CNRS Nantes University UFIP UFIP
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***  1w1g  ***

elNémo ID: 1901302327388388

Job options:

ID        	=	 1901302327388388
JOBID     	=	 1w1g
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 1w1g

HEADER    TRANSFERASE                             21-JUN-04   1W1G              
TITLE     CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN HOMOLOGY (PH)                
TITLE    2 DOMAIN BOUND TO DIC4-PHOSPHATIDYLINOSITOL (3,4,5)-                   
TITLE    3 TRISPHOSPHATE                                                        
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, PIP3 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 1W1G    1       VERSN                                    
REVDAT   1   19-NOV-04 1W1G    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   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 25241                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 545                             
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1834                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 44                           
REMARK   3   BIN FREE R VALUE                    : 0.3080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1206                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 163                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.58000                                              
REMARK   3    B22 (A**2) : -0.83000                                             
REMARK   3    B33 (A**2) : -0.73000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.089         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.081         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.471         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.972                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1273 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1115 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1731 ; 1.703 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2588 ; 0.860 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   142 ; 6.622 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    67 ;34.693 ;23.731       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   219 ;13.710 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;17.708 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   184 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1363 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   263 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   267 ; 0.221 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1116 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   613 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   672 ; 0.107 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   117 ; 0.159 ; 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):     8 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    39 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    17 ; 0.274 ; 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):   746 ; 1.727 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   287 ; 0.745 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1168 ; 2.305 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   612 ; 3.614 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   563 ; 4.923 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   414        A   466                          
REMARK   3    RESIDUE RANGE :   A   472        A   487                          
REMARK   3    RESIDUE RANGE :   A   494        A   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.5388  27.1746  24.0723              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0377 T22:   0.0133                                     
REMARK   3      T33:  -0.0088 T12:  -0.0001                                     
REMARK   3      T13:  -0.0004 T23:  -0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1679 L22:   1.4071                                     
REMARK   3      L33:   0.4956 L12:   0.1263                                     
REMARK   3      L13:  -0.1429 L23:  -0.5604                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0012 S12:  -0.0141 S13:   0.0265                       
REMARK   3      S21:  -0.0763 S22:   0.0301 S23:  -0.0092                       
REMARK   3      S31:   0.0443 S32:  -0.0069 S33:  -0.0288                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   408        A   413                          
REMARK   3    RESIDUE RANGE :   A   466        A   471                          
REMARK   3    RESIDUE RANGE :   A   544        A   549                          
REMARK   3    RESIDUE RANGE :   A   488        A   493                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5684  26.7739  22.8190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0232 T22:  -0.0096                                     
REMARK   3      T33:  -0.0304 T12:  -0.0101                                     
REMARK   3      T13:  -0.0146 T23:  -0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4742 L22:   1.4621                                     
REMARK   3      L33:   0.4845 L12:   0.2713                                     
REMARK   3      L13:  -0.2195 L23:  -0.8330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0278 S12:   0.0203 S13:   0.0334                       
REMARK   3      S21:  -0.0906 S22:   0.0671 S23:   0.0777                       
REMARK   3      S31:   0.0498 S32:   0.0051 S33:  -0.0950                       
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   : 1.20                                          
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. THE ACYL-CHAINS OF THE LIGAND WERE      
REMARK   3  NOT MODELLED DUE TO DISORDER.                                       
REMARK   4                                                                      
REMARK   4 1W1G 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-20199.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-SEP-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE (RAXIS 4)              
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25810                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDK1PH INSP4 MODEL                                   
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: 25 % PEG 4000, 0.1 M SODIUM              
REMARK 280  ACETATE [PH 4.2], 0.3 M AMMONIUM ACETATE                            
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       29.47150            
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     GLU A 503    CG   CD   OE1  OE2                                  
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   NE2  GLN A   429  -  O    HOH A  2041              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 464   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 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       64.84     39.46                                   
REMARK 500    PHE A 470     -137.16   -121.79                                   
REMARK 500    ASN A 510     -154.91   -160.56                                   
REMARK 500    GLN A 548     -163.18   -119.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     4PT A 1550                                                       
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 4PT 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: 1W1D   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN                            
REMARK 900  HOMOLOGY (PH) DOMAIN BOUND TO INOSITOL (1,                          
