5    -59       C  
ATOM    146  CG  GLU A 425      10.495  29.011  33.270  1.00 17.18           C  
ANISOU  146  CG  GLU A 425     2171   2197   2159    -38    -81     -7       C  
ATOM    147  CD  GLU A 425      11.916  29.484  33.057  1.00 17.30           C  
ANISOU  147  CD  GLU A 425     2140   2118   2316   -104    -59     31       C  
ATOM    148  OE1 GLU A 425      12.278  30.176  32.061  1.00 14.29           O  
ANISOU  148  OE1 GLU A 425     1594   1852   1984   -169   -320   -242       O  
ATOM    149  OE2 GLU A 425      12.713  29.136  33.881  1.00 23.15           O  
ANISOU  149  OE2 GLU A 425     2808   3027   2959    -82   -352    309       O  
ATOM    150  N   LEU A 426       8.667  25.464  32.952  1.00 10.64           N  
ANISOU  150  N   LEU A 426     1478   1390   1175    204    120    -67       N  
ATOM    151  CA  LEU A 426       8.472  24.366  33.870  1.00 10.84           C  
ANISOU  151  CA  LEU A 426     1505   1420   1193     34    112    -12       C  
ATOM    152  C   LEU A 426       9.738  23.895  34.517  1.00 10.97           C  
ANISOU  152  C   LEU A 426     1541   1366   1260     82     69    -57       C  
ATOM    153  O   LEU A 426      10.801  23.828  33.904  1.00 11.98           O  
ANISOU  153  O   LEU A 426     1500   1724   1327    135     29    246       O  
ATOM    154  CB  LEU A 426       7.922  23.151  33.188  1.00 11.89           C  
ANISOU  154  CB  LEU A 426     1726   1642   1148     68    -10    -13       C  
ATOM    155  CG  LEU A 426       6.428  23.045  32.978  1.00 15.26           C  
ANISOU  155  CG  LEU A 426     1939   1938   1918   -215   -123    -24       C  
ATOM    156  CD1 LEU A 426       5.679  24.249  32.450  1.00 20.57           C  
ANISOU  156  CD1 LEU A 426     2633   2522   2661    126   -125   -155       C  
ATOM    157  CD2 LEU A 426       6.140  21.724  32.255  1.00 13.53           C  
ANISOU  157  CD2 LEU A 426     1843   1634   1660    -22   -115    146       C  
ATOM    158  N   ASP A 427       9.644  23.594  35.805  1.00 11.61           N  
ANISOU  158  N   ASP A 427     1594   1372   1444     30     -8     93       N  
ATOM    159  CA  ASP A 427      10.668  22.800  36.465  1.00 11.50           C  
ANISOU  159  CA  ASP A 427     1548   1350   1471     89    -74     29       C  
ATOM    160  C   ASP A 427      10.620  21.387  35.897  1.00 11.21           C  
ANISOU  160  C   ASP A 427     1543   1348   1367     47   -114    105       C  
ATOM    161  O   ASP A 427       9.562  20.867  35.566  1.00 11.82           O  
ANISOU  161  O   ASP A 427     1359   1305   1826    145    -99    158       O  
ATOM    162  CB  ASP A 427      10.304  22.684  37.933  1.00 12.67           C  
ANISOU  162  CB  ASP A 427     1755   1555   1501     97    -50     50       C  
ATOM    163  CG  ASP A 427      10.266  23.993  38.644  1.00 14.00           C  
ANISOU  163  CG  ASP A 427     1855   1737   1724    162     75    -37       C  
ATOM    164  OD1 ASP A 427      11.101  24.872  38.360  1.00 16.04           O  
ANISOU  164  OD1 ASP A 427     2104   1975   2013    110    205   -351       O  
ATOM    165  OD2 ASP A 427       9.401  24.223  39.532  1.00 18.22           O  
ANISOU  165  OD2 ASP A 427     2691   2576   1654    397    279   -135       O  
ATOM    166  N   LEU A 428      11.776  20.774  35.724  1.00 11.46           N  
ANISOU  166  N   LEU A 428     1430   1421   1501     70    -49    104       N  
ATOM    167  CA  LEU A 428      11.869  19.521  34.958  1.00 11.86           C  
ANISOU  167  CA  LEU A 428     1619   1443   1445     52   -109    -11       C  
ATOM    168  C   LEU A 428      11.868  18.223  35.704  1.00 13.73           C  
ANISOU  168  C   LEU A 428     1884   1610   1723     73    -28    -62       C  
ATOM    169  O   LEU A 428      11.955  17.174  35.099  1.00 16.45           O  
ANISOU  169  O   LEU A 428     2542   1629   2079    154    -56   -231       O  
ATOM    170  CB  LEU A 428      13.099  19.554  34.042  1.00 13.04           C  
ANISOU  170  CB  LEU A 428     1779   1612   1562     37    -66    -77       C  
ATOM    171  CG  LEU A 428      13.146  20.696  33.023  1.00 13.07           C  
ANISOU  171  CG  LEU A 428     1608   1721   1634    -45    109    -74       C  
ATOM    172  CD1 LEU A 428      14.305  20.484  32.053  1.00 16.17           C  
ANISOU  172  CD1 LEU A 428     1897   2331   1915     50    182   -103       C  
ATOM    173  CD2 LEU A 428      11.791  20.788  32.302  1.00 13.89           C  
ANISOU  173  CD2 LEU A 428     1935   1625   1715     81     20     24       C  
ATOM    174  N   GLN A 429      11.762  18.278  37.005  1.00 15.55           N  
ANISOU  174  N   GLN A 429     2092   1904   1912     55    -19    137       N  
ATOM    175  CA  GLN A 429      12.040  17.065  37.844  1.00 15.29           C  
ANISOU  175  CA  GLN A 429     1992   1889   1927    -10    -21    163       C  
ATOM    176  C   GLN A 429      10.793  16.220  38.194  1.00 16.14           C  
ANISOU  176  C   GLN A 429     2082   2066   1985   -114    -97    183       C  
ATOM    177  O   GLN A 429      10.871  15.264  39.020  1.00 18.62           O  
ANISOU  177  O   GLN A 429     2459   2244   2372    -43   -120    333       O  
ATOM    178  CB AGLN A 429      12.661  17.503  39.159  0.50 16.78           C  
ANISOU  178  CB AGLN A 429     2153   2098   2125    -45    -94    136       C  
ATOM    179  CG AGLN A 429      13.952  18.291  39.035  0.50 16.50           C  
ANISOU  179  CG AGLN A 429     2063   2173   2031    -90    -57     70       C  
ATOM    180  CD AGLN A 429      13.791  19.765  38.642  0.50 16.80           C  
ANISOU  180  CD AGLN A 429     1953   2348   2080     67    -66    141       C  
ATOM    181  OE1AGLN A 429      14.634  20.285  37.948  0.50 16.94           O  
ANISOU  181  OE1AGLN A 429     1984   2510   1943   -248   -154    448       O  
ATOM    182  NE2AGLN A 429      12.739  20.418  39.087  0.50 16.23           N  
ANISOU  182  NE2AGLN A 429     2169   2238   1758     54     74    -28       N  
ATOM    183  CB BGLN A 429      12.863  17.422  39.067  0.50 15.69           C  
ANISOU  183  CB BGLN A 429     2039   1979   1940      2    -17     96       C  
ATOM    184  CG BGLN A 429      12.062  17.915  40.281  0.50 12.21           C  
ANISOU  184  CG BGLN A 429     1393   1704   1542    -88    -77     40       C  
ATOM    185  CD BGLN A 429      11.499  19.313  40.138  0.50 12.57           C  
ANISOU  185  CD BGLN A 429     1330   1828   1616    -55   -171     31       C  
ATOM    186  OE1BGLN A 429      11.838  20.016  39.207  0.50 12.86           O  
ANISOU  186  OE1BGLN A 429     1392   1681   1812     30   -328    110       O  
ATOM    187  NE2BGLN A 429      10.631  19.702  41.042  0.50 14.32           N  
ANISOU  187  NE2BGLN A 429     1656   2071   1711    103   -158     22       N  
ATOM    188  N   PHE A 430       9.659  16.562  37.631  1.00 13.67           N  
ANISOU  188  N   PHE A 430     1861   1668   1662    -53     63    132       N  
ATOM    189  CA  PHE A 430       8.430  15.843  37.927  1.00 13.13           C  
ANISOU  189  CA  PHE A 430     1785   1657   1546    -90    -22    -57       C  
ATOM    190  C   PHE A 430       8.472  14.407  37.382  1.00 12.86           C  
ANISOU  190  C   PHE A 430     1763   1582   1540     47     25     72       C  
ATOM    191  O   PHE A 430       9.254  14.063  36.528  1.00 14.29           O  
ANISOU  191  O   PHE A 430     2187   1653   1588      4    138    237       O  
ATOM    192  CB  PHE A 430       7.263  16.627  37.361  1.00 11.92           C  
ANISOU  192  CB  PHE A 430     1681   1474   1374    -76     68   -127       C  
ATOM    193  CG  PHE A 430       7.434  16.986  35.913  1.00 12.68           C  
ANISOU  193  CG  PHE A 430     1693   1577   1548     61     76    -76       C  
ATOM    194  CD1 PHE A 430       7.247  16.048  34.920  1.00 13.09           C  
ANISOU  194  CD1 PHE A 430     1825   1719   1427    -26   -121    -22       C  
ATOM    195  CD2 PHE A 430       7.815  18.254  35.563  1.00 11.09           C  
ANISOU  195  CD2 PHE A 430     1232   1589   1390    121    -23     70       C  
ATOM    196  CE1 PHE A 430       7.422  16.392  33.577  1.00 12.66           C  
ANISOU  196  CE1 PHE A 430     1804   1535   1471     84     97     98       C  
ATOM    197  CE2 PHE A 430       8.053  18.592  34.231  1.00 10.64           C  
ANISOU  197  CE2 PHE A 430     1586   1179   1277     45   -124    146       C  
ATOM    198  CZ  PHE A 430       7.871  17.646  33.245  1.00 10.38           C  
ANISOU  198  CZ  PHE A 430     1335   1444   1162    114   -133     10       C  
ATOM    199  N   SER A 431       7.610  13.588  37.917  1.00 12.71           N  
ANISOU  199  N   SER A 431     1668   1518   1640    -82   -213     51       N  
ATOM    200  CA  SER A 431       7.509  12.172  37.538  1.00 12.70           C  
ANISOU  200  CA  SER A 431     1723   1520   1582     17   -171    -42       C  
ATOM    201  C   SER A 431       6.699  11.932  36.288  1.00 13.89           C  
ANISOU  201  C   SER A 431     1972   1636   1669     65   -223     -1       C  
ATOM    202  O   SER A 431       6.034  12.827  35.794  1.00 12.90           O  
ANISOU  202  O   SER A 431     1996   1367   1538   -160   -370    172       O  
ATOM    203  CB  SER A 431       6.856  11.401  38.667  1.00 13.48           C  
ANISOU  203  CB  SER A 431     1884   1599   1638   -139   -143    -87       C  
ATOM    204  OG  SER A 431       5.468  11.714  38.761  1.00 13.49           O  
ANISOU  204  OG  SER A 431     2019   1640   1466    -64   -309    115       O  
ATOM    205  N   GLU A 432       6.824  10.721  35.754  1.00 13.32           N  
ANISOU  205  N   GLU A 432     1923   1544   1591    -54   -279     78       N  
ATOM    206  CA  GLU A 432       6.057  10.312  34.580  1.00 14.18           C  
ANISOU  206  CA  GLU A 432     1996   1703   1687    -61   -136     36       C  
ATOM    207  C   GLU A 432       4.586  10.497  34.827  1.00 13.04           C  
ANISOU  207  C   GLU A 432     1957   1457   1539      4    -51     -1       C  
ATOM    208  O   GLU A 432       3.894  10.971  33.928  1.00 13.58           O  
ANISOU  208  O   GLU A 432     2074   1501   1582    -50   -165     52       O  
ATOM    209  CB  GLU A 432       6.390   8.869  34.215  1.00 15.79           C  
ANISOU  209  CB  GLU A 432     2262   1814   1924    -64   -106     70       C  
ATOM    210  CG  GLU A 432       5.658   8.358  33.017  1.00 20.08           C  
ANISOU  210  CG  GLU A 432     2823   2516   2290   -121   -105     16       C  
ATOM    211  CD  GLU A 432       6.094   6.968  32.585  1.00 25.44           C  
ANISOU  211  CD  GLU A 432     3363   3042   3259    122    -20   -123       C  
ATOM    212  OE1 GLU A 432       6.738   6.238  33.390  1.00 28.32           O  
ANISOU  212  OE1 GLU A 432     4025   3378   3356    148     -2     36       O  
ATOM    213  OE2 GLU A 432       5.776   6.617  31.403  1.00 29.39           O  
ANISOU  213  OE2 GLU A 432     3951   3837   3379     80     68   -116       O  
ATOM    214  N   ASP A 433       4.072  10.145  36.023  1.00 13.43           N  
ANISOU  214  N   ASP A 433     1972   1585   1543   -103   -117     63       N  
ATOM    215  CA  ASP A 433       2.669  10.342  36.365  1.00 13.70           C  
ANISOU  215  CA  ASP A 433     1983   1753   1467    -80   -160     22       C  
ATOM    216  C   ASP A 433       2.284  11.812  36.430  1.00 13.76           C  
ANISOU  216  C   ASP A 433     1825   1786   1614   -111    -50     35       C  
ATOM    217  O   ASP A 433       1.231  12.200  35.987  1.00 15.22           O  
ANISOU  217  O   ASP A 433     2189   1810   1784   -223   -374     73       O  
ATOM    218  CB  ASP A 433       2.272   9.583  37.648  1.00 15.75           C  
ANISOU  218  CB  ASP A 433     2187   1882   1915   -264   -125    165       C  
ATOM    219  CG  ASP A 433       2.396   8.074  37.494  1.00 16.77           C  
ANISOU  219  CG  ASP A 433     2323   2092   1957     -9   -121    -28       C  
ATOM    220  OD1 ASP A 433       1.966   7.545  36.439  1.00 21.35           O  
ANISOU  220  OD1 ASP A 433     3365   2054   2691   -415   -547     -6       O  
ATOM    221  OD2 ASP A 433       2.922   7.332  38.336  1.00 17.03           O  
ANISOU  221  OD2 ASP A 433     2537   1799   2132   -373   -188    223       O  
ATOM    222  N   GLU A 434       3.126  12.648  37.013  1.00 12.70           N  
ANISOU  222  N   GLU A 434     1846   1560   1417   -134   -190     56       N  
ATOM    223  CA  GLU A 434       2.859  14.078  37.059  1.00 12.02           C  
ANISOU  223  CA  GLU A 434     1629   1542   1393   -108   -173     25       C  
ATOM    224  C   GLU A 434       2.868  14.635  35.651  1.00 11.87           C  
ANISOU  224  C   GLU A 434     1579   1516   1412   -149    -45     19       C  
ATOM    225  O   GLU A 434       2.066  15.529  35.341  1.00 13.04           O  
ANISOU  225  O   GLU A 434     1884   1675   1395   -163    -44    162       O  
ATOM    226  CB  GLU A 434       3.920  14.789  37.919  1.00 12.76           C  
ANISOU  226  CB  GLU A 434     1753   1584   1510   -128   -155     31       C  
ATOM    227  CG  GLU A 434       3.679  14.531  39.397  1.00 12.07           C  
ANISOU  227  CG  GLU A 434     1475   1548   1562   -184   -112     45       C  
ATOM    228  CD  GLU A 434       4.797  15.069  40.267  1.00 11.09           C  
ANISOU  228  CD  GLU A 434     1429   1338   1444    -93   -142    -71       C  
ATOM    229  OE1 GLU A 434       5.976  14.803  39.973  1.00 12.45           O  
ANISOU  229  OE1 GLU A 434     1847   1830   1051    -35     23     -4       O  
ATOM    230  OE2 GLU A 434       4.442  15.714  41.271  1.00 14.98           O  
ANISOU  230  OE2 GLU A 434     2019   2020   1651   -386     31   -236       O  
ATOM    231  N   LYS A 435       3.742  14.126  34.801  1.00 12.37           N  
ANISOU  231  N   LYS A 435     1671   1530   1499    -20    -98     97       N  
ATOM    232  CA  LYS A 435       3.781  14.605  33.412  1.00 12.07           C  
ANISOU  232  CA  LYS A 435     1522   1558   1506    -47    -14     13       C  
ATOM    233  C   LYS A 435       2.434  14.414  32.744  1.00 12.11           C  
ANISOU  233  C   LYS A 435     1549   1514   1537     14    -48     49       C  
ATOM    234  O   LYS A 435       2.037  15.263  31.947  1.00 12.24           O  
ANISOU  234  O   LYS A 435     1713   1513   1422     82    -75    115       O  
ATOM    235  CB  LYS A 435       4.798  13.846  32.600  1.00 11.91           C  
ANISOU  235  CB  LYS A 435     1662   1403   1459    -72    -22   -142       C  
ATOM    236  CG  LYS A 435       4.868  14.399  31.194  1.00 14.92           C  
ANISOU  236  CG  LYS A 435     2123   1868   1676    -28     19    -14       C  
ATOM    237  CD  LYS A 435       6.040  13.863  30.410  1.00 19.59           C  
ANISOU  237  CD  LYS A 435     2220   2622   2598    138     28      9       C  
ATOM    238  CE  LYS A 435       5.714  12.633  29.712  1.00 23.13           C  
ANISOU  238  CE  LYS A 435     2877   2995   2915    -81      0   -165       C  
ATOM    239  NZ  LYS A 435       6.581  12.415  28.491  1.00 21.93           N  
ANISOU  239  NZ  LYS A 435     2792   2720   2817    -70    255   -116       N  
ATOM    240  N   ARG A 436       1.777  13.265  32.980  1.00 11.80           N  
ANISOU  240  N   ARG A 436     1585   1417   1482    -25    -69     54       N  
ATOM    241  CA  ARG A 436       0.478  13.030  32.347  1.00 13.53           C  
ANISOU  241  CA  ARG A 436     1727   1803   1610   -124    -96     97       C  
ATOM    242  C   ARG A 436      -0.478  14.123  32.676  1.00 12.95           C  
ANISOU  242  C   ARG A 436     1694   1656   1569   -193    -76    116       C  
ATOM    243  O   ARG A 436      -1.258  14.572  31.834  1.00 13.88           O  
ANISOU  243  O   ARG A 436     1742   2001   1530   -283    -10    172       O  
ATOM    244  CB  ARG A 436      -0.091  11.683  32.818  1.00 14.93           C  
ANISOU  244  CB  ARG A 436     2058   1864   1747   -165   -207     41       C  
ATOM    245  CG  ARG A 436      -1.434  11.281  32.249  1.00 18.12           C  
ANISOU  245  CG  ARG A 436     2197   2435   2251   -161    -90    106       C  
ATOM    246  CD  ARG A 436      -1.781   9.816  32.592  1.00 21.34           C  
ANISOU  246  CD  ARG A 436     2916   2506   2686   -269   -243     30       C  
ATOM    247  NE  ARG A 436      -0.612   9.008  32.153  1.00 29.59           N  
ANISOU  247  NE  ARG A 436     3875   3680   3686    106    -43     36       N  
ATOM    248  CZ  ARG A 436       0.285   8.364  32.933  1.00 31.65           C  
ANISOU  248  CZ  ARG A 436     4056   4114   3855     31   -155    -26       C  
ATOM    249  NH1 ARG A 436       0.170   8.314  34.284  1.00 27.76           N  
ANISOU  249  NH1 ARG A 436     3777   3414   3354   -183    -58     48       N  
ATOM    250  NH2 ARG A 436       1.282   7.714  32.323  1.00 34.23           N  
ANISOU  250  NH2 ARG A 436     4177   4503   4322     62    -70   -191       N  
ATOM    251  N   LEU A 437      -0.450  14.573  33.926  1.00 13.15           N  
ANISOU  251  N   LEU A 437     1752   1622   1620   -122    -45    109       N  
ATOM    252  CA  LEU A 437      -1.387  15.550  34.394  1.00 14.22           C  
ANISOU  252  CA  LEU A 437     1766   1914   1721    -88      0     16       C  
ATOM    253  C   LEU A 437      -1.018  16.932  33.855  1.00 12.54           C  
ANISOU  253  C   LEU A 437     1429   1675   1657   -102     59    -39       C  
ATOM    254  O   LEU A 437      -1.869  17.694  33.430  1.00 14.40           O  
ANISOU  254  O   LEU A 437     1684   2003   1782   -326    126    129       O  
ATOM    255  CB  LEU A 437      -1.488  15.473  35.920  1.00 15.20           C  
ANISOU  255  CB  LEU A 437     1921   2102   1751   -124    -37     -1       C  
ATOM    256  CG  LEU A 437      -2.636  16.185  36.578  1.00 19.99           C  
ANISOU  256  CG  LEU A 437     2502   2677   2414     51    -12    -89       C  
ATOM    257  CD1 LEU A 437      -3.946  15.472  36.206  1.00 22.38           C  
ANISOU  257  CD1 LEU A 437     2492   3324   2686    -14     49      0       C  
ATOM    258  CD2 LEU A 437      -2.432  16.069  38.101  1.00 22.47           C  
ANISOU  258  CD2 LEU A 437     2936   3087   2514    116     88      1       C  
ATOM    259  N   LEU A 438       0.271  17.236  33.780  1.00 10.47           N  
ANISOU  259  N   LEU A 438     1091   1501   1384     32    122    117       N  
ATOM    260  CA  LEU A 438       0.717  18.453  33.149  1.00 11.14           C  
ANISOU  260  CA  LEU A 438     1369   1436   1424    -46     15     19       C  
ATOM    261  C   LEU A 438       0.295  18.517  31.696  1.00 10.76           C  
ANISOU  261  C   LEU A 438     1246   1419   1420    -99    -14    140       C  
ATOM    262  O   LEU A 438      -0.093  19.577  31.189  1.00 10.06           O  
ANISOU  262  O   LEU A 438     1125   1324   1370    237     62     75       O  
ATOM    263  CB  LEU A 438       2.221  18.594  33.270  1.00 10.44           C  
ANISOU  263  CB  LEU A 438     1342   1464   1158   -102    172    181       C  
ATOM    264  CG  LEU A 438       2.683  18.985  34.668  1.00  9.65           C  
ANISOU  264  CG  LEU A 438      955   1324   1384   -198     78    -19       C  
ATOM    265  CD1 LEU A 438       4.178  18.681  34.924  1.00  9.93           C  
ANISOU  265  CD1 LEU A 438     1184   1358   1230     58    -44    104       C  
ATOM    266  CD2 LEU A 438       2.424  20.446  34.915  1.00 11.10           C  
ANISOU  266  CD2 LEU A 438     1311   1623   1282    149     18     -7       C  
ATOM    267  N   LEU A 439       0.415  17.408  31.001  1.00 10.15           N  
ANISOU  267  N   LEU A 439     1309   1229   1316   -124    101    187       N  
ATOM    268  CA  LEU A 439       0.013  17.343  29.591  1.00 10.50           C  
ANISOU  268  CA  LEU A 439     1264   1339   1384   -111    -34    103       C  
ATOM    269  C   LEU A 439      -1.512  17.519  29.430  1.00 11.54           C  
ANISOU  269  C   LEU A 439     1299   1563   1520    -23    133    164       C  
ATOM    270  O   LEU A 439      -1.967  18.167  28.476  1.00 11.22           O  
ANISOU  270  O   LEU A 439     1077   1760   1423    -82    102    176       O  
ATOM    271  CB  LEU A 439       0.504  16.074  28.940  1.00 10.09           C  
ANISOU  271  CB  LEU A 439     1193   1333   1307   -263    120    195       C  
ATOM    272  CG  LEU A 439       0.420  15.994  27.417  1.00 11.47           C  
ANISOU  272  CG  LEU A 439     1362   1475   1520   -206     19     19       C  
ATOM    273  CD1 LEU A 439       1.222  17.103  26.718  1.00 11.85           C  
ANISOU  273  CD1 LEU A 439     1736   1458   1307   -237    174    -51       C  
ATOM    274  CD2 LEU A 439       0.807  14.632  26.942  1.00 13.31           C  
ANISOU  274  CD2 LEU A 439     1754   1593   1710   -177   -134   -125       C  
ATOM    275  N   GLU A 440      -2.312  16.907  30.318  1.00 12.87           N  
ANISOU  275  N   GLU A 440     1475   1791   1622    -84    -29    240       N  
ATOM    276  CA  GLU A 440      -3.754  17.049  30.244  1.00 14.12           C  
ANISOU  276  CA  GLU A 440     1647   1949   1770    -41     12    127       C  
ATOM    277  C   GLU A 440      -4.108  18.506  30.423  1.00 13.67           C  
ANISOU  277  C   GLU A 440     1505   1958   1730   -119     96    187       C  
ATOM    278  O   GLU A 440      -4.970  19.053  29.722  1.00 12.97           O  
ANISOU  278  O   GLU A 440     1013   2140   1773   -168    198    432       O  
ATOM    279  CB AGLU A 440      -4.469  16.152  31.293  0.50 15.42           C  
ANISOU  279  CB AGLU A 440     1865   2094   1898    -79     42    114       C  
ATOM    280  CG AGLU A 440      -5.195  15.004  30.620  0.50 18.67           C  
ANISOU  280  CG AGLU A 440     2417   2314   2362   -118     18     30       C  
ATOM    281  CD AGLU A 440      -5.997  14.096  31.539  0.50 19.98           C  
ANISOU  281  CD AGLU A 440     2611   2562   2417     20     92    163       C  
ATOM    282  OE1AGLU A 440      -5.812  12.869  31.442  0.50 21.22           O  
ANISOU  282  OE1AGLU A 440     2943   2613   2505   -111     51    161       O  
ATOM    283  OE2AGLU A 440      -6.859  14.598  32.259  0.50 20.63           O  
ANISOU  283  OE2AGLU A 440     2712   2956   2171    -23     54     30       O  
ATOM    284  CB BGLU A 440      -4.409  16.148  31.305  0.50 14.76           C  
ANISOU  284  CB BGLU A 440     1754   2010   1842   -102     10     92       C  
ATOM    285  CG BGLU A 440      -5.720  16.663  31.846  0.50 16.00           C  
ANISOU  285  CG BGLU A 440     1813   2212   2053     25    -11    127       C  
ATOM    286  CD BGLU A 440      -6.118  15.930  33.119  0.50 17.31           C  
ANISOU  286  CD BGLU A 440     2033   2298   2244    -27     90     88       C  
ATOM    287  OE1BGLU A 440      -5.987  14.695  33.089  0.50 19.90           O  
ANISOU  287  OE1BGLU A 440     2281   2451   2828   -220      7    225       O  
ATOM    288  OE2BGLU A 440      -6.491  16.607  34.114  0.50 17.59           O  
ANISOU  288  OE2BGLU A 440     2102   2794   1788   -272     70    132       O  
ATOM    289  N   LYS A 441      -3.462  19.162  31.368  1.00 13.42           N  
ANISOU  289  N   LYS A 441     1396   1958   1745     27     12    115       N  
ATOM    290  CA  LYS A 441      -3.657  20.588  31.604  1.00 13.84           C  
ANISOU  290  CA  LYS A 441     1536   1878   1841     20     83     24       C  
ATOM    291  C   LYS A 441      -3.344  21.402  30.366  1.00 12.88           C  
ANISOU  291  C   LYS A 441     1426   1693   1773     90    105     42       C  
ATOM    292  O   LYS A 441      -4.109  22.251  29.966  1.00 14.19           O  
ANISOU  292  O   LYS A 441     1540   2002   1848    170    100    197       O  
ATOM    293  CB  LYS A 441      -2.856  21.066  32.804  1.00 14.82           C  
ANISOU  293  CB  LYS A 441     1711   1976   1943    -43    114     50       C  
ATOM    294  CG  LYS A 441      -3.141  22.504  33.173  1.00 18.49           C  
ANISOU  294  CG  LYS A 441     2398   2381   2244    185     92    -98       C  
ATOM    295  CD  LYS A 441      -2.088  23.049  34.097  1.00 21.88           C  
ANISOU  295  CD  LYS A 441     2712   2835   2765    -95    -45   -124       C  
ATOM    296  CE  LYS A 441      -2.270  24.557  34.353  1.00 23.95           C  
ANISOU  296  CE  LYS A 441     3004   2995   3100    148    -71   -172       C  
ATOM    297  NZ  LYS A 441      -3.653  24.954  34.855  1.00 28.17           N  
ANISOU  297  NZ  LYS A 441     3344   3781   3577    101    167   -106       N  
ATOM    298  N   GLN A 442      -2.200  21.117  29.743  1.00 13.13           N  
ANISOU  298  N   GLN A 442     1409   1763   1814     75      4    -12       N  
ATOM    299  CA  GLN A 442      -1.814  21.772  28.508  1.00 11.89           C  
ANISOU  299  CA  GLN A 442     1306   1535   1676     94     32     62       C  
ATOM    300  C   GLN A 442      -2.820  21.580  27.392  1.00 11.93           C  
ANISOU  300  C   GLN A 442     1244   1583   1704     41     25      0       C  
ATOM    301  O   GLN A 442      -3.203  22.529  26.690  1.00 12.10           O  
ANISOU  301  O   GLN A 442      977   1646   1973   -160   -181    124       O  
ATOM    302  CB  GLN A 442      -0.463  21.238  28.043  1.00 11.00           C  
ANISOU  302  CB  GLN A 442     1138   1519   1521     36     61   -113       C  
ATOM    303  CG  GLN A 442       0.082  21.788  26.740  1.00 11.33           C  
ANISOU  303  CG  GLN A 442     1416   1312   1575    122   -120    153       C  
ATOM    304  CD  GLN A 442       1.380  21.190  26.384  1.00  8.86           C  
ANISOU  304  CD  GLN A 442     1186    990   1187   -105    -50     65       C  
ATOM    305  OE1 GLN A 442       2.300  21.313  27.161  1.00  9.29           O  
ANISOU  305  OE1 GLN A 442      714   1306   1507   -202   -104    222       O  
ATOM    306  NE2 GLN A 442       1.481  20.555  25.221  1.00  8.78           N  
ANISOU  306  NE2 GLN A 442      655   1234   1444   -252    166    -36       N  
ATOM    307  N   ALA A 443      -3.234  20.343  27.200  1.00 12.21           N  
ANISOU  307  N   ALA A 443     1359   1605   1675    -75    -97    126       N  
ATOM    308  CA  ALA A 443      -4.188  20.024  26.123  1.00 13.83           C  
ANISOU  308  CA  ALA A 443     1634   1832   1788     -6   -136     18       C  
ATOM    309  C   ALA A 443      -5.490  20.767  26.287  1.00 15.32           C  
ANISOU  309  C   ALA A 443     1644   2113   2062    -92    -23     85       C  
ATOM    310  O   ALA A 443      -6.107  21.185  25.297  1.00 17.04           O  
ANISOU  310  O   ALA A 443     1471   2606   2396    -13   -151    232       O  
ATOM    311  CB  ALA A 443      -4.438  18.520  26.048  1.00 13.91           C  
ANISOU  311  CB  ALA A 443     1517   1833   1933    -42   -133    102       C  
ATOM    312  N   GLY A 444      -5.886  20.951  27.521  1.00 16.38           N  
ANISOU  312  N   GLY A 444     1974   2115   2132    -28   -133     -5       N  
ATOM    313  CA  GLY A 444      -7.125  21.655  27.841  1.00 18.34           C  
ANISOU  313  CA  GLY A 444     2090   2383   2492     36     43     24       C  
ATOM    314  C   GLY A 444      -7.021  23.158  27.703  1.00 19.75           C  
ANISOU  314  C   GLY A 444     2259   2478   2768     20    -46     58       C  
ATOM    315  O   GLY A 444      -7.971  23.838  27.248  1.00 21.71           O  
ANISOU  315  O   GLY A 444     2154   2751   3340    126     -6    147       O  
ATOM    316  N   GLY A 445      -5.879  23.727  28.059  1.00 18.07           N  
ANISOU  316  N   GLY A 445     1939   2378   2547     42     86     17       N  
ATOM    317  CA  GLY A 445      -5.849  25.143  28.338  1.00 17.15           C  
ANISOU  317  CA  GLY A 445     1919   2233   2362     69     25     14       C  
ATOM    318  C   GLY A 445      -4.814  25.959  27.611  1.00 17.26           C  
ANISOU  318  C   GLY A 445     2065   2083   2408     80    110      9       C  
ATOM    319  O   GLY A 445      -4.842  27.164  27.668  1.00 19.40           O  
ANISOU  319  O   GLY A 445     2308   2258   2805    165     94    -77       O  
ATOM    320  N   ASN A 446      -3.882  25.298  26.929  1.00 14.31           N  
ANISOU  320  N   ASN A 446     1759   1745   1933    153    114      0       N  
ATOM    321  CA  ASN A 446      -2.828  26.024  26.245  1.00 13.04           C  
ANISOU  321  CA  ASN A 446     1418   1667   1866    151    -10     -7       C  
ATOM    322  C   ASN A 446      -3.178  26.196  24.787  1.00 13.67           C  
ANISOU  322  C   ASN A 446     1375   1828   1990    113    -16     76       C  
ATOM    323  O   ASN A 446      -3.354  25.207  24.072  1.00 14.51           O  
ANISOU  323  O   ASN A 446     1223   2195   2093    122   -152     17       O  
ATOM    324  CB  ASN A 446      -1.472  25.280  26.403  1.00 11.44           C  
ANISOU  324  CB  ASN A 446     1300   1469   1578    166     -3     80       C  
ATOM    325  CG  ASN A 446      -0.286  26.116  25.953  1.00 12.12           C  
ANISOU  325  CG  ASN A 446     1309   1462   1831     53    -99    132       C  
ATOM    326  OD1 ASN A 446      -0.333  26.759  24.914  1.00 14.63           O  
ANISOU  326  OD1 ASN A 446     1566   2138   1852     88   -124    322       O  
ATOM    327  ND2 ASN A 446       0.831  26.021  26.687  1.00 12.67           N  
ANISOU  327  ND2 ASN A 446     1396   1729   1688     46   -367    -50       N  
ATOM    328  N   PRO A 447      -3.300  27.452  24.328  1.00 14.35           N  
ANISOU  328  N   PRO A 447     1380   2003   2067    100    -98     95       N  
ATOM    329  CA  PRO A 447      -3.716  27.683  22.938  1.00 15.91           C  
ANISOU  329  CA  PRO A 447     1874   2107   2062     65    -13     52       C  
ATOM    330  C   PRO A 447      -2.724  27.220  21.876  1.00 15.44           C  
ANISOU  330  C   PRO A 447     1660   2200   2006     46    -87     80       C  
ATOM    331  O   PRO A 447      -3.050  27.186  20.695  1.00 16.41           O  
ANISOU  331  O   PRO A 447     1682   2468   2083     13   -196    161       O  
ATOM    332  CB  PRO A 447      -3.962  29.195  22.885  1.00 16.73           C  
ANISOU  332  CB  PRO A 447     2016   2158   2181    150   -103    194       C  
ATOM    333  CG  PRO A 447      -3.254  29.754  23.946  1.00 17.91           C  
ANISOU  333  CG  PRO A 447     2298   2129   2376      4   -115    140       C  
ATOM    334  CD  PRO A 447      -3.090  28.693  25.062  1.00 14.53           C  
ANISOU  334  CD  PRO A 447     1537   1962   2020    -16    117    187       C  
ATOM    335  N   TRP A 448      -1.497  26.888  22.299  1.00 13.60           N  
ANISOU  335  N   TRP A 448     1412   1844   1909    -41   -228     50       N  
ATOM    336  CA  TRP A 448      -0.474  26.428  21.387  1.00 12.85           C  
ANISOU  336  CA  TRP A 448     1467   1710   1704   -102   -154     47       C  
ATOM    337  C   TRP A 448      -0.303  24.928  21.329  1.00 12.92           C  
ANISOU  337  C   TRP A 448     1427   1757   1722   -105   -139     20       C  
ATOM    338  O   TRP A 448       0.516  24.419  20.569  1.00 12.22           O  
ANISOU  338  O   TRP A 448     1142   1835   1665   -216   -152    135       O  
ATOM    339  CB  TRP A 448       0.871  27.114  21.723  1.00 11.92           C  
ANISOU  339  CB  TRP A 448     1062   1699   1767    -10   -267      5       C  
ATOM    340  CG  TRP A 448       0.721  28.579  21.938  1.00 12.33           C  
ANISOU  340  CG  TRP A 448      940   1890   1854   -110   -316    115       C  
ATOM    341  CD1 TRP A 448       0.579  29.202  23.120  1.00 14.45           C  
ANISOU  341  CD1 TRP A 448     1530   1781   2178    115    -65     51       C  
ATOM    342  CD2 TRP A 448       0.643  29.591  20.936  1.00 13.57           C  
ANISOU  342  CD2 TRP A 448     1142   1803   2207   -204   -172    124       C  
ATOM    343  NE1 TRP A 448       0.402  30.550  22.937  1.00 13.73           N  
ANISOU  343  NE1 TRP A 448     1372   1791   2052   -100   -137     39       N  
ATOM    344  CE2 TRP A 448       0.414  30.815  21.601  1.00 15.97           C  
ANISOU  344  CE2 TRP A 448     1756   2172   2137   -196    126    111       C  
ATOM    345  CE3 TRP A 448       0.688  29.575  19.543  1.00 16.99           C  
ANISOU  345  CE3 TRP A 448     1885   2203   2365     87    122     72       C  
ATOM    346  CZ2 TRP A 448       0.262  32.028  20.930  1.00 17.38           C  
ANISOU  346  CZ2 TRP A 448     2122   1891   2588    129    125    -51       C  
ATOM    347  CZ3 TRP A 448       0.521  30.801  18.844  1.00 19.93           C  
ANISOU  347  CZ3 TRP A 448     2708   2464   2398    -28    155    153       C  
ATOM    348  CH2 TRP A 448       0.319  32.001  19.546  1.00 21.25           C  
ANISOU  348  CH2 TRP A 448     2950   2431   2691     15     11    112       C  
ATOM    349  N   HIS A 449      -1.110  24.201  22.091  1.00 12.48           N  
ANISOU  349  N   HIS A 449     1296   1776   1668   -107   -135     83       N  
ATOM    350  CA  HIS A 449      -0.959  22.763  22.151  1.00 12.96           C  
ANISOU  350  CA  HIS A 449     1327   1826   1769   -115    -66     35       C  
ATOM    351  C   HIS A 449      -1.028  22.140  20.765  1.00 12.53           C  
ANISOU  351  C   HIS A 449     1348   1747   1666   -198     22    166       C  
ATOM    352  O   HIS A 449      -0.336  21.180  20.475  1.00 12.75           O  
ANISOU  352  O   HIS A 449     1168   1808   1868   -309   -143    148       O  
ATOM    353  CB  HIS A 449      -2.057  22.193  23.016  1.00 12.34           C  
ANISOU  353  CB  HIS A 449     1355   1789   1543     -9     19     40       C  
ATOM    354  CG  HIS A 449      -2.038  20.721  23.166  1.00 11.64           C  
ANISOU  354  CG  HIS A 449     1234   1780   1407    -64     16     63       C  
ATOM    355  ND1 HIS A 449      -1.099  20.069  23.938  1.00 12.05           N  
ANISOU  355  ND1 HIS A 449     1157   1821   1599    -62    -15    252       N  
ATOM    356  CD2 HIS A 449      -2.774  19.753  22.561  1.00 12.71           C  
ANISOU  356  CD2 HIS A 449     1294   1873   1660   -117   -128     84       C  
ATOM    357  CE1 HIS A 449      -1.306  18.770  23.849  1.00 13.84           C  
ANISOU  357  CE1 HIS A 449     1687   1773   1799    -71   -354    132       C  
ATOM    358  NE2 HIS A 449      -2.326  18.549  23.026  1.00 12.54           N  
ANISOU  358  NE2 HIS A 449     1122   1823   1818   -365   -219    222       N  
ATOM    359  N   GLN A 450      -1.941  22.659  19.925  1.00 12.66           N  
ANISOU  359  N   GLN A 450     1263   1742   1804   -184    -36    104       N  
ATOM    360  CA  GLN A 450      -2.110  22.084  18.598  1.00 13.56           C  
ANISOU  360  CA  GLN A 450     1544   1800   1806   -201     -7     54       C  
ATOM    361  C   GLN A 450      -0.879  21.990  17.716  1.00 13.23           C  
ANISOU  361  C   GLN A 450     1572   1772   1681    -85   -135     84       C  
ATOM    362  O   GLN A 450      -0.816  21.191  16.788  1.00 14.38           O  
ANISOU  362  O   GLN A 450     1674   1808   1978   -173   -201    -15       O  
ATOM    363  CB  GLN A 450      -3.248  22.809  17.869  1.00 14.98           C  
ANISOU  363  CB  GLN A 450     1718   2129   1843   -105    -36     62       C  
ATOM    364  CG  GLN A 450      -2.899  24.171  17.363  1.00 18.17           C  
ANISOU  364  CG  GLN A 450     2170   2226   2504    109    -98    151       C  
ATOM    365  CD  GLN A 450      -4.051  24.841  16.544  1.00 21.06           C  
ANISOU  365  CD  GLN A 450     2483   2656   2862     92   -207    103       C  
ATOM    366  OE1 GLN A 450      -4.201  24.622  15.322  1.00 24.01           O  
ANISOU  366  OE1 GLN A 450     2862   3226   3034    -79   -146    346       O  
ATOM    367  NE2 GLN A 450      -4.815  25.633  17.221  1.00 22.53           N  
ANISOU  367  NE2 GLN A 450     2654   2550   3354    -31    199    218       N  
ATOM    368  N   PHE A 451       0.122  22.809  18.059  1.00 12.65           N  
ANISOU  368  N   PHE A 451     1392   1743   1669    -85   -172    136       N  
ATOM    369  CA  PHE A 451       1.293  22.988  17.228  1.00 11.71           C  
ANISOU  369  CA  PHE A 451     1327   1631   1492    -22    -53    118       C  
ATOM    370  C   PHE A 451       2.494  22.122  17.623  1.00 11.39           C  
ANISOU  370  C   PHE A 451     1148   1652   1527   -169    -98    210       C  
ATOM    371  O   PHE A 451       3.486  22.091  16.911  1.00 12.70           O  
ANISOU  371  O   PHE A 451     1218   1972   1635     69    -64     26       O  
ATOM    372  CB  PHE A 451       1.721  24.464  17.199  1.00 12.61           C  
ANISOU  372  CB  PHE A 451     1476   1666   1649    -73    -48    109       C  
ATOM    373  CG  PHE A 451       0.631  25.416  16.783  1.00 12.01           C  
ANISOU  373  CG  PHE A 451     1175   1661   1727   -265    119    185       C  
ATOM    374  CD1 PHE A 451       0.158  25.414  15.479  1.00 14.58           C  
ANISOU  374  CD1 PHE A 451     1542   1954   2041    -99      9     76       C  
ATOM    375  CD2 PHE A 451       0.069  26.289  17.698  1.00 13.42           C  
ANISOU  375  CD2 PHE A 451     1584   1689   1823    -12     33    186       C  
ATOM    376  CE1 PHE A 451      -0.854  26.266  15.112  1.00 13.43           C  
ANISOU  376  CE1 PHE A 451     1508   1723   1871   -193    -90    199       C  
ATOM    377  CE2 PHE A 451      -0.998  27.120  17.337  1.00 13.89           C  
ANISOU  377  CE2 PHE A 451     1627   1679   1968   -114      1     59       C  
ATOM    378  CZ  PHE A 451      -1.399  27.134  16.037  1.00 14.96           C  
ANISOU  378  CZ  PHE A 451     1729   1805   2148   -145    -16    228       C  
ATOM    379  N   VAL A 452       2.427  21.476  18.768  1.00 11.11           N  
ANISOU  379  N   VAL A 452     1143   1651   1427   -184    -94     69       N  
ATOM    380  CA  VAL A 452       3.602  20.854  19.336  1.00 11.36           C  
ANISOU  380  CA  VAL A 452     1405   1455   1456      5    -94     19       C  
ATOM    381  C   VAL A 452       3.577  19.315  19.396  1.00 10.59           C  
ANISOU  381  C   VAL A 452     1287   1356   1380   -103   -126    -86       C  
ATOM    382  O   VAL A 452       4.333  18.702  20.130  1.00 10.48           O  
ANISOU  382  O   VAL A 452     1302   1351   1327    -20    -99    -44       O  
ATOM    383  CB  VAL A 452       3.877  21.435  20.759  1.00 10.36           C  
ANISOU  383  CB  VAL A 452     1269   1246   1419    -17    -57   -113       C  
ATOM    384  CG1 VAL A 452       4.088  22.891  20.671  1.00  9.74           C  
ANISOU  384  CG1 VAL A 452     1149   1284   1266     95    116     16       C  
ATOM    385  CG2 VAL A 452       2.734  21.115  21.755  1.00 12.02           C  
ANISOU  385  CG2 VAL A 452     1603   1384   1579   -121    -40     36       C  
ATOM    386  N   GLU A 453       2.732  18.669  18.597  1.00 12.09           N  
ANISOU  386  N   GLU A 453     1494   1572   1527    -95   -213    -40       N  
ATOM    387  CA  GLU A 453       2.807  17.221  18.416  1.00 11.34           C  
ANISOU  387  CA  GLU A 453     1478   1502   1326    -96   -144     20       C  
ATOM    388  C   GLU A 453       2.634  16.426  19.701  1.00 12.03           C  
ANISOU  388  C   GLU A 453     1505   1611   1452   -253   -172    -54       C  
ATOM    389  O   GLU A 453       3.278  15.405  19.886  1.00 12.68           O  
ANISOU  389  O   GLU A 453     1615   1753   1448   -227   -139     69       O  
ATOM    390  CB  GLU A 453       4.016  16.778  17.624  1.00 11.61           C  
ANISOU  390  CB  GLU A 453     1475   1576   1358   -169   -180     60       C  
ATOM    391  CG  GLU A 453       4.162  17.512  16.322  1.00 12.24           C  
ANISOU  391  CG  GLU A 453     1463   1751   1436   -150   -120     42       C  
ATOM    392  CD  GLU A 453       5.378  17.004  15.593  1.00 14.20           C  
ANISOU  392  CD  GLU A 453     1703   1793   1899     89    128   -118       C  
ATOM    393  OE1 GLU A 453       6.555  17.247  16.024  1.00 15.59           O  
ANISOU  393  OE1 GLU A 453     2564   1551   1808   -161   -436   -115       O  
ATOM    394  OE2 GLU A 453       5.180  16.331  14.571  1.00 18.81           O  
ANISOU  394  OE2 GLU A 453     2314   2594   2237   -326    133   -282       O  
ATOM    395  N   ASN A 454       1.735  16.920  20.543  1.00 12.53           N  
ANISOU  395  N   ASN A 454     1485   1600   1674   -282   -173    -29       N  
ATOM    396  CA  ASN A 454       1.449  16.317  21.830  1.00 12.19           C  
ANISOU  396  CA  ASN A 454     1506   1593   1532   -176     -9    -20       C  
ATOM    397  C   ASN A 454       2.631  16.235  22.798  1.00 12.81           C  
ANISOU  397  C   ASN A 454     1673   1603   1591   -122    -12     46       C  
ATOM    398  O   ASN A 454       2.585  15.484  23.771  1.00 12.87           O  
ANISOU  398  O   ASN A 454     1556   1785   1546   -173    157    108       O  
ATOM    399  CB  ASN A 454       0.805  14.939  21.651  1.00 14.15           C  
ANISOU  399  CB  ASN A 454     1807   1839   1729   -259    -79    -58       C  
ATOM    400  CG  ASN A 454      -0.014  14.536  22.857  1.00 16.05           C  
ANISOU  400  CG  ASN A 454     2103   2099   1893   -198    -27    -47       C  
ATOM    401  OD1 ASN A 454      -0.688  15.379  23.452  1.00 17.56           O  
ANISOU  401  OD1 ASN A 454     1614   2889   2166   -256    178    148       O  
ATOM    402  ND2 ASN A 454       0.086  13.261  23.250  1.00 20.19           N  
ANISOU  402  ND2 ASN A 454     2755   2543   2372   -307   -221    172       N  
ATOM    403  N   ASN A 455       3.669  17.042  22.521  1.00 11.14           N  
ANISOU  403  N   ASN A 455     1361   1520   1352   -101    -14     74       N  
ATOM    404  CA  ASN A 455       4.787  17.140  23.402  1.00  9.25           C  
ANISOU  404  CA  ASN A 455     1136   1065   1313    -80    -28    -26       C  
ATOM    405  C   ASN A 455       4.481  18.145  24.526  1.00  9.48           C  
ANISOU  405  C   ASN A 455     1093   1162   1345    -53     28     -7       C  
ATOM    406  O   ASN A 455       3.935  19.208  24.278  1.00  9.80           O  
ANISOU  406  O   ASN A 455     1063   1252   1409     -3    -59   -151       O  
ATOM    407  CB  ASN A 455       6.016  17.574  22.620  1.00  9.53           C  
ANISOU  407  CB  ASN A 455     1160   1145   1315     20     -8    -49       C  
ATOM    408  CG  ASN A 455       6.504  16.496  21.701  1.00 10.38           C  
ANISOU  408  CG  ASN A 455     1256   1300   1387   -117    -99   -155       C  
ATOM    409  OD1 ASN A 455       6.755  15.367  22.140  1.00 12.89           O  
ANISOU  409  OD1 ASN A 455     2233   1319   1344    -30   -163    138       O  
ATOM    410  ND2 ASN A 455       6.669  16.826  20.456  1.00 10.24           N  
ANISOU  410  ND2 ASN A 455     1180   1374   1335   -160   -213     55       N  
ATOM    411  N   LEU A 456       4.865  17.815  25.750  1.00  9.02           N  
ANISOU  411  N   LEU A 456     1149    998   1277   -147     74     27       N  
ATOM    412  CA  LEU A 456       4.778  18.743  26.842  1.00  8.33           C  
ANISOU  412  CA  LEU A 456      878   1139   1146     10    123     61       C  
ATOM    413  C   LEU A 456       5.671  19.958  26.596  1.00  8.06           C  
ANISOU  413  C   LEU A 456      842    931   1288      6    -20     98       C  
ATOM    414  O   LEU A 456       6.895  19.816  26.394  1.00  8.44           O  
ANISOU  414  O   LEU A 456      798   1038   1368     26    112     45       O  
ATOM    415  CB  LEU A 456       5.184  18.087  28.159  1.00  9.26           C  
ANISOU  415  CB  LEU A 456      954   1257   1306     97     62     77       C  
ATOM    416  CG  LEU A 456       4.913  18.973  29.391  1.00  9.32           C  
ANISOU  416  CG  LEU A 456     1057   1309   1176    -44    107     47       C  
ATOM    417  CD1 LEU A 456       3.429  19.149  29.700  1.00 11.44           C  
ANISOU  417  CD1 LEU A 456     1364   1588   1394    191    184    115       C  
ATOM    418  CD2 LEU A 456       5.598  18.389  30.619  1.00  9.33           C  
ANISOU  418  CD2 LEU A 456      811   1631   1100    -32    345    128       C  
ATOM    419  N   ILE A 457       5.087  21.148  26.740  1.00  7.37           N  
ANISOU  419  N   ILE A 457      706    957   1134      1    -59     38       N  
ATOM    420  CA  ILE A 457       5.790  22.412  26.633  1.00  7.41           C  
ANISOU  420  CA  ILE A 457      825   1046    944    -42     -5     34       C  
ATOM    421  C   ILE A 457       6.479  22.748  27.946  1.00  7.80           C  
ANISOU  421  C   ILE A 457      843   1063   1055      1    -36    -98       C  
ATOM    422  O   ILE A 457       5.860  22.847  28.988  1.00  8.80           O  
ANISOU  422  O   ILE A 457     1021   1162   1159    -76    -29    -40       O  
ATOM    423  CB  ILE A 457       4.826  23.531  26.217  1.00  7.67           C  
ANISOU  423  CB  ILE A 457      979    905   1029     41     70    -50       C  
ATOM    424  CG1 ILE A 457       4.170  23.210  24.859  1.00  7.45           C  
ANISOU  424  CG1 ILE A 457      572   1135   1123    -23     64    183       C  
ATOM    425  CG2 ILE A 457       5.525  24.862  26.157  1.00  8.81           C  
ANISOU  425  CG2 ILE A 457      994   1271   1081    -59     90     77       C  
ATOM    426  CD1 ILE A 457       2.877  24.020  24.591  1.00  9.39           C  
ANISOU  426  CD1 ILE A 457     1111   1249   1208    -24      7     10       C  
ATOM    427  N   LEU A 458       7.796  22.837  27.855  1.00  7.97           N  
ANISOU  427  N   LEU A 458      798   1103   1125    -32     97    -84       N  
ATOM    428  CA  LEU A 458       8.681  23.142  28.979  1.00  7.55           C  
ANISOU  428  CA  LEU A 458      893   1005    969     91     79    -77       C  
ATOM    429  C   LEU A 458       9.010  24.613  29.147  1.00  7.41           C  
ANISOU  429  C   LEU A 458      806   1091    916    -79     74    -12       C  
ATOM    430  O   LEU A 458       9.311  25.054  30.248  1.00  8.27           O  
ANISOU  430  O   LEU A 458     1186   1168    787    -97     16     31       O  
ATOM    431  CB  LEU A 458       9.982  22.344  28.828  1.00  7.40           C  
ANISOU  431  CB  LEU A 458      843    922   1044    104     78    -62       C  
ATOM    432  CG  LEU A 458       9.788  20.842  28.554  1.00  7.72           C  
ANISOU  432  CG  LEU A 458      779   1025   1128   -108    -25   -118       C  
ATOM    433  CD1 LEU A 458      11.171  20.167  28.281  1.00  9.82           C  
ANISOU  433  CD1 LEU A 458     1120   1246   1362    216   -145     -1       C  
ATOM    434  CD2 LEU A 458       8.998  20.157  29.620  1.00  9.85           C  
ANISOU  434  CD2 LEU A 458     1027   1232   1481   -123     10     66       C  
ATOM    435  N   LYS A 459       8.941  25.362  28.064  1.00  7.13           N  
ANISOU  435  N   LYS A 459      758   1022    929    -61     79     76       N  
ATOM    436  CA  LYS A 459       9.046  26.819  28.095  1.00  6.38           C  
ANISOU  436  CA  LYS A 459      497   1039    887     32     -6     11       C  
ATOM    437  C   LYS A 459       8.435  27.396  26.843  1.00  6.63           C  
ANISOU  437  C   LYS A 459      670   1034    814    -46     79     63       C  
ATOM    438  O   LYS A 459       8.580  26.833  25.779  1.00  7.69           O  
ANISOU  438  O   LYS A 459     1040   1011    869     78     13     16       O  
ATOM    439  CB  LYS A 459      10.469  27.326  28.310  1.00  6.43           C  
ANISOU  439  CB  LYS A 459      593   1107    742   -103    129     29       C  
ATOM    440  CG  LYS A 459      10.633  28.846  28.276  1.00  7.91           C  
ANISOU  440  CG  LYS A 459      933   1173    899     34    -28   -164       C  
ATOM    441  CD  LYS A 459      12.095  29.244  28.633  1.00  8.42           C  
ANISOU  441  CD  LYS A 459      958   1190   1048     49    216     -6       C  
ATOM    442  CE  LYS A 459      12.266  30.781  28.706  1.00 10.14           C  
ANISOU  442  CE  LYS A 459     1126   1323   1403    -36    195   -112       C  
ATOM    443  NZ  LYS A 459      11.441  31.431  29.757  1.00 10.55           N  
ANISOU  443  NZ  LYS A 459     1225   1223   1558    206    352   -128       N  
ATOM    444  N   MET A 460       7.693  28.499  26.969  1.00  7.60           N  
ANISOU  444  N   MET A 460      889   1049    947      9      0    -42       N  
ATOM    445  CA  MET A 460       7.191  29.196  25.773  1.00  6.83           C  
ANISOU  445  CA  MET A 460      796    875    922      1     62     41       C  
ATOM    446  C   MET A 460       7.122  30.657  26.025  1.00  7.21           C  
ANISOU  446  C   MET A 460      826    955    957    103    -35     38       C  
ATOM    447  O   MET A 460       7.002  31.092  27.150  1.00  9.02           O  
ANISOU  447  O   MET A 460     1267   1083   1075    145     33     71       O  
ATOM    448  CB  MET A 460       5.825  28.673  25.303  1.00  7.25           C  
ANISOU  448  CB  MET A 460      792    808   1155     34     64     45       C  
ATOM    449  CG  MET A 460       4.673  29.075  26.136  1.00  7.98           C  
ANISOU  449  CG  MET A 460      982    857   1191    213    -75     74       C  
ATOM    450  SD  MET A 460       3.092  28.584  25.517  1.00 10.45           S  
ANISOU  450  SD  MET A 460      854   1647   1466    -31     -6    165       S  
ATOM    451  CE  MET A 460       1.963  29.625  26.409  1.00 11.48           C  
ANISOU  451  CE  MET A 460     1277   1584   1500   -156     95     13       C  
ATOM    452  N   GLY A 461       7.161  31.415  24.934  1.00  8.46           N  
ANISOU  452  N   GLY A 461     1211   1019    983     57     19      0       N  
ATOM    453  CA  GLY A 461       6.941  32.842  24.960  1.00  8.00           C  
ANISOU  453  CA  GLY A 461      939   1016   1085     -6   -140    -25       C  
ATOM    454  C   GLY A 461       7.291  33.466  23.636  1.00  8.03           C  
ANISOU  454  C   GLY A 461      865   1100   1086     36     38     -8       C  
ATOM    455  O   GLY A 461       7.833  32.809  22.705  1.00  8.92           O  
ANISOU  455  O   GLY A 461      973   1215   1200    -26     16    110       O  
ATOM    456  N   PRO A 462       6.883  34.723  23.471  1.00  8.84           N  
ANISOU  456  N   PRO A 462     1080   1106   1172     76    165     95       N  
ATOM    457  CA  PRO A 462       7.093  35.445  22.214  1.00  8.30           C  
ANISOU  457  CA  PRO A 462      983   1064   1105    111     35    113       C  
ATOM    458  C   PRO A 462       8.541  35.883  22.034  1.00  7.97           C  
ANISOU  458  C   PRO A 462      905   1105   1016    107    -26     66       C  
ATOM    459  O   PRO A 462       9.199  36.288  22.945  1.00  9.95           O  
ANISOU  459  O   PRO A 462     1128   1325   1327     46   -123     67       O  
ATOM    460  CB  PRO A 462       6.161  36.653  22.348  1.00 10.45           C  
ANISOU  460  CB  PRO A 462     1270   1293   1407    101    114    181       C  
ATOM    461  CG  PRO A 462       6.045  36.872  23.772  1.00 11.13           C  
ANISOU  461  CG  PRO A 462     1531   1351   1345    234    153     88       C  
ATOM    462  CD  PRO A 462       6.136  35.538  24.463  1.00  8.22           C  
ANISOU  462  CD  PRO A 462      983   1064   1074     24    102     80       C  
ATOM    463  N   VAL A 463       8.999  35.809  20.792  1.00  8.12           N  
ANISOU  463  N   VAL A 463      954   1144    987     30    -61      3       N  
ATOM    464  CA  VAL A 463      10.294  36.321  20.405  1.00  8.07           C  
ANISOU  464  CA  VAL A 463      876   1120   1068     46     72    -94       C  
ATOM    465  C   VAL A 463      10.185  36.956  19.048  1.00  8.60           C  
ANISOU  465  C   VAL A 463     1059   1084   1125     52    -64    -22       C  
ATOM    466  O   VAL A 463       9.277  36.642  18.290  1.00 10.00           O  
ANISOU  466  O   VAL A 463     1161   1267   1370    -22   -162     -4       O  
ATOM    467  CB  VAL A 463      11.401  35.203  20.330  1.00  8.63           C  
ANISOU  467  CB  VAL A 463     1080    968   1230     25     20     86       C  
ATOM    468  CG1 VAL A 463      11.621  34.560  21.727  1.00 10.17           C  
ANISOU  468  CG1 VAL A 463     1230   1359   1272    -48    -25     62       C  
ATOM    469  CG2 VAL A 463      11.071  34.177  19.229  1.00  8.18           C  
ANISOU  469  CG2 VAL A 463      894   1041   1171     99    154     89       C  
ATOM    470  N   ASP A 464      11.098  37.856  18.743  1.00  8.31           N  
ANISOU  470  N   ASP A 464     1010   1146   1000    -14      9    -51       N  
ATOM    471  CA  ASP A 464      11.249  38.389  17.388  1.00  8.82           C  
ANISOU  471  CA  ASP A 464     1209   1111   1030     53     13    -14       C  
ATOM    472  C   ASP A 464      12.439  37.715  16.733  1.00  9.05           C  
ANISOU  472  C   ASP A 464     1028   1301   1108    -20     48    -28       C  
ATOM    473  O   ASP A 464      13.559  37.860  17.208  1.00 10.23           O  
ANISOU  473  O   ASP A 464     1102   1723   1060    106     37   -216       O  
ATOM    474  CB  ASP A 464      11.377  39.908  17.388  1.00  9.53           C  
ANISOU  474  CB  ASP A 464     1270   1218   1133   -121    -29     15       C  
ATOM    475  CG  ASP A 464      10.196  40.539  18.055  1.00 11.12           C  
ANISOU  475  CG  ASP A 464     1494   1552   1179    119   -125     18       C  
ATOM    476  OD1 ASP A 464       9.075  40.345  17.578  1.00 13.11           O  
ANISOU  476  OD1 ASP A 464     1612   1569   1800    121    -20   -170       O  
ATOM    477  OD2 ASP A 464      10.256  41.237  19.100  1.00 12.69           O  
ANISOU  477  OD2 ASP A 464     1623   1669   1528     27   -125   -150       O  
ATOM    478  N   LYS A 465      12.171  36.928  15.696  1.00  7.91           N  
ANISOU  478  N   LYS A 465      788   1236    981      5    -99     21       N  
ATOM    479  CA  LYS A 465      13.215  36.175  15.018  1.00  8.89           C  
ANISOU  479  CA  LYS A 465     1099   1153   1124     87    -34     21       C  
ATOM    480  C   LYS A 465      13.719  36.961  13.848  1.00  9.03           C  
ANISOU  480  C   LYS A 465     1016   1095   1316     42     66    -50       C  
ATOM    481  O   LYS A 465      12.972  37.252  12.894  1.00 10.10           O  
ANISOU  481  O   LYS A 465     1607   1104   1127    -35    118     78       O  
ATOM    482  CB  LYS A 465      12.699  34.807  14.541  1.00 10.19           C  