REMARK 900  3,4,5)-TETRAKISPHOSPHATE                                            
REMARK 900 RELATED ID: 1W1H   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN                            
REMARK 900  HOMOLOGY (PH) DOMAIN                                                
DBREF  1W1G A  406   408  PDB    1W1G     1W1G           406    408             
DBREF  1W1G 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    4PT  A1550      33                                                       
HETNAM     4PT (2R)-3-{[(S)-{[(2S,3R,5S,6S)-2,6-DIHYDROXY-3,                    
HETNAM   2 4PT  4,5-TRIS(PHOSPHONOOXY)CYCLOHEXYL]OXY}                           
HETNAM   3 4PT  (HYDROXY)PHOSPHORYL]OXY}-2-(1-HYDROXYBUTOXY)PROPYL              
HETNAM   4 4PT  BUTYRATE                                                        
HETSYN     4PT DIC4-PHOSPHATIDYLINOSITOL(3,4,5)TRISPHOSPHATE                    
FORMUL   2  4PT    C17 H36 O22 P4                                               
FORMUL   3  HOH   *163(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  ALA A 508 -1  O  ARG A 505   N  HIS A 517           
CISPEP   1 GLY A  481    PRO A  482          0        -0.22                     
SITE     1 AC1 14 HIS A 417  LEU A 419  LYS A 465  LYS A 467                    
SITE     2 AC1 14 ARG A 472  ARG A 474  TYR A 486  LYS A 495                    
SITE     3 AC1 14 ARG A 521  HOH A2029  HOH A2084  HOH A2155                    
SITE     4 AC1 14 HOH A2156  HOH A2157                                          
CRYST1   35.264   58.943   36.440  90.00 102.33  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      0.028357  0.000000  0.006201        0.00000                         
SCALE2      0.000000  0.016966  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.028091        0.00000                         
ATOM      1  N   PRO A 407      -5.585  14.795  41.241  1.00 46.76           N  
ANISOU    1  N   PRO A 407     5916   5940   5910    -15      1     22       N  
ATOM      2  CA  PRO A 407      -5.941  14.176  42.515  1.00 46.02           C  
ANISOU    2  CA  PRO A 407     5807   5856   5820     -9     49     13       C  
ATOM      3  C   PRO A 407      -5.911  15.194  43.626  1.00 45.07           C  
ANISOU    3  C   PRO A 407     5668   5726   5729    -17     77     27       C  
ATOM      4  O   PRO A 407      -5.131  16.145  43.569  1.00 44.14           O  
ANISOU    4  O   PRO A 407     5402   5684   5684   -168    310    136       O  
ATOM      5  CB  PRO A 407      -4.819  13.143  42.739  1.00 46.04           C  
ANISOU    5  CB  PRO A 407     5844   5824   5823    -11      0     12       C  
ATOM      6  CG  PRO A 407      -4.369  12.781  41.370  1.00 46.84           C  
ANISOU    6  CG  PRO A 407     5862   5961   5970     20     40     38       C  
ATOM      7  CD  PRO A 407      -4.511  14.054  40.557  1.00 46.93           C  
ANISOU    7  CD  PRO A 407     5949   5950   5930      7     40     21       C  
ATOM      8  N   LEU A 408      -6.736  14.990  44.643  1.00 43.14           N  
ANISOU    8  N   LEU A 408     5411   5518   5460    -50    111     54       N  
ATOM      9  CA  LEU A 408      -6.689  15.845  45.811  1.00 42.23           C  
ANISOU    9  CA  LEU A 408     5311   5382   5351    -20     60     31       C  
ATOM     10  C   LEU A 408      -5.245  16.016  46.285  1.00 40.70           C  
ANISOU   10  C   LEU A 408     5069   5220   5172    -15    109     29       C  
ATOM     11  O   LEU A 408      -4.516  15.034  46.476  1.00 39.79           O  
ANISOU   11  O   LEU A 408     4846   5147   5124    -11    114    107       O  
ATOM     12  CB  LEU A 408      -7.559  15.272  46.936  1.00 42.28           C  
ANISOU   12  CB  LEU A 408     5330   5424   5310    -31    107     57       C  
ATOM     13  N   GLY A 409      -4.837  17.273  46.438  1.00 39.70           N  
ANISOU   13  N   GLY A 409     4938   5100   5046     16     97     31       N  
ATOM     14  CA  GLY A 409      -3.498  17.614  46.916  1.00 38.85           C  
ANISOU   14  CA  GLY A 409     4846   4962   4952      6     73    -22       C  
ATOM     15  C   GLY A 409      -2.382  17.532  45.882  1.00 38.37           C  
ANISOU   15  C   GLY A 409     4758   4902   4916     32     82    -61       C  
ATOM     16  O   GLY A 409      -1.204  17.730  46.251  1.00 38.58           O  
ANISOU   16  O   GLY A 409     4654   4963   5040    127    136   -219       O  
ATOM     17  N   SER A 410      -2.712  17.282  44.608  1.00 36.48           N  
ANISOU   17  N   SER A 410     4541   4642   4676     28     32     -1       N  
ATOM     18  CA  SER A 410      -1.663  17.097  43.575  1.00 35.55           C  
ANISOU   18  CA  SER A 410     4440   4445   4622     25     38     77       C  
ATOM     19  C   SER A 410      -1.068  18.439  43.117  1.00 36.36           C  
ANISOU   19  C   SER A 410     4507   4550   4756    -19     87     26       C  
ATOM     20  O   SER A 410       0.146  18.541  42.875  1.00 34.75           O  
ANISOU   20  O   SER A 410     4224   4289   4689    -17    169    -45       O  
ATOM     21  CB  SER A 410      -2.196  16.319  42.384  1.00 35.59           C  
ANISOU   21  CB  SER A 410     4424   4517   4579     39     95     96       C  
ATOM     22  OG  SER A 410      -3.326  16.955  41.791  1.00 34.36           O  
ANISOU   22  OG  SER A 410     4036   4220   4797    140   -114    274       O  
ATOM     23  N   ASN A 411      -1.925  19.462  43.038  1.00 36.28           N  
ANISOU   23  N   ASN A 411     4493   4527   4764    -42     67     91       N  
ATOM     24  CA  ASN A 411      -1.504  20.840  42.698  1.00 37.14           C  
ANISOU   24  CA  ASN A 411     4669   4656   4784    -28     58     23       C  
ATOM     25  C   ASN A 411      -0.434  20.885  41.609  1.00 36.56           C  
ANISOU   25  C   ASN A 411     4592   4589   4710    -65     77     64       C  
ATOM     26  O   ASN A 411       0.712  21.322  41.820  1.00 36.84           O  
ANISOU   26  O   ASN A 411     4438   4770   4787    -62    353    133       O  
ATOM     27  CB  ASN A 411      -1.010  21.583  43.929  1.00 37.92           C  
ANISOU   27  CB  ASN A 411     4768   4759   4878    -97     19     40       C  
ATOM     28  CG  ASN A 411      -0.671  23.073  43.634  1.00 39.77           C  
ANISOU   28  CG  ASN A 411     5003   5099   5007    -43   -100     48       C  
ATOM     29  OD1 ASN A 411       0.292  23.615  44.176  1.00 39.77           O  
ANISOU   29  OD1 ASN A 411     4712   5512   4884   -514     38    114       O  
ATOM     30  ND2 ASN A 411      -1.461  23.721  42.763  1.00 41.01           N  
ANISOU   30  ND2 ASN A 411     5244   5148   5191   -196    -30    212       N  
ATOM     31  N   ILE A 412      -0.825  20.443  40.432  1.00 35.57           N  
ANISOU   31  N   ILE A 412     4494   4420   4598    -82     72    102       N  
ATOM     32  CA  ILE A 412       0.098  20.338  39.329  1.00 35.24           C  
ANISOU   32  CA  ILE A 412     4502   4347   4540     45     29    -35       C  
ATOM     33  C   ILE A 412       0.665  21.695  38.921  1.00 34.39           C  
ANISOU   33  C   ILE A 412     4370   4220   4473     46    134    -26       C  
ATOM     34  O   ILE A 412       1.764  21.793  38.376  1.00 33.60           O  
ANISOU   34  O   ILE A 412     4341   3968   4458     23    306   -203       O  
ATOM     35  CB  ILE A 412      -0.602  19.622  38.167  1.00 36.28           C  
ANISOU   35  CB  ILE A 412     4634   4430   4719    -52    -40     42       C  
ATOM     36  CG1 ILE A 412       0.421  18.869  37.360  1.00 35.21           C  
ANISOU   36  CG1 ILE A 412     4277   4621   4478    -12     -5    -73       C  
ATOM     37  CG2 ILE A 412      -1.477  20.547  37.331  1.00 37.69           C  
ANISOU   37  CG2 ILE A 412     4714   4693   4911    -52   -141     63       C  
ATOM     38  CD1 ILE A 412       0.975  17.641  38.087  1.00 36.92           C  
ANISOU   38  CD1 ILE A 412     4767   4632   4626   -216    186     56       C  
ATOM     39  N   GLU A 413      -0.077  22.761  39.230  1.00 34.20           N  
ANISOU   39  N   GLU A 413     4360   4191   4442     65    215    -53       N  
ATOM     40  CA  GLU A 413       0.362  24.117  38.895  1.00 33.52           C  
ANISOU   40  CA  GLU A 413     4289   4110   4336    144    176    -63       C  
ATOM     41  C   GLU A 413       1.685  24.508  39.584  1.00 32.13           C  
ANISOU   41  C   GLU A 413     4147   3932   4129    165    260   -117       C  
ATOM     42  O   GLU A 413       2.322  25.517  39.205  1.00 32.37           O  
ANISOU   42  O   GLU A 413     4035   4011   4250    344    514    -26       O  
ATOM     43  CB  GLU A 413      -0.749  25.116  39.242  1.00 33.87           C  
ANISOU   43  CB  GLU A 413     4329   4100   4440    140    167    -13       C  
ATOM     44  CG  GLU A 413      -1.911  25.079  38.260  1.00 36.70           C  
ANISOU   44  CG  GLU A 413     4730   4542   4672     59     19   -167       C  
ATOM     45  CD  GLU A 413      -2.889  23.933  38.474  1.00 40.93           C  
ANISOU   45  CD  GLU A 413     5457   5118   4977     62     -3   -180       C  
ATOM     46  OE1 GLU A 413      -2.911  23.389  39.604  1.00 43.29           O  
ANISOU   46  OE1 GLU A 413     5972   5593   4883   -210    281   -635       O  
ATOM     47  OE2 GLU A 413      -3.639  23.570  37.501  1.00 43.48           O  
ANISOU   47  OE2 GLU A 413     5854   5271   5396     -2   -224   -391       O  
ATOM     48  N   GLN A 414       2.115  23.729  40.591  1.00 30.78           N  
ANISOU   48  N   GLN A 414     4101   3722   3869    181    334   -107       N  
ATOM     49  CA  GLN A 414       3.398  23.984  41.248  1.00 29.96           C  
ANISOU   49  CA  GLN A 414     4014   3658   3710     33    173   -113       C  
ATOM     50  C   GLN A 414       4.591  23.997  40.286  1.00 29.31           C  
ANISOU   50  C   GLN A 414     3897   3605   3632    -16    147   -100       C  
ATOM     51  O   GLN A 414       5.596  24.664  40.539  1.00 29.98           O  
ANISOU   51  O   GLN A 414     4443   3478   3470   -273    255   -291       O  
ATOM     52  CB  GLN A 414       3.684  22.964  42.342  1.00 31.73           C  
ANISOU   52  CB  GLN A 414     4168   3945   3941     12    157   -181       C  
ATOM     53  CG  GLN A 414       3.910  21.535  41.842  1.00 31.69           C  
ANISOU   53  CG  GLN A 414     4338   3642   4060   -101    123     89       C  
ATOM     54  CD  GLN A 414       4.000  20.535  42.958  1.00 30.68           C  
ANISOU   54  CD  GLN A 414     4129   3803   3724    -44     57    -82       C  
ATOM     55  OE1 GLN A 414       5.061  20.397  43.600  1.00 33.86           O  
ANISOU   55  OE1 GLN A 414     4870   4243   3752   -557    163   -195       O  
ATOM     56  NE2 GLN A 414       2.907  19.807  43.187  1.00 29.65           N  
ANISOU   56  NE2 GLN A 414     4591   2956   3718   -475    295    139       N  
ATOM     57  N   TYR A 415       4.500  23.223  39.213  1.00 28.07           N  
ANISOU   57  N   TYR A 415     3747   3423   3493    -31    141   -162       N  
ATOM     58  CA  TYR A 415       5.593  23.128  38.235  1.00 28.15           C  
ANISOU   58  CA  TYR A 415     3774   3478   3442      0    106      7       C  
ATOM     59  C   TYR A 415       5.561  24.256  37.185  1.00 28.58           C  
ANISOU   59  C   TYR A 415     3832   3490   3535    -29    143     35       C  
ATOM     60  O   TYR A 415       6.467  24.350  36.392  1.00 28.52           O  
ANISOU   60  O   TYR A 415     4037   3451   3346     83    405    -13       O  
ATOM     61  CB  TYR A 415       5.584  21.755  37.546  1.00 26.93           C  
ANISOU   61  CB  TYR A 415     3596   3382   3254    -74     49    -72       C  
ATOM     62  CG  TYR A 415       5.605  20.627  38.569  1.00 24.95           C  
ANISOU   62  CG  TYR A 415     3345   2924   3211    -94     77   -118       C  
ATOM     63  CD1 TYR A 415       6.736  20.403  39.342  1.00 28.23           C  
ANISOU   63  CD1 TYR A 415     4059   3448   3217   -136    -69     42       C  
ATOM     64  CD2 TYR A 415       4.473  19.831  38.801  1.00 26.13           C  
ANISOU   64  CD2 TYR A 415     3290   3629   3007    110    -84   -206       C  
ATOM     65  CE1 TYR A 415       6.772  19.376  40.334  1.00 28.43           C  
ANISOU   65  CE1 TYR A 415     3699   3593   3509    101   -486    147       C  
ATOM     66  CE2 TYR A 415       4.489  18.824  39.798  1.00 26.21           C  
ANISOU   66  CE2 TYR A 415     3297   3428   3231   -196   -280   -136       C  
ATOM     67  CZ  TYR A 415       5.655  18.591  40.556  1.00 28.15           C  
ANISOU   67  CZ  TYR A 415     3747   3532   3416     44   -132   -240       C  
ATOM     68  OH  TYR A 415       5.649  17.587  41.527  1.00 29.04           O  
ANISOU   68  OH  TYR A 415     3725   3704   3603    -78   -130   -119       O  
ATOM     69  N   ILE A 416       4.504  25.066  37.177  1.00 28.54           N  
ANISOU   69  N   ILE A 416     3862   3440   3541     45    166    -25       N  
ATOM     70  CA  ILE A 416       4.264  26.030  36.096  1.00 29.21           C  
ANISOU   70  CA  ILE A 416     3824   3640   3634     49    105    -64       C  
ATOM     71  C   ILE A 416       4.602  27.435  36.613  1.00 29.56           C  
ANISOU   71  C   ILE A 416     4005   3634   3591     21    135    -33       C  
ATOM     72  O   ILE A 416       4.096  27.835  37.663  1.00 29.65           O  
ANISOU   72  O   ILE A 416     4168   3596   3501    149    477   -241       O  
ATOM     73  CB  ILE A 416       2.790  26.009  35.626  1.00 29.39           C  
ANISOU   73  CB  ILE A 416     3813   3758   3596     50    193    -75       C  
ATOM     74  CG1 ILE A 416       2.378  24.611  35.179  1.00 30.33           C  
ANISOU   74  CG1 ILE A 416     3673   3942   3907    -26     36     54       C  
ATOM     75  CG2 ILE A 416       2.595  26.970  34.469  1.00 30.39           C  
ANISOU   75  CG2 ILE A 416     3563   3789   4193    232    -17    -53       C  
ATOM     76  CD1 ILE A 416       0.913  24.429  34.873  1.00 29.31           C  
ANISOU   76  CD1 ILE A 416     3593   3736   3808     82    133     58       C  
ATOM     77  N   HIS A 417       5.379  28.185  35.840  1.00 28.84           N  
ANISOU   77  N   HIS A 417     3772   3608   3577     24    177    -50       N  
ATOM     78  CA  HIS A 417       5.835  29.509  36.242  1.00 29.57           C  
ANISOU   78  CA  HIS A 417     3852   3748   3633     46     32     16       C  
ATOM     79  C   HIS A 417       5.472  30.490  35.129  1.00 28.99           C  
ANISOU   79  C   HIS A 417     3790   3689   3533     65     40     54       C  
ATOM     80  O   HIS A 417       6.127  30.538  34.084  1.00 28.11           O  
ANISOU   80  O   HIS A 417     3700   3636   3344      9      0    -21       O  
ATOM     81  CB  HIS A 417       7.305  29.469  36.591  1.00 30.69           C  
ANISOU   81  CB  HIS A 417     4103   3878   3678     79    -25     39       C  
ATOM     82  CG  HIS A 417       7.571  28.498  37.696  1.00 31.82           C  
ANISOU   82  CG  HIS A 417     4597   3898   3595    226   -147    175       C  
ATOM     83  ND1 HIS A 417       7.217  28.770  38.998  1.00 36.72           N  
ANISOU   83  ND1 HIS A 417     5442   4480   4029    432   -169    269       N  
ATOM     84  CD2 HIS A 417       8.010  27.218  37.677  1.00 35.50           C  
ANISOU   84  CD2 HIS A 417     5178   4360   3949    270    -11     67       C  