ANISOU  482  CB  LYS A 465     1372   1179   1321    110     -7     10       C  
ATOM    483  CG  LYS A 465      13.756  33.998  13.763  1.00  9.10           C  
ANISOU  483  CG  LYS A 465     1131   1267   1059    -53     24     85       C  
ATOM    484  CD  LYS A 465      13.489  32.464  13.624  1.00  9.69           C  
ANISOU  484  CD  LYS A 465     1173   1297   1211    121    226    101       C  
ATOM    485  CE  LYS A 465      12.091  32.153  13.149  1.00  8.21           C  
ANISOU  485  CE  LYS A 465      949    909   1260    -92    210     10       C  
ATOM    486  NZ  LYS A 465      11.777  32.588  11.731  1.00  8.06           N  
ANISOU  486  NZ  LYS A 465     1254    733   1072   -176    -81   -285       N  
ATOM    487  N   ARG A 466      15.000  37.322  13.940  1.00 10.09           N  
ANISOU  487  N   ARG A 466      985   1422   1426    -14     20    107       N  
ATOM    488  CA  ARG A 466      15.683  38.120  12.905  1.00  9.93           C  
ANISOU  488  CA  ARG A 466     1202   1208   1363    139     49     -3       C  
ATOM    489  C   ARG A 466      16.061  37.252  11.730  1.00 11.59           C  
ANISOU  489  C   ARG A 466     1356   1509   1537     98    126     -3       C  
ATOM    490  O   ARG A 466      16.655  36.201  11.902  1.00 13.07           O  
ANISOU  490  O   ARG A 466     1949   1287   1728    146    -25      0       O  
ATOM    491  CB  ARG A 466      16.938  38.759  13.505  1.00 10.52           C  
ANISOU  491  CB  ARG A 466     1150   1316   1530    120     76    -75       C  
ATOM    492  CG  ARG A 466      16.763  39.909  14.427  1.00 11.94           C  
ANISOU  492  CG  ARG A 466     1469   1555   1512    115    135    -68       C  
ATOM    493  CD  ARG A 466      16.579  41.216  13.755  1.00 12.43           C  
ANISOU  493  CD  ARG A 466     1720   1355   1646    172     67   -160       C  
ATOM    494  NE  ARG A 466      17.863  41.688  13.308  1.00 14.44           N  
ANISOU  494  NE  ARG A 466     2019   1683   1783    121     41    100       N  
ATOM    495  CZ  ARG A 466      18.267  41.718  12.044  1.00 13.84           C  
ANISOU  495  CZ  ARG A 466     1879   1606   1773    -16     44    -76       C  
ATOM    496  NH1 ARG A 466      17.458  41.373  11.060  1.00 14.67           N  
ANISOU  496  NH1 ARG A 466     1726   1848   1999    256    -49     13       N  
ATOM    497  NH2 ARG A 466      19.488  42.165  11.764  1.00 17.29           N  
ANISOU  497  NH2 ARG A 466     1960   2178   2430    -13    178    -90       N  
ATOM    498  N   LYS A 467      15.756  37.737  10.540  1.00 10.93           N  
ANISOU  498  N   LYS A 467     1313   1350   1488     53    171     -4       N  
ATOM    499  CA  LYS A 467      16.145  37.073   9.304  1.00 12.70           C  
ANISOU  499  CA  LYS A 467     1607   1657   1561    -59    210     18       C  
ATOM    500  C   LYS A 467      16.037  38.118   8.200  1.00 12.66           C  
ANISOU  500  C   LYS A 467     1580   1564   1664     -4    124      1       C  
ATOM    501  O   LYS A 467      15.019  38.797   8.029  1.00 13.34           O  
ANISOU  501  O   LYS A 467     1452   1890   1725    124    271    157       O  
ATOM    502  CB  LYS A 467      15.235  35.872   9.018  1.00 14.11           C  
ANISOU  502  CB  LYS A 467     2021   1628   1711    -79     32    -77       C  
ATOM    503  CG  LYS A 467      15.699  34.862   7.914  1.00 18.07           C  
ANISOU  503  CG  LYS A 467     2379   2087   2399   -119    297   -101       C  
ATOM    504  CD  LYS A 467      17.045  34.389   8.100  1.00 20.26           C  
ANISOU  504  CD  LYS A 467     2659   2447   2591   -156    -45      7       C  
ATOM    505  CE  LYS A 467      17.302  33.097   7.394  1.00 22.14           C  
ANISOU  505  CE  LYS A 467     2883   2617   2911    -19    149     23       C  
ATOM    506  NZ  LYS A 467      18.092  33.309   6.166  1.00 23.66           N  
ANISOU  506  NZ  LYS A 467     3247   3021   2721   -174    143    -67       N  
ATOM    507  N   GLY A 468      17.114  38.289   7.456  1.00 12.60           N  
ANISOU  507  N   GLY A 468     1585   1585   1617    -25    265   -144       N  
ATOM    508  CA  GLY A 468      17.176  39.396   6.532  1.00 12.60           C  
ANISOU  508  CA  GLY A 468     1648   1632   1507     25    167    -49       C  
ATOM    509  C   GLY A 468      17.377  40.692   7.287  1.00 11.91           C  
ANISOU  509  C   GLY A 468     1556   1505   1463    -40    110      8       C  
ATOM    510  O   GLY A 468      18.004  40.713   8.331  1.00 12.50           O  
ANISOU  510  O   GLY A 468     1909   1482   1358     51    276    -45       O  
ATOM    511  N   LEU A 469      16.870  41.771   6.727  1.00 11.60           N  
ANISOU  511  N   LEU A 469     1472   1549   1386    -44     93     92       N  
ATOM    512  CA  LEU A 469      16.966  43.094   7.344  1.00 10.37           C  
ANISOU  512  CA  LEU A 469     1266   1430   1244     50     58     97       C  
ATOM    513  C   LEU A 469      16.108  43.227   8.567  1.00  9.30           C  
ANISOU  513  C   LEU A 469     1104   1271   1158      6     79      5       C  
ATOM    514  O   LEU A 469      16.389  44.025   9.419  1.00 10.70           O  
ANISOU  514  O   LEU A 469     1242   1415   1406   -226    121    119       O  
ATOM    515  CB  LEU A 469      16.573  44.249   6.390  1.00 11.40           C  
ANISOU  515  CB  LEU A 469     1482   1597   1252      8    168    199       C  
ATOM    516  CG  LEU A 469      17.542  44.600   5.296  1.00 14.03           C  
ANISOU  516  CG  LEU A 469     1475   2182   1674     10    239    178       C  
ATOM    517  CD1 LEU A 469      16.929  45.700   4.469  1.00 15.87           C  
ANISOU  517  CD1 LEU A 469     1690   2054   2284     34    101    126       C  
ATOM    518  CD2 LEU A 469      18.891  44.997   5.862  1.00 14.74           C  
ANISOU  518  CD2 LEU A 469     1781   1912   1908   -151    173    -10       C  
ATOM    519  N   PHE A 470      15.022  42.469   8.642  1.00  9.44           N  
ANISOU  519  N   PHE A 470     1154   1268   1164   -130    169     38       N  
ATOM    520  CA  PHE A 470      14.080  42.692   9.707  1.00 10.04           C  
ANISOU  520  CA  PHE A 470     1338   1274   1200     37     54     61       C  
ATOM    521  C   PHE A 470      13.791  41.400  10.451  1.00  8.91           C  
ANISOU  521  C   PHE A 470     1087   1133   1163   -107     -9     67       C  
ATOM    522  O   PHE A 470      14.729  40.688  10.784  1.00  9.58           O  
ANISOU  522  O   PHE A 470     1306   1229   1105    -36    109    184       O  
ATOM    523  CB  PHE A 470      12.855  43.464   9.190  1.00 10.36           C  
ANISOU  523  CB  PHE A 470     1217   1371   1348    -26    103     51       C  
ATOM    524  CG  PHE A 470      13.235  44.753   8.547  1.00 10.77           C  
ANISOU  524  CG  PHE A 470     1340   1401   1351     57     11     26       C  
ATOM    525  CD1 PHE A 470      13.826  45.764   9.313  1.00 10.98           C  
ANISOU  525  CD1 PHE A 470     1155   1520   1497    -16     99    -39       C  
ATOM    526  CD2 PHE A 470      13.071  44.954   7.183  1.00  9.46           C  
ANISOU  526  CD2 PHE A 470      865   1335   1391    -59     36     -5       C  
ATOM    527  CE1 PHE A 470      14.245  46.945   8.722  1.00 11.23           C  
ANISOU  527  CE1 PHE A 470     1323   1373   1568    -14    -14    -88       C  
ATOM    528  CE2 PHE A 470      13.483  46.143   6.583  1.00 11.36           C  
ANISOU  528  CE2 PHE A 470     1273   1513   1529   -118    -48    117       C  
ATOM    529  CZ  PHE A 470      14.106  47.109   7.341  1.00 10.57           C  
ANISOU  529  CZ  PHE A 470     1391   1096   1528     50     12     26       C  
ATOM    530  N   ALA A 471      12.542  41.106  10.740  1.00  8.14           N  
ANISOU  530  N   ALA A 471     1038   1103    950    -46    104    274       N  
ATOM    531  CA  ALA A 471      12.232  40.060  11.738  1.00  8.22           C  
ANISOU  531  CA  ALA A 471      990   1079   1054    -58     35    101       C  
ATOM    532  C   ALA A 471      10.750  39.743  11.678  1.00  7.51           C  
ANISOU  532  C   ALA A 471      861    903   1088    -13      0     16       C  
ATOM    533  O   ALA A 471       9.947  40.467  11.100  1.00  9.06           O  
ANISOU  533  O   ALA A 471     1150   1093   1197    131     99    144       O  
ATOM    534  CB  ALA A 471      12.655  40.483  13.187  1.00  8.26           C  
ANISOU  534  CB  ALA A 471     1105    939   1093    -54     67    177       C  
ATOM    535  N   ARG A 472      10.375  38.653  12.319  1.00  7.99           N  
ANISOU  535  N   ARG A 472     1027    899   1109     90     48     28       N  
ATOM    536  CA  ARG A 472       8.986  38.287  12.495  1.00  8.07           C  
ANISOU  536  CA  ARG A 472      920    987   1158     -7    -60    -29       C  
ATOM    537  C   ARG A 472       8.748  37.847  13.956  1.00  8.03           C  
ANISOU  537  C   ARG A 472      953    927   1169      0    -51     20       C  
ATOM    538  O   ARG A 472       9.564  37.177  14.572  1.00  8.77           O  
ANISOU  538  O   ARG A 472      839   1095   1398    268     -5    -15       O  
ATOM    539  CB  ARG A 472       8.603  37.144  11.570  1.00  8.81           C  
ANISOU  539  CB  ARG A 472      953   1111   1281    -21     26      0       C  
ATOM    540  CG  ARG A 472       8.676  37.441  10.109  1.00  9.74           C  
ANISOU  540  CG  ARG A 472     1249   1194   1256   -211   -106   -247       C  
ATOM    541  CD  ARG A 472       7.695  38.452   9.613  1.00  9.62           C  
ANISOU  541  CD  ARG A 472     1006   1376   1270   -213    -93    -48       C  
ATOM    542  NE  ARG A 472       7.836  38.749   8.192  1.00 10.75           N  
ANISOU  542  NE  ARG A 472     1214   1504   1365    -13   -154     32       N  
ATOM    543  CZ  ARG A 472       7.297  39.801   7.584  1.00 10.42           C  
ANISOU  543  CZ  ARG A 472     1473   1127   1357    -21    -89    -48       C  
ATOM    544  NH1 ARG A 472       6.496  40.657   8.224  1.00 13.00           N  
ANISOU  544  NH1 ARG A 472     1700   1699   1538     -3    -74    -52       N  
ATOM    545  NH2 ARG A 472       7.559  40.000   6.306  1.00 13.16           N  
ANISOU  545  NH2 ARG A 472     1992   1573   1435     72   -116    -62       N  
ATOM    546  N   ARG A 473       7.644  38.301  14.525  1.00  8.36           N  
ANISOU  546  N   ARG A 473     1071   1042   1063     43     31     62       N  
ATOM    547  CA  ARG A 473       7.198  37.873  15.829  1.00  8.79           C  
ANISOU  547  CA  ARG A 473      926   1288   1122     49    124      9       C  
ATOM    548  C   ARG A 473       6.661  36.454  15.733  1.00  7.78           C  
ANISOU  548  C   ARG A 473      851   1176    926     39     98      2       C  
ATOM    549  O   ARG A 473       5.699  36.185  14.990  1.00  8.47           O  
ANISOU  549  O   ARG A 473     1136   1250    830    -40    -41    126       O  
ATOM    550  CB  ARG A 473       6.108  38.825  16.356  1.00  8.93           C  
ANISOU  550  CB  ARG A 473     1034   1035   1322    132     75    -20       C  
ATOM    551  CG  ARG A 473       5.463  38.386  17.681  1.00 11.29           C  
ANISOU  551  CG  ARG A 473     1314   1483   1492     77    -79    205       C  
ATOM    552  CD  ARG A 473       6.381  38.184  18.813  1.00 11.36           C  
ANISOU  552  CD  ARG A 473     1509   1494   1313     -9    159     59       C  
ATOM    553  NE  ARG A 473       7.103  39.358  19.248  1.00 12.92           N  
ANISOU  553  NE  ARG A 473     1515   1740   1654     99      3    -18       N  
ATOM    554  CZ  ARG A 473       6.761  40.150  20.243  1.00 14.57           C  
ANISOU  554  CZ  ARG A 473     2051   1859   1624    -64    257     73       C  
ATOM    555  NH1 ARG A 473       5.580  40.027  20.860  1.00 15.83           N  
ANISOU  555  NH1 ARG A 473     1895   1928   2190     43    226    -72       N  
ATOM    556  NH2 ARG A 473       7.598  41.120  20.573  1.00 18.24           N  
ANISOU  556  NH2 ARG A 473     2517   2285   2126     28     88   -177       N  
ATOM    557  N   ARG A 474       7.224  35.551  16.529  1.00  8.04           N  
ANISOU  557  N   ARG A 474      980   1233    839    -51     44    -39       N  
ATOM    558  CA  ARG A 474       6.807  34.174  16.660  1.00  7.97           C  
ANISOU  558  CA  ARG A 474      921   1199    906    -66    -16    -11       C  
ATOM    559  C   ARG A 474       6.645  33.764  18.109  1.00  8.31           C  
ANISOU  559  C   ARG A 474      931   1232    994   -148    -77     47       C  
ATOM    560  O   ARG A 474       7.275  34.327  18.982  1.00  9.47           O  
ANISOU  560  O   ARG A 474     1075   1617    903   -364   -208    237       O  
ATOM    561  CB  ARG A 474       7.871  33.278  16.032  1.00  8.01           C  
ANISOU  561  CB  ARG A 474      751   1157   1133    -35      0    -11       C  
ATOM    562  CG  ARG A 474       8.086  33.582  14.574  1.00  8.44           C  
ANISOU  562  CG  ARG A 474      921   1178   1106     25      9    -82       C  
ATOM    563  CD  ARG A 474       6.912  33.157  13.712  1.00  9.91           C  
ANISOU  563  CD  ARG A 474     1352   1179   1234    -96   -114     37       C  
ATOM    564  NE  ARG A 474       7.011  33.519  12.308  1.00  8.86           N  
ANISOU  564  NE  ARG A 474      914   1332   1120    -40    -17    -92       N  
ATOM    565  CZ  ARG A 474       6.186  34.379  11.692  1.00 10.08           C  
ANISOU  565  CZ  ARG A 474     1351   1312   1165    -29    -12    120       C  
ATOM    566  NH1 ARG A 474       5.341  35.120  12.363  1.00  9.25           N  
ANISOU  566  NH1 ARG A 474     1260   1383    871   -224   -115     -8       N  
ATOM    567  NH2 ARG A 474       6.294  34.568  10.381  1.00  9.90           N  
ANISOU  567  NH2 ARG A 474     1004   1439   1318   -251     36     29       N  
ATOM    568  N   GLN A 475       5.738  32.826  18.365  1.00  8.92           N  
ANISOU  568  N   GLN A 475      985   1274   1129    -45     -3     56       N  
ATOM    569  CA  GLN A 475       5.670  32.141  19.617  1.00  7.98           C  
ANISOU  569  CA  GLN A 475      966   1011   1053     -5     26     -4       C  
ATOM    570  C   GLN A 475       6.666  30.991  19.566  1.00  8.05           C  
ANISOU  570  C   GLN A 475      759   1128   1170    -43      6     14       C  
ATOM    571  O   GLN A 475       6.548  30.129  18.710  1.00  8.15           O  
ANISOU  571  O   GLN A 475      615   1218   1260      9    -68    -72       O  
ATOM    572  CB  GLN A 475       4.257  31.626  19.880  1.00  9.66           C  
ANISOU  572  CB  GLN A 475     1138   1260   1271    -31    -20     44       C  
ATOM    573  CG  GLN A 475       4.063  31.003  21.281  1.00  9.62           C  
ANISOU  573  CG  GLN A 475      876   1467   1312    -18    132    117       C  
ATOM    574  CD  GLN A 475       4.029  31.991  22.415  1.00  8.42           C  
ANISOU  574  CD  GLN A 475      660   1306   1233    -98     64    145       C  
ATOM    575  OE1 GLN A 475       4.198  33.173  22.209  1.00 10.86           O  
ANISOU  575  OE1 GLN A 475     1284   1411   1431   -135    255    152       O  
ATOM    576  NE2 GLN A 475       3.803  31.510  23.644  1.00  9.79           N  
ANISOU  576  NE2 GLN A 475     1000   1682   1037     74    130    376       N  
ATOM    577  N   LEU A 476       7.604  30.981  20.507  1.00  7.45           N  
ANISOU  577  N   LEU A 476      888   1031    911    -54    -38    -22       N  
ATOM    578  CA  LEU A 476       8.658  29.959  20.573  1.00  5.80           C  
ANISOU  578  CA  LEU A 476      558    854    791   -116     24    -20       C  
ATOM    579  C   LEU A 476       8.298  28.968  21.643  1.00  6.66           C  
ANISOU  579  C   LEU A 476      783    950    798     36    -44     12       C  
ATOM    580  O   LEU A 476       7.962  29.355  22.769  1.00  6.93           O  
ANISOU  580  O   LEU A 476     1018    911    701     64    181    -16       O  
ATOM    581  CB  LEU A 476      10.000  30.599  20.835  1.00  7.54           C  
ANISOU  581  CB  LEU A 476      899   1088    876    -85     21    -79       C  
ATOM    582  CG  LEU A 476      11.229  29.692  20.770  1.00  7.48           C  
ANISOU  582  CG  LEU A 476      859    887   1094   -108     14     20       C  
ATOM    583  CD1 LEU A 476      11.426  29.144  19.425  1.00  9.19           C  
ANISOU  583  CD1 LEU A 476     1022   1266   1201     -4     18    -74       C  
ATOM    584  CD2 LEU A 476      12.500  30.491  21.265  1.00  8.51           C  
ANISOU  584  CD2 LEU A 476      986   1327    920    -24     66    170       C  
ATOM    585  N   LEU A 477       8.373  27.681  21.313  1.00  7.04           N  
ANISOU  585  N   LEU A 477      899    906    870    -55    163     -2       N  
ATOM    586  CA  LEU A 477       8.031  26.609  22.254  1.00  7.04           C  
ANISOU  586  CA  LEU A 477      870   1004    801    -60     41     31       C  
ATOM    587  C   LEU A 477       9.130  25.558  22.354  1.00  7.14           C  
ANISOU  587  C   LEU A 477      912    904    896   -133     16     21       C  
ATOM    588  O   LEU A 477       9.406  24.850  21.400  1.00  8.17           O  
ANISOU  588  O   LEU A 477      743   1290   1070     13    -48    -26       O  
ATOM    589  CB  LEU A 477       6.714  25.997  21.816  1.00  7.89           C  
ANISOU  589  CB  LEU A 477     1017   1057    924   -130    153     84       C  
ATOM    590  CG  LEU A 477       5.555  26.986  21.666  1.00 10.50           C  
ANISOU  590  CG  LEU A 477     1337   1194   1456     27      6    156       C  
ATOM    591  CD1 LEU A 477       5.154  27.134  20.213  1.00 12.07           C  
ANISOU  591  CD1 LEU A 477     1430   1652   1504     98     92     24       C  
ATOM    592  CD2 LEU A 477       4.335  26.603  22.499  1.00  8.99           C  
ANISOU  592  CD2 LEU A 477     1024   1124   1268    100    -49     93       C  
ATOM    593  N   LEU A 478       9.736  25.466  23.549  1.00  6.93           N  
ANISOU  593  N   LEU A 478      879    864    888   -125     82     30       N  
ATOM    594  CA  LEU A 478      10.641  24.413  23.927  1.00  6.74           C  
ANISOU  594  CA  LEU A 478      795    995    769     -1    221     -9       C  
ATOM    595  C   LEU A 478       9.841  23.290  24.573  1.00  6.52           C  
ANISOU  595  C   LEU A 478      747    925    805    -20    157    -27       C  
ATOM    596  O   LEU A 478       9.181  23.549  25.579  1.00  8.80           O  
ANISOU  596  O   LEU A 478     1301   1169    873     -8    303   -222       O  
ATOM    597  CB  LEU A 478      11.687  24.987  24.898  1.00  7.45           C  
ANISOU  597  CB  LEU A 478      778   1121    929    -25    186    112       C  
ATOM    598  CG  LEU A 478      12.733  24.042  25.508  1.00  8.15           C  
ANISOU  598  CG  LEU A 478      720   1177   1197     19     99     76       C  
ATOM    599  CD1 LEU A 478      13.678  23.422  24.403  1.00  9.12           C  
ANISOU  599  CD1 LEU A 478      965   1338   1162     38    149    -86       C  
ATOM    600  CD2 LEU A 478      13.525  24.761  26.568  1.00  8.49           C  
ANISOU  600  CD2 LEU A 478      760   1137   1330    320     -1    -46       C  
ATOM    601  N   THR A 479       9.933  22.093  24.036  1.00  6.88           N  
ANISOU  601  N   THR A 479      782   1069    761    -67    159     39       N  
ATOM    602  CA  THR A 479       9.158  20.961  24.472  1.00  7.63           C  
ANISOU  602  CA  THR A 479      923    945   1030    -53     56     36       C  
ATOM    603  C   THR A 479      10.002  19.773  24.754  1.00  8.46           C  
ANISOU  603  C   THR A 479     1008   1051   1152     -5     74     50       C  
ATOM    604  O   THR A 479      11.171  19.721  24.380  1.00  8.77           O  
ANISOU  604  O   THR A 479      961   1190   1180    -94    106     66       O  
ATOM    605  CB  THR A 479       8.088  20.561  23.410  1.00  8.54           C  
ANISOU  605  CB  THR A 479     1205   1153    886    -73    102    117       C  
ATOM    606  OG1 THR A 479       8.695  19.921  22.267  1.00  8.67           O  
ANISOU  606  OG1 THR A 479     1172   1025   1097     36     82    -92       O  
ATOM    607  CG2 THR A 479       7.313  21.782  22.862  1.00  8.26           C  
ANISOU  607  CG2 THR A 479     1055   1242    842    -13     60     67       C  
ATOM    608  N   GLU A 480       9.381  18.773  25.371  1.00  8.74           N  
ANISOU  608  N   GLU A 480      980    998   1343     72    121     89       N  
ATOM    609  CA  GLU A 480       9.985  17.455  25.452  1.00  9.78           C  
ANISOU  609  CA  GLU A 480     1115   1189   1409     96      5     37       C  
ATOM    610  C   GLU A 480      10.285  16.955  24.045  1.00  9.33           C  
ANISOU  610  C   GLU A 480     1105   1118   1319     22    -10     56       C  
ATOM    611  O   GLU A 480       9.688  17.435  23.070  1.00  9.78           O  
ANISOU  611  O   GLU A 480     1286   1080   1349    -99   -209    -24       O  
ATOM    612  CB  GLU A 480       9.057  16.514  26.212  1.00 12.40           C  
ANISOU  612  CB  GLU A 480     1515   1328   1868    131     32     50       C  
ATOM    613  CG  GLU A 480       7.915  16.014  25.414  1.00 14.07           C  
ANISOU  613  CG  GLU A 480     1627   1939   1779   -111    117    -59       C  
ATOM    614  CD  GLU A 480       7.067  14.969  26.143  1.00 12.40           C  
ANISOU  614  CD  GLU A 480     1347   1416   1946   -242     38    -19       C  
ATOM    615  OE1 GLU A 480       7.547  13.885  26.497  1.00 16.09           O  
ANISOU  615  OE1 GLU A 480     1683   2085   2344     56    336    220       O  
ATOM    616  OE2 GLU A 480       5.897  15.245  26.392  1.00 11.18           O  
ANISOU  616  OE2 GLU A 480     1481   1310   1455     77    490    185       O  
ATOM    617  N   GLY A 481      11.259  16.043  23.963  1.00  9.28           N  
ANISOU  617  N   GLY A 481     1157   1019   1349    -95     49    -16       N  
ATOM    618  CA  GLY A 481      11.769  15.519  22.702  1.00 10.22           C  
ANISOU  618  CA  GLY A 481     1382   1200   1301     -8    -21    -11       C  
ATOM    619  C   GLY A 481      13.277  15.481  22.734  1.00 10.56           C  
ANISOU  619  C   GLY A 481     1413   1259   1337    -20     59     25       C  
ATOM    620  O   GLY A 481      13.862  14.388  22.731  1.00 11.23           O  
ANISOU  620  O   GLY A 481     1616   1245   1406      7    263     34       O  
ATOM    621  N   PRO A 482      13.966  16.639  22.716  1.00 10.28           N  
ANISOU  621  N   PRO A 482     1353   1238   1311     18      3     20       N  
ATOM    622  CA  PRO A 482      13.359  17.988  22.688  1.00 10.12           C  
ANISOU  622  CA  PRO A 482     1414   1243   1186    -10     -8    -51       C  
ATOM    623  C   PRO A 482      12.981  18.472  21.305  1.00  9.56           C  
ANISOU  623  C   PRO A 482     1275   1120   1236     68     27    -26       C  
ATOM    624  O   PRO A 482      13.466  17.958  20.296  1.00 10.93           O  
ANISOU  624  O   PRO A 482     1574   1583    996    -11    121     37       O  
ATOM    625  CB  PRO A 482      14.472  18.879  23.253  1.00 11.03           C  
ANISOU  625  CB  PRO A 482     1495   1455   1238    -36      5    -30       C  
ATOM    626  CG  PRO A 482      15.704  18.167  22.861  1.00 12.54           C  
ANISOU  626  CG  PRO A 482     1554   1459   1752    -34     -4    125       C  
ATOM    627  CD  PRO A 482      15.436  16.700  22.746  1.00 10.72           C  
ANISOU  627  CD  PRO A 482     1378   1427   1266   -128    -29     33       C  
ATOM    628  N   HIS A 483      12.148  19.531  21.338  1.00  9.18           N  
ANISOU  628  N   HIS A 483     1194   1086   1204     85     29    -54       N  
ATOM    629  CA  HIS A 483      11.818  20.354  20.213  1.00  9.19           C  
ANISOU  629  CA  HIS A 483     1188   1205   1098     -4    -58    -47       C  
ATOM    630  C   HIS A 483      11.869  21.818  20.560  1.00  8.37           C  
ANISOU  630  C   HIS A 483      929   1172   1076     71    -19     11       C  
ATOM    631  O   HIS A 483      11.673  22.192  21.722  1.00  9.62           O  
ANISOU  631  O   HIS A 483     1349   1263   1041    160    -89    -25       O  
ATOM    632  CB  HIS A 483      10.437  20.048  19.674  1.00  9.77           C  
ANISOU  632  CB  HIS A 483     1115   1404   1192      3     95    -31       C  
ATOM    633  CG  HIS A 483      10.270  18.675  19.110  1.00  9.44           C  
ANISOU  633  CG  HIS A 483     1120   1417   1048    113     63    -25       C  
ATOM    634  ND1 HIS A 483       9.972  17.561  19.871  1.00 13.78           N  
ANISOU  634  ND1 HIS A 483     1837   1481   1916     88     93   -179       N  
ATOM    635  CD2 HIS A 483      10.349  18.246  17.831  1.00  7.90           C  
ANISOU  635  CD2 HIS A 483      831   1254    916    171     -5   -232       C  
ATOM    636  CE1 HIS A 483       9.908  16.501  19.081  1.00 12.03           C  
ANISOU  636  CE1 HIS A 483     1900   1124   1545    -81   -242    -34       C  
ATOM    637  NE2 HIS A 483      10.142  16.893  17.844  1.00 13.46           N  
ANISOU  637  NE2 HIS A 483     1687   1640   1786    -98    -24   -212       N  
ATOM    638  N   LEU A 484      12.176  22.637  19.549  1.00  9.36           N  
ANISOU  638  N   LEU A 484     1185   1321   1050     46     23    -43       N  
ATOM    639  CA  LEU A 484      11.983  24.086  19.587  1.00  9.45           C  
ANISOU  639  CA  LEU A 484     1095   1304   1190     14     86    -16       C  
ATOM    640  C   LEU A 484      11.135  24.464  18.355  1.00 10.07           C  
ANISOU  640  C   LEU A 484     1161   1429   1234    -48     37    -20       C  
ATOM    641  O   LEU A 484      11.645  24.552  17.233  1.00 12.37           O  
ANISOU  641  O   LEU A 484     1304   2018   1377     25     75    124       O  
ATOM    642  CB  LEU A 484      13.345  24.813  19.522  1.00  9.91           C  
ANISOU  642  CB  LEU A 484     1060   1282   1422    -29   -114    -41       C  
ATOM    643  CG  LEU A 484      13.986  25.098  20.869  1.00  9.28           C  
ANISOU  643  CG  LEU A 484     1104   1334   1085     54    175      0       C  
ATOM    644  CD1 LEU A 484      15.493  25.384  20.735  1.00  9.73           C  
ANISOU  644  CD1 LEU A 484     1039   1415   1242     86    190   -234       C  
ATOM    645  CD2 LEU A 484      13.239  26.193  21.578  1.00 10.72           C  
ANISOU  645  CD2 LEU A 484     1249   1403   1421     44    125   -167       C  
ATOM    646  N   TYR A 485       9.842  24.551  18.547  1.00  9.57           N  
ANISOU  646  N   TYR A 485     1225   1302   1107      3     88    -71       N  
ATOM    647  CA  TYR A 485       8.887  24.966  17.543  1.00  8.72           C  
ANISOU  647  CA  TYR A 485     1069   1232   1009    -29     62    -17       C  
ATOM    648  C   TYR A 485       8.716  26.485  17.544  1.00  7.47           C  
ANISOU  648  C   TYR A 485      894   1147    797     34     75     18       C  
ATOM    649  O   TYR A 485       8.780  27.128  18.581  1.00  8.55           O  
ANISOU  649  O   TYR A 485     1139   1329    780   -130     19   -101       O  
ATOM    650  CB  TYR A 485       7.500  24.375  17.837  1.00  9.26           C  
ANISOU  650  CB  TYR A 485     1202   1242   1072   -101    105     52       C  