ATOM     85  CE1 HIS A 417       7.477  27.707  39.747  1.00 38.34           C  
ANISOU   85  CE1 HIS A 417     5747   4707   4112    388    -59    146       C  
ATOM     86  NE2 HIS A 417       7.972  26.757  38.972  1.00 35.74           N  
ANISOU   86  NE2 HIS A 417     5425   4182   3970    581    -27    -40       N  
ATOM     87  N   ASP A 418       4.353  31.194  35.351  1.00 30.00           N  
ANISOU   87  N   ASP A 418     3972   3799   3626     23    -59     23       N  
ATOM     88  CA  ASP A 418       3.869  32.167  34.372  1.00 31.24           C  
ANISOU   88  CA  ASP A 418     4109   3973   3786     20     24     -8       C  
ATOM     89  C   ASP A 418       4.706  33.442  34.394  1.00 31.79           C  
ANISOU   89  C   ASP A 418     4257   3954   3866     47     -8     19       C  
ATOM     90  O   ASP A 418       4.958  34.026  35.458  1.00 31.93           O  
ANISOU   90  O   ASP A 418     4432   4107   3590     -6    -36    116       O  
ATOM     91  CB  ASP A 418       2.405  32.487  34.633  1.00 31.08           C  
ANISOU   91  CB  ASP A 418     4105   3994   3708     -9      1     19       C  
ATOM     92  CG  ASP A 418       1.475  31.312  34.338  1.00 32.62           C  
ANISOU   92  CG  ASP A 418     4331   4347   3717   -251    239    -59       C  
ATOM     93  OD1 ASP A 418       1.527  30.727  33.220  1.00 33.54           O  
ANISOU   93  OD1 ASP A 418     4498   4437   3807    -75    250     17       O  
ATOM     94  OD2 ASP A 418       0.663  30.894  35.205  1.00 37.71           O  
ANISOU   94  OD2 ASP A 418     5365   5401   3562   -393    485     -6       O  
ATOM     95  N   LEU A 419       5.105  33.896  33.204  1.00 32.61           N  
ANISOU   95  N   LEU A 419     4347   4155   3887    -32     79    -58       N  
ATOM     96  CA  LEU A 419       5.795  35.188  33.002  1.00 34.38           C  
ANISOU   96  CA  LEU A 419     4470   4266   4325     -7     16    -52       C  
ATOM     97  C   LEU A 419       4.873  36.272  32.465  1.00 35.88           C  
ANISOU   97  C   LEU A 419     4718   4365   4547    -34     23     -7       C  
ATOM     98  O   LEU A 419       5.080  37.445  32.778  1.00 36.36           O  
ANISOU   98  O   LEU A 419     4951   4138   4725   -155    -24    -20       O  
ATOM     99  CB  LEU A 419       6.961  35.054  32.028  1.00 34.58           C  
ANISOU   99  CB  LEU A 419     4492   4266   4378    -29     61    -38       C  
ATOM    100  CG  LEU A 419       8.144  34.303  32.643  1.00 35.68           C  
ANISOU  100  CG  LEU A 419     4391   4650   4515     17     64    -92       C  
ATOM    101  CD1 LEU A 419       9.202  33.831  31.617  1.00 38.29           C  
ANISOU  101  CD1 LEU A 419     4726   4935   4886    121    202    -19       C  
ATOM    102  CD2 LEU A 419       8.801  35.160  33.745  1.00 38.98           C  
ANISOU  102  CD2 LEU A 419     5080   4778   4951     72      0    -74       C  
ATOM    103  N   ASP A 420       3.879  35.865  31.669  1.00 35.66           N  
ANISOU  103  N   ASP A 420     4567   4465   4516     58    -27     56       N  
ATOM    104  CA  ASP A 420       2.907  36.753  31.046  1.00 37.24           C  
ANISOU  104  CA  ASP A 420     4732   4660   4755      5     58     61       C  
ATOM    105  C   ASP A 420       1.759  35.853  30.555  1.00 36.45           C  
ANISOU  105  C   ASP A 420     4585   4592   4671     31     12     43       C  
ATOM    106  O   ASP A 420       1.836  34.610  30.669  1.00 36.70           O  
ANISOU  106  O   ASP A 420     4620   4594   4729     19     12     68       O  
ATOM    107  CB  ASP A 420       3.568  37.510  29.874  1.00 37.87           C  
ANISOU  107  CB  ASP A 420     4810   4719   4859     93     78    195       C  
ATOM    108  CG  ASP A 420       2.894  38.839  29.564  1.00 41.30           C  
ANISOU  108  CG  ASP A 420     5158   5311   5220    -28    237    339       C  
ATOM    109  OD1 ASP A 420       1.812  39.110  30.130  1.00 43.40           O  
ANISOU  109  OD1 ASP A 420     5092   5810   5587    -55    490    499       O  
ATOM    110  OD2 ASP A 420       3.384  39.687  28.778  1.00 44.90           O  
ANISOU  110  OD2 ASP A 420     5565   5987   5507   -352    337    946       O  
ATOM    111  N   SER A 421       0.709  36.459  30.015  1.00 36.34           N  
ANISOU  111  N   SER A 421     4637   4518   4652     14     -5     -8       N  
ATOM    112  CA  SER A 421      -0.480  35.733  29.569  1.00 35.59           C  
ANISOU  112  CA  SER A 421     4464   4498   4558     46    -25     47       C  
ATOM    113  C   SER A 421      -0.143  34.742  28.441  1.00 35.31           C  
ANISOU  113  C   SER A 421     4468   4456   4489    -20    -28     60       C  
ATOM    114  O   SER A 421      -0.853  33.740  28.242  1.00 36.89           O  
ANISOU  114  O   SER A 421     4586   4700   4729    -12    -44     95       O  
ATOM    115  CB  SER A 421      -1.503  36.745  29.048  1.00 36.30           C  
ANISOU  115  CB  SER A 421     4602   4583   4605    -23    -26     68       C  
ATOM    116  OG  SER A 421      -0.906  37.564  28.069  1.00 38.00           O  
ANISOU  116  OG  SER A 421     4986   4568   4883    147   -334    292       O  
ATOM    117  N   ASN A 422       0.926  35.025  27.691  1.00 33.44           N  
ANISOU  117  N   ASN A 422     4133   4324   4248     -4      8     79       N  
ATOM    118  CA  ASN A 422       1.383  34.088  26.652  1.00 32.02           C  
ANISOU  118  CA  ASN A 422     4054   4142   3970     52     26     62       C  
ATOM    119  C   ASN A 422       2.799  33.492  26.849  1.00 29.97           C  
ANISOU  119  C   ASN A 422     3878   3818   3688     10     26    124       C  
ATOM    120  O   ASN A 422       3.446  32.981  25.916  1.00 28.84           O  
ANISOU  120  O   ASN A 422     3913   3753   3291    -57    101    247       O  
ATOM    121  CB  ASN A 422       1.253  34.732  25.274  1.00 33.45           C  
ANISOU  121  CB  ASN A 422     4240   4287   4179    140     48    115       C  
ATOM    122  CG  ASN A 422       2.088  35.973  25.114  1.00 34.81           C  
ANISOU  122  CG  ASN A 422     4264   4668   4293    165   -126    223       C  
ATOM    123  OD1 ASN A 422       1.946  36.711  24.103  1.00 39.49           O  
ANISOU  123  OD1 ASN A 422     4904   5235   4865    501   -165    845       O  
ATOM    124  ND2 ASN A 422       2.988  36.224  26.067  1.00 37.96           N  
ANISOU  124  ND2 ASN A 422     4697   5354   4372    568   -322    636       N  
ATOM    125  N   SER A 423       3.263  33.531  28.083  1.00 27.74           N  
ANISOU  125  N   SER A 423     3489   3681   3369     -3     10     89       N  
ATOM    126  CA  SER A 423       4.628  33.165  28.394  1.00 26.10           C  
ANISOU  126  CA  SER A 423     3272   3430   3212     49     51     56       C  
ATOM    127  C   SER A 423       4.713  32.451  29.748  1.00 26.15           C  
ANISOU  127  C   SER A 423     3347   3299   3288    114     25     72       C  
ATOM    128  O   SER A 423       4.209  32.953  30.742  1.00 26.89           O  
ANISOU  128  O   SER A 423     3972   3235   3007    356     98    166       O  
ATOM    129  CB ASER A 423       5.469  34.426  28.411  0.50 26.85           C  
ANISOU  129  CB ASER A 423     3341   3501   3359     52     40    111       C  
ATOM    130  OG ASER A 423       6.818  34.066  28.568  0.50 26.59           O  
ANISOU  130  OG ASER A 423     2765   3747   3591    111     53     26       O  
ATOM    131  CB BSER A 423       5.472  34.444  28.433  0.50 26.71           C  
ANISOU  131  CB BSER A 423     3317   3482   3349     24     63    115       C  
ATOM    132  OG BSER A 423       5.299  35.221  27.260  0.50 24.98           O  
ANISOU  132  OG BSER A 423     2488   3578   3422   -264    349     19       O  
ATOM    133  N   PHE A 424       5.317  31.267  29.753  1.00 25.62           N  
ANISOU  133  N   PHE A 424     3218   3271   3244    154     10      1       N  
ATOM    134  CA  PHE A 424       5.593  30.536  30.976  1.00 24.47           C  
ANISOU  134  CA  PHE A 424     3077   3034   3185    248     56     16       C  
ATOM    135  C   PHE A 424       6.747  29.564  30.777  1.00 25.06           C  
ANISOU  135  C   PHE A 424     3069   3183   3269    157   -124     83       C  
ATOM    136  O   PHE A 424       7.128  29.279  29.658  1.00 25.20           O  
ANISOU  136  O   PHE A 424     3308   3172   3094    337   -292    119       O  
ATOM    137  CB  PHE A 424       4.374  29.736  31.424  1.00 25.26           C  
ANISOU  137  CB  PHE A 424     3153   3203   3241    105    -22     48       C  
ATOM    138  CG  PHE A 424       4.047  28.563  30.550  1.00 25.51           C  
ANISOU  138  CG  PHE A 424     3220   3060   3412    495   -313     64       C  
ATOM    139  CD1 PHE A 424       4.719  27.349  30.656  1.00 27.26           C  
ANISOU  139  CD1 PHE A 424     3235   3231   3889    379   -102   -234       C  
ATOM    140  CD2 PHE A 424       3.059  28.671  29.582  1.00 25.70           C  
ANISOU  140  CD2 PHE A 424     3253   2986   3526    394   -278    -87       C  
ATOM    141  CE1 PHE A 424       4.378  26.290  29.831  1.00 29.29           C  
ANISOU  141  CE1 PHE A 424     3490   3583   4055    173     32    -81       C  
ATOM    142  CE2 PHE A 424       2.740  27.583  28.755  1.00 29.33           C  
ANISOU  142  CE2 PHE A 424     3589   3707   3848     16    130    105       C  
ATOM    143  CZ  PHE A 424       3.420  26.421  28.890  1.00 27.06           C  
ANISOU  143  CZ  PHE A 424     3873   3123   3283     -3    176    109       C  
ATOM    144  N   GLU A 425       7.232  29.026  31.886  1.00 24.95           N  
ANISOU  144  N   GLU A 425     3125   3192   3160     15   -205    103       N  
ATOM    145  CA  GLU A 425       8.170  27.917  31.831  1.00 25.86           C  
ANISOU  145  CA  GLU A 425     3263   3302   3258    -33     -2    150       C  
ATOM    146  C   GLU A 425       7.865  26.938  32.923  1.00 25.22           C  
ANISOU  146  C   GLU A 425     3198   3249   3135    104   -108    239       C  
ATOM    147  O   GLU A 425       7.242  27.308  33.930  1.00 27.08           O  
ANISOU  147  O   GLU A 425     3721   3258   3309    203    -34    523       O  
ATOM    148  CB  GLU A 425       9.619  28.380  31.855  1.00 26.64           C  
ANISOU  148  CB  GLU A 425     3310   3343   3468    -69   -228     99       C  
ATOM    149  CG  GLU A 425      10.104  29.090  33.104  1.00 29.31           C  
ANISOU  149  CG  GLU A 425     3449   4001   3684     55   -107     31       C  
ATOM    150  CD  GLU A 425      11.488  29.709  32.967  1.00 29.98           C  
ANISOU  150  CD  GLU A 425     3903   3734   3752   -227     40    232       C  
ATOM    151  OE1 GLU A 425      11.871  30.321  31.951  1.00 28.62           O  
ANISOU  151  OE1 GLU A 425     3592   3463   3818   -860    302    150       O  
ATOM    152  OE2 GLU A 425      12.213  29.611  33.963  1.00 38.79           O  
ANISOU  152  OE2 GLU A 425     4745   4865   5128   -267    -80    889       O  
ATOM    153  N   LEU A 426       8.278  25.704  32.702  1.00 26.06           N  
ANISOU  153  N   LEU A 426     3368   3344   3186     41     66    106       N  
ATOM    154  CA  LEU A 426       8.030  24.614  33.653  1.00 27.21           C  
ANISOU  154  CA  LEU A 426     3486   3442   3410     40     45     75       C  
ATOM    155  C   LEU A 426       9.301  24.170  34.345  1.00 25.91           C  
ANISOU  155  C   LEU A 426     3222   3375   3244     49    169     80       C  
ATOM    156  O   LEU A 426      10.370  24.107  33.741  1.00 27.90           O  
ANISOU  156  O   LEU A 426     3273   3723   3605    335    378    214       O  
ATOM    157  CB  LEU A 426       7.511  23.372  32.927  1.00 27.72           C  
ANISOU  157  CB  LEU A 426     3495   3610   3424    -58    142     65       C  
ATOM    158  CG  LEU A 426       6.018  23.198  32.747  1.00 29.97           C  
ANISOU  158  CG  LEU A 426     3679   3783   3925     -9   -264    118       C  
ATOM    159  CD1 LEU A 426       5.238  24.432  32.414  1.00 33.28           C  
ANISOU  159  CD1 LEU A 426     4079   4327   4238     87    -30   -211       C  
ATOM    160  CD2 LEU A 426       5.789  22.074  31.741  1.00 28.93           C  
ANISOU  160  CD2 LEU A 426     3423   3761   3807     85    168    -60       C  
ATOM    161  N   ASP A 427       9.197  23.790  35.616  1.00 26.06           N  
ANISOU  161  N   ASP A 427     3401   3275   3225     11    336     41       N  
ATOM    162  CA  ASP A 427      10.226  23.016  36.252  1.00 26.82           C  
ANISOU  162  CA  ASP A 427     3522   3288   3378     41    155    -55       C  
ATOM    163  C   ASP A 427      10.173  21.581  35.704  1.00 27.11           C  
ANISOU  163  C   ASP A 427     3527   3245   3527     -4    120    -28       C  
ATOM    164  O   ASP A 427       9.081  21.048  35.465  1.00 28.55           O  
ANISOU  164  O   ASP A 427     3789   3245   3811     54    138   -202       O  
ATOM    165  CB  ASP A 427      10.031  22.903  37.765  1.00 27.61           C  
ANISOU  165  CB  ASP A 427     3844   3203   3442     65    218    -62       C  
ATOM    166  CG  ASP A 427       9.905  24.223  38.444  1.00 29.53           C  
ANISOU  166  CG  ASP A 427     4114   3544   3562    141    232   -178       C  
ATOM    167  OD1 ASP A 427      10.724  25.146  38.166  1.00 30.06           O  
ANISOU  167  OD1 ASP A 427     4405   3166   3851   -129    213   -539       O  
ATOM    168  OD2 ASP A 427       8.989  24.398  39.283  1.00 34.50           O  
ANISOU  168  OD2 ASP A 427     4699   4156   4250    745    258   -332       O  
ATOM    169  N   LEU A 428      11.344  20.955  35.532  1.00 27.73           N  
ANISOU  169  N   LEU A 428     3509   3415   3612    -35     44     48       N  
ATOM    170  CA  LEU A 428      11.407  19.681  34.770  1.00 27.81           C  
ANISOU  170  CA  LEU A 428     3562   3399   3603    118     12     29       C  
ATOM    171  C   LEU A 428      11.443  18.395  35.599  1.00 29.53           C  
ANISOU  171  C   LEU A 428     3809   3547   3861     -9     80    -43       C  
ATOM    172  O   LEU A 428      11.485  17.295  35.029  1.00 29.92           O  
ANISOU  172  O   LEU A 428     3830   3246   4292    324     55   -214       O  
ATOM    173  CB  LEU A 428      12.604  19.685  33.829  1.00 29.24           C  
ANISOU  173  CB  LEU A 428     3920   3543   3644     46     52    -25       C  
ATOM    174  CG  LEU A 428      12.721  20.865  32.861  1.00 30.10           C  
ANISOU  174  CG  LEU A 428     3853   3737   3845     -8    162     16       C  
ATOM    175  CD1 LEU A 428      13.926  20.695  31.920  1.00 32.19           C  
ANISOU  175  CD1 LEU A 428     4247   3944   4036    -94    177   -310       C  
ATOM    176  CD2 LEU A 428      11.418  21.079  32.088  1.00 33.61           C  
ANISOU  176  CD2 LEU A 428     4718   3938   4111     -2    166   -144       C  
ATOM    177  N   GLN A 429      11.461  18.498  36.917  1.00 29.36           N  
ANISOU  177  N   GLN A 429     3732   3638   3784    -18     40    107       N  
ATOM    178  CA  GLN A 429      11.627  17.278  37.729  1.00 30.19           C  
ANISOU  178  CA  GLN A 429     3826   3728   3915    -66     43    102       C  
ATOM    179  C   GLN A 429      10.367  16.378  37.955  1.00 29.63           C  
ANISOU  179  C   GLN A 429     3674   3678   3904    -64     66    239       C  
ATOM    180  O   GLN A 429      10.465  15.329  38.648  1.00 31.82           O  