ATOM    651  CG  TYR A 485       7.371  22.866  17.898  1.00  8.56           C  
ANISOU  651  CG  TYR A 485      883   1116   1253    -80     82   -108       C  
ATOM    652  CD1 TYR A 485       7.240  22.114  16.748  1.00  9.21           C  
ANISOU  652  CD1 TYR A 485      995   1497   1005   -130     27    115       C  
ATOM    653  CD2 TYR A 485       7.407  22.192  19.115  1.00  9.01           C  
ANISOU  653  CD2 TYR A 485     1125   1106   1192   -115     -9    -88       C  
ATOM    654  CE1 TYR A 485       7.095  20.721  16.825  1.00 11.62           C  
ANISOU  654  CE1 TYR A 485     1783   1298   1333    -12   -132   -159       C  
ATOM    655  CE2 TYR A 485       7.257  20.834  19.192  1.00  8.94           C  
ANISOU  655  CE2 TYR A 485     1201   1082   1111   -134     43      0       C  
ATOM    656  CZ  TYR A 485       7.103  20.109  18.055  1.00 10.59           C  
ANISOU  656  CZ  TYR A 485     1506   1129   1387      6    -10    -36       C  
ATOM    657  OH  TYR A 485       6.958  18.758  18.166  1.00 12.35           O  
ANISOU  657  OH  TYR A 485     1577   1241   1872   -140   -235    -27       O  
ATOM    658  N   TYR A 486       8.443  27.078  16.377  1.00  8.15           N  
ANISOU  658  N   TYR A 486     1086   1163    847    -85     27     72       N  
ATOM    659  CA  TYR A 486       8.024  28.481  16.338  1.00  8.53           C  
ANISOU  659  CA  TYR A 486     1018   1114   1109      7    -25     24       C  
ATOM    660  C   TYR A 486       6.794  28.681  15.423  1.00  9.18           C  
ANISOU  660  C   TYR A 486     1139   1218   1129   -113    -45     56       C  
ATOM    661  O   TYR A 486       6.674  28.121  14.320  1.00 10.07           O  
ANISOU  661  O   TYR A 486     1259   1443   1121    -43   -199    -79       O  
ATOM    662  CB  TYR A 486       9.194  29.451  15.963  1.00  8.80           C  
ANISOU  662  CB  TYR A 486     1001   1198   1143    -60     -8     41       C  
ATOM    663  CG  TYR A 486       9.966  29.103  14.708  1.00 10.14           C  
ANISOU  663  CG  TYR A 486     1437   1150   1265   -113    -56      9       C  
ATOM    664  CD1 TYR A 486      11.112  28.312  14.751  1.00 10.84           C  
ANISOU  664  CD1 TYR A 486     1515   1209   1395    -72    168      9       C  
ATOM    665  CD2 TYR A 486       9.576  29.627  13.460  1.00  8.95           C  
ANISOU  665  CD2 TYR A 486      978   1104   1315   -124   -267     98       C  
ATOM    666  CE1 TYR A 486      11.784  27.990  13.612  1.00  9.60           C  
ANISOU  666  CE1 TYR A 486     1431    911   1303   -110     18    -30       C  
ATOM    667  CE2 TYR A 486      10.226  29.298  12.313  1.00  9.98           C  
ANISOU  667  CE2 TYR A 486     1070   1145   1576   -143   -237     18       C  
ATOM    668  CZ  TYR A 486      11.352  28.490  12.372  1.00  9.33           C  
ANISOU  668  CZ  TYR A 486     1216    963   1366     42    -21    -10       C  
ATOM    669  OH  TYR A 486      12.045  28.146  11.221  1.00 11.62           O  
ANISOU  669  OH  TYR A 486     1973    880   1558    121    182      5       O  
ATOM    670  N   VAL A 487       5.881  29.445  15.942  1.00  9.86           N  
ANISOU  670  N   VAL A 487     1262   1259   1225    -63   -132    -43       N  
ATOM    671  CA  VAL A 487       4.514  29.553  15.422  1.00  9.83           C  
ANISOU  671  CA  VAL A 487     1134   1368   1232     45    -32    -10       C  
ATOM    672  C   VAL A 487       4.191  31.026  15.126  1.00  9.82           C  
ANISOU  672  C   VAL A 487     1318   1295   1118    -86    -69     30       C  
ATOM    673  O   VAL A 487       4.498  31.901  15.901  1.00  9.55           O  
ANISOU  673  O   VAL A 487     1106   1453   1068   -320    -40    244       O  
ATOM    674  CB  VAL A 487       3.497  29.008  16.463  1.00 10.24           C  
ANISOU  674  CB  VAL A 487     1225   1391   1273    -16   -135    132       C  
ATOM    675  CG1 VAL A 487       2.048  29.156  15.901  1.00  9.41           C  
ANISOU  675  CG1 VAL A 487      931   1381   1261   -208     41    278       C  
ATOM    676  CG2 VAL A 487       3.745  27.523  16.815  1.00 11.82           C  
ANISOU  676  CG2 VAL A 487     1251   1608   1629    -42     11     70       C  
ATOM    677  N   ASP A 488       3.501  31.287  14.016  1.00 10.97           N  
ANISOU  677  N   ASP A 488     1301   1516   1350   -199   -142     72       N  
ATOM    678  CA  ASP A 488       2.976  32.599  13.686  1.00 10.51           C  
ANISOU  678  CA  ASP A 488     1184   1425   1383   -109   -112    -62       C  
ATOM    679  C   ASP A 488       1.726  32.802  14.566  1.00 11.25           C  
ANISOU  679  C   ASP A 488     1246   1459   1569    -47    -90     93       C  
ATOM    680  O   ASP A 488       0.734  32.051  14.384  1.00 12.53           O  
ANISOU  680  O   ASP A 488     1547   1487   1727   -216   -268     63       O  
ATOM    681  CB  ASP A 488       2.678  32.676  12.171  1.00 12.08           C  
ANISOU  681  CB  ASP A 488     1510   1523   1555    -34   -108    -85       C  
ATOM    682  CG  ASP A 488       1.948  33.932  11.749  1.00 11.94           C  
ANISOU  682  CG  ASP A 488     1497   1653   1384   -221   -319    -48       C  
ATOM    683  OD1 ASP A 488       1.390  34.702  12.596  1.00 13.09           O  
ANISOU  683  OD1 ASP A 488     1442   1763   1767    143   -336    129       O  
ATOM    684  OD2 ASP A 488       1.876  34.171  10.540  1.00 17.87           O  
ANISOU  684  OD2 ASP A 488     2633   2499   1657    240   -398    318       O  
ATOM    685  N   PRO A 489       1.766  33.747  15.516  1.00 12.57           N  
ANISOU  685  N   PRO A 489     1448   1764   1564    -41    -57    142       N  
ATOM    686  CA  PRO A 489       0.720  33.930  16.550  1.00 14.40           C  
ANISOU  686  CA  PRO A 489     1668   1969   1832     43    -29    109       C  
ATOM    687  C   PRO A 489      -0.531  34.646  16.055  1.00 15.91           C  
ANISOU  687  C   PRO A 489     1715   2222   2107    103     96    144       C  
ATOM    688  O   PRO A 489      -1.566  34.618  16.755  1.00 17.27           O  
ANISOU  688  O   PRO A 489     1448   2610   2504    104    112    276       O  
ATOM    689  CB  PRO A 489       1.430  34.777  17.591  1.00 15.30           C  
ANISOU  689  CB  PRO A 489     1794   2031   1987    -26     80     73       C  
ATOM    690  CG  PRO A 489       2.457  35.579  16.827  1.00 14.61           C  
ANISOU  690  CG  PRO A 489     1676   1999   1874     38    -22     46       C  
ATOM    691  CD  PRO A 489       2.896  34.683  15.730  1.00 12.33           C  
ANISOU  691  CD  PRO A 489     1527   1670   1488    -97   -113     11       C  
ATOM    692  N   VAL A 490      -0.444  35.256  14.872  1.00 16.09           N  
ANISOU  692  N   VAL A 490     1623   2215   2273    -15    -48    140       N  
ATOM    693  CA  VAL A 490      -1.580  35.967  14.296  1.00 16.97           C  
ANISOU  693  CA  VAL A 490     1988   2208   2250     54    -79    185       C  
ATOM    694  C   VAL A 490      -2.346  35.026  13.408  1.00 17.86           C  
ANISOU  694  C   VAL A 490     2045   2253   2487      3    -37    156       C  
ATOM    695  O   VAL A 490      -3.573  34.867  13.513  1.00 19.11           O  
ANISOU  695  O   VAL A 490     1915   2521   2822     78    -96    395       O  
ATOM    696  CB  VAL A 490      -1.081  37.185  13.547  1.00 16.05           C  
ANISOU  696  CB  VAL A 490     1871   2151   2075     94   -115    152       C  
ATOM    697  CG1 VAL A 490      -2.286  37.891  12.874  1.00 16.64           C  
ANISOU  697  CG1 VAL A 490     1763   2253   2306    125   -165    214       C  
ATOM    698  CG2 VAL A 490      -0.382  38.151  14.493  1.00 17.02           C  
ANISOU  698  CG2 VAL A 490     1982   2162   2323     52    -40    158       C  
ATOM    699  N   ASN A 491      -1.648  34.358  12.537  1.00 17.99           N  
ANISOU  699  N   ASN A 491     2067   2322   2444    -87    -32    139       N  
ATOM    700  CA  ASN A 491      -2.269  33.459  11.590  1.00 18.96           C  
ANISOU  700  CA  ASN A 491     2242   2372   2590    -17   -123    105       C  
ATOM    701  C   ASN A 491      -2.465  32.061  12.168  1.00 18.35           C  
ANISOU  701  C   ASN A 491     2169   2337   2465    -84   -129    114       C  
ATOM    702  O   ASN A 491      -3.121  31.253  11.561  1.00 18.78           O  
ANISOU  702  O   ASN A 491     2093   2468   2573    -42   -324    180       O  
ATOM    703  CB  ASN A 491      -1.468  33.457  10.333  1.00 19.29           C  
ANISOU  703  CB  ASN A 491     2289   2370   2667    -47   -142     25       C  
ATOM    704  CG  ASN A 491      -1.472  34.826   9.671  1.00 19.93           C  
ANISOU  704  CG  ASN A 491     2214   2691   2666   -142    -30    399       C  
ATOM    705  OD1 ASN A 491      -2.550  35.318   9.267  1.00 22.93           O  
ANISOU  705  OD1 ASN A 491     2663   2908   3140      0    -47    472       O  
ATOM    706  ND2 ASN A 491      -0.286  35.479   9.588  1.00 21.84           N  
ANISOU  706  ND2 ASN A 491     2605   2779   2911   -358   -110     79       N  
ATOM    707  N   LYS A 492      -1.872  31.780  13.339  1.00 17.24           N  
ANISOU  707  N   LYS A 492     1948   2220   2379    -84   -119    107       N  
ATOM    708  CA  LYS A 492      -2.015  30.486  13.996  1.00 17.14           C  
ANISOU  708  CA  LYS A 492     1952   2239   2320    -58    -74    101       C  
ATOM    709  C   LYS A 492      -1.567  29.308  13.142  1.00 15.22           C  
ANISOU  709  C   LYS A 492     1709   2050   2023    -84   -129    136       C  
ATOM    710  O   LYS A 492      -2.322  28.349  12.905  1.00 16.78           O  
ANISOU  710  O   LYS A 492     1857   2260   2258   -150   -156    319       O  
ATOM    711  CB  LYS A 492      -3.472  30.319  14.415  1.00 18.27           C  
ANISOU  711  CB  LYS A 492     2144   2306   2490   -128     86    198       C  
ATOM    712  CG  LYS A 492      -4.032  31.446  15.245  1.00 22.24           C  
ANISOU  712  CG  LYS A 492     2825   2672   2953    -47    145     61       C  
ATOM    713  CD  LYS A 492      -3.150  31.834  16.348  1.00 26.98           C  
ANISOU  713  CD  LYS A 492     3325   3508   3418   -118    -29     79       C  
ATOM    714  CE  LYS A 492      -3.896  32.557  17.486  1.00 31.15           C  
ANISOU  714  CE  LYS A 492     3919   3965   3951     41     50    -59       C  
ATOM    715  NZ  LYS A 492      -5.071  33.377  17.039  1.00 32.95           N  
ANISOU  715  NZ  LYS A 492     4185   4104   4228    122    -42     27       N  
ATOM    716  N   VAL A 493      -0.321  29.375  12.677  1.00 14.79           N  
ANISOU  716  N   VAL A 493     1637   1928   2053      9   -176    141       N  
ATOM    717  CA  VAL A 493       0.298  28.392  11.826  1.00 14.64           C  
ANISOU  717  CA  VAL A 493     1730   1946   1887    -75   -126     55       C  
ATOM    718  C   VAL A 493       1.735  28.140  12.307  1.00 14.47           C  
ANISOU  718  C   VAL A 493     1718   1860   1918    -60   -121     43       C  
ATOM    719  O   VAL A 493       2.463  29.073  12.547  1.00 13.29           O  
ANISOU  719  O   VAL A 493     1750   1666   1632   -223   -159     87       O  
ATOM    720  CB AVAL A 493       0.192  28.667  10.307  0.50 16.13           C  
ANISOU  720  CB AVAL A 493     1929   2128   2071      1    -43     71       C  
ATOM    721  CG1AVAL A 493       1.087  29.800   9.866  0.50 14.73           C  
ANISOU  721  CG1AVAL A 493     1687   1970   1938     -5   -120     18       C  
ATOM    722  CG2AVAL A 493       0.451  27.396   9.534  0.50 17.95           C  
ANISOU  722  CG2AVAL A 493     2245   2356   2217    -11    -78     21       C  
ATOM    723  CB BVAL A 493       0.288  28.918  10.365  0.50 15.50           C  
ANISOU  723  CB BVAL A 493     1772   2092   2026    -16    -61     43       C  
ATOM    724  CG1BVAL A 493       1.273  28.223   9.472  0.50 14.45           C  
ANISOU  724  CG1BVAL A 493     1735   1786   1969   -143    -10    -20       C  
ATOM    725  CG2BVAL A 493      -1.131  28.805   9.796  0.50 14.45           C  
ANISOU  725  CG2BVAL A 493     1694   2048   1746    -26   -188    -11       C  
ATOM    726  N   LEU A 494       2.137  26.875  12.371  1.00 14.43           N  
ANISOU  726  N   LEU A 494     1818   1870   1793   -182   -198     39       N  
ATOM    727  CA  LEU A 494       3.492  26.492  12.651  1.00 13.88           C  
ANISOU  727  CA  LEU A 494     1671   1739   1864   -124    -26    -20       C  
ATOM    728  C   LEU A 494       4.345  26.949  11.473  1.00 13.98           C  
ANISOU  728  C   LEU A 494     1682   1923   1704   -153     -8   -110       C  
ATOM    729  O   LEU A 494       4.034  26.671  10.312  1.00 15.69           O  
ANISOU  729  O   LEU A 494     1560   2412   1989   -272   -186    -64       O  
ATOM    730  CB  LEU A 494       3.628  24.965  12.785  1.00 14.61           C  
ANISOU  730  CB  LEU A 494     1825   1759   1964   -188    -80    -25       C  
ATOM    731  CG  LEU A 494       5.016  24.419  13.036  1.00 17.57           C  
ANISOU  731  CG  LEU A 494     2263   2071   2339    -61   -109    -49       C  
ATOM    732  CD1 LEU A 494       5.463  24.806  14.440  1.00 17.09           C  
ANISOU  732  CD1 LEU A 494     2238   2127   2128    -62    -77     83       C  
ATOM    733  CD2 LEU A 494       5.120  22.898  12.820  1.00 19.08           C  
ANISOU  733  CD2 LEU A 494     2484   2143   2623    -78   -108    -91       C  
ATOM    734  N   LYS A 495       5.434  27.652  11.783  1.00 11.60           N  
ANISOU  734  N   LYS A 495     1463   1543   1401   -151    -46   -143       N  
ATOM    735  CA  LYS A 495       6.341  28.097  10.722  1.00 11.99           C  
ANISOU  735  CA  LYS A 495     1478   1676   1400   -142    -47      0       C  
ATOM    736  C   LYS A 495       7.607  27.287  10.593  1.00 12.25           C  
ANISOU  736  C   LYS A 495     1685   1600   1366    -61    -26     20       C  
ATOM    737  O   LYS A 495       8.213  27.222   9.526  1.00 14.79           O  
ANISOU  737  O   LYS A 495     1867   2185   1567    -76     74      2       O  
ATOM    738  CB  LYS A 495       6.666  29.580  10.856  1.00 11.93           C  
ANISOU  738  CB  LYS A 495     1608   1586   1339    -69     23     -5       C  
ATOM    739  CG  LYS A 495       5.498  30.569  10.795  1.00 12.15           C  
ANISOU  739  CG  LYS A 495     1686   1419   1511   -180    -31    146       C  
ATOM    740  CD  LYS A 495       4.646  30.401   9.585  1.00 16.51           C  
ANISOU  740  CD  LYS A 495     1978   2120   2175    -57   -238     34       C  
ATOM    741  CE  LYS A 495       5.349  30.673   8.280  1.00 22.53           C  
ANISOU  741  CE  LYS A 495     2680   3144   2736     26    -68    105       C  
ATOM    742  NZ  LYS A 495       4.291  31.053   7.210  1.00 25.71           N  
ANISOU  742  NZ  LYS A 495     3411   3522   2836     71   -270    188       N  
ATOM    743  N   GLY A 496       8.033  26.618  11.650  1.00 11.25           N  
ANISOU  743  N   GLY A 496     1618   1452   1202    -81    -53    -43       N  
ATOM    744  CA  GLY A 496       9.203  25.792  11.606  1.00 10.46           C  
ANISOU  744  CA  GLY A 496     1381   1453   1139   -132     63   -105       C  
ATOM    745  C   GLY A 496       9.671  25.347  12.986  1.00 10.44           C  
ANISOU  745  C   GLY A 496     1406   1351   1207    -15      9      0       C  
ATOM    746  O   GLY A 496       8.964  25.544  14.001  1.00  9.93           O  
ANISOU  746  O   GLY A 496     1222   1572    979   -113   -166   -119       O  
ATOM    747  N   GLU A 497      10.803  24.653  12.997  1.00 11.27           N  
ANISOU  747  N   GLU A 497     1552   1516   1211     -8     12    -99       N  
ATOM    748  CA  GLU A 497      11.494  24.191  14.175  1.00 11.38           C  
ANISOU  748  CA  GLU A 497     1402   1573   1348      0     20    -44       C  
ATOM    749  C   GLU A 497      12.956  24.560  14.067  1.00 11.64           C  
ANISOU  749  C   GLU A 497     1343   1722   1356     40     73    -23       C  
ATOM    750  O   GLU A 497      13.540  24.523  12.969  1.00 15.73           O  
ANISOU  750  O   GLU A 497     2075   2373   1526    -22     99      7       O  
ATOM    751  CB  GLU A 497      11.427  22.675  14.261  1.00 10.33           C  
ANISOU  751  CB  GLU A 497     1170   1631   1124    -32     79    112       C  
ATOM    752  CG  GLU A 497      10.072  22.120  14.644  1.00 11.77           C  
ANISOU  752  CG  GLU A 497     1259   1861   1351    -46    123    -10       C  
ATOM    753  CD  GLU A 497      10.166  20.637  14.927  1.00 14.56           C  
ANISOU  753  CD  GLU A 497     2015   1842   1675   -107    -57     -4       C  
ATOM    754  OE1 GLU A 497      10.934  20.255  15.859  1.00 14.74           O  
ANISOU  754  OE1 GLU A 497     2191   1564   1843    -85     39    107       O  
ATOM    755  OE2 GLU A 497       9.517  19.858  14.168  1.00 15.50           O  
ANISOU  755  OE2 GLU A 497     2520   1787   1580   -146   -283   -120       O  
ATOM    756  N   ILE A 498      13.573  24.867  15.194  1.00 11.57           N  
ANISOU  756  N   ILE A 498     1471   1614   1311      4    173    -29       N  
ATOM    757  CA  ILE A 498      14.999  24.896  15.285  1.00 10.43           C  
ANISOU  757  CA  ILE A 498     1300   1557   1106   -157     67     32       C  
ATOM    758  C   ILE A 498      15.479  23.472  15.491  1.00 11.82           C  
ANISOU  758  C   ILE A 498     1284   1784   1421     -9     13    -71       C  
ATOM    759  O   ILE A 498      15.051  22.802  16.448  1.00 13.00           O  
ANISOU  759  O   ILE A 498     1584   1887   1466    136    -19    115       O  
ATOM    760  CB  ILE A 498      15.452  25.846  16.450  1.00 11.15           C  
ANISOU  760  CB  ILE A 498     1313   1677   1247    -74    112    -28       C  
ATOM    761  CG1 ILE A 498      14.942  27.271  16.236  1.00 11.61           C  
ANISOU  761  CG1 ILE A 498     1408   1772   1229   -145     20    -84       C  
ATOM    762  CG2 ILE A 498      16.981  25.755  16.604  1.00 11.61           C  
ANISOU  762  CG2 ILE A 498     1280   1831   1297    -62    188    -49       C  
ATOM    763  CD1 ILE A 498      15.366  28.217  17.337  1.00 10.84           C  
ANISOU  763  CD1 ILE A 498     1452   1552   1112    226    165   -169       C  
ATOM    764  N   PRO A 499      16.339  22.958  14.617  1.00 12.75           N  
ANISOU  764  N   PRO A 499     1571   1739   1535    112    123    -80       N  
ATOM    765  CA  PRO A 499      16.708  21.524  14.679  1.00 12.31           C  
ANISOU  765  CA  PRO A 499     1536   1662   1477     88    202    -64       C  
ATOM    766  C   PRO A 499      17.596  21.188  15.840  1.00 11.61           C  
ANISOU  766  C   PRO A 499     1420   1587   1403     61    104   -200       C  
ATOM    767  O   PRO A 499      18.600  21.852  16.080  1.00 12.87           O  
ANISOU  767  O   PRO A 499     1538   1661   1689    -74    -85    -64       O  
ATOM    768  CB  PRO A 499      17.467  21.261  13.359  1.00 13.19           C  
ANISOU  768  CB  PRO A 499     1721   1862   1426    154    175   -185       C  
ATOM    769  CG  PRO A 499      18.023  22.567  12.997  1.00 12.98           C  
ANISOU  769  CG  PRO A 499     1589   1849   1495    197    242   -118       C  
ATOM    770  CD  PRO A 499      16.980  23.638  13.487  1.00 12.87           C  
ANISOU  770  CD  PRO A 499     1712   1429   1747    107    126   -123       C  
ATOM    771  N   TRP A 500      17.220  20.182  16.591  1.00 11.91           N  
ANISOU  771  N   TRP A 500     1368   1613   1542    -81    -57   -173       N  
ATOM    772  CA  TRP A 500      18.048  19.680  17.675  1.00 13.09           C  
ANISOU  772  CA  TRP A 500     1591   1666   1716     -2     37    -92       C  
ATOM    773  C   TRP A 500      19.052  18.650  17.216  1.00 14.38           C  
ANISOU  773  C   TRP A 500     1831   1823   1806     12     67   -163       C  
ATOM    774  O   TRP A 500      18.747  17.732  16.448  1.00 16.36           O  
ANISOU  774  O   TRP A 500     2171   1960   2083   -136    -11   -356       O  
ATOM    775  CB  TRP A 500      17.203  19.060  18.791  1.00 11.20           C  
ANISOU  775  CB  TRP A 500     1443   1467   1343    106    122   -140       C  
ATOM    776  CG  TRP A 500      16.655  20.117  19.725  1.00  9.46           C  
ANISOU  776  CG  TRP A 500     1272   1255   1064     24    125   -121       C  
ATOM    777  CD1 TRP A 500      15.525  20.862  19.569  1.00 10.51           C  
ANISOU  777  CD1 TRP A 500     1327   1455   1211   -121    -73    -37       C  
ATOM    778  CD2 TRP A 500      17.265  20.563  20.942  1.00 10.06           C  
ANISOU  778  CD2 TRP A 500     1112   1335   1373    -59   -128   -201       C  
ATOM    779  NE1 TRP A 500      15.362  21.717  20.636  1.00 10.28           N  
ANISOU  779  NE1 TRP A 500      947   1502   1456     36      9    -61       N  
ATOM    780  CE2 TRP A 500      16.411  21.536  21.503  1.00  9.04           C  
ANISOU  780  CE2 TRP A 500      896   1420   1117     11    109   -155       C  
ATOM    781  CE3 TRP A 500      18.419  20.213  21.642  1.00  9.86           C  
ANISOU  781  CE3 TRP A 500     1166   1252   1327    120     55   -104       C  
ATOM    782  CZ2 TRP A 500      16.698  22.190  22.682  1.00 10.35           C  
ANISOU  782  CZ2 TRP A 500     1303   1329   1301    -78    -61    -46       C  
ATOM    783  CZ3 TRP A 500      18.664  20.826  22.843  1.00 11.04           C  
ANISOU  783  CZ3 TRP A 500     1295   1511   1389    113    232    -54       C  
ATOM    784  CH2 TRP A 500      17.835  21.831  23.327  1.00 10.35           C  
ANISOU  784  CH2 TRP A 500     1262   1325   1344     -9     57   -166       C  
ATOM    785  N   SER A 501      20.222  18.787  17.775  1.00 13.54           N  
ANISOU  785  N   SER A 501     1518   1853   1773    150     70   -145       N  
ATOM    786  CA  SER A 501      21.267  17.778  17.716  1.00 14.22           C  
ANISOU  786  CA  SER A 501     1821   1769   1812     80     34   -128       C  
ATOM    787  C   SER A 501      22.252  18.102  18.883  1.00 14.72           C  
ANISOU  787  C   SER A 501     1648   1833   2112     59    -15   -128       C  
ATOM    788  O   SER A 501      22.163  19.157  19.539  1.00 13.53           O  
ANISOU  788  O   SER A 501     1585   1683   1870    213    180   -196       O  
ATOM    789  CB  SER A 501      21.958  17.843  16.383  1.00 15.82           C  
ANISOU  789  CB  SER A 501     1917   2001   2090     88     25   -120       C  
ATOM    790  OG  SER A 501      22.766  18.965  16.350  1.00 14.75           O  
ANISOU  790  OG  SER A 501     1729   2021   1854   -117    547   -140       O  
ATOM    791  N   GLN A 502      23.182  17.197  19.138  1.00 15.03           N  
ANISOU  791  N   GLN A 502     1752   1874   2082    270    125   -103       N  
ATOM    792  CA  GLN A 502      24.174  17.411  20.167  1.00 15.32           C  
ANISOU  792  CA  GLN A 502     1828   1888   2104    232    107    -67       C  
ATOM    793  C   GLN A 502      24.983  18.666  19.915  1.00 14.98           C  
ANISOU  793  C   GLN A 502     1746   1906   2038    258    159    -56       C  
ATOM    794  O   GLN A 502      25.515  19.250  20.838  1.00 14.78           O  
ANISOU  794  O   GLN A 502     1474   2155   1987    384    328    -23       O  
ATOM    795  CB  GLN A 502      25.096  16.167  20.282  1.00 16.11           C  
ANISOU  795  CB  GLN A 502     1973   1885   2264    292     49   -135       C  
ATOM    796  CG  GLN A 502      26.035  16.248  21.432  1.00 18.34           C  
ANISOU  796  CG  GLN A 502     2116   2282   2567    144    -49    -44       C  
ATOM    797  CD  GLN A 502      26.517  14.899  21.915  1.00 22.56           C  
ANISOU  797  CD  GLN A 502     2620   2571   3377    138     19    247       C  
ATOM    798  OE1 GLN A 502      25.734  13.947  22.093  1.00 22.54           O  
ANISOU  798  OE1 GLN A 502     2140   2774   3650    204   -291   -127       O  
ATOM    799  NE2 GLN A 502      27.814  14.804  22.150  1.00 27.02           N  
ANISOU  799  NE2 GLN A 502     2905   3676   3684   -129   -314     -3       N  
ATOM    800  N   GLU A 503      25.062  19.095  18.655  1.00 15.23           N  
ANISOU  800  N   GLU A 503     1801   1935   2049    277     73    -65       N  
ATOM    801  CA  GLU A 503      25.803  20.277  18.289  1.00 14.79           C  
ANISOU  801  CA  GLU A 503     1709   1965   1944    141     70    -47       C  
ATOM    802  C   GLU A 503      25.031  21.614  18.486  1.00 14.77           C  
ANISOU  802  C   GLU A 503     1617   1977   2015     82    180    -13       C  
ATOM    803  O   GLU A 503      25.612  22.691  18.344  1.00 14.65           O  
ANISOU  803  O   GLU A 503     1314   2029   2224    215    331   -138       O  
ATOM    804  CB  GLU A 503      26.252  20.123  16.824  1.00 15.85           C  
ANISOU  804  CB  GLU A 503     1774   2182   2064    -66     92     11       C  
ATOM    805  CG  GLU A 503      27.286  19.003  16.568  1.00 20.44           C  
ANISOU  805  CG  GLU A 503     2350   2758   2656    212    178   -226       C  
ATOM    806  CD  GLU A 503      26.876  17.548  16.892  1.00 27.11           C  
ANISOU  806  CD  GLU A 503     3220   3431   3648     26    120     22       C  
ATOM    807  OE1 GLU A 503      25.792  17.086  16.443  1.00 28.03           O  
ANISOU  807  OE1 GLU A 503     3555   3668   3424     73     28   -394       O  
ATOM    808  OE2 GLU A 503      27.687  16.809  17.583  1.00 32.98           O  
ANISOU  808  OE2 GLU A 503     4109   4224   4197    126     25    179       O  
ATOM    809  N   LEU A 504      23.735  21.566  18.876  1.00 14.03           N  
ANISOU  809  N   LEU A 504     1517   1860   1953     11    150    -41       N  
ATOM    810  CA  LEU A 504      22.976  22.783  19.128  1.00 13.10           C  
ANISOU  810  CA  LEU A 504     1454   1729   1793     -4    107     18       C  
ATOM    811  C   LEU A 504      23.546  23.443  20.395  1.00 13.35           C  
ANISOU  811  C   LEU A 504     1363   1779   1930    -36     44     40       C  
ATOM    812  O   LEU A 504      23.828  22.762  21.374  1.00 14.77           O  
ANISOU  812  O   LEU A 504     1471   2091   2050    -76   -118     11       O  
ATOM    813  CB  LEU A 504      21.492  22.416  19.369  1.00 13.18           C  
ANISOU  813  CB  LEU A 504     1465   1733   1809     85    214     45       C  
ATOM    814  CG  LEU A 504      20.566  23.598  19.705  1.00 10.78           C  
ANISOU  814  CG  LEU A 504     1249   1331   1512    111      3     40       C  
ATOM    815  CD1 LEU A 504      19.141  23.306  19.163  1.00 11.91           C  
ANISOU  815  CD1 LEU A 504     1143   1611   1768    241     15    -49       C  
ATOM    816  CD2 LEU A 504      20.477  23.829  21.213  1.00 11.23           C  
ANISOU  816  CD2 LEU A 504     1245   1492   1529     69     63     55       C  
ATOM    817  N   ARG A 505      23.675  24.775  20.395  1.00 14.07           N  
ANISOU  817  N   ARG A 505     1562   1772   2008    118     48     39       N  
ATOM    818  CA  ARG A 505      24.200  25.525  21.511  1.00 14.80           C  
ANISOU  818  CA  ARG A 505     1666   1896   2059     78      7      9       C  
ATOM    819  C   ARG A 505      23.495  26.892  21.619  1.00 14.27           C  