ANISOU  180  O   GLN A 429     4078   3701   4310   -351    244    390       O  
ATOM    181  CB  GLN A 429      12.235  17.631  39.072  1.00 31.90           C  
ANISOU  181  CB  GLN A 429     4027   4013   4080    -65     17    152       C  
ATOM    182  CG  GLN A 429      11.251  18.222  40.058  1.00 32.91           C  
ANISOU  182  CG  GLN A 429     4190   4215   4098     41     32    107       C  
ATOM    183  CD  GLN A 429      10.987  19.724  39.931  1.00 35.57           C  
ANISOU  183  CD  GLN A 429     4537   4512   4466    143    375    -13       C  
ATOM    184  OE1 GLN A 429      10.214  20.255  40.733  1.00 40.05           O  
ANISOU  184  OE1 GLN A 429     4967   5206   5044    453    584    131       O  
ATOM    185  NE2 GLN A 429      11.657  20.418  38.983  1.00 33.92           N  
ANISOU  185  NE2 GLN A 429     5051   4440   3396    198    454    -28       N  
ATOM    186  N   PHE A 430       9.212  16.756  37.414  1.00 28.59           N  
ANISOU  186  N   PHE A 430     3641   3476   3746   -138     52    216       N  
ATOM    187  CA  PHE A 430       7.972  16.002  37.659  1.00 27.57           C  
ANISOU  187  CA  PHE A 430     3464   3484   3524    -55     86     57       C  
ATOM    188  C   PHE A 430       7.973  14.577  37.114  1.00 26.62           C  
ANISOU  188  C   PHE A 430     3339   3325   3447    -73    136     82       C  
ATOM    189  O   PHE A 430       8.768  14.225  36.220  1.00 27.69           O  
ANISOU  189  O   PHE A 430     3513   3389   3619   -113    192    196       O  
ATOM    190  CB  PHE A 430       6.764  16.740  37.095  1.00 26.22           C  
ANISOU  190  CB  PHE A 430     3409   3224   3328    105    156    -59       C  
ATOM    191  CG  PHE A 430       6.927  17.133  35.658  1.00 26.88           C  
ANISOU  191  CG  PHE A 430     3607   3309   3295     52     52     72       C  
ATOM    192  CD1 PHE A 430       6.792  16.202  34.654  1.00 26.15           C  
ANISOU  192  CD1 PHE A 430     3340   3500   3092   -115     84    -99       C  
ATOM    193  CD2 PHE A 430       7.301  18.419  35.317  1.00 27.30           C  
ANISOU  193  CD2 PHE A 430     3573   3369   3430    -26    224   -116       C  
ATOM    194  CE1 PHE A 430       6.977  16.564  33.308  1.00 25.81           C  
ANISOU  194  CE1 PHE A 430     3655   3179   2971    100     47     48       C  
ATOM    195  CE2 PHE A 430       7.485  18.781  33.976  1.00 25.54           C  
ANISOU  195  CE2 PHE A 430     3817   2861   3024   -291    -17    264       C  
ATOM    196  CZ  PHE A 430       7.348  17.833  32.983  1.00 24.61           C  
ANISOU  196  CZ  PHE A 430     3350   3168   2829   -190    -20    -14       C  
ATOM    197  N   SER A 431       7.049  13.763  37.640  1.00 26.69           N  
ANISOU  197  N   SER A 431     3345   3352   3444   -135    -21     67       N  
ATOM    198  CA  SER A 431       6.979  12.340  37.290  1.00 26.50           C  
ANISOU  198  CA  SER A 431     3313   3273   3483   -112    -24     50       C  
ATOM    199  C   SER A 431       6.228  12.123  35.982  1.00 26.71           C  
ANISOU  199  C   SER A 431     3554   3226   3369    -56    -36      5       C  
ATOM    200  O   SER A 431       5.528  13.014  35.483  1.00 27.14           O  
ANISOU  200  O   SER A 431     3597   2944   3770   -130   -345   -183       O  
ATOM    201  CB  SER A 431       6.226  11.587  38.399  1.00 25.79           C  
ANISOU  201  CB  SER A 431     3202   3245   3349   -205    -62     33       C  
ATOM    202  OG  SER A 431       4.845  11.894  38.390  1.00 26.52           O  
ANISOU  202  OG  SER A 431     3088   3355   3634    118   -265    384       O  
ATOM    203  N   GLU A 432       6.275  10.887  35.477  1.00 27.20           N  
ANISOU  203  N   GLU A 432     3631   3220   3484    -57   -146     19       N  
ATOM    204  CA  GLU A 432       5.527  10.547  34.278  1.00 28.38           C  
ANISOU  204  CA  GLU A 432     3774   3415   3593    -50    -50      1       C  
ATOM    205  C   GLU A 432       4.015  10.721  34.511  1.00 27.23           C  
ANISOU  205  C   GLU A 432     3599   3323   3423   -144   -172      3       C  
ATOM    206  O   GLU A 432       3.284  11.207  33.627  1.00 28.04           O  
ANISOU  206  O   GLU A 432     3984   3420   3249   -207   -225    192       O  
ATOM    207  CB  GLU A 432       5.867   9.107  33.871  1.00 27.87           C  
ANISOU  207  CB  GLU A 432     3641   3403   3544   -113    -57     86       C  
ATOM    208  CG  GLU A 432       5.040   8.571  32.758  1.00 31.71           C  
ANISOU  208  CG  GLU A 432     4486   3711   3852    -35     12     10       C  
ATOM    209  CD  GLU A 432       5.557   7.235  32.237  1.00 32.86           C  
ANISOU  209  CD  GLU A 432     4526   3817   4140    194   -108     36       C  
ATOM    210  OE1 GLU A 432       6.204   6.463  32.999  1.00 38.51           O  
ANISOU  210  OE1 GLU A 432     5991   3754   4885    605   -282     27       O  
ATOM    211  OE2 GLU A 432       5.292   6.960  31.050  1.00 38.87           O  
ANISOU  211  OE2 GLU A 432     5804   4338   4625    169    198    -75       O  
ATOM    212  N   ASP A 433       3.510  10.367  35.704  1.00 27.02           N  
ANISOU  212  N   ASP A 433     3552   3360   3352    -61    -67    134       N  
ATOM    213  CA  ASP A 433       2.074  10.589  35.998  1.00 27.99           C  
ANISOU  213  CA  ASP A 433     3609   3490   3534   -142   -148     47       C  
ATOM    214  C   ASP A 433       1.703  12.095  36.080  1.00 27.70           C  
ANISOU  214  C   ASP A 433     3577   3488   3458    -98   -136     75       C  
ATOM    215  O   ASP A 433       0.619  12.529  35.659  1.00 27.70           O  
ANISOU  215  O   ASP A 433     3316   3487   3718   -294   -255    -28       O  
ATOM    216  CB  ASP A 433       1.672   9.926  37.298  1.00 29.31           C  
ANISOU  216  CB  ASP A 433     3825   3600   3710   -153   -280     75       C  
ATOM    217  CG  ASP A 433       1.762   8.414  37.225  1.00 31.60           C  
ANISOU  217  CG  ASP A 433     4552   3622   3831   -304   -474    210       C  
ATOM    218  OD1 ASP A 433       1.410   7.850  36.147  1.00 37.06           O  
ANISOU  218  OD1 ASP A 433     5577   3966   4535   -699   -611    453       O  
ATOM    219  OD2 ASP A 433       2.170   7.719  38.172  1.00 31.81           O  
ANISOU  219  OD2 ASP A 433     4234   3791   4059   -343   -627    668       O  
ATOM    220  N   GLU A 434       2.576  12.868  36.701  1.00 27.71           N  
ANISOU  220  N   GLU A 434     3717   3363   3445   -183    -95     74       N  
ATOM    221  CA  GLU A 434       2.407  14.322  36.733  1.00 28.03           C  
ANISOU  221  CA  GLU A 434     3664   3547   3436    -33   -119      1       C  
ATOM    222  C   GLU A 434       2.399  14.907  35.315  1.00 26.85           C  
ANISOU  222  C   GLU A 434     3497   3326   3377    -49    -61     80       C  
ATOM    223  O   GLU A 434       1.606  15.790  34.981  1.00 28.11           O  
ANISOU  223  O   GLU A 434     3442   3997   3241    195   -200    144       O  
ATOM    224  CB  GLU A 434       3.516  14.954  37.580  1.00 27.73           C  
ANISOU  224  CB  GLU A 434     3590   3414   3529   -130   -103     30       C  
ATOM    225  CG  GLU A 434       3.276  14.654  39.043  1.00 26.39           C  
ANISOU  225  CG  GLU A 434     3397   3496   3134   -231   -196    135       C  
ATOM    226  CD  GLU A 434       4.328  15.203  39.977  1.00 26.99           C  
ANISOU  226  CD  GLU A 434     3335   3713   3206   -469    193     59       C  
ATOM    227  OE1 GLU A 434       5.520  14.980  39.693  1.00 31.60           O  
ANISOU  227  OE1 GLU A 434     4196   4404   3404   -273    235    177       O  
ATOM    228  OE2 GLU A 434       3.936  15.805  41.019  1.00 29.83           O  
ANISOU  228  OE2 GLU A 434     3915   3728   3691   -328    384    188       O  
ATOM    229  N   LYS A 435       3.291  14.413  34.486  1.00 27.11           N  
ANISOU  229  N   LYS A 435     3429   3470   3402     34    -80    -21       N  
ATOM    230  CA  LYS A 435       3.334  14.832  33.095  1.00 27.05           C  
ANISOU  230  CA  LYS A 435     3385   3409   3483    -49     20    -24       C  
ATOM    231  C   LYS A 435       1.974  14.660  32.431  1.00 26.03           C  
ANISOU  231  C   LYS A 435     3229   3325   3335     25    -33      0       C  
ATOM    232  O   LYS A 435       1.549  15.527  31.687  1.00 25.03           O  
ANISOU  232  O   LYS A 435     2698   3297   3514     54    -89     79       O  
ATOM    233  CB  LYS A 435       4.374  14.070  32.300  1.00 28.48           C  
ANISOU  233  CB  LYS A 435     3724   3431   3665     21    -90    -19       C  
ATOM    234  CG  LYS A 435       4.612  14.694  30.941  1.00 29.58           C  
ANISOU  234  CG  LYS A 435     3809   3734   3693   -142    127    -62       C  
ATOM    235  CD  LYS A 435       5.715  14.006  30.189  1.00 34.26           C  
ANISOU  235  CD  LYS A 435     4345   4319   4352   -103     96    -96       C  
ATOM    236  CE  LYS A 435       5.210  12.886  29.343  1.00 38.19           C  
ANISOU  236  CE  LYS A 435     4770   4828   4910    -89     88   -281       C  
ATOM    237  NZ  LYS A 435       6.250  12.356  28.389  1.00 39.01           N  
ANISOU  237  NZ  LYS A 435     4673   5044   5104     96    601   -525       N  
ATOM    238  N   ARG A 436       1.322  13.515  32.648  1.00 26.39           N  
ANISOU  238  N   ARG A 436     3247   3323   3456    -72   -180     81       N  
ATOM    239  CA  ARG A 436       0.024  13.281  31.993  1.00 27.49           C  
ANISOU  239  CA  ARG A 436     3460   3489   3495   -112    -62     24       C  
ATOM    240  C   ARG A 436      -0.961  14.388  32.337  1.00 27.59           C  
ANISOU  240  C   ARG A 436     3517   3550   3413    -81    -73     63       C  
ATOM    241  O   ARG A 436      -1.687  14.907  31.472  1.00 27.63           O  
ANISOU  241  O   ARG A 436     3341   3816   3339   -164   -217    -74       O  
ATOM    242  CB  ARG A 436      -0.572  11.958  32.423  1.00 28.90           C  
ANISOU  242  CB  ARG A 436     3773   3600   3606    -49    -24     46       C  
ATOM    243  CG  ARG A 436      -1.895  11.682  31.775  1.00 32.59           C  
ANISOU  243  CG  ARG A 436     4244   3997   4139    -25   -101     90       C  
ATOM    244  CD  ARG A 436      -2.656  10.521  32.395  1.00 39.14           C  
ANISOU  244  CD  ARG A 436     5041   4815   5014     -6    -66     93       C  
ATOM    245  NE  ARG A 436      -1.694   9.494  32.761  1.00 42.89           N  
ANISOU  245  NE  ARG A 436     5507   5145   5643   -110   -160     41       N  
ATOM    246  CZ  ARG A 436      -1.169   9.320  33.982  1.00 43.86           C  
ANISOU  246  CZ  ARG A 436     5711   5377   5575    -37   -181     10       C  
ATOM    247  NH1 ARG A 436      -1.523  10.080  35.040  1.00 45.06           N  
ANISOU  247  NH1 ARG A 436     5616   5690   5812     29     -9    137       N  
ATOM    248  NH2 ARG A 436      -0.278   8.363  34.145  1.00 44.67           N  
ANISOU  248  NH2 ARG A 436     5748   5460   5764    -78   -241    -93       N  
ATOM    249  N   LEU A 437      -0.973  14.790  33.605  1.00 27.08           N  
ANISOU  249  N   LEU A 437     3473   3490   3325    -86     19    117       N  
ATOM    250  CA  LEU A 437      -1.896  15.833  34.035  1.00 27.95           C  
ANISOU  250  CA  LEU A 437     3553   3617   3449    -11     23     32       C  
ATOM    251  C   LEU A 437      -1.506  17.183  33.430  1.00 27.54           C  
ANISOU  251  C   LEU A 437     3547   3532   3382     30     24      8       C  
ATOM    252  O   LEU A 437      -2.369  17.927  32.974  1.00 27.27           O  
ANISOU  252  O   LEU A 437     3279   3795   3286    160    -83     46       O  
ATOM    253  CB  LEU A 437      -1.919  15.958  35.552  1.00 29.33           C  
ANISOU  253  CB  LEU A 437     3771   3848   3523    -22    -17    115       C  
ATOM    254  CG  LEU A 437      -3.191  15.594  36.302  1.00 34.18           C  
ANISOU  254  CG  LEU A 437     4241   4521   4224    126    -46    -99       C  
ATOM    255  CD1 LEU A 437      -2.978  16.022  37.744  1.00 36.32           C  
ANISOU  255  CD1 LEU A 437     4742   4775   4283    144    -12     -9       C  
ATOM    256  CD2 LEU A 437      -4.424  16.277  35.758  1.00 35.74           C  
ANISOU  256  CD2 LEU A 437     4520   4686   4373     79   -238   -223       C  
ATOM    257  N   LEU A 438      -0.212  17.477  33.426  1.00 25.98           N  
ANISOU  257  N   LEU A 438     3219   3448   3201    -99    -97    110       N  
ATOM    258  CA  LEU A 438       0.307  18.724  32.803  1.00 25.31           C  
ANISOU  258  CA  LEU A 438     3093   3291   3231    -66    -74     34       C  
ATOM    259  C   LEU A 438      -0.103  18.805  31.335  1.00 25.99           C  
ANISOU  259  C   LEU A 438     3192   3311   3369   -132    -78     26       C  
ATOM    260  O   LEU A 438      -0.544  19.886  30.845  1.00 26.15           O  
ANISOU  260  O   LEU A 438     3234   3287   3413     86   -217   -114       O  
ATOM    261  CB  LEU A 438       1.831  18.856  32.977  1.00 26.34           C  
ANISOU  261  CB  LEU A 438     3288   3384   3335     -6    -56     34       C  
ATOM    262  CG  LEU A 438       2.301  19.244  34.394  1.00 24.08           C  
ANISOU  262  CG  LEU A 438     2773   3295   3081      9    -28    -58       C  
ATOM    263  CD1 LEU A 438       3.770  18.942  34.690  1.00 23.68           C  
ANISOU  263  CD1 LEU A 438     2810   3079   3108    187    220     31       C  
ATOM    264  CD2 LEU A 438       2.026  20.729  34.696  1.00 27.12           C  
ANISOU  264  CD2 LEU A 438     3325   3616   3362    -13     64   -140       C  
ATOM    265  N   LEU A 439      -0.008  17.671  30.644  1.00 24.94           N  
ANISOU  265  N   LEU A 439     3046   3168   3262     14     70     -6       N  
ATOM    266  CA  LEU A 439      -0.382  17.609  29.233  1.00 25.85           C  
ANISOU  266  CA  LEU A 439     3139   3354   3328    -22      3    -29       C  
ATOM    267  C   LEU A 439      -1.898  17.779  29.053  1.00 25.84           C  
ANISOU  267  C   LEU A 439     3211   3360   3246    -13      9    -11       C  
ATOM    268  O   LEU A 439      -2.344  18.474  28.146  1.00 27.92           O  
ANISOU  268  O   LEU A 439     3575   3638   3395     73     87    157       O  
ATOM    269  CB  LEU A 439       0.090  16.314  28.601  1.00 26.06           C  
ANISOU  269  CB  LEU A 439     3347   3271   3283   -113      5     25       C  
ATOM    270  CG  LEU A 439       0.061  16.150  27.085  1.00 27.21           C  
ANISOU  270  CG  LEU A 439     3609   3259   3470    -82     47     49       C  
ATOM    271  CD1 LEU A 439       0.880  17.243  26.403  1.00 28.89           C  
ANISOU  271  CD1 LEU A 439     4206   3478   3289   -318    131   -173       C  
ATOM    272  CD2 LEU A 439       0.637  14.802  26.691  1.00 26.98           C  
ANISOU  272  CD2 LEU A 439     3423   3395   3431   -110     69    -66       C  
ATOM    273  N   GLU A 440      -2.683  17.150  29.931  1.00 26.75           N  
ANISOU  273  N   GLU A 440     3417   3445   3299    -44    -14     51       N  
ATOM    274  CA  GLU A 440      -4.108  17.351  29.903  1.00 26.69           C  
ANISOU  274  CA  GLU A 440     3341   3398   3400    -21     -1     42       C  
ATOM    275  C   GLU A 440      -4.488  18.825  30.063  1.00 27.52           C  
ANISOU  275  C   GLU A 440     3457   3539   3460     44      4      1       C  