ANISOU  819  C   ARG A 505     1552   1903   1966      6     -7    -22       C  
ATOM    820  O   ARG A 505      23.508  27.624  20.641  1.00 13.32           O  
ANISOU  820  O   ARG A 505     1173   1925   1962    269      0     15       O  
ATOM    821  CB AARG A 505      25.703  25.767  21.280  0.50 15.94           C  
ANISOU  821  CB AARG A 505     1804   2040   2211     56     23    -11       C  
ATOM    822  CG AARG A 505      26.438  26.262  22.459  0.50 17.01           C  
ANISOU  822  CG AARG A 505     2047   2085   2328     64    -46     17       C  
ATOM    823  CD AARG A 505      27.944  26.490  22.159  0.50 19.74           C  
ANISOU  823  CD AARG A 505     2258   2531   2709     71    115      0       C  
ATOM    824  NE AARG A 505      28.195  27.692  21.344  0.50 20.10           N  
ANISOU  824  NE AARG A 505     2307   2587   2742    -18     55     16       N  
ATOM    825  CZ AARG A 505      28.099  28.947  21.804  0.50 20.74           C  
ANISOU  825  CZ AARG A 505     2449   2622   2808     42     20     -3       C  
ATOM    826  NH1AARG A 505      27.788  29.202  23.084  0.50 22.20           N  
ANISOU  826  NH1AARG A 505     2879   2665   2888     20   -129      8       N  
ATOM    827  NH2AARG A 505      28.352  29.952  20.997  0.50 20.97           N  
ANISOU  827  NH2AARG A 505     2439   2636   2893    155    -91     15       N  
ATOM    828  CB BARG A 505      25.742  25.665  21.344  0.50 16.40           C  
ANISOU  828  CB BARG A 505     1826   2162   2240     68     19     -1       C  
ATOM    829  CG BARG A 505      26.393  26.819  22.038  0.50 18.93           C  
ANISOU  829  CG BARG A 505     2276   2368   2546     23     19    -15       C  
ATOM    830  CD BARG A 505      27.832  26.549  22.576  0.50 21.88           C  
ANISOU  830  CD BARG A 505     2550   2896   2864     41     25     64       C  
ATOM    831  NE BARG A 505      28.162  27.497  23.638  0.50 24.67           N  
ANISOU  831  NE BARG A 505     2963   3219   3189     35    -82    -49       N  
ATOM    832  CZ BARG A 505      28.255  27.209  24.937  0.50 24.74           C  
ANISOU  832  CZ BARG A 505     2946   3272   3179      6     38     20       C  
ATOM    833  NH1BARG A 505      28.080  25.973  25.374  0.50 26.10           N  
ANISOU  833  NH1BARG A 505     3141   3345   3430     26    -58     30       N  
ATOM    834  NH2BARG A 505      28.549  28.178  25.803  0.50 25.49           N  
ANISOU  834  NH2BARG A 505     2983   3446   3255    -20     20    -21       N  
ATOM    835  N   PRO A 506      22.879  27.216  22.779  1.00 12.74           N  
ANISOU  835  N   PRO A 506     1274   1688   1879    -24    -16     28       N  
ATOM    836  CA  PRO A 506      22.351  28.557  22.977  1.00 13.03           C  
ANISOU  836  CA  PRO A 506     1506   1670   1775    -41     -6    -35       C  
ATOM    837  C   PRO A 506      23.442  29.512  23.494  1.00 12.80           C  
ANISOU  837  C   PRO A 506     1309   1650   1904     -7     23    -16       C  
ATOM    838  O   PRO A 506      24.431  29.099  24.173  1.00 14.57           O  
ANISOU  838  O   PRO A 506     1372   1758   2405     -6   -100     74       O  
ATOM    839  CB  PRO A 506      21.281  28.337  24.065  1.00 12.00           C  
ANISOU  839  CB  PRO A 506     1440   1510   1607    -46      0     20       C  
ATOM    840  CG  PRO A 506      21.913  27.272  24.928  1.00 11.91           C  
ANISOU  840  CG  PRO A 506     1187   1668   1670    -76     13     66       C  
ATOM    841  CD  PRO A 506      22.618  26.356  23.957  1.00 13.24           C  
ANISOU  841  CD  PRO A 506     1475   1725   1828    -42    -19     -7       C  
ATOM    842  N   GLU A 507      23.216  30.795  23.248  1.00 14.52           N  
ANISOU  842  N   GLU A 507     1608   1783   2124     23    -47     39       N  
ATOM    843  CA  GLU A 507      24.113  31.860  23.697  1.00 15.92           C  
ANISOU  843  CA  GLU A 507     1899   1943   2206     20   -106      0       C  
ATOM    844  C   GLU A 507      23.306  33.132  23.923  1.00 16.39           C  
ANISOU  844  C   GLU A 507     2036   1990   2199     44    -85    -15       C  
ATOM    845  O   GLU A 507      22.610  33.531  23.011  1.00 18.19           O  
ANISOU  845  O   GLU A 507     2127   2173   2612    130   -365   -117       O  
ATOM    846  CB  GLU A 507      25.157  32.124  22.602  1.00 16.22           C  
ANISOU  846  CB  GLU A 507     1871   2068   2220     69    -91   -105       C  
ATOM    847  CG  GLU A 507      26.112  33.268  22.917  1.00 20.73           C  
ANISOU  847  CG  GLU A 507     2508   2437   2929   -103   -117   -112       C  
ATOM    848  CD  GLU A 507      27.028  33.689  21.758  1.00 25.92           C  
ANISOU  848  CD  GLU A 507     3153   3312   3380   -121     75     14       C  
ATOM    849  OE1 GLU A 507      26.865  33.251  20.602  1.00 30.45           O  
ANISOU  849  OE1 GLU A 507     3980   3753   3833    -85      1    -14       O  
ATOM    850  OE2 GLU A 507      27.934  34.526  22.002  1.00 30.43           O  
ANISOU  850  OE2 GLU A 507     3530   3780   4250   -362   -116    -72       O  
ATOM    851  N   ALA A 508      23.428  33.790  25.081  1.00 17.12           N  
ANISOU  851  N   ALA A 508     2015   2192   2298     39   -215     13       N  
ATOM    852  CA  ALA A 508      22.771  35.091  25.264  1.00 18.14           C  
ANISOU  852  CA  ALA A 508     2278   2285   2328    -66   -106    -51       C  
ATOM    853  C   ALA A 508      23.792  36.157  25.093  1.00 18.11           C  
ANISOU  853  C   ALA A 508     2156   2379   2344    -70    -87    -29       C  
ATOM    854  O   ALA A 508      24.884  36.111  25.710  1.00 20.65           O  
ANISOU  854  O   ALA A 508     2425   2700   2720    -34   -439    111       O  
ATOM    855  CB  ALA A 508      22.108  35.215  26.556  1.00 18.65           C  
ANISOU  855  CB  ALA A 508     2245   2371   2469   -133    -47   -198       C  
ATOM    856  N   LYS A 509      23.477  37.084  24.210  1.00 17.75           N  
ANISOU  856  N   LYS A 509     2118   2272   2351     -9    -59    -67       N  
ATOM    857  CA  LYS A 509      24.327  38.230  23.949  1.00 18.93           C  
ANISOU  857  CA  LYS A 509     2294   2419   2480    -71    -23     -5       C  
ATOM    858  C   LYS A 509      24.111  39.303  25.077  1.00 18.97           C  
ANISOU  858  C   LYS A 509     2229   2383   2596    -98    -25   -103       C  
ATOM    859  O   LYS A 509      25.041  39.923  25.628  1.00 21.01           O  
ANISOU  859  O   LYS A 509     2530   2663   2786   -210   -237    -86       O  
ATOM    860  CB  LYS A 509      24.015  38.775  22.548  1.00 19.56           C  
ANISOU  860  CB  LYS A 509     2445   2440   2544    145     11    -39       C  
ATOM    861  N   ASN A 510      22.871  39.483  25.450  1.00 16.94           N  
ANISOU  861  N   ASN A 510     2035   2117   2283   -169     56    -81       N  
ATOM    862  CA  ASN A 510      22.486  40.407  26.527  1.00 15.67           C  
ANISOU  862  CA  ASN A 510     1980   1976   1995    -21    -93    -63       C  
ATOM    863  C   ASN A 510      21.098  40.004  27.019  1.00 15.50           C  
ANISOU  863  C   ASN A 510     2005   1852   2029   -122   -152    -81       C  
ATOM    864  O   ASN A 510      20.663  38.894  26.756  1.00 16.57           O  
ANISOU  864  O   ASN A 510     2363   1558   2375   -227   -168   -111       O  
ATOM    865  CB  ASN A 510      22.531  41.889  26.067  1.00 16.08           C  
ANISOU  865  CB  ASN A 510     2059   2021   2030   -239     43   -140       C  
ATOM    866  CG  ASN A 510      21.736  42.165  24.801  1.00 17.59           C  
ANISOU  866  CG  ASN A 510     1953   2251   2476    -80    -43     55       C  
ATOM    867  OD1 ASN A 510      20.611  41.675  24.631  1.00 16.11           O  
ANISOU  867  OD1 ASN A 510     1876   1884   2358   -141     58   -252       O  
ATOM    868  ND2 ASN A 510      22.325  42.935  23.877  1.00 21.91           N  
ANISOU  868  ND2 ASN A 510     2822   2847   2654   -195     16     74       N  
ATOM    869  N   PHE A 511      20.360  40.879  27.702  1.00 14.50           N  
ANISOU  869  N   PHE A 511     1881   1705   1922   -144   -225   -207       N  
ATOM    870  CA  PHE A 511      19.113  40.485  28.341  1.00 14.82           C  
ANISOU  870  CA  PHE A 511     1933   1843   1854     21   -125   -105       C  
ATOM    871  C   PHE A 511      17.987  40.343  27.309  1.00 13.88           C  
ANISOU  871  C   PHE A 511     1773   1597   1901     -3   -105   -117       C  
ATOM    872  O   PHE A 511      16.960  39.770  27.612  1.00 12.24           O  
ANISOU  872  O   PHE A 511     1687   1295   1665    121   -214   -172       O  
ATOM    873  CB  PHE A 511      18.667  41.448  29.454  1.00 14.68           C  
ANISOU  873  CB  PHE A 511     1810   1857   1909   -143    -73   -144       C  
ATOM    874  CG  PHE A 511      19.693  41.639  30.552  1.00 16.63           C  
ANISOU  874  CG  PHE A 511     1947   2257   2116    -98    -77    -55       C  
ATOM    875  CD1 PHE A 511      20.115  40.599  31.295  1.00 18.62           C  
ANISOU  875  CD1 PHE A 511     2307   2588   2180   -307   -180     83       C  
ATOM    876  CD2 PHE A 511      20.252  42.903  30.763  1.00 18.03           C  
ANISOU  876  CD2 PHE A 511     2325   2263   2261    -53   -155   -170       C  
ATOM    877  CE1 PHE A 511      21.121  40.785  32.284  1.00 18.71           C  
ANISOU  877  CE1 PHE A 511     2536   2382   2190    -73   -254    194       C  
ATOM    878  CE2 PHE A 511      21.211  43.080  31.700  1.00 18.12           C  
ANISOU  878  CE2 PHE A 511     2392   2385   2105    -24   -169   -156       C  
ATOM    879  CZ  PHE A 511      21.614  42.016  32.492  1.00 17.16           C  
ANISOU  879  CZ  PHE A 511     2140   2384   1996   -132   -234    -94       C  
ATOM    880  N   LYS A 512      18.200  40.896  26.124  1.00 13.61           N  
ANISOU  880  N   LYS A 512     1835   1636   1700    -31   -208   -289       N  
ATOM    881  CA  LYS A 512      17.138  40.939  25.115  1.00 14.50           C  
ANISOU  881  CA  LYS A 512     1841   1841   1827    -17   -135    -31       C  
ATOM    882  C   LYS A 512      17.510  40.257  23.807  1.00 13.39           C  
ANISOU  882  C   LYS A 512     1593   1669   1824    -73    -49    -50       C  
ATOM    883  O   LYS A 512      16.797  40.393  22.818  1.00 14.55           O  
ANISOU  883  O   LYS A 512     1642   1988   1897     -9    -65    -14       O  
ATOM    884  CB  LYS A 512      16.712  42.407  24.872  1.00 15.66           C  
ANISOU  884  CB  LYS A 512     1991   1927   2031     13   -167    -74       C  
ATOM    885  CG  LYS A 512      16.075  43.055  26.077  1.00 15.65           C  
ANISOU  885  CG  LYS A 512     2031   1961   1954    -32    -92    -71       C  
ATOM    886  CD  LYS A 512      15.607  44.456  25.850  1.00 16.65           C  
ANISOU  886  CD  LYS A 512     2165   2259   1902    124    -20    -25       C  
ATOM    887  CE  LYS A 512      15.183  45.085  27.165  1.00 16.65           C  
ANISOU  887  CE  LYS A 512     2432   2106   1786    116   -100   -132       C  
ATOM    888  NZ  LYS A 512      14.892  46.526  26.983  1.00 18.29           N  
ANISOU  888  NZ  LYS A 512     2647   2266   2032    397    122    -27       N  
ATOM    889  N   THR A 513      18.637  39.592  23.749  1.00 13.68           N  
ANISOU  889  N   THR A 513     1562   1753   1883   -114   -191   -123       N  
ATOM    890  CA  THR A 513      19.080  38.926  22.540  1.00 14.04           C  
ANISOU  890  CA  THR A 513     1611   1789   1933    -48   -119    -51       C  
ATOM    891  C   THR A 513      19.704  37.595  22.887  1.00 13.56           C  
ANISOU  891  C   THR A 513     1598   1681   1873    -58   -169    -82       C  
ATOM    892  O   THR A 513      20.532  37.530  23.758  1.00 13.03           O  
ANISOU  892  O   THR A 513     1497   1606   1847    -76   -269   -143       O  
ATOM    893  CB  THR A 513      20.106  39.801  21.873  1.00 16.31           C  
ANISOU  893  CB  THR A 513     2111   2031   2052    -29    -27    138       C  
ATOM    894  OG1 THR A 513      19.472  41.020  21.474  1.00 19.23           O  
ANISOU  894  OG1 THR A 513     2167   2176   2961    332    264    132       O  
ATOM    895  CG2 THR A 513      20.559  39.223  20.599  1.00 18.03           C  
ANISOU  895  CG2 THR A 513     2263   2377   2210     37      1   -113       C  
ATOM    896  N   PHE A 514      19.214  36.524  22.276  1.00 12.47           N  
ANISOU  896  N   PHE A 514     1473   1473   1792     36   -243   -234       N  
ATOM    897  CA  PHE A 514      19.887  35.232  22.338  1.00 11.31           C  
ANISOU  897  CA  PHE A 514     1223   1438   1633     41   -153   -179       C  
ATOM    898  C   PHE A 514      19.943  34.582  20.979  1.00 10.70           C  
ANISOU  898  C   PHE A 514     1143   1461   1462     52    -75    -51       C  
ATOM    899  O   PHE A 514      19.124  34.798  20.132  1.00 12.01           O  
ANISOU  899  O   PHE A 514     1230   1583   1748    176   -174   -341       O  
ATOM    900  CB  PHE A 514      19.321  34.301  23.403  1.00 12.58           C  
ANISOU  900  CB  PHE A 514     1467   1533   1780     56    -59   -243       C  
ATOM    901  CG  PHE A 514      17.929  33.805  23.113  1.00 10.51           C  
ANISOU  901  CG  PHE A 514     1248   1205   1541     79   -101    -47       C  
ATOM    902  CD1 PHE A 514      17.705  32.459  22.683  1.00 13.71           C  
ANISOU  902  CD1 PHE A 514     1526   1496   2187     58   -148   -128       C  
ATOM    903  CD2 PHE A 514      16.841  34.598  23.303  1.00 11.66           C  
ANISOU  903  CD2 PHE A 514     1296   1700   1434    130   -193   -148       C  
ATOM    904  CE1 PHE A 514      16.458  31.977  22.404  1.00 13.56           C  
ANISOU  904  CE1 PHE A 514     1751   1698   1701    -38    -67     33       C  
ATOM    905  CE2 PHE A 514      15.526  34.093  23.001  1.00 13.08           C  
ANISOU  905  CE2 PHE A 514     1525   1937   1507   -181    122     -2       C  
ATOM    906  CZ  PHE A 514      15.349  32.806  22.582  1.00 12.85           C  
ANISOU  906  CZ  PHE A 514     1640   1823   1416     55     -4     13       C  
ATOM    907  N   PHE A 515      20.939  33.735  20.809  1.00 11.43           N  
ANISOU  907  N   PHE A 515     1054   1616   1670     60     26   -174       N  
ATOM    908  CA  PHE A 515      21.146  32.967  19.586  1.00 11.48           C  
ANISOU  908  CA  PHE A 515     1204   1577   1579    100     26    -68       C  
ATOM    909  C   PHE A 515      20.990  31.481  19.895  1.00 12.08           C  
ANISOU  909  C   PHE A 515     1367   1621   1600    141     51    -97       C  
ATOM    910  O   PHE A 515      21.250  31.048  21.013  1.00 12.43           O  
ANISOU  910  O   PHE A 515     1325   1645   1749    168    148    -90       O  
ATOM    911  CB  PHE A 515      22.583  33.175  19.096  1.00 14.53           C  
ANISOU  911  CB  PHE A 515     1515   1918   2087      9     47    -54       C  
ATOM    912  CG  PHE A 515      22.983  34.611  18.909  1.00 17.87           C  
ANISOU  912  CG  PHE A 515     2144   2164   2479   -129    129     46       C  
ATOM    913  CD1 PHE A 515      22.319  35.425  18.036  1.00 22.94           C  
ANISOU  913  CD1 PHE A 515     2808   2840   3066      7    -50    151       C  
ATOM    914  CD2 PHE A 515      24.029  35.144  19.648  1.00 24.94           C  
ANISOU  914  CD2 PHE A 515     2962   3154   3360   -139   -217     28       C  
ATOM    915  CE1 PHE A 515      22.686  36.797  17.868  1.00 24.62           C  
ANISOU  915  CE1 PHE A 515     3062   2913   3377     21     15     47       C  
ATOM    916  CE2 PHE A 515      24.416  36.511  19.479  1.00 26.73           C  
ANISOU  916  CE2 PHE A 515     3376   3189   3592    -94   -138     81       C  
ATOM    917  CZ  PHE A 515      23.723  37.315  18.576  1.00 26.86           C  
ANISOU  917  CZ  PHE A 515     3488   3195   3521    -19   -102     25       C  
ATOM    918  N   VAL A 516      20.563  30.720  18.893  1.00 12.21           N  
ANISOU  918  N   VAL A 516     1392   1538   1709    178     37    -81       N  
ATOM    919  CA  VAL A 516      20.642  29.265  18.957  1.00 11.68           C  
ANISOU  919  CA  VAL A 516     1376   1514   1545     90    129    -19       C  
ATOM    920  C   VAL A 516      21.467  28.828  17.762  1.00 12.63           C  
ANISOU  920  C   VAL A 516     1520   1582   1697    177     48    -13       C  
ATOM    921  O   VAL A 516      21.050  28.892  16.634  1.00 12.51           O  
ANISOU  921  O   VAL A 516     1397   1563   1791    195    -24   -209       O  
ATOM    922  CB  VAL A 516      19.261  28.574  19.016  1.00 11.47           C  
ANISOU  922  CB  VAL A 516     1322   1511   1523     70    -42   -138       C  
ATOM    923  CG1 VAL A 516      19.432  27.087  19.212  1.00 12.23           C  
ANISOU  923  CG1 VAL A 516     1491   1576   1577     42    115   -169       C  
ATOM    924  CG2 VAL A 516      18.443  29.153  20.153  1.00 12.87           C  
ANISOU  924  CG2 VAL A 516     1492   1710   1686     79    149    -97       C  
ATOM    925  N   HIS A 517      22.662  28.331  18.074  1.00 13.76           N  
ANISOU  925  N   HIS A 517     1594   1697   1937    233    -20     23       N  
ATOM    926  CA  HIS A 517      23.567  27.826  17.059  1.00 13.14           C  
ANISOU  926  CA  HIS A 517     1582   1770   1638      1    116     80       C  
ATOM    927  C   HIS A 517      23.268  26.389  16.664  1.00 13.26           C  
ANISOU  927  C   HIS A 517     1482   1814   1739    211     66     39       C  
ATOM    928  O   HIS A 517      23.160  25.518  17.522  1.00 12.97           O  
ANISOU  928  O   HIS A 517     1430   1753   1746    293    169    -30       O  
ATOM    929  CB  HIS A 517      24.972  27.939  17.580  1.00 13.65           C  
ANISOU  929  CB  HIS A 517     1662   1791   1730    154     51     61       C  
ATOM    930  CG  HIS A 517      25.365  29.335  17.993  1.00 16.76           C  
ANISOU  930  CG  HIS A 517     1932   2156   2276   -118     92     70       C  
ATOM    931  ND1 HIS A 517      25.623  30.338  17.076  1.00 21.71           N  
ANISOU  931  ND1 HIS A 517     2907   2532   2809   -156    207    267       N  
ATOM    932  CD2 HIS A 517      25.470  29.917  19.213  1.00 17.83           C  
ANISOU  932  CD2 HIS A 517     2295   2153   2323    127     10     59       C  
ATOM    933  CE1 HIS A 517      25.932  31.450  17.717  1.00 22.62           C  
ANISOU  933  CE1 HIS A 517     2946   2785   2862    -82    114     21       C  
ATOM    934  NE2 HIS A 517      25.861  31.227  19.015  1.00 18.31           N  
ANISOU  934  NE2 HIS A 517     1964   2343   2647    -29     86    280       N  
ATOM    935  N   THR A 518      23.132  26.111  15.363  1.00 13.33           N  
ANISOU  935  N   THR A 518     1460   1845   1758    144    115     -6       N  
ATOM    936  CA  THR A 518      23.012  24.740  14.855  1.00 14.92           C  
ANISOU  936  CA  THR A 518     1639   2056   1973     29     93    -40       C  
ATOM    937  C   THR A 518      24.032  24.647  13.713  1.00 16.96           C  
ANISOU  937  C   THR A 518     2046   2185   2213     84    224    -38       C  
ATOM    938  O   THR A 518      24.519  25.691  13.270  1.00 16.67           O  
ANISOU  938  O   THR A 518     1760   2339   2233    185    566    -27       O  
ATOM    939  CB  THR A 518      21.546  24.430  14.425  1.00 15.26           C  
ANISOU  939  CB  THR A 518     1778   2009   2008    111     25    -60       C  
ATOM    940  OG1 THR A 518      21.241  25.138  13.234  1.00 17.05           O  
ANISOU  940  OG1 THR A 518     1851   2520   2104    168    -83     64       O  
ATOM    941  CG2 THR A 518      20.577  24.932  15.475  1.00 15.08           C  
ANISOU  941  CG2 THR A 518     1817   2129   1784    105    -21     58       C  
ATOM    942  N   PRO A 519      24.393  23.429  13.283  1.00 18.08           N  
ANISOU  942  N   PRO A 519     2129   2376   2361     88    262    -55       N  
ATOM    943  CA  PRO A 519      25.548  23.288  12.356  1.00 19.84           C  
ANISOU  943  CA  PRO A 519     2394   2636   2508    118    188    -39       C  
ATOM    944  C   PRO A 519      25.520  24.142  11.103  1.00 20.89           C  
ANISOU  944  C   PRO A 519     2577   2695   2663     90    100    -21       C  
ATOM    945  O   PRO A 519      26.559  24.668  10.702  1.00 22.12           O  
ANISOU  945  O   PRO A 519     2664   3002   2739    197    195     15       O  
ATOM    946  CB  PRO A 519      25.550  21.790  12.032  1.00 20.42           C  
ANISOU  946  CB  PRO A 519     2480   2620   2658    106    178      4       C  
ATOM    947  CG  PRO A 519      24.895  21.164  13.285  1.00 20.11           C  
ANISOU  947  CG  PRO A 519     2637   2495   2510    190    213    -45       C  
ATOM    948  CD  PRO A 519      23.806  22.133  13.652  1.00 18.68           C  
ANISOU  948  CD  PRO A 519     2235   2361   2501    123     87    -35       C  
ATOM    949  N   ASN A 520      24.360  24.273  10.479  1.00 22.08           N  
ANISOU  949  N   ASN A 520     2733   2856   2797    186    138    -62       N  
ATOM    950  CA  ASN A 520      24.260  25.031   9.248  1.00 23.37           C  
ANISOU  950  CA  ASN A 520     2958   3011   2911     87    101    -12       C  
ATOM    951  C   ASN A 520      23.493  26.323   9.381  1.00 22.94           C  
ANISOU  951  C   ASN A 520     2878   3076   2762    132    106     21       C  
ATOM    952  O   ASN A 520      23.159  26.943   8.372  1.00 23.97           O  
ANISOU  952  O   ASN A 520     3043   3222   2842    308    213    196       O  
ATOM    953  CB  ASN A 520      23.670  24.144   8.164  1.00 25.02           C  
ANISOU  953  CB  ASN A 520     3166   3290   3049     49      5    -47       C  
ATOM    954  CG  ASN A 520      24.584  22.952   7.858  1.00 27.57           C  
ANISOU  954  CG  ASN A 520     3509   3496   3468     73    116   -138       C  
ATOM    955  OD1 ASN A 520      25.827  23.100   7.794  1.00 32.19           O  
ANISOU  955  OD1 ASN A 520     3783   4518   3930     86    101   -101       O  
ATOM    956  ND2 ASN A 520      24.008  21.772   7.767  1.00 31.09           N  
ANISOU  956  ND2 ASN A 520     3968   3837   4005   -110    -40   -195       N  
ATOM    957  N   ARG A 521      23.173  26.737  10.618  1.00 21.29           N  
ANISOU  957  N   ARG A 521     2677   2860   2551    115     67    -14       N  
ATOM    958  CA  ARG A 521      22.428  27.987  10.792  1.00 19.94           C  
ANISOU  958  CA  ARG A 521     2429   2656   2490     29     36      6       C  
ATOM    959  C   ARG A 521      22.421  28.432  12.238  1.00 18.51           C  
ANISOU  959  C   ARG A 521     2122   2517   2391    168    104     15       C  
ATOM    960  O   ARG A 521      22.158  27.630  13.151  1.00 17.51           O  
ANISOU  960  O   ARG A 521     1767   2410   2473    329     84     87       O  
ATOM    961  CB  ARG A 521      20.966  27.843  10.350  1.00 19.27           C  
ANISOU  961  CB  ARG A 521     2458   2638   2224     98     28     98       C  
ATOM    962  CG  ARG A 521      20.184  29.076  10.585  1.00 21.07           C  
ANISOU  962  CG  ARG A 521     2581   2837   2586      4     57     64       C  
ATOM    963  CD  ARG A 521      18.893  29.029   9.899  1.00 21.47           C  
ANISOU  963  CD  ARG A 521     2730   2804   2623     62     18     22       C  
ATOM    964  NE  ARG A 521      18.093  30.208  10.209  1.00 19.89           N  
ANISOU  964  NE  ARG A 521     2432   2847   2277    133    227    356       N  
ATOM    965  CZ  ARG A 521      16.808  30.276   9.916  1.00 16.18           C  
ANISOU  965  CZ  ARG A 521     2313   2161   1672     96    -32    368       C  
ATOM    966  NH1 ARG A 521      16.200  29.262   9.306  1.00 17.63           N  
ANISOU  966  NH1 ARG A 521     2256   2459   1982    201    212    259       N  
ATOM    967  NH2 ARG A 521      16.138  31.357  10.276  1.00 18.12           N  
ANISOU  967  NH2 ARG A 521     2429   2218   2238    145     63    313       N  
ATOM    968  N   THR A 522      22.659  29.727  12.442  1.00 17.69           N  
ANISOU  968  N   THR A 522     1964   2448   2307    131    189     56       N  
ATOM    969  CA  THR A 522      22.457  30.327  13.761  1.00 17.74           C  
ANISOU  969  CA  THR A 522     2124   2304   2310    195     66     60       C  
ATOM    970  C   THR A 522      21.150  31.124  13.729  1.00 15.41           C  
ANISOU  970  C   THR A 522     1883   1980   1993    208    229    154       C  
ATOM    971  O   THR A 522      20.970  32.007  12.895  1.00 19.09           O  
ANISOU  971  O   THR A 522     2208   2658   2388    356    434    368       O  
ATOM    972  CB  THR A 522      23.623  31.217  14.102  1.00 18.24           C  
ANISOU  972  CB  THR A 522     2099   2407   2424    167     56    113       C  
ATOM    973  OG1 THR A 522      24.795  30.400  14.327  1.00 20.81           O  
ANISOU  973  OG1 THR A 522     2170   2826   2910    393    130     92       O  
ATOM    974  CG2 THR A 522      23.407  32.010  15.396  1.00 21.01           C  
ANISOU  974  CG2 THR A 522     2625   2727   2628     97    119     38       C  
ATOM    975  N   TYR A 523      20.255  30.818  14.645  1.00 12.56           N  
ANISOU  975  N   TYR A 523     1553   1548   1668    143    202    109       N  
ATOM    976  CA  TYR A 523      18.965  31.501  14.788  1.00 12.15           C  
ANISOU  976  CA  TYR A 523     1524   1500   1590     70     62     27       C  
ATOM    977  C   TYR A 523      19.152  32.696  15.743  1.00 12.41           C  
ANISOU  977  C   TYR A 523     1555   1634   1522     43     67     10       C  
ATOM    978  O   TYR A 523      19.802  32.581  16.771  1.00 12.81           O  
ANISOU  978  O   TYR A 523     1553   1748   1567    216     41     60       O  
ATOM    979  CB  TYR A 523      17.902  30.538  15.327  1.00 12.60           C  
ANISOU  979  CB  TYR A 523     1717   1465   1605     38     83    -47       C  
ATOM    980  CG  TYR A 523      17.525  29.454  14.342  1.00  9.84           C  
ANISOU  980  CG  TYR A 523     1280   1229   1227      4     41     71       C  
ATOM    981  CD1 TYR A 523      18.337  28.343  14.131  1.00 10.75           C  
ANISOU  981  CD1 TYR A 523     1145   1403   1535     43     93     71       C  
ATOM    982  CD2 TYR A 523      16.354  29.525  13.655  1.00 11.15           C  
ANISOU  982  CD2 TYR A 523     1392   1460   1381    -54   -124    208       C  
ATOM    983  CE1 TYR A 523      17.979  27.391  13.183  1.00 11.82           C  
ANISOU  983  CE1 TYR A 523     1133   1532   1825    244    175    -16       C  
ATOM    984  CE2 TYR A 523      15.996  28.559  12.746  1.00 12.36           C  
ANISOU  984  CE2 TYR A 523     1629   1599   1465    220    -74    -14       C  
ATOM    985  CZ  TYR A 523      16.818  27.496  12.498  1.00 12.44           C  
ANISOU  985  CZ  TYR A 523     1561   1672   1491     15    122     14       C  
ATOM    986  OH  TYR A 523      16.446  26.538  11.608  1.00 14.56           O  
ANISOU  986  OH  TYR A 523     2170   1908   1452     95    303   -163       O  
ATOM    987  N   TYR A 524      18.588  33.835  15.388  1.00 11.92           N  
ANISOU  987  N   TYR A 524     1460   1522   1544     74     16    -80       N  
ATOM    988  CA  TYR A 524      18.826  35.095  16.096  1.00 12.12           C  
ANISOU  988  CA  TYR A 524     1480   1548   1576     41     49    -32       C  
ATOM    989  C   TYR A 524      17.468  35.518  16.648  1.00 11.35           C  
ANISOU  989  C   TYR A 524     1369   1416   1528     70     14    -48       C  
ATOM    990  O   TYR A 524      16.591  35.870  15.887  1.00 11.10           O  
ANISOU  990  O   TYR A 524     1227   1355   1633    -15    -55    -51       O  
ATOM    991  CB  TYR A 524      19.388  36.121  15.091  1.00 12.65           C  
ANISOU  991  CB  TYR A 524     1538   1543   1723    -17      8     66       C  
ATOM    992  CG  TYR A 524      19.737  37.515  15.597  1.00 17.86           C  
ANISOU  992  CG  TYR A 524     2422   2083   2278   -151    -60    -21       C  
ATOM    993  CD1 TYR A 524      19.242  38.061  16.800  1.00 18.81           C  
ANISOU  993  CD1 TYR A 524     2560   2155   2428    -91    106    -20       C  
ATOM    994  CD2 TYR A 524      20.515  38.350  14.802  1.00 21.87           C  
ANISOU  994  CD2 TYR A 524     2762   2815   2730   -228    202     92       C  
ATOM    995  CE1 TYR A 524      19.575  39.376  17.188  1.00 21.12           C  
ANISOU  995  CE1 TYR A 524     2677   2496   2850    -26     27    -74       C  
ATOM    996  CE2 TYR A 524      20.840  39.658  15.209  1.00 22.58           C  
ANISOU  996  CE2 TYR A 524     2947   2729   2900    -13    108    -64       C  
ATOM    997  CZ  TYR A 524      20.395  40.138  16.388  1.00 22.99           C  
ANISOU  997  CZ  TYR A 524     3130   2711   2890    -14     93     40       C  
ATOM    998  OH  TYR A 524      20.737  41.421  16.763  1.00 25.90           O  
ANISOU  998  OH  TYR A 524     3505   2830   3505   -248    -43     -2       O  
ATOM    999  N   LEU A 525      17.336  35.481  17.954  1.00 10.83           N  
ANISOU  999  N   LEU A 525     1258   1333   1522      4     71    -98       N  
ATOM   1000  CA  LEU A 525      16.060  35.772  18.625  1.00 10.22           C  
ANISOU 1000  CA  LEU A 525     1173   1317   1391     57      6   -111       C  
ATOM   1001  C   LEU A 525      16.161  36.992  19.563  1.00 10.19           C  
ANISOU 1001  C   LEU A 525     1195   1271   1404    -84      3   -117       C  
ATOM   1002  O   LEU A 525      17.134  37.168  20.315  1.00 12.87           O  
ANISOU 1002  O   LEU A 525     1426   1547   1915    124   -241   -439       O  
ATOM   1003  CB  LEU A 525      15.633  34.607  19.484  1.00 10.63           C  
ANISOU 1003  CB  LEU A 525     1271   1360   1407     15    -43    -10       C  
ATOM   1004  CG  LEU A 525      15.268  33.294  18.816  1.00 13.90           C  
ANISOU 1004  CG  LEU A 525     1759   1669   1853    -99   -129    -25       C  
ATOM   1005  CD1 LEU A 525      14.460  33.389  17.477  1.00 13.23           C  
ANISOU 1005  CD1 LEU A 525     1551   1479   1997      8   -285    111       C  
ATOM   1006  CD2 LEU A 525      16.399  32.397  18.674  1.00 12.78           C  
ANISOU 1006  CD2 LEU A 525     1495   1584   1775   -171    -63   -361       C  
ATOM   1007  N   MET A 526      15.191  37.865  19.460  1.00 10.93           N  
ANISOU 1007  N   MET A 526     1190   1488   1471    -40    -75   -216       N  
ATOM   1008  CA  MET A 526      15.089  39.043  20.366  1.00 11.86           C  
ANISOU 1008  CA  MET A 526     1439   1507   1557    -12   -122   -128       C  
ATOM   1009  C   MET A 526      13.931  38.816  21.320  1.00 12.73           C  
ANISOU 1009  C   MET A 526     1529   1695   1612     26   -114   -120       C  
ATOM   1010  O   MET A 526      12.860  38.376  20.927  1.00 10.84           O  
ANISOU 1010  O   MET A 526     1093   1436   1587    229    -46   -242       O  
ATOM   1011  CB  MET A 526      14.923  40.317  19.548  1.00 14.15           C  
ANISOU 1011  CB  MET A 526     1742   1635   1997    -14     23    -62       C  
ATOM   1012  CG  MET A 526      16.041  40.540  18.526  1.00 16.29           C  
ANISOU 1012  CG  MET A 526     2002   2050   2136    -15     34    -39       C  
ATOM   1013  SD  MET A 526      15.936  42.033  17.540  1.00 24.77           S  
ANISOU 1013  SD  MET A 526     3530   2712   3169    123    388     59       S  
ATOM   1014  CE  MET A 526      14.466  41.968  16.872  1.00 25.09           C  
ANISOU 1014  CE  MET A 526     3309   3005   3217   -109    161    -10       C  
ATOM   1015  N   ASP A 527      14.168  39.148  22.587  1.00 12.11           N  
ANISOU 1015  N   ASP A 527     1353   1794   1451    -47   -163   -168       N  
ATOM   1016  CA  ASP A 527      13.210  39.042  23.683  1.00 13.20           C  
ANISOU 1016  CA  ASP A 527     1651   1756   1608     54    -50   -124       C  
ATOM   1017  C   ASP A 527      13.094  40.406  24.332  1.00 13.60           C  
ANISOU 1017  C   ASP A 527     1741   1746   1679     66    -21     15       C  
ATOM   1018  O   ASP A 527      13.846  40.702  25.200  1.00 12.47           O  
ANISOU 1018  O   ASP A 527     1718   1507   1511    220    -72    -77       O  
ATOM   1019  CB  ASP A 527      13.655  37.974  24.697  1.00 13.64           C  
ANISOU 1019  CB  ASP A 527     1736   1764   1681      1     -5   -155       C  
ATOM   1020  CG  ASP A 527      12.704  37.849  25.878  1.00 15.74           C  
ANISOU 1020  CG  ASP A 527     2135   2090   1755     75     26   -101       C  
ATOM   1021  OD1 ASP A 527      11.603  38.465  25.841  1.00 14.35           O  
ANISOU 1021  OD1 ASP A 527     2165   1927   1357     70   -108   -307       O  
ATOM   1022  OD2 ASP A 527      12.958  37.137  26.850  1.00 14.34           O  
ANISOU 1022  OD2 ASP A 527     2155   1789   1502    411    -52   -295       O  
ATOM   1023  N   PRO A 528      12.160  41.252  23.881  1.00 14.24           N  
ANISOU 1023  N   PRO A 528     1914   1785   1709    179    -60      3       N  
ATOM   1024  CA  PRO A 528      12.052  42.589  24.479  1.00 14.05           C  
ANISOU 1024  CA  PRO A 528     1857   1803   1679    188    -38     13       C  
ATOM   1025  C   PRO A 528      11.610  42.589  25.943  1.00 12.93           C  
ANISOU 1025  C   PRO A 528     1916   1591   1403    101    -78    -10       C  
ATOM   1026  O   PRO A 528      11.721  43.675  26.598  1.00 14.84           O  
ANISOU 1026  O   PRO A 528     2355   1669   1612    187   -138     -7       O  
ATOM   1027  CB  PRO A 528      11.025  43.295  23.601  1.00 14.73           C  
ANISOU 1027  CB  PRO A 528     2122   1788   1686    261    -97    160       C  
ATOM   1028  CG  PRO A 528      10.284  42.206  22.878  1.00 15.57           C  
ANISOU 1028  CG  PRO A 528     1897   1975   2042    181    -79     77       C  
ATOM   1029  CD  PRO A 528      11.251  41.059  22.735  1.00 14.92           C  
ANISOU 1029  CD  PRO A 528     1970   1848   1849     66     65     21       C  
ATOM   1030  N   SER A 529      11.262  41.427  26.497  1.00 12.62           N  
ANISOU 1030  N   SER A 529     1730   1705   1359    129   -113     21       N  
ATOM   1031  CA  SER A 529      10.954  41.355  27.944  1.00 12.34           C  
ANISOU 1031  CA  SER A 529     1694   1554   1441    205     48   -115       C  
ATOM   1032  C   SER A 529      12.191  41.378  28.850  1.00 12.15           C  
ANISOU 1032  C   SER A 529     1648   1503   1462    103    -13    -34       C  
ATOM   1033  O   SER A 529      12.111  41.595  30.064  1.00 13.39           O  
ANISOU 1033  O   SER A 529     1752   1981   1352    176    -48    -33       O  
ATOM   1034  CB  SER A 529      10.123  40.135  28.299  1.00 13.66           C  
ANISOU 1034  CB  SER A 529     1680   1870   1641     51    -70    -96       C  
ATOM   1035  OG  SER A 529      10.883  38.939  28.275  1.00 13.40           O  
ANISOU 1035  OG  SER A 529     1661   1712   1717     27     35    -67       O  
ATOM   1036  N   GLY A 530      13.350  41.225  28.260  1.00 12.01           N  
ANISOU 1036  N   GLY A 530     1590   1448   1523     86    -75    -79       N  
ATOM   1037  CA  GLY A 530      14.582  41.169  29.015  1.00 11.88           C  
ANISOU 1037  CA  GLY A 530     1562   1436   1515     94   -209     -4       C  
ATOM   1038  C   GLY A 530      14.906  39.841  29.669  1.00 12.51           C  
ANISOU 1038  C   GLY A 530     1743   1470   1537    -67   -120    -18       C  
ATOM   1039  O   GLY A 530      15.706  39.815  30.596  1.00 12.44           O  
ANISOU 1039  O   GLY A 530     1705   1320   1700     83   -251   -125       O  
ATOM   1040  N   ASN A 531      14.327  38.761  29.161  1.00 12.60           N  
ANISOU 1040  N   ASN A 531     1736   1432   1620    -15    -39    -60       N  
ATOM   1041  CA  ASN A 531      14.503  37.429  29.744  1.00 11.84           C  
ANISOU 1041  CA  ASN A 531     1588   1460   1447     54    -67      9       C  
ATOM   1042  C   ASN A 531      15.303  36.488  28.835  1.00 11.74           C  
ANISOU 1042  C   ASN A 531     1632   1338   1488     15   -144    -48       C  
ATOM   1043  O   ASN A 531      15.135  35.286  28.897  1.00 11.28           O  
ANISOU 1043  O   ASN A 531     1691   1115   1477     59   -312    -34       O  
ATOM   1044  CB  ASN A 531      13.147  36.844  30.136  1.00 12.29           C  
ANISOU 1044  CB  ASN A 531     1642   1493   1533     35    -67    -70       C  
ATOM   1045  CG  ASN A 531      12.510  37.577  31.311  1.00 13.05           C  
ANISOU 1045  CG  ASN A 531     1902   1585   1469    127   -253   -249       C  
ATOM   1046  OD1 ASN A 531      13.041  37.502  32.412  1.00 14.44           O  
ANISOU 1046  OD1 ASN A 531     2608   1389   1487     95   -296   -114       O  
ATOM   1047  ND2 ASN A 531      11.384  38.271  31.082  1.00 12.44           N  
ANISOU 1047  ND2 ASN A 531     2039   1604   1082    293    147   -320       N  
ATOM   1048  N   ALA A 532      16.160  37.016  27.984  1.00 10.74           N  
ANISOU 1048  N   ALA A 532     1481   1167   1430     62   -170   -156       N  
ATOM   1049  CA  ALA A 532      16.935  36.179  27.080  1.00 11.00           C  
ANISOU 1049  CA  ALA A 532     1432   1302   1444     24    -62   -136       C  
ATOM   1050  C   ALA A 532      17.816  35.187  27.808  1.00 10.83           C  
ANISOU 1050  C   ALA A 532     1396   1392   1324    -12    -85    -70       C  
ATOM   1051  O   ALA A 532      18.029  34.071  27.320  1.00  9.97           O  
ANISOU 1051  O   ALA A 532     1189   1265   1333     40    -80   -161       O  
ATOM   1052  CB  ALA A 532      17.783  36.997  26.176  1.00 11.14           C  
ANISOU 1052  CB  ALA A 532     1544   1255   1432     17    -56    -93       C  
ATOM   1053  N   HIS A 533      18.346  35.556  28.963  1.00 11.36           N  
ANISOU 1053  N   HIS A 533     1448   1341   1525    -54   -192    -59       N  
ATOM   1054  CA  HIS A 533      19.143  34.582  29.715  1.00 11.61           C  
ANISOU 1054  CA  HIS A 533     1453   1478   1479     55   -203    -64       C  
ATOM   1055  C   HIS A 533      18.290  33.404  30.185  1.00 11.17           C  
ANISOU 1055  C   HIS A 533     1415   1426   1399     -9   -238   -140       C  
ATOM   1056  O   HIS A 533      18.796  32.330  30.381  1.00 11.32           O  
ANISOU 1056  O   HIS A 533     1272   1417   1610    -64   -321   -234       O  
ATOM   1057  CB  HIS A 533      19.772  35.224  30.940  1.00 12.50           C  
ANISOU 1057  CB  HIS A 533     1464   1636   1646    196   -217    -63       C  
ATOM   1058  CG  HIS A 533      20.903  36.133  30.624  1.00 17.11           C  
ANISOU 1058  CG  HIS A 533     1976   2093   2430    -24   -127    -91       C  
ATOM   1059  ND1 HIS A 533      20.734  37.467  30.365  1.00 27.46           N  
ANISOU 1059  ND1 HIS A 533     3359   3199   3875    -95    -81    239       N  
ATOM   1060  CD2 HIS A 533      22.240  35.926  30.664  1.00 25.89           C  
ANISOU 1060  CD2 HIS A 533     2701   3406   3729      8    -49    195       C  
ATOM   1061  CE1 HIS A 533      21.911  38.036  30.205  1.00 26.59           C  
ANISOU 1061  CE1 HIS A 533     3193   3209   3699   -106    -24    150       C  
ATOM   1062  NE2 HIS A 533      22.844  37.122  30.357  1.00 25.89           N  
ANISOU 1062  NE2 HIS A 533     3056   2994   3784   -153   -164    -49       N  
ATOM   1063  N   LYS A 534      17.007  33.636  30.473  1.00 11.19           N  
ANISOU 1063  N   LYS A 534     1410   1348   1492    -76    -97   -147       N  
ATOM   1064  CA  LYS A 534      16.134  32.539  30.916  1.00 10.95           C  
ANISOU 1064  CA  LYS A 534     1457   1340   1361    -20    -99     -9       C  
ATOM   1065  C   LYS A 534      15.929  31.567  29.764  1.00  9.61           C  
ANISOU 1065  C   LYS A 534     1140   1224   1287     82    -60    -13       C  
ATOM   1066  O   LYS A 534      15.881  30.376  29.978  1.00 10.44           O  
ANISOU 1066  O   LYS A 534     1358   1221   1386   -113   -124     79       O  
ATOM   1067  CB  LYS A 534      14.794  32.997  31.427  1.00 12.43           C  
ANISOU 1067  CB  LYS A 534     1760   1465   1495     68   -155    -96       C  
ATOM   1068  CG  LYS A 534      14.892  33.888  32.662  1.00 12.68           C  
ANISOU 1068  CG  LYS A 534     1843   1552   1422    -19    -37    -98       C  
ATOM   1069  CD ALYS A 534      13.510  34.183  33.192  0.50 14.31           C  
ANISOU 1069  CD ALYS A 534     1845   1767   1823     53    -58    -32       C  
ATOM   1070  CE ALYS A 534      12.967  33.087  34.063  0.50 15.61           C  
ANISOU 1070  CE ALYS A 534     2097   1936   1898   -100     77    -71       C  
ATOM   1071  NZ ALYS A 534      13.747  33.041  35.343  0.50 18.32           N  
ANISOU 1071  NZ ALYS A 534     2283   2378   2300     50   -108     92       N  
ATOM   1072  CD BLYS A 534      13.562  34.040  33.354  0.50 14.09           C  
ANISOU 1072  CD BLYS A 534     1840   1693   1821     81    -54      9       C  
ATOM   1073  CE BLYS A 534      13.684  34.720  34.731  0.50 15.80           C  
ANISOU 1073  CE BLYS A 534     2162   1855   1984     67    -73    -81       C  
ATOM   1074  NZ BLYS A 534      14.923  34.458  35.548  0.50 17.99           N  
ANISOU 1074  NZ BLYS A 534     2312   2254   2267     90   -150    -21       N  
ATOM   1075  N   TRP A 535      15.848  32.065  28.535  1.00  9.14           N  
ANISOU 1075  N   TRP A 535     1056   1197   1218     86     -7    -11       N  
ATOM   1076  CA  TRP A 535      15.756  31.202  27.384  1.00  9.44           C  
ANISOU 1076  CA  TRP A 535     1196   1116   1275      1    -86    -21       C  
ATOM   1077  C   TRP A 535      17.062  30.415  27.219  1.00  9.11           C  
ANISOU 1077  C   TRP A 535     1090   1113   1257      5   -119    -65       C  
ATOM   1078  O   TRP A 535      17.037  29.199  27.011  1.00  9.52           O  
ANISOU 1078  O   TRP A 535     1177   1070   1368    -76   -215    -66       O  
ATOM   1079  CB  TRP A 535      15.494  32.016  26.118  1.00  8.49           C  
ANISOU 1079  CB  TRP A 535     1117   1121    986    -11    -92    -89       C  
ATOM   1080  CG  TRP A 535      14.020  32.189  25.787  1.00  8.23           C  
ANISOU 1080  CG  TRP A 535     1027   1137    963     -3    205     75       C  
ATOM   1081  CD1 TRP A 535      13.287  33.322  25.830  1.00 10.12           C  
ANISOU 1081  CD1 TRP A 535     1268   1176   1400   -121     -5     78       C  
ATOM   1082  CD2 TRP A 535      13.139  31.154  25.369  1.00  9.00           C  
ANISOU 1082  CD2 TRP A 535      929   1117   1369     -2    -53     80       C  
ATOM   1083  NE1 TRP A 535      12.004  33.078  25.423  1.00 10.62           N  
ANISOU 1083  NE1 TRP A 535     1357   1515   1164    -13    -74    -49       N  
ATOM   1084  CE2 TRP A 535      11.878  31.745  25.136  1.00  9.46           C  
ANISOU 1084  CE2 TRP A 535     1115   1256   1223      0   -113     23       C  
ATOM   1085  CE3 TRP A 535      13.294  29.778  25.126  1.00  9.95           C  
ANISOU 1085  CE3 TRP A 535     1289   1244   1246    -40    -65     22       C  
ATOM   1086  CZ2 TRP A 535      10.763  31.001  24.704  1.00 10.33           C  
ANISOU 1086  CZ2 TRP A 535     1274   1694    954   -228    110     54       C  
ATOM   1087  CZ3 TRP A 535      12.179  29.044  24.687  1.00 10.78           C  
ANISOU 1087  CZ3 TRP A 535     1586   1235   1274   -103    -17     95       C  
ATOM   1088  CH2 TRP A 535      10.943  29.648  24.517  1.00 10.94           C  
ANISOU 1088  CH2 TRP A 535     1302   1641   1213    -97    -72    -26       C  
ATOM   1089  N   CYS A 536      18.208  31.100  27.321  1.00 10.00           N  
ANISOU 1089  N   CYS A 536     1086   1220   1492    137   -173    -28       N  
ATOM   1090  CA  CYS A 536      19.486  30.419  27.194  1.00  9.89           C  
ANISOU 1090  CA  CYS A 536      980   1278   1499    -27    -24    -50       C  
ATOM   1091  C   CYS A 536      19.617  29.326  28.221  1.00 10.14           C  
ANISOU 1091  C   CYS A 536     1047   1292   1510    -58    -76   -101       C  
ATOM   1092  O   CYS A 536      19.927  28.185  27.884  1.00 10.88           O  
ANISOU 1092  O   CYS A 536     1092   1294   1745    -21    -69   -101       O  
ATOM   1093  CB  CYS A 536      20.605  31.467  27.339  1.00 11.15           C  
ANISOU 1093  CB  CYS A 536     1028   1460   1746    -92   -315     50       C  
ATOM   1094  SG  CYS A 536      22.250  30.782  26.986  1.00 14.37           S  
ANISOU 1094  SG  CYS A 536     1253   1788   2418   -252   -146    -18       S  
ATOM   1095  N   ARG A 537      19.327  29.632  29.476  1.00 10.52           N  
ANISOU 1095  N   ARG A 537     1230   1316   1449     36    -15    -19       N  
ATOM   1096  CA  ARG A 537      19.512  28.711  30.585  1.00 11.02           C  
ANISOU 1096  CA  ARG A 537     1361   1354   1471     14    -68     39       C  
ATOM   1097  C   ARG A 537      18.627  27.509  30.401  1.00 10.08           C  
ANISOU 1097  C   ARG A 537     1109   1307   1412     28   -117    -46       C  
ATOM   1098  O   ARG A 537      19.039  26.410  30.669  1.00 11.91           O  
ANISOU 1098  O   ARG A 537     1161   1492   1870     15     22   -158       O  
ATOM   1099  CB  ARG A 537      19.179  29.331  31.954  1.00 13.04           C  
ANISOU 1099  CB  ARG A 537     1737   1580   1637     16    -45      7       C  
ATOM   1100  CG  ARG A 537      20.215  30.322  32.512  1.00 18.09           C  
ANISOU 1100  CG  ARG A 537     2240   2148   2485    -55   -192    106       C  
ATOM   1101  CD  ARG A 537      19.631  31.139  33.766  1.00 23.43           C  
ANISOU 1101  CD  ARG A 537     2978   3092   2831    -73     -5   -106       C  
ATOM   1102  NE  ARG A 537      20.337  32.417  33.988  1.00 24.64           N  
ANISOU 1102  NE  ARG A 537     3195   2979   3186    152     33   -138       N  
ATOM   1103  CZ  ARG A 537      19.797  33.631  34.049  1.00 26.26           C  
ANISOU 1103  CZ  ARG A 537     3328   3233   3416    148    -67    -47       C  
ATOM   1104  NH1 ARG A 537      18.466  33.820  33.949  1.00 25.68           N  
ANISOU 1104  NH1 ARG A 537     3296   3148   3313     57   -141      8       N  
ATOM   1105  NH2 ARG A 537      20.608  34.674  34.245  1.00 27.48           N  
ANISOU 1105  NH2 ARG A 537     3434   3392   3613    136    -76    111       N  
ATOM   1106  N   LYS A 538      17.367  27.716  29.988  1.00  9.68           N  
ANISOU 1106  N   LYS A 538     1207   1201   1270    138    -70    -98       N  
ATOM   1107  CA  LYS A 538      16.457  26.607  29.848  1.00  9.57           C  
ANISOU 1107  CA  LYS A 538     1222   1235   1178      4   -118    -36       C  
ATOM   1108  C   LYS A 538      16.799  25.682  28.669  1.00  7.52           C  
ANISOU 1108  C   LYS A 538      713    986   1156    -17     22    -41       C  
ATOM   1109  O   LYS A 538      16.766  24.452  28.789  1.00 10.13           O  
ANISOU 1109  O   LYS A 538      958   1290   1597     61     45    -79       O  
ATOM   1110  CB  LYS A 538      15.001  27.081  29.781  1.00 10.42           C  
ANISOU 1110  CB  LYS A 538     1305   1265   1389     91   -157   -186       C  
ATOM   1111  CG  LYS A 538      13.964  25.987  30.054  1.00 12.80           C  
ANISOU 1111  CG  LYS A 538     1550   1550   1763    121    -90    139       C  
ATOM   1112  CD  LYS A 538      13.978  25.714  31.542  1.00 15.95           C  
ANISOU 1112  CD  LYS A 538     1693   2335   2032    121    -54    158       C  
ATOM   1113  CE  LYS A 538      13.090  24.705  32.055  1.00 17.94           C  
ANISOU 1113  CE  LYS A 538     2294   2313   2208     16     18    122       C  
ATOM   1114  NZ  LYS A 538      13.439  24.610  33.579  1.00 18.71           N  
ANISOU 1114  NZ  LYS A 538     2514   2306   2287     45    -11    140       N  
ATOM   1115  N   ILE A 539      17.173  26.285  27.559  1.00  8.45           N  
ANISOU 1115  N   ILE A 539      971   1093   1146    -53   -111    -43       N  
ATOM   1116  CA  ILE A 539      17.650  25.489  26.429  1.00  8.56           C  
ANISOU 1116  CA  ILE A 539      905   1159   1189     -2    -56    -61       C  
ATOM   1117  C   ILE A 539      18.882  24.691  26.828  1.00  9.39           C  
ANISOU 1117  C   ILE A 539     1139   1032   1395     48   -103    -77       C  
ATOM   1118  O   ILE A 539      18.970  23.512  26.519  1.00  9.45           O  
ANISOU 1118  O   ILE A 539     1139    968   1482    368   -171   -233       O  
ATOM   1119  CB  ILE A 539      17.897  26.342  25.180  1.00  9.71           C  
ANISOU 1119  CB  ILE A 539     1201   1011   1475     30   -141    -62       C  
ATOM   1120  CG1 ILE A 539      16.552  26.946  24.702  1.00  8.75           C  
ANISOU 1120  CG1 ILE A 539      956   1273   1094     32   -106    -56       C  
ATOM   1121  CG2 ILE A 539      18.601  25.565  24.071  1.00  9.71           C  
ANISOU 1121  CG2 ILE A 539     1263   1163   1260      2   -188     11       C  
ATOM   1122  CD1 ILE A 539      16.715  28.118  23.724  1.00 10.33           C  
ANISOU 1122  CD1 ILE A 539     1362   1364   1199    -48    -63    -52       C  
ATOM   1123  N   GLN A 540      19.778  25.301  27.603  1.00  9.46           N  
ANISOU 1123  N   GLN A 540     1034   1048   1511    -37    -48    -98       N  
ATOM   1124  CA  GLN A 540      21.003  24.590  28.024  1.00 10.13           C  
ANISOU 1124  CA  GLN A 540     1167   1206   1473     -6   -101    -33       C  
ATOM   1125  C   GLN A 540      20.687  23.463  29.035  1.00 10.77           C  
ANISOU 1125  C   GLN A 540     1389   1316   1385     24   -100   -100       C  
ATOM   1126  O   GLN A 540      21.295  22.414  28.999  1.00  9.68           O  
ANISOU 1126  O   GLN A 540     1029   1109   1538    157   -133    -16       O  
ATOM   1127  CB  GLN A 540      21.993  25.552  28.650  1.00 10.65           C  
ANISOU 1127  CB  GLN A 540     1269   1194   1581     18    -41     16       C  
ATOM   1128  CG  GLN A 540      23.348  24.944  28.884  1.00 13.46           C  
ANISOU 1128  CG  GLN A 540     1367   1680   2067    137   -287    130       C  
ATOM   1129  CD  GLN A 540      23.984  24.368  27.614  1.00 16.83           C  
ANISOU 1129  CD  GLN A 540     1639   2248   2507     81     69    157       C  
ATOM   1130  OE1 GLN A 540      23.832  24.894  26.536  1.00 24.34           O  
ANISOU 1130  OE1 GLN A 540     2725   3235   3287    502   -125    279       O  
ATOM   1131  NE2 GLN A 540      24.745  23.287  27.765  1.00 20.21           N  
ANISOU 1131  NE2 GLN A 540     1867   2357   3454    282     77    189       N  
ATOM   1132  N   GLU A 541      19.726  23.672  29.923  1.00  9.77           N  
ANISOU 1132  N   GLU A 541     1053   1317   1339      9   -172    -92       N  
ATOM   1133  CA  GLU A 541      19.269  22.653  30.831  1.00 10.43           C  
ANISOU 1133  CA  GLU A 541     1211   1413   1336      5   -153    -45       C  
ATOM   1134  C   GLU A 541      18.739  21.474  30.086  1.00  9.89           C  
ANISOU 1134  C   GLU A 541     1173   1259   1322     18    -66      5       C  
ATOM   1135  O   GLU A 541      19.074  20.320  30.395  1.00 10.50           O  
ANISOU 1135  O   GLU A 541     1029   1426   1532    144   -178   -102       O  
ATOM   1136  CB  GLU A 541      18.204  23.232  31.779  1.00 11.42           C  
ANISOU 1136  CB  GLU A 541     1394   1476   1466    -55     34    -56       C  
ATOM   1137  CG  GLU A 541      17.795  22.252  32.852  1.00 12.74           C  
ANISOU 1137  CG  GLU A 541     1531   1724   1583    188    -73    127       C  
ATOM   1138  CD  GLU A 541      16.575  22.642  33.712  1.00 14.25           C  
ANISOU 1138  CD  GLU A 541     1531   2018   1865     53    159    101       C  
ATOM   1139  OE1 GLU A 541      15.900  23.687  33.484  1.00 17.27           O  
ANISOU 1139  OE1 GLU A 541     2160   2088   2314    165    210    299       O  
ATOM   1140  OE2 GLU A 541      16.327  21.898  34.674  1.00 17.70           O  
ANISOU 1140  OE2 GLU A 541     1993   2218   2511     64    100    171       O  
ATOM   1141  N   VAL A 542      17.917  21.749  29.081  1.00  9.15           N  
ANISOU 1141  N   VAL A 542     1198    990   1289     91   -104    -84       N  
ATOM   1142  CA  VAL A 542      17.387  20.691  28.254  1.00  8.52           C  
ANISOU 1142  CA  VAL A 542     1082   1043   1110     23      1    -86       C  
ATOM   1143  C   VAL A 542      18.518  19.957  27.510  1.00  9.49           C  
ANISOU 1143  C   VAL A 542     1018   1169   1418      4    -16    -98       C  
ATOM   1144  O   VAL A 542      18.502  18.707  27.439  1.00 10.21           O  
ANISOU 1144  O   VAL A 542     1168   1170   1541    208     32   -173       O  
ATOM   1145  CB  VAL A 542      16.286  21.218  27.319  1.00  8.04           C  
ANISOU 1145  CB  VAL A 542      932   1020   1099     92     83    -44       C  
ATOM   1146  CG1 VAL A 542      15.989  20.211  26.261  1.00  8.60           C  
ANISOU 1146  CG1 VAL A 542     1068   1050   1149   -266    -85    132       C  
ATOM   1147  CG2 VAL A 542      15.045  21.481  28.125  1.00  8.88           C  
ANISOU 1147  CG2 VAL A 542      822   1345   1205    -52     46    -15       C  
ATOM   1148  N   TRP A 543      19.467  20.707  26.948  1.00  9.92           N  
ANISOU 1148  N   TRP A 543     1233   1203   1332     45     37   -196       N  
ATOM   1149  CA  TRP A 543      20.593  20.134  26.224  1.00  8.73           C  
ANISOU 1149  CA  TRP A 543      963   1016   1337    -37     -2    -48       C  
ATOM   1150  C   TRP A 543      21.354  19.162  27.184  1.00  9.24           C  
ANISOU 1150  C   TRP A 543     1107    992   1411     56    -56    -48       C  
ATOM   1151  O   TRP A 543      21.678  18.039  26.806  1.00  9.71           O  
ANISOU 1151  O   TRP A 543     1027    990   1672      4    -76    -36       O  
ATOM   1152  CB  TRP A 543      21.508  21.259  25.758  1.00  9.59           C  
ANISOU 1152  CB  TRP A 543     1039   1028   1574      4     25    -61       C  
ATOM   1153  CG  TRP A 543      22.702  20.740  24.929  1.00  9.46           C  
ANISOU 1153  CG  TRP A 543      684   1269   1641   -141     27   -178       C  
ATOM   1154  CD1 TRP A 543      22.783  20.713  23.580  1.00  9.73           C  
ANISOU 1154  CD1 TRP A 543     1109   1051   1534    115     94   -213       C  
ATOM   1155  CD2 TRP A 543      23.930  20.162  25.409  1.00 12.62           C  
ANISOU 1155  CD2 TRP A 543     1592   1259   1942    169     42     85       C  
ATOM   1156  NE1 TRP A 543      23.949  20.102  23.164  1.00 11.33           N  
ANISOU 1156  NE1 TRP A 543      855   1394   2053    -25    211     -9       N  
ATOM   1157  CE2 TRP A 543      24.679  19.777  24.271  1.00 11.74           C  
ANISOU 1157  CE2 TRP A 543     1222   1249   1986    -92    108    139       C  
ATOM   1158  CE3 TRP A 543      24.469  19.931  26.677  1.00 12.14           C  
ANISOU 1158  CE3 TRP A 543      984   1552   2075     47     52    169       C  
ATOM   1159  CZ2 TRP A 543      25.932  19.166  24.378  1.00 13.84           C  
ANISOU 1159  CZ2 TRP A 543     1268   1964   2025    140    195    -43       C  
ATOM   1160  CZ3 TRP A 543      25.724  19.313  26.778  1.00 11.69           C  
ANISOU 1160  CZ3 TRP A 543     1067   1415   1959     60     48    155       C  
ATOM   1161  CH2 TRP A 543      26.414  18.931  25.628  1.00 12.66           C  
ANISOU 1161  CH2 TRP A 543     1265   1533   2008    -42    194    174       C  
ATOM   1162  N   ARG A 544      21.606  19.578  28.422  1.00 10.45           N  
ANISOU 1162  N   ARG A 544     1252   1120   1596     84   -163     29       N  
ATOM   1163  CA  ARG A 544      22.311  18.695  29.384  1.00 10.65           C  
ANISOU 1163  CA  ARG A 544     1288   1319   1438      7   -143     41       C  
ATOM   1164  C   ARG A 544      21.509  17.405  29.620  1.00 10.92           C  
ANISOU 1164  C   ARG A 544     1326   1246   1577     36    -38   -105       C  
ATOM   1165  O   ARG A 544      22.064  16.289  29.693  1.00 12.19           O  
ANISOU 1165  O   ARG A 544     1388   1317   1927     32   -377   -136       O  
ATOM   1166  CB  ARG A 544      22.533  19.404  30.706  1.00 12.69           C  
ANISOU 1166  CB  ARG A 544     1563   1474   1784    107    -72    -10       C  
ATOM   1167  CG  ARG A 544      23.639  20.394  30.739  1.00 17.15           C  
ANISOU 1167  CG  ARG A 544     2085   2161   2267    -27    -44     98       C  
ATOM   1168  CD  ARG A 544      23.993  20.752  32.194  1.00 19.86           C  
ANISOU 1168  CD  ARG A 544     2358   2649   2537   -152   -142   -264       C  
ATOM   1169  NE  ARG A 544      22.863  21.400  32.918  1.00 22.77           N  
ANISOU 1169  NE  ARG A 544     2922   2863   2866     20   -100   -185       N  
ATOM   1170  CZ  ARG A 544      22.610  22.704  32.867  1.00 23.18           C  
ANISOU 1170  CZ  ARG A 544     2914   2926   2966     81    -96   -179       C  
ATOM   1171  NH1 ARG A 544      23.411  23.522  32.192  1.00 23.17           N  
ANISOU 1171  NH1 ARG A 544     3273   2772   2757    199     64   -141       N  
ATOM   1172  NH2 ARG A 544      21.602  23.205  33.566  1.00 24.04           N  
ANISOU 1172  NH2 ARG A 544     2955   3221   2957     63     -6   -161       N  
ATOM   1173  N   GLN A 545      20.203  17.536  29.792  1.00 11.01           N  
ANISOU 1173  N   GLN A 545     1274   1273   1636     -7   -226    -66       N  
ATOM   1174  CA  GLN A 545      19.343  16.363  30.031  1.00 11.36           C  
ANISOU 1174  CA  GLN A 545     1398   1357   1560    -45   -156    -60       C  
ATOM   1175  C   GLN A 545      19.302  15.426  28.835  1.00 10.82           C  
ANISOU 1175  C   GLN A 545     1226   1315   1568     -4   -129     -2       C  
ATOM   1176  O   GLN A 545      19.257  14.197  29.000  1.00 12.10           O  
ANISOU 1176  O   GLN A 545     1485   1200   1911    -46   -369   -190       O  
ATOM   1177  CB  GLN A 545      17.936  16.774  30.466  1.00 13.34           C  
ANISOU 1177  CB  GLN A 545     1583   1571   1911   -120    -30    -16       C  
ATOM   1178  CG  GLN A 545      17.840  17.344  31.883  1.00 17.05           C  
ANISOU 1178  CG  GLN A 545     2209   2119   2150     10    -23   -109       C  
ATOM   1179  CD  GLN A 545      16.575  16.950  32.655  1.00 23.44           C  
ANISOU 1179  CD  GLN A 545     2819   3166   2921     73    184    -12       C  
ATOM   1180  OE1 GLN A 545      15.850  16.013  32.288  1.00 29.76           O  
ANISOU 1180  OE1 GLN A 545     3775   3759   3773     53      1   -101       O  
ATOM   1181  NE2 GLN A 545      16.289  17.709  33.733  1.00 28.91           N  
ANISOU 1181  NE2 GLN A 545     3749   3932   3300    161    104   -162       N  
ATOM   1182  N   ARG A 546      19.393  16.000  27.653  1.00  9.97           N  
ANISOU 1182  N   ARG A 546     1164   1200   1422   -132    -42    -77       N  
ATOM   1183  CA  ARG A 546      19.270  15.239  26.423  1.00 11.17           C  
ANISOU 1183  CA  ARG A 546     1344   1407   1491    -14     46    -48       C  
ATOM   1184  C   ARG A 546      20.580  14.530  26.059  1.00 10.49           C  
ANISOU 1184  C   ARG A 546     1303   1136   1545     34    -55    -28       C  
ATOM   1185  O   ARG A 546      20.565  13.409  25.519  1.00 10.50           O  
ANISOU 1185  O   ARG A 546     1269   1151   1569    -25   -246   -205       O  
ATOM   1186  CB  ARG A 546      18.757  16.146  25.277  1.00 10.98           C  
ANISOU 1186  CB  ARG A 546     1335   1326   1509    -20     16     15       C  
ATOM   1187  CG  ARG A 546      18.811  15.512  23.895  1.00 11.69           C  
ANISOU 1187  CG  ARG A 546     1438   1246   1757    126   -224     23       C  
ATOM   1188  CD  ARG A 546      17.951  14.235  23.745  1.00 12.11           C  
ANISOU 1188  CD  ARG A 546     1526   1484   1589   -187    -42     80       C  
ATOM   1189  NE  ARG A 546      18.095  13.640  22.402  1.00 12.22           N  
ANISOU 1189  NE  ARG A 546     1692   1299   1649   -381    115     29       N  
ATOM   1190  CZ  ARG A 546      19.111  12.882  22.030  1.00 13.14           C  
ANISOU 1190  CZ  ARG A 546     1829   1513   1649    -44    -72     40       C  
ATOM   1191  NH1 ARG A 546      20.089  12.534  22.894  1.00 12.49           N  
ANISOU 1191  NH1 ARG A 546     1893   1134   1718    277   -144    -37       N  
ATOM   1192  NH2 ARG A 546      19.174  12.471  20.762  1.00 13.39           N  
ANISOU 1192  NH2 ARG A 546     1929   1517   1639    102   -108    -87       N  
ATOM   1193  N   TYR A 547      21.700  15.207  26.266  1.00 11.25           N  
ANISOU 1193  N   TYR A 547     1257   1354   1661     24     45    -86       N  
ATOM   1194  CA  TYR A 547      22.990  14.757  25.668  1.00 12.42           C  
ANISOU 1194  CA  TYR A 547     1532   1490   1696     93     23    -16       C  
ATOM   1195  C   TYR A 547      23.972  14.288  26.714  1.00 12.87           C  
ANISOU 1195  C   TYR A 547     1474   1637   1780     47    -26     54       C  
ATOM   1196  O   TYR A 547      24.938  13.658  26.371  1.00 16.01           O  
ANISOU 1196  O   TYR A 547     1910   1983   2190    239     73    178       O  
ATOM   1197  CB  TYR A 547      23.624  15.785  24.718  1.00 10.85           C  
ANISOU 1197  CB  TYR A 547     1313   1258   1549    100     40   -207       C  
ATOM   1198  CG  TYR A 547      22.703  16.139  23.605  1.00 12.00           C  
ANISOU 1198  CG  TYR A 547     1471   1372   1716    129    -57   -131       C  
ATOM   1199  CD1 TYR A 547      22.378  15.178  22.626  1.00 11.21           C  
ANISOU 1199  CD1 TYR A 547     1142   1420   1696    293     84   -267       C  
ATOM   1200  CD2 TYR A 547      22.121  17.392  23.507  1.00 10.63           C  
ANISOU 1200  CD2 TYR A 547     1181   1150   1705   -162    -18    -36       C  
ATOM   1201  CE1 TYR A 547      21.492  15.453  21.615  1.00 13.05           C  
ANISOU 1201  CE1 TYR A 547     1977   1469   1511    168   -112   -346       C  
ATOM   1202  CE2 TYR A 547      21.245  17.674  22.491  1.00 12.44           C  
ANISOU 1202  CE2 TYR A 547     1796   1483   1444     40     25    -51       C  
ATOM   1203  CZ  TYR A 547      20.962  16.730  21.515  1.00 13.73           C  
ANISOU 1203  CZ  TYR A 547     1743   1538   1936     43   -237    -54       C  
ATOM   1204  OH  TYR A 547      20.044  17.041  20.528  1.00 15.72           O  
ANISOU 1204  OH  TYR A 547     1958   2044   1969     54   -357      1       O  
ATOM   1205  N   GLN A 548      23.722  14.568  27.976  1.00 14.50           N  
ANISOU 1205  N   GLN A 548     1704   1806   1997    149    -55    153       N  
ATOM   1206  CA  GLN A 548      24.627  14.097  29.032  1.00 16.17           C  
ANISOU 1206  CA  GLN A 548     1985   2044   2114    100   -134     73       C  
ATOM   1207  C   GLN A 548      23.890  13.025  29.852  1.00 19.35           C  
ANISOU 1207  C   GLN A 548     2339   2430   2583    -22    -33     64       C  
ATOM   1208  O   GLN A 548      22.694  12.884  29.734  1.00 16.91           O  
ANISOU 1208  O   GLN A 548     2173   2018   2232      2     78    -48       O  
ATOM   1209  CB  GLN A 548      25.222  15.272  29.781  1.00 14.75           C  
ANISOU 1209  CB  GLN A 548     1632   1956   2015    252   -155     75       C  
ATOM   1210  CG  GLN A 548      26.039  16.040  28.795  1.00 16.14           C  
ANISOU 1210  CG  GLN A 548     2004   2070   2056     31   -131     29       C  
ATOM   1211  CD  GLN A 548      26.947  17.170  29.331  1.00 14.86           C  
ANISOU 1211  CD  GLN A 548     1642   2081   1923    -96    153     33       C  
ATOM   1212  OE1 GLN A 548      26.535  17.902  30.272  1.00 17.95           O  
ANISOU 1212  OE1 GLN A 548     2233   2229   2357    283    -28   -222       O  
ATOM   1213  NE2 GLN A 548      28.173  17.385  28.648  1.00 14.03           N  
ANISOU 1213  NE2 GLN A 548     1348   2055   1928    -56    172    155       N  
ATOM   1214  N   SER A 549      24.639  12.182  30.567  1.00 25.08           N  
ANISOU 1214  N   SER A 549     3167   3117   3241    -12   -100    113       N  
ATOM   1215  CA  SER A 549      24.015  11.096  31.370  1.00 28.50           C  
ANISOU 1215  CA  SER A 549     3529   3623   3676   -112     11     68       C  
ATOM   1216  C   SER A 549      23.083  11.648  32.456  1.00 30.22           C  
ANISOU 1216  C   SER A 549     3831   3862   3788   -129     51      1       C  
ATOM   1217  O   SER A 549      23.404  12.648  33.081  1.00 31.56           O  
ANISOU 1217  O   SER A 549     4014   4031   3944   -273    145      1       O  
ATOM   1218  CB  SER A 549      25.052  10.143  31.955  1.00 30.07           C  
ANISOU 1218  CB  SER A 549     3793   3749   3881    -19      1     34       C  
ATOM   1219  OG  SER A 549      25.015   8.912  31.250  1.00 34.58           O  
ANISOU 1219  OG  SER A 549     4342   4336   4459    -57    155   -217       O  
ATOM   1220  N   HIS A 550      21.946  11.153  32.730  1.00 31.73           N  
ANISOU 1220  N   HIS A 550     3838   4221   3994   -135    139    -14       N  
TER    1221      HIS A 550                                                      
HETATM 1222  C1  GOL A1550      20.465  38.021   9.683  1.00 36.21           C  
ANISOU 1222  C1  GOL A1550     4395   4635   4726     56    -22    -39       C  
HETATM 1223  O1  GOL A1550      19.464  38.922  10.187  1.00 34.84           O  
ANISOU 1223  O1  GOL A1550     4323   4322   4591     48    -44   -164       O  
HETATM 1224  C2  GOL A1550      19.807  36.737   9.172  1.00 35.24           C  
ANISOU 1224  C2  GOL A1550     4303   4547   4539     52     48    -26       C  
HETATM 1225  O2  GOL A1550      19.625  36.827   7.767  1.00 31.35           O  
ANISOU 1225  O2  GOL A1550     3411   4164   4337     84    126     72       O  
HETATM 1226  C3  GOL A1550      20.658  35.515   9.576  1.00 35.86           C  
ANISOU 1226  C3  GOL A1550     4341   4620   4661    109     -7     22       C  
HETATM 1227  O3  GOL A1550      20.197  34.247   9.025  1.00 37.46           O  
ANISOU 1227  O3  GOL A1550     4649   4895   4686    -43     39      0       O  
HETATM 1228 AU  A AU A1551      22.787  29.569  28.742  0.85 18.11          AU  
ANISOU 1228 AU  A AU A1551     1494   2207   3178     48   -474   -122      AU  
HETATM 1229 AU  B AU A1551      23.672  32.318  28.077  0.15 22.06          AU  
ANISOU 1229 AU  B AU A1551     2408   2881   3092     49   -824   -285      AU  
HETATM 1230  C1  4IP A1552      11.090  35.168   6.150  1.00 11.72           C  
ANISOU 1230  C1  4IP A1552     1923   1337   1193    130    170    137       C  
HETATM 1231  O1  4IP A1552      10.984  36.543   5.877  1.00 13.09           O  
ANISOU 1231  O1  4IP A1552     2369   1547   1056    -28    105    151       O  
HETATM 1232  C2  4IP A1552      10.792  34.868   7.630  1.00  9.93           C  
ANISOU 1232  C2  4IP A1552     1595   1043   1134   -179    117    157       C  
HETATM 1233  O2  4IP A1552      11.841  35.446   8.426  1.00 12.04           O  
ANISOU 1233  O2  4IP A1552     1655   1608   1310   -237    134     -8       O  
HETATM 1234  C3  4IP A1552      10.811  33.343   7.772  1.00  8.76           C  
ANISOU 1234  C3  4IP A1552     1348   1028    952   -101    207     62       C  
HETATM 1235  O3  4IP A1552      10.454  33.059   9.142  1.00 10.73           O  
ANISOU 1235  O3  4IP A1552     1959   1151    967   -161    236    241       O  
HETATM 1236  C4  4IP A1552      12.194  32.806   7.470  1.00 11.35           C  
ANISOU 1236  C4  4IP A1552     1712   1275   1323    139    414     20       C  
HETATM 1237  O4  4IP A1552      12.189  31.362   7.529  1.00 13.17           O  
ANISOU 1237  O4  4IP A1552     1803   1359   1841    268    336     64       O  
HETATM 1238  C5  4IP A1552      12.535  33.091   5.985  1.00 14.75           C  
ANISOU 1238  C5  4IP A1552     2294   1908   1401     98     97    375       C  
HETATM 1239  O5  4IP A1552      13.937  32.770   5.892  1.00 17.54           O  
ANISOU 1239  O5  4IP A1552     2613   1987   2063    352    356    196       O  
HETATM 1240  C6  4IP A1552      12.467  34.601   5.742  1.00 12.29           C  
ANISOU 1240  C6  4IP A1552     1985   1455   1227    261    279    -38       C  
HETATM 1241  O6  4IP A1552      12.671  34.845   4.334  1.00 15.43           O  
ANISOU 1241  O6  4IP A1552     2436   1927   1499    377    491    133       O  
HETATM 1242  P1  4IP A1552       9.600  37.137   5.292  1.00 13.29           P  
ANISOU 1242  P1  4IP A1552     2150   1543   1357   -124     80    -66       P  
HETATM 1243  O1P 4IP A1552       9.338  36.501   3.944  1.00 17.18           O  
ANISOU 1243  O1P 4IP A1552     2828   2105   1593    146   -173     36       O  
HETATM 1244  O2P 4IP A1552       8.500  36.763   6.236  1.00 14.82           O  
ANISOU 1244  O2P 4IP A1552     1876   1974   1781     -1     99   -308       O  
HETATM 1245  O3P 4IP A1552       9.908  38.607   5.169  1.00 13.96           O  
ANISOU 1245  O3P 4IP A1552     1942   1784   1578     63    213     68       O  
HETATM 1246  P3  4IP A1552       9.111  32.299   9.499  1.00 10.91           P  
ANISOU 1246  P3  4IP A1552     1520   1268   1355     80     74    -20       P  
HETATM 1247  O4P 4IP A1552       9.338  30.845   8.831  1.00 12.87           O  
ANISOU 1247  O4P 4IP A1552     1984   1489   1415    100    265      1       O  
HETATM 1248  O5P 4IP A1552       7.932  32.960   8.844  1.00 11.74           O  
ANISOU 1248  O5P 4IP A1552     1426   1637   1394    203     73     13       O  
HETATM 1249  O6P 4IP A1552       9.131  32.191  10.992  1.00 10.32           O  
ANISOU 1249  O6P 4IP A1552     1280   1373   1267    -76     86     89       O  
HETATM 1250  P4  4IP A1552      12.687  30.535   8.814  1.00 12.39           P  
ANISOU 1250  P4  4IP A1552     1668   1293   1744    188    329     58       P  
HETATM 1251  O7P 4IP A1552      13.425  31.479   9.834  1.00 13.54           O  
ANISOU 1251  O7P 4IP A1552     1727   1678   1739    308    385     29       O  
HETATM 1252  O8P 4IP A1552      11.472  29.839   9.354  1.00 12.90           O  
ANISOU 1252  O8P 4IP A1552     1869   1457   1575   -106    435    113       O  
HETATM 1253  O9P 4IP A1552      13.714  29.630   8.262  1.00 15.61           O  
ANISOU 1253  O9P 4IP A1552     2031   1540   2358    248    363    -17       O  
HETATM 1254  P5  4IP A1552      14.614  31.625   5.011  1.00 26.71           P  
ANISOU 1254  P5  4IP A1552     4132   2793   3220    277    380     17       P  
HETATM 1255  OPF 4IP A1552      13.512  31.256   4.096  1.00 19.52           O  
ANISOU 1255  OPF 4IP A1552     3035   2563   1816    821    667   -482       O  
HETATM 1256  OPG 4IP A1552      14.848  30.590   6.129  1.00 26.50           O  
ANISOU 1256  OPG 4IP A1552     3910   3202   2955    228    240     78       O  
HETATM 1257  OPH 4IP A1552      15.836  32.040   4.362  1.00 28.88           O  
ANISOU 1257  OPH 4IP A1552     3989   3657   3328    -19    321    112       O  
HETATM 1258  O   HOH A2001      12.129  44.816  17.507  1.00 18.56           O  
ANISOU 1258  O   HOH A2001     2580   2411   2061    144     86   -123       O  
HETATM 1259  O   HOH A2002       7.595  40.365  25.307  1.00 25.11           O  
ANISOU 1259  O   HOH A2002     3369   3155   3013     66     56   -198       O  
HETATM 1260  O   HOH A2003       2.393  39.762  16.066  1.00 17.69           O  
ANISOU 1260  O   HOH A2003     1663   2469   2586    -75     80    223       O  
HETATM 1261  O   HOH A2004       1.824  39.194  18.646  1.00 21.74           O  
ANISOU 1261  O   HOH A2004     2258   3138   2864    151    321    246       O  
HETATM 1262  O   HOH A2005       7.959  44.731  24.350  1.00 32.10           O  
ANISOU 1262  O   HOH A2005     4134   3953   4107    170    -79    -93       O  
HETATM 1263  O   HOH A2006       0.019  35.518  20.919  1.00 30.37           O  
ANISOU 1263  O   HOH A2006     3772   3238   4528     81    141     82       O  
HETATM 1264  O   HOH A2007       3.229  11.601  27.126  1.00 27.90           O  
ANISOU 1264  O   HOH A2007     3686   3023   3892   -147    305     52       O  
HETATM 1265  O   HOH A2008       0.608  39.682  11.430  1.00 26.49           O  
ANISOU 1265  O   HOH A2008     3384   2954   3725    -51   -135    454       O  
HETATM 1266  O   HOH A2009      16.473  22.611   9.640  1.00 23.13           O  
ANISOU 1266  O   HOH A2009     2881   3136   2769     -1    244   -540       O  
HETATM 1267  O   HOH A2010      14.092  19.210  13.249  1.00 33.29           O  
ANISOU 1267  O   HOH A2010     4290   4315   4043    242    -80   -234       O  
HETATM 1268  O   HOH A2011      20.848  19.383  13.127  1.00 25.58           O  
ANISOU 1268  O   HOH A2011     3252   3382   3085    162    -97   -451       O  
HETATM 1269  O   HOH A2012      18.821  17.507  12.795  1.00 29.39           O  
ANISOU 1269  O   HOH A2012     3233   3957   3975    -73    -50    100       O  
HETATM 1270  O   HOH A2013      23.661  17.964  10.206  1.00 39.39           O  
ANISOU 1270  O   HOH A2013     4934   5243   4786     42    138   -105       O  
HETATM 1271  O   HOH A2014      23.182  15.036  14.195  1.00 33.16           O  
ANISOU 1271  O   HOH A2014     4197   4051   4349    -61     40    -42       O  
HETATM 1272  O   HOH A2015      30.396  10.983  19.203  1.00 41.50           O  
ANISOU 1272  O   HOH A2015     5249   5257   5259     86    -35   -139       O  
HETATM 1273  O   HOH A2016      28.050  22.414  14.607  1.00 31.78           O  
ANISOU 1273  O   HOH A2016     3783   4078   4212    163    269    299       O  
HETATM 1274  O   HOH A2017      26.297  12.420  16.010  1.00 35.82           O  
ANISOU 1274  O   HOH A2017     4494   4342   4771   -167     32    -81       O  
HETATM 1275  O   HOH A2018      30.580  19.595  18.853  1.00 33.67           O  
ANISOU 1275  O   HOH A2018     3847   4416   4530   -262    -84      0       O  
HETATM 1276  O   HOH A2019      18.517  44.815  22.530  1.00 24.05           O  
ANISOU 1276  O   HOH A2019     3205   3141   2792   -167   -295    122       O  
HETATM 1277  O   HOH A2020      20.934  20.728  11.034  1.00 34.57           O  
ANISOU 1277  O   HOH A2020     4423   4567   4145    107    126    -83       O  
HETATM 1278  O   HOH A2021      20.177  24.353   8.718  1.00 28.64           O  
ANISOU 1278  O   HOH A2021     3137   3755   3988     27    -14   -113       O  
HETATM 1279  O   HOH A2022      10.695  47.909  25.103  1.00 34.54           O  
ANISOU 1279  O   HOH A2022     4409   4235   4477   -159   -104      6       O  
HETATM 1280  O   HOH A2023      13.281  45.726  22.965  1.00 27.87           O  
ANISOU 1280  O   HOH A2023     4097   3175   3316     -6    112   -135       O  
HETATM 1281  O   HOH A2024      16.188  28.054  34.632  1.00 34.37           O  
ANISOU 1281  O   HOH A2024     4575   4140   4341     88     95   -115       O  
HETATM 1282  O   HOH A2025      23.401  28.042  30.854  1.00 24.43           O  
ANISOU 1282  O   HOH A2025     2321   2942   4018   -429   -241   -506       O  
HETATM 1283  O   HOH A2026      18.205  37.391   3.785  1.00 37.98           O  
ANISOU 1283  O   HOH A2026     4986   4998   4447    -21     -8   -324       O  
HETATM 1284  O   HOH A2027       8.412  32.796   4.633  1.00 28.72           O  
ANISOU 1284  O   HOH A2027     4396   3635   2878   -360    218   -220       O  
HETATM 1285  O   HOH A2028      -0.530  37.869  18.953  1.00 31.51           O  
ANISOU 1285  O   HOH A2028     3456   4209   4305    188    107    236       O  
HETATM 1286  O   HOH A2029      18.324  20.354   9.694  1.00 32.19           O  
ANISOU 1286  O   HOH A2029     4495   3751   3982     73     14    -83       O  
HETATM 1287  O   HOH A2030      31.053  19.787  16.298  1.00 37.63           O  
ANISOU 1287  O   HOH A2030     4740   4463   5094     30    -36     51       O  
HETATM 1288  O   HOH A2031       1.453  15.885  46.768  1.00 21.21           O  
ANISOU 1288  O   HOH A2031     2701   2403   2954     91    -69     35       O  
HETATM 1289  O   HOH A2032      -2.911  19.092  40.880  1.00 34.52           O  
ANISOU 1289  O   HOH A2032     3678   4544   4893     65     29     98       O  
HETATM 1290  O   HOH A2033      -0.663  26.620  42.764  1.00 30.87           O  
ANISOU 1290  O   HOH A2033     4152   3635   3940    133    -81     61       O  
HETATM 1291  O   HOH A2034       2.235  22.176  46.269  1.00 25.16           O  
ANISOU 1291  O   HOH A2034     3314   2876   3366   -103   -163   -185       O  
HETATM 1292  O   HOH A2035      -4.047  21.648  41.686  1.00 34.99           O  
ANISOU 1292  O   HOH A2035     4430   4481   4380   -117     64     48       O  
HETATM 1293  O   HOH A2036       4.703  21.619  46.219  1.00 27.73           O  
ANISOU 1293  O   HOH A2036     3701   3534   3299    -73     63    118       O  
HETATM 1294  O   HOH A2037       7.553  22.422  43.355  1.00 32.88           O  
ANISOU 1294  O   HOH A2037     4414   4612   3468    -19   -128    -98       O  
HETATM 1295  O   HOH A2038       7.216  25.506  43.286  1.00 25.78           O  
ANISOU 1295  O   HOH A2038     3253   3152   3387    -12   -131   -106       O  
HETATM 1296  O   HOH A2039       2.539  27.848  39.372  1.00 29.72           O  
ANISOU 1296  O   HOH A2039     3906   3760   3627    -48    338   -180       O  
HETATM 1297  O   HOH A2040       4.636  27.479  40.861  1.00 33.70           O  
ANISOU 1297  O   HOH A2040     4651   4267   3886   -155    187   -173       O  
HETATM 1298  O   HOH A2041       9.737  32.041  35.154  1.00 39.35           O  
ANISOU 1298  O   HOH A2041     4994   5047   4909    130    178     27       O  
HETATM 1299  O   HOH A2042       0.749  28.657  33.364  1.00 32.78           O  
ANISOU 1299  O   HOH A2042     4222   4062   4170     85    177    166       O  
HETATM 1300  O   HOH A2043       3.010  30.353  38.209  1.00 25.40           O  
ANISOU 1300  O   HOH A2043     3728   2827   3094    468    312   -127       O  
HETATM 1301  O   HOH A2044       7.895  38.640  30.802  1.00 26.66           O  
ANISOU 1301  O   HOH A2044     3623   3374   3131     75     59     29       O  
HETATM 1302  O   HOH A2045       1.570  32.163  31.505  1.00 35.38           O  
ANISOU 1302  O   HOH A2045     4191   4675   4577    -60    222    -14       O  
HETATM 1303  O   HOH A2046       0.671  30.867  29.286  1.00 28.75           O  
ANISOU 1303  O   HOH A2046     3796   3547   3578     79     62   -142       O  
HETATM 1304  O   HOH A2047       3.109  39.043  23.155  1.00 31.23           O  
ANISOU 1304  O   HOH A2047     4099   3905   3862    220    109      3       O  
HETATM 1305  O   HOH A2048       4.618  38.191  26.971  1.00 28.38           O  
ANISOU 1305  O   HOH A2048     3073   3868   3841    312    321   -370       O  
HETATM 1306  O   HOH A2049       8.510  36.766  28.937  1.00 20.68           O  
ANISOU 1306  O   HOH A2049     2840   2604   2413    427    336   -318       O  
HETATM 1307  O   HOH A2050       8.898  32.072  28.877  1.00 13.86           O  
ANISOU 1307  O   HOH A2050     1356   1964   1945   -302   -248   -422       O  
HETATM 1308  O   HOH A2051      11.091  29.390  36.770  1.00 40.47           O  
ANISOU 1308  O   HOH A2051     5136   5227   5013   -140    104     84       O  
HETATM 1309  O   HOH A2052       9.526  22.269  41.549  1.00 21.24           O  
ANISOU 1309  O   HOH A2052     2931   2530   2608   -140    164   -117       O  
HETATM 1310  O   HOH A2053      13.776  24.684  37.375  1.00 28.93           O  
ANISOU 1310  O   HOH A2053     3628   3333   4028     67    -27   -455       O  
HETATM 1311  O   HOH A2054      11.078  26.813  36.447  1.00 36.34           O  
ANISOU 1311  O   HOH A2054     4694   4625   4488    -92    -36     15       O  
HETATM 1312  O   HOH A2055       9.638  17.470  42.587  1.00 43.00           O  
ANISOU 1312  O   HOH A2055     5384   5689   5262    141    -65    117       O  
HETATM 1313  O   HOH A2056      10.684  12.706  39.817  1.00 27.40           O  
ANISOU 1313  O   HOH A2056     3502   3263   3646    165     12    424       O  
HETATM 1314  O   HOH A2057       9.159  12.940  33.239  1.00 38.54           O  
ANISOU 1314  O   HOH A2057     4888   4838   4915   -145    -18    107       O  
HETATM 1315  O   HOH A2058       3.230  10.323  31.305  1.00 17.97           O  
ANISOU 1315  O   HOH A2058     2633   2159   2034   -150   -462     20       O  
HETATM 1316  O   HOH A2059       5.049   8.671  29.901  1.00 35.54           O  
ANISOU 1316  O   HOH A2059     4512   4317   4673     72     35    198       O  
HETATM 1317  O   HOH A2060       9.496   6.754  34.768  1.00 33.84           O  
ANISOU 1317  O   HOH A2060     4623   4125   4107    191    -94     42       O  
HETATM 1318  O   HOH A2061       3.095   8.372  40.964  1.00 13.06           O  
ANISOU 1318  O   HOH A2061     1601   1658   1703    -93   -584    428       O  
HETATM 1319  O   HOH A2062      -0.633   8.185  37.619  1.00 45.29           O  
ANISOU 1319  O   HOH A2062     5922   5897   5387     -9   -160    -13       O  
HETATM 1320  O   HOH A2063      -0.978  10.453  35.952  1.00 31.09           O  
ANISOU 1320  O   HOH A2063     3647   4487   3678   -108   -100     18       O  
HETATM 1321  O   HOH A2064       8.045  15.171  41.629  1.00 20.74           O  
ANISOU 1321  O   HOH A2064     2650   2607   2622    -22   -127    -33       O  
HETATM 1322  O   HOH A2065       2.309  16.068  42.694  1.00 18.35           O  
ANISOU 1322  O   HOH A2065     2594   2149   2228    -36    311    211       O  
HETATM 1323  O   HOH A2066       8.316  11.489  31.180  1.00 33.57           O  
ANISOU 1323  O   HOH A2066     3855   4289   4611    100    269   -136       O  
HETATM 1324  O   HOH A2067      -2.117  13.271  29.454  1.00 17.32           O  
ANISOU 1324  O   HOH A2067     1989   2332   2257   -330   -283     61       O  
HETATM 1325  O   HOH A2068      -1.572   8.993  29.328  1.00 38.15           O  
ANISOU 1325  O   HOH A2068     5115   4521   4858    -35     80     -8       O  
HETATM 1326  O   HOH A2069       1.193  22.000  31.602  1.00 14.93           O  
ANISOU 1326  O   HOH A2069     1506   1908   2258   -114     25    176       O  
HETATM 1327  O   HOH A2070      -4.235  11.585  30.026  1.00 25.77           O  
ANISOU 1327  O   HOH A2070     2976   3232   3583   -235   -423    203       O  
HETATM 1328  O   HOH A2071      -4.405  18.555  34.655  1.00 26.69           O  
ANISOU 1328  O   HOH A2071     2794   3541   3805     41    168    405       O  
HETATM 1329  O   HOH A2072      -3.446  14.902  27.526  1.00 19.24           O  
ANISOU 1329  O   HOH A2072     2083   2829   2398     25   -227    155       O  
HETATM 1330  O   HOH A2073      -2.643  25.260  30.234  1.00 28.73           O  
ANISOU 1330  O   HOH A2073     3441   3537   3935    -66   -274    -61       O  
HETATM 1331  O   HOH A2074      -6.001  23.343  31.639  1.00 33.20           O  
ANISOU 1331  O   HOH A2074     4164   4569   3881    104    199    228       O  
HETATM 1332  O   HOH A2075       3.029  22.661  29.433  1.00 10.55           O  
ANISOU 1332  O   HOH A2075     1002   1308   1695    -87     41    108       O  
HETATM 1333  O   HOH A2076      -6.427  20.244  22.875  1.00 23.58           O  
ANISOU 1333  O   HOH A2076     2518   3871   2568   -351     41    -52       O  
HETATM 1334  O   HOH A2077      -8.310  22.563  23.959  1.00 29.48           O  
ANISOU 1334  O   HOH A2077     3491   3627   4081     45    250    119       O  
HETATM 1335  O   HOH A2078      -8.204  25.371  30.528  1.00 35.98           O  
ANISOU 1335  O   HOH A2078     4518   4894   4258   -119    318    -26       O  
HETATM 1336  O   HOH A2079      -5.552  23.808  23.824  1.00 26.62           O  
ANISOU 1336  O   HOH A2079     3096   3813   3205   -274   -300    265       O  
HETATM 1337  O   HOH A2080       0.851  24.420  28.920  1.00 15.73           O  
ANISOU 1337  O   HOH A2080     1847   1954   2174     16   -394    155       O  
HETATM 1338  O   HOH A2081      -3.934  24.873  20.098  1.00 26.44           O  
ANISOU 1338  O   HOH A2081     2631   3555   3860    -65   -473   -215       O  
HETATM 1339  O   HOH A2082      -3.316  29.280  18.727  1.00 36.72           O  
ANISOU 1339  O   HOH A2082     4575   4724   4651     49    179    159       O  
HETATM 1340  O   HOH A2083      -0.529  32.505  24.743  1.00 33.13           O  
ANISOU 1340  O   HOH A2083     3820   4270   4496   -172   -111   -152       O  
HETATM 1341  O   HOH A2084      -3.989  16.192  22.663  1.00 35.94           O  
ANISOU 1341  O   HOH A2084     4524   4328   4802     34   -137   -116       O  
HETATM 1342  O   HOH A2085      -0.513  18.564  19.652  1.00 21.28           O  
ANISOU 1342  O   HOH A2085     2495   2257   3332   -242   -546    -53       O  
HETATM 1343  O   HOH A2086       0.997  19.287  16.262  1.00 17.59           O  
ANISOU 1343  O   HOH A2086     2278   2504   1901   -163   -690    -38       O  
HETATM 1344  O   HOH A2087      -7.442  26.329  17.846  1.00 34.38           O  
ANISOU 1344  O   HOH A2087     4045   4423   4593     61    113    -10       O  
HETATM 1345  O   HOH A2088      -5.285  28.360  16.662  1.00 37.26           O  
ANISOU 1345  O   HOH A2088     4612   4613   4931    -87    -40     38       O  
HETATM 1346  O   HOH A2089       2.819  20.760  14.617  1.00 29.42           O  
ANISOU 1346  O   HOH A2089     4359   3330   3488   -359   -222     35       O  
HETATM 1347  O   HOH A2090       6.849  14.255  14.392  1.00 27.42           O  
ANISOU 1347  O   HOH A2090     3541   3425   3450    -56   -174    -60       O  
HETATM 1348  O   HOH A2091       4.919  13.866  19.037  1.00 23.46           O  
ANISOU 1348  O   HOH A2091     2732   2838   3343   -217    426    236       O  
HETATM 1349  O   HOH A2092       2.537  15.623  14.044  1.00 26.98           O  
ANISOU 1349  O   HOH A2092     2746   3748   3755   -126    197   -120       O  
HETATM 1350  O   HOH A2093       7.333  15.087  17.967  1.00 16.18           O  
ANISOU 1350  O   HOH A2093     2230   1964   1950    -14   -117   -177       O  
HETATM 1351  O   HOH A2094      -0.462  11.450  25.683  1.00 26.99           O  
ANISOU 1351  O   HOH A2094     3625   3200   3429   -388     91   -237       O  
HETATM 1352  O   HOH A2095      -2.720  14.752  25.034  1.00 26.07           O  
ANISOU 1352  O   HOH A2095     3440   3487   2978   -252    -65     36       O  
HETATM 1353  O   HOH A2096       5.605  12.885  23.211  1.00 27.93           O  
ANISOU 1353  O   HOH A2096     3433   3658   3520     10     56    -52       O  
HETATM 1354  O   HOH A2097      12.166  34.031  29.125  1.00 15.62           O  
ANISOU 1354  O   HOH A2097     1929   1556   2449   -241   -575    -43       O  
HETATM 1355  O   HOH A2098      12.035  43.148  19.699  1.00 17.80           O  
ANISOU 1355  O   HOH A2098     2066   2456   2240   -396     11    147       O  
HETATM 1356  O   HOH A2099       7.956  43.037  17.896  1.00 22.47           O  
ANISOU 1356  O   HOH A2099     2759   2954   2823    437    681    311       O  
HETATM 1357  O   HOH A2100      11.689  35.303  11.230  1.00 11.00           O  
ANISOU 1357  O   HOH A2100     1621   1100   1458   -125     59      7       O  
HETATM 1358  O   HOH A2101      19.270  43.365  15.162  1.00 24.24           O  
ANISOU 1358  O   HOH A2101     3206   3294   2710   -305   -588     42       O  
HETATM 1359  O   HOH A2102      17.220  33.713  12.807  1.00 12.73           O  
ANISOU 1359  O   HOH A2102     1784   1506   1547    162     40   -143       O  
HETATM 1360  O   HOH A2103      13.672  37.817   5.673  1.00 23.73           O  
ANISOU 1360  O   HOH A2103     3358   2670   2985   -275    262    -46       O  
HETATM 1361  O   HOH A2104      19.630  30.590   6.677  1.00 35.44           O  
ANISOU 1361  O   HOH A2104     4642   4341   4479    130    249    -91       O  
HETATM 1362  O   HOH A2105      15.610  41.338   4.025  1.00 22.98           O  
ANISOU 1362  O   HOH A2105     3087   3464   2178   -137   -340   -209       O  
HETATM 1363  O   HOH A2106      13.585  41.065   6.499  1.00 18.62           O  
ANISOU 1363  O   HOH A2106     2204   3029   1841   -402     62   -565       O  
HETATM 1364  O   HOH A2107       4.828  40.040  10.835  1.00 20.85           O  
ANISOU 1364  O   HOH A2107     2516   2680   2726     81    -31    135       O  
HETATM 1365  O   HOH A2108       3.355  37.767  14.460  1.00 15.08           O  
ANISOU 1365  O   HOH A2108     1400   2061   2267    411     21    243       O  
HETATM 1366  O   HOH A2109       5.287  40.678  23.973  1.00 35.18           O  
ANISOU 1366  O   HOH A2109     4494   4516   4356    235    -66   -359       O  
HETATM 1367  O   HOH A2110       3.403  38.008  20.581  1.00 16.62           O  
ANISOU 1367  O   HOH A2110     1714   2034   2564    231     93    318       O  
HETATM 1368  O   HOH A2111       7.202  43.631  22.018  1.00 35.78           O  
ANISOU 1368  O   HOH A2111     4456   4630   4508     84    -15   -252       O  
HETATM 1369  O   HOH A2112       4.875  36.363   8.641  1.00 25.92           O  
ANISOU 1369  O   HOH A2112     3092   3387   3368   -195   -365     26       O  
HETATM 1370  O   HOH A2113       4.368  37.239  10.429  1.00 19.57           O  
ANISOU 1370  O   HOH A2113     1978   2193   3266    384     86    378       O  
HETATM 1371  O   HOH A2114       2.936  35.166  20.751  1.00 19.63           O  
ANISOU 1371  O   HOH A2114     2143   2490   2823    -92    -49    154       O  
HETATM 1372  O   HOH A2115       4.059  13.690  25.278  1.00 17.39           O  
ANISOU 1372  O   HOH A2115     2566   1887   2155    -69     14    -52       O  
HETATM 1373  O   HOH A2116      14.024  17.069  17.810  1.00 19.80           O  
ANISOU 1373  O   HOH A2116     2894   2541   2088    207    284   -427       O  
HETATM 1374  O   HOH A2117       2.199  37.290  12.004  1.00 16.89           O  
ANISOU 1374  O   HOH A2117     1896   2263   2256   -184   -267    425       O  
HETATM 1375  O   HOH A2118      -3.387  38.084   9.232  1.00 25.76           O  
ANISOU 1375  O   HOH A2118     3140   3259   3386    146   -146     36       O  
HETATM 1376  O   HOH A2119      -2.282  25.706  11.527  1.00 27.51           O  
ANISOU 1376  O   HOH A2119     2928   3875   3650   -104    -28    137       O  
HETATM 1377  O   HOH A2120       0.224  24.761  11.560  1.00 17.95           O  
ANISOU 1377  O   HOH A2120     1958   1901   2959   -587   -408   -210       O  
HETATM 1378  O   HOH A2121       2.210  32.630   8.223  1.00 41.68           O  
ANISOU 1378  O   HOH A2121     5468   5332   5035     98    -63     -1       O  
HETATM 1379  O   HOH A2122       2.918  29.349   6.641  1.00 48.51           O  
ANISOU 1379  O   HOH A2122     6124   6252   6056    -28     50     60       O  
HETATM 1380  O   HOH A2123      10.474  25.909   8.426  1.00 18.45           O  
ANISOU 1380  O   HOH A2123     2995   2317   1697    157    141    -57       O  
HETATM 1381  O   HOH A2124       7.920  28.670   6.849  1.00 36.50           O  
ANISOU 1381  O   HOH A2124     4429   4904   4532    178   -118      0       O  
HETATM 1382  O   HOH A2125       7.453  20.008  12.675  1.00 27.30           O  
ANISOU 1382  O   HOH A2125     3843   3176   3351    182   -280    167       O  
HETATM 1383  O   HOH A2126      10.716  20.044  11.558  1.00 31.35           O  
ANISOU 1383  O   HOH A2126     4076   3905   3928     -4     18   -106       O  
HETATM 1384  O   HOH A2127      11.827  24.331  10.208  1.00 15.37           O  
ANISOU 1384  O   HOH A2127     1892   2635   1310    166    389   -469       O  
HETATM 1385  O   HOH A2128      14.179  21.826  11.781  1.00 30.37           O  
ANISOU 1385  O   HOH A2128     3728   4033   3777    270    201   -460       O  
HETATM 1386  O   HOH A2129       9.030  17.323  14.784  1.00 21.59           O  
ANISOU 1386  O   HOH A2129     2901   2896   2404    124   -305   -185       O  
HETATM 1387  O   HOH A2130      13.073  21.159  17.213  1.00 11.02           O  
ANISOU 1387  O   HOH A2130     1923   1186   1076    160    142   -178       O  
HETATM 1388  O   HOH A2131      21.190  21.071  15.398  1.00 17.84           O  
ANISOU 1388  O   HOH A2131     1930   2639   2209    152    301   -290       O  
HETATM 1389  O   HOH A2132      17.067  16.382  14.914  1.00 25.57           O  
ANISOU 1389  O   HOH A2132     3160   3406   3149   -143     12   -307       O  
HETATM 1390  O   HOH A2133      19.574  14.874  15.896  1.00 26.88           O  
ANISOU 1390  O   HOH A2133     3466   3306   3438    164    -36   -404       O  
HETATM 1391  O   HOH A2134      14.518  18.879  16.153  1.00 21.05           O  
ANISOU 1391  O   HOH A2134     2432   2397   3167   -126   -326     60       O  
HETATM 1392  O   HOH A2135      23.012  17.711  13.049  1.00 33.68           O  
ANISOU 1392  O   HOH A2135     4188   4130   4477     -8    228    -59       O  
HETATM 1393  O   HOH A2136      22.854  14.083  18.385  1.00 21.50           O  
ANISOU 1393  O   HOH A2136     2483   3202   2480    157     13   -335       O  
HETATM 1394  O   HOH A2137      23.874  12.313  20.595  1.00 19.99           O  
ANISOU 1394  O   HOH A2137     2540   2173   2881     -4    330   -278       O  
HETATM 1395  O   HOH A2138      27.018  21.500  21.707  1.00 30.83           O  
ANISOU 1395  O   HOH A2138     3264   4343   4106   -245    124    150       O  
HETATM 1396  O   HOH A2139      28.732  12.034  23.339  1.00 31.81           O  
ANISOU 1396  O   HOH A2139     3953   3619   4515    379   -120   -182       O  
HETATM 1397  O   HOH A2140      29.127  17.634  22.621  1.00 27.59           O  
ANISOU 1397  O   HOH A2140     2626   3938   3918   -192   -115   -111       O  
HETATM 1398  O   HOH A2141      27.844  11.717  20.287  1.00 29.59           O  
ANISOU 1398  O   HOH A2141     3750   3402   4089    182   -146    -51       O  
HETATM 1399  O   HOH A2142      29.212  17.402  19.756  1.00 40.71           O  
ANISOU 1399  O   HOH A2142     5237   5142   5088     60     92    -45       O  
HETATM 1400  O   HOH A2143      24.410  14.689  16.422  1.00 29.65           O  
ANISOU 1400  O   HOH A2143     3897   3796   3569    -66     -8     29       O  
HETATM 1401  O   HOH A2144      28.314  23.002  18.629  1.00 27.24           O  
ANISOU 1401  O   HOH A2144     2639   3721   3989   -235    -52      0       O  
HETATM 1402  O   HOH A2145      25.379  17.848  14.124  1.00 37.29           O  
ANISOU 1402  O   HOH A2145     4841   4583   4742     28     19    120       O  
HETATM 1403  O   HOH A2146      25.937  24.244  15.933  1.00 26.56           O  
ANISOU 1403  O   HOH A2146     2692   3550   3848    409     48    333       O  
HETATM 1404  O   HOH A2147      28.746  29.006  18.503  1.00 47.27           O  
ANISOU 1404  O   HOH A2147     5871   6132   5956     81   -101    -74       O  
HETATM 1405  O   HOH A2148      27.924  35.470  25.470  1.00 41.06           O  
ANISOU 1405  O   HOH A2148     4974   5386   5241    -85     11   -116       O  
HETATM 1406  O   HOH A2149      25.747  32.786  26.855  1.00 27.50           O  
ANISOU 1406  O   HOH A2149     3536   3348   3561     73   -543     71       O  
HETATM 1407  O   HOH A2150      19.786  43.813  27.213  1.00 18.78           O  
ANISOU 1407  O   HOH A2150     2356   2078   2700   -167    -97   -252       O  
HETATM 1408  O   HOH A2151      16.968  42.751  21.367  1.00 21.84           O  
ANISOU 1408  O   HOH A2151     3008   2753   2537    164    120    -83       O  
HETATM 1409  O   HOH A2152      17.348  47.470  25.931  1.00 22.62           O  
ANISOU 1409  O   HOH A2152     2983   2749   2860   -227    283    136       O  
HETATM 1410  O   HOH A2153      19.282  42.538  19.174  1.00 26.54           O  
ANISOU 1410  O   HOH A2153     4035   3358   2687   -318    207    237       O  
HETATM 1411  O   HOH A2154      28.227  29.236  15.562  1.00 35.43           O  
ANISOU 1411  O   HOH A2154     4027   4751   4682     87     85    -26       O  
HETATM 1412  O   HOH A2155      21.505  23.328  10.948  1.00 24.62           O  
ANISOU 1412  O   HOH A2155     3283   3293   2777   -171     22     -7       O  
HETATM 1413  O   HOH A2156      27.059  26.640  15.042  1.00 31.44           O  
ANISOU 1413  O   HOH A2156     3579   4553   3814   -143    292    139       O  
HETATM 1414  O   HOH A2157      25.533  28.090  13.070  1.00 32.95           O  
ANISOU 1414  O   HOH A2157     3721   4355   4441    294    109    -50       O  
HETATM 1415  O   HOH A2158      27.121  24.992   7.267  1.00 41.44           O  
ANISOU 1415  O   HOH A2158     5143   5324   5276    -40     53   -155       O  
HETATM 1416  O   HOH A2159      19.016  32.652  11.017  1.00 21.23           O  
ANISOU 1416  O   HOH A2159     2530   2860   2673    475    479    287       O  
HETATM 1417  O   HOH A2160      16.943  26.616   7.648  1.00 23.68           O  
ANISOU 1417  O   HOH A2160     2389   3838   2767    302     54      0       O  
HETATM 1418  O   HOH A2161      23.303  31.511  10.319  1.00 25.75           O  
ANISOU 1418  O   HOH A2161     3779   3083   2921    103    409    387       O  
HETATM 1419  O   HOH A2162      22.113  34.925  13.111  1.00 35.09           O  
ANISOU 1419  O   HOH A2162     4828   4232   4272   -108    181    156       O  
HETATM 1420  O   HOH A2163      17.845  24.914   9.819  1.00 21.75           O  
ANISOU 1420  O   HOH A2163     2814   2732   2716    242    174   -111       O  
HETATM 1421  O   HOH A2164      14.047  26.452  10.710  1.00 17.01           O  
ANISOU 1421  O   HOH A2164     2315   2126   2019    244    235   -169       O  
HETATM 1422  O   HOH A2165      10.897  35.716  27.695  1.00 18.75           O  
ANISOU 1422  O   HOH A2165     3342   2090   1693    159   -228   -169       O  
HETATM 1423  O   HOH A2166       9.321  38.621  24.387  1.00 17.91           O  
ANISOU 1423  O   HOH A2166     2468   2042   2294    337   -404   -341       O  
HETATM 1424  O   HOH A2167      14.013  43.201  21.698  1.00 23.17           O  
ANISOU 1424  O   HOH A2167     2559   3306   2936   -155   -360   -231       O  
HETATM 1425  O   HOH A2168      12.406  45.998  25.486  1.00 23.51           O  
ANISOU 1425  O   HOH A2168     3056   2997   2881    216     78    -43       O  
HETATM 1426  O   HOH A2169       8.139  42.733  26.349  1.00 28.94           O  
ANISOU 1426  O   HOH A2169     3830   3510   3654    443   -166   -222       O  
HETATM 1427  O   HOH A2170       9.772  39.794  33.007  1.00 23.86           O  
ANISOU 1427  O   HOH A2170     3252   2747   3064    127    119   -529       O  
HETATM 1428  O   HOH A2171      12.122  38.209  34.880  1.00 19.06           O  
ANISOU 1428  O   HOH A2171     2961   2190   2090   -415   -367     49       O  
HETATM 1429  O   HOH A2172      15.335  37.670  33.839  1.00 17.05           O  
ANISOU 1429  O   HOH A2172     2477   1949   2050    102   -418   -356       O  
HETATM 1430  O   HOH A2173      24.469  38.333  28.183  1.00 30.69           O  
ANISOU 1430  O   HOH A2173     3721   4048   3890   -106    -47    -99       O  
HETATM 1431  O   HOH A2174      22.906  39.868  29.976  1.00 19.51           O  
ANISOU 1431  O   HOH A2174     2511   2376   2523   -514    -11      1       O  
HETATM 1432  O   HOH A2175      16.218  31.624  34.587  1.00 30.87           O  
ANISOU 1432  O   HOH A2175     3837   4190   3700     42    -67    117       O  
HETATM 1433  O   HOH A2176      15.307  29.650  32.695  1.00 14.95           O  
ANISOU 1433  O   HOH A2176     2095   1890   1692      3   -168    166       O  
HETATM 1434  O   HOH A2177       9.827  34.891  25.347  1.00 11.59           O  
ANISOU 1434  O   HOH A2177     1061   1908   1431    508   -117    -42       O  
HETATM 1435  O   HOH A2178      21.042  25.855  32.527  1.00 21.73           O  
ANISOU 1435  O   HOH A2178     2495   2875   2884    251   -384    155       O  
HETATM 1436  O   HOH A2179      13.021  26.730  34.914  1.00 27.06           O  
ANISOU 1436  O   HOH A2179     3708   3332   3242    175    141    -45       O  
HETATM 1437  O   HOH A2180      25.569  22.644  30.410  1.00 28.61           O  
ANISOU 1437  O   HOH A2180     3113   3959   3798    -10    185     49       O  
HETATM 1438  O   HOH A2181      24.842  23.289  24.184  1.00 24.87           O  
ANISOU 1438  O   HOH A2181     3208   2549   3690   -196   -191    283       O  
HETATM 1439  O   HOH A2182      25.277  27.361  26.300  1.00 32.88           O  
ANISOU 1439  O   HOH A2182     3823   4339   4331   -269    -93    140       O  
HETATM 1440  O   HOH A2183      20.049  19.635  33.029  1.00 26.02           O  
ANISOU 1440  O   HOH A2183     3614   3142   3129    109      0   -188       O  
HETATM 1441  O   HOH A2184      17.098  26.278  33.631  1.00 40.46           O  
ANISOU 1441  O   HOH A2184     5141   5027   5202   -165    126   -160       O  
HETATM 1442  O   HOH A2185      14.214  22.403  36.139  1.00 14.87           O  
ANISOU 1442  O   HOH A2185     1931   1614   2105    218    113   -116       O  
HETATM 1443  O   HOH A2186      17.501  19.543  34.888  1.00 31.41           O  
ANISOU 1443  O   HOH A2186     4291   3651   3992    302     88    173       O  
HETATM 1444  O   HOH A2187      19.786  12.943  31.494  1.00 28.77           O  
ANISOU 1444  O   HOH A2187     4429   3246   3255   -101    164    -74       O  
HETATM 1445  O   HOH A2188      18.223  12.202  27.365  1.00 11.07           O  
ANISOU 1445  O   HOH A2188     1513   1383   1310    194   -349   -181       O  
HETATM 1446  O   HOH A2189      -0.640  27.255  35.930  1.00 36.43           O  
ANISOU 1446  O   HOH A2189     4888   4315   4636     93     98   -187       O  
HETATM 1447  O   HOH A2190       1.166  26.691  31.959  1.00 28.85           O  
ANISOU 1447  O   HOH A2190     3768   3503   3688   -333    -57    177       O  
HETATM 1448  O   HOH A2191       6.642  40.606  29.549  1.00 32.14           O  
ANISOU 1448  O   HOH A2191     4165   3785   4258    153    -86     88       O  
HETATM 1449  O   HOH A2192      15.859  13.757  20.716  1.00 15.87           O  
ANISOU 1449  O   HOH A2192     2151   1969   1908    166    300     40       O  
HETATM 1450  O   HOH A2193      22.392  10.920  22.458  1.00 15.64           O  
ANISOU 1450  O   HOH A2193     1332   2331   2279     59     77  -1149       O  
HETATM 1451  O   HOH A2194       7.165  38.104  26.872  1.00 28.80           O  
ANISOU 1451  O   HOH A2194     3653   3746   3544   -206    157     69       O  
HETATM 1452  O   HOH A2195      18.577  15.129  19.301  1.00 17.32           O  
ANISOU 1452  O   HOH A2195     2121   1911   2546   -159     41    219       O  
HETATM 1453  O   HOH A2196      25.332  12.053  24.336  1.00 27.21           O  
ANISOU 1453  O   HOH A2196     2966   3664   3707    164      2   -202       O  
HETATM 1454  O   HOH A2197      27.238  20.614  30.955  1.00 25.72           O  
ANISOU 1454  O   HOH A2197     3031   3153   3587   -374     46     -7       O  
HETATM 1455  O   HOH A2198      29.322  15.376  27.224  1.00 24.42           O  
ANISOU 1455  O   HOH A2198     2548   3331   3400   -273    142    -12       O  
HETATM 1456  O   HOH A2199      25.411  17.327  32.477  1.00 35.46           O  
ANISOU 1456  O   HOH A2199     4740   4364   4368    186     72    101       O  
HETATM 1457  O   HOH A2200       2.139  12.005  29.440  1.00 23.37           O  
ANISOU 1457  O   HOH A2200     2918   2848   3112    -13   -299    -88       O  
HETATM 1458  O   HOH A2201      21.858  14.842  32.309  1.00 35.69           O  
ANISOU 1458  O   HOH A2201     4527   5017   4016    131    -84    -40       O  
HETATM 1459  O   HOH A2202      -0.402  11.416  28.491  1.00 20.32           O  
ANISOU 1459  O   HOH A2202     2700   2469   2550   -252     45    238       O  
HETATM 1460  O   HOH A2203      21.732  39.757  11.695  1.00 47.67           O  
ANISOU 1460  O   HOH A2203     5936   6130   6045     99      3    -37       O  
HETATM 1461  O   HOH A2204      19.319  35.664   5.534  1.00 39.74           O  
ANISOU 1461  O   HOH A2204     5110   4905   5084     48    234    -74       O  
HETATM 1462  O   HOH A2205      12.315  38.068   8.815  1.00 11.83           O  
ANISOU 1462  O   HOH A2205     1676   1222   1595    129    108    -98       O  
HETATM 1463  O   HOH A2206      11.269  39.938   7.099  1.00 13.59           O  
ANISOU 1463  O   HOH A2206     1753   1665   1745    -93    223    -30       O  
HETATM 1464  O   HOH A2207       7.462  34.282   6.568  1.00 19.53           O  
ANISOU 1464  O   HOH A2207     2993   2416   2009    190   -331    312       O  
HETATM 1465  O   HOH A2208      12.357  27.300   7.295  1.00 23.31           O  
ANISOU 1465  O   HOH A2208     3390   2402   3064   -101    166   -197       O  
HETATM 1466  O   HOH A2209       8.791  34.522   2.832  1.00 30.95           O  
ANISOU 1466  O   HOH A2209     4091   3538   4129   -395   -257   -249       O  
HETATM 1467  O   HOH A2210      15.600  36.473   4.561  1.00 30.18           O  
ANISOU 1467  O   HOH A2210     4302   4058   3105     66    298     22       O  
HETATM 1468  O   HOH A2211       5.975  37.078   5.787  1.00 31.83           O  
ANISOU 1468  O   HOH A2211     4171   3595   4327   -134   -111     -7       O  
HETATM 1469  O   HOH A2212      10.818  29.704   5.106  1.00 36.04           O  
ANISOU 1469  O   HOH A2212     4638   4483   4572   -192   -375    -26       O  
HETATM 1470  O   HOH A2213      -0.388  24.405  31.498  1.00 20.28           O  
ANISOU 1470  O   HOH A2213     2821   2472   2413    294    169    130       O  
HETATM 1471  O   HOH A2214      -4.385  18.955  37.274  1.00 35.85           O  
ANISOU 1471  O   HOH A2214     4239   4642   4739    -90    -95   -105       O  
HETATM 1472  O   HOH A2215      -3.509  32.006  20.546  1.00 39.31           O  
ANISOU 1472  O   HOH A2215     4823   4999   5113     45     43    180       O  
HETATM 1473  O   HOH A2216       0.272  16.846  14.883  1.00 38.04           O  
ANISOU 1473  O   HOH A2216     4719   4883   4850    108     70   -167       O  
HETATM 1474  O   HOH A2217       0.690  22.444  13.250  1.00 26.52           O  
ANISOU 1474  O   HOH A2217     3535   2785   3754   -297     29    220       O  
CONECT 1222 1223 1224                                                           
CONECT 1223 1222                                                                
CONECT 1224 1222 1225 1226                                                      
CONECT 1225 1224                                                                
CONECT 1226 1224 1227                                                           
CONECT 1227 1226                                                                
CONECT 1230 1231 1232 1240                                                      
CONECT 1231 1230 1242                                                           
CONECT 1232 1230 1233 1234                                                      
CONECT 1233 1232                                                                
CONECT 1234 1232 1235 1236                                                      
CONECT 1235 1234 1246                                                           
CONECT 1236 1234 1237 1238                                                      
CONECT 1237 1236 1250                                                           
CONECT 1238 1236 1239 1240                                                      
CONECT 1239 1238 1254                                                           
CONECT 1240 1230 1238 1241                                                      
CONECT 1241 1240                                                                
CONECT 1242 1231 1243 1244 1245                                                 
CONECT 1243 1242                                                                
CONECT 1244 1242                                                                
CONECT 1245 1242                                                                
CONECT 1246 1235 1247 1248 1249                                                 
CONECT 1247 1246                                                                
CONECT 1248 1246                                                                
CONECT 1249 1246                                                                
CONECT 1250 1237 1251 1252 1253                                                 
CONECT 1251 1250                                                                
CONECT 1252 1250                                                                
CONECT 1253 1250                                                                
CONECT 1254 1239 1255 1256 1257                                                 
CONECT 1255 1254                                                                
CONECT 1256 1254                                                                
CONECT 1257 1254                                                                
MASTER      369    0    3    4   12    0    8    6 1473    1   34   12          
END                                                                             



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