ATOM    276  O   GLU A 440      -5.319  19.338  29.308  1.00 27.37           O  
ANISOU  276  O   GLU A 440     3141   3520   3738    171     32    -73       O  
ATOM    277  CB  GLU A 440      -4.778  16.512  30.980  1.00 28.25           C  
ANISOU  277  CB  GLU A 440     3681   3533   3520    -35     10     29       C  
ATOM    278  CG  GLU A 440      -4.986  15.072  30.540  1.00 32.00           C  
ANISOU  278  CG  GLU A 440     4315   3788   4054    -13    135    181       C  
ATOM    279  CD  GLU A 440      -5.996  14.332  31.414  1.00 35.80           C  
ANISOU  279  CD  GLU A 440     5039   4107   4455   -163    563    234       C  
ATOM    280  OE1 GLU A 440      -6.169  13.113  31.208  1.00 39.99           O  
ANISOU  280  OE1 GLU A 440     5772   4595   4827   -157    536    220       O  
ATOM    281  OE2 GLU A 440      -6.635  14.960  32.289  1.00 37.54           O  
ANISOU  281  OE2 GLU A 440     5513   4221   4529    238    551    327       O  
ATOM    282  N   LYS A 441      -3.867  19.504  31.021  1.00 28.13           N  
ANISOU  282  N   LYS A 441     3505   3524   3659     26    -87     57       N  
ATOM    283  CA  LYS A 441      -4.037  20.950  31.205  1.00 29.35           C  
ANISOU  283  CA  LYS A 441     3639   3737   3775     60   -112     -8       C  
ATOM    284  C   LYS A 441      -3.707  21.704  29.922  1.00 27.87           C  
ANISOU  284  C   LYS A 441     3337   3503   3749      2    -40     47       C  
ATOM    285  O   LYS A 441      -4.485  22.565  29.483  1.00 28.53           O  
ANISOU  285  O   LYS A 441     3389   3640   3809    153   -314      0       O  
ATOM    286  CB  LYS A 441      -3.177  21.472  32.349  1.00 30.46           C  
ANISOU  286  CB  LYS A 441     3830   3762   3980     59    -91    -12       C  
ATOM    287  CG  LYS A 441      -3.504  22.896  32.790  1.00 32.32           C  
ANISOU  287  CG  LYS A 441     4033   4081   4165     -5   -145   -118       C  
ATOM    288  CD  LYS A 441      -2.507  23.359  33.850  1.00 33.12           C  
ANISOU  288  CD  LYS A 441     4078   4224   4281     41   -161    -61       C  
ATOM    289  CE  LYS A 441      -2.606  24.869  34.082  1.00 36.76           C  
ANISOU  289  CE  LYS A 441     4471   4634   4860     77   -178   -226       C  
ATOM    290  NZ  LYS A 441      -4.015  25.315  34.301  1.00 41.05           N  
ANISOU  290  NZ  LYS A 441     5052   5278   5264    131    -10   -321       N  
ATOM    291  N   GLN A 442      -2.566  21.390  29.325  1.00 27.33           N  
ANISOU  291  N   GLN A 442     3198   3594   3592      9    -94     53       N  
ATOM    292  CA  GLN A 442      -2.175  22.014  28.077  1.00 27.25           C  
ANISOU  292  CA  GLN A 442     3209   3440   3704    -23    -30     63       C  
ATOM    293  C   GLN A 442      -3.183  21.821  26.977  1.00 27.25           C  
ANISOU  293  C   GLN A 442     3148   3474   3729    -18    -18    102       C  
ATOM    294  O   GLN A 442      -3.576  22.785  26.328  1.00 27.70           O  
ANISOU  294  O   GLN A 442     3240   3167   4118    -55     59    212       O  
ATOM    295  CB  GLN A 442      -0.871  21.449  27.602  1.00 26.61           C  
ANISOU  295  CB  GLN A 442     3101   3457   3551    120     36    115       C  
ATOM    296  CG  GLN A 442      -0.337  22.054  26.348  1.00 26.42           C  
ANISOU  296  CG  GLN A 442     2957   3192   3889     95    171    158       C  
ATOM    297  CD  GLN A 442       0.962  21.391  25.954  1.00 27.50           C  
ANISOU  297  CD  GLN A 442     3315   3127   4003    194     34    460       C  
ATOM    298  OE1 GLN A 442       1.900  21.372  26.754  1.00 27.11           O  
ANISOU  298  OE1 GLN A 442     2516   3776   4008    -88    401    -16       O  
ATOM    299  NE2 GLN A 442       1.033  20.873  24.706  1.00 26.11           N  
ANISOU  299  NE2 GLN A 442     2657   3134   4129   -247   -143   -263       N  
ATOM    300  N   ALA A 443      -3.575  20.566  26.738  1.00 27.61           N  
ANISOU  300  N   ALA A 443     3370   3364   3756    -24    -52    112       N  
ATOM    301  CA  ALA A 443      -4.601  20.263  25.729  1.00 28.80           C  
ANISOU  301  CA  ALA A 443     3580   3595   3765    -49    -15     56       C  
ATOM    302  C   ALA A 443      -5.905  21.053  25.877  1.00 29.12           C  
ANISOU  302  C   ALA A 443     3645   3605   3813     -9    -61     57       C  
ATOM    303  O   ALA A 443      -6.505  21.467  24.885  1.00 30.42           O  
ANISOU  303  O   ALA A 443     3539   3962   4054    150    119     73       O  
ATOM    304  CB  ALA A 443      -4.883  18.765  25.692  1.00 29.11           C  
ANISOU  304  CB  ALA A 443     3637   3684   3738    -51    -98    -30       C  
ATOM    305  N   GLY A 444      -6.378  21.207  27.102  1.00 29.40           N  
ANISOU  305  N   GLY A 444     3574   3730   3867     11    -53    -15       N  
ATOM    306  CA  GLY A 444      -7.638  21.918  27.344  1.00 31.56           C  
ANISOU  306  CA  GLY A 444     4008   3895   4086    -14    -23     19       C  
ATOM    307  C   GLY A 444      -7.500  23.419  27.209  1.00 32.70           C  
ANISOU  307  C   GLY A 444     4131   4036   4256     42   -100      8       C  
ATOM    308  O   GLY A 444      -8.446  24.090  26.748  1.00 33.45           O  
ANISOU  308  O   GLY A 444     4097   4184   4427   -148   -454     -7       O  
ATOM    309  N   GLY A 445      -6.322  23.928  27.576  1.00 31.99           N  
ANISOU  309  N   GLY A 445     4067   3934   4154    -24    -87     59       N  
ATOM    310  CA  GLY A 445      -6.143  25.332  27.949  1.00 32.26           C  
ANISOU  310  CA  GLY A 445     4040   3997   4219     21      3     30       C  
ATOM    311  C   GLY A 445      -5.120  26.138  27.171  1.00 31.93           C  
ANISOU  311  C   GLY A 445     3974   3887   4268     38    -17     74       C  
ATOM    312  O   GLY A 445      -5.152  27.378  27.199  1.00 34.09           O  
ANISOU  312  O   GLY A 445     4210   3962   4781    -43    148    -79       O  
ATOM    313  N   ASN A 446      -4.206  25.477  26.474  1.00 30.24           N  
ANISOU  313  N   ASN A 446     3744   3723   4023     42    -38     79       N  
ATOM    314  CA  ASN A 446      -3.134  26.202  25.817  1.00 29.80           C  
ANISOU  314  CA  ASN A 446     3535   3777   4011     47    -94     85       C  
ATOM    315  C   ASN A 446      -3.462  26.474  24.345  1.00 30.15           C  
ANISOU  315  C   ASN A 446     3550   3838   4068     50   -136    120       C  
ATOM    316  O   ASN A 446      -3.588  25.545  23.566  1.00 30.23           O  
ANISOU  316  O   ASN A 446     3332   3780   4374     19   -312    160       O  
ATOM    317  CB  ASN A 446      -1.826  25.416  25.931  1.00 29.75           C  
ANISOU  317  CB  ASN A 446     3639   3804   3858    120   -208    142       C  
ATOM    318  CG  ASN A 446      -0.596  26.252  25.521  1.00 30.45           C  
ANISOU  318  CG  ASN A 446     3757   3805   4006     90   -326    369       C  
ATOM    319  OD1 ASN A 446      -0.584  26.878  24.468  1.00 34.83           O  
ANISOU  319  OD1 ASN A 446     4605   4207   4422    -23   -386    299       O  
ATOM    320  ND2 ASN A 446       0.447  26.219  26.337  1.00 27.43           N  
ANISOU  320  ND2 ASN A 446     3246   3527   3649    732   -958    427       N  
ATOM    321  N   PRO A 447      -3.553  27.739  23.938  1.00 30.64           N  
ANISOU  321  N   PRO A 447     3615   3900   4126     57   -198     96       N  
ATOM    322  CA  PRO A 447      -3.870  28.064  22.520  1.00 31.95           C  
ANISOU  322  CA  PRO A 447     4007   3967   4165      0   -110     67       C  
ATOM    323  C   PRO A 447      -2.968  27.422  21.483  1.00 31.30           C  
ANISOU  323  C   PRO A 447     3884   3929   4076   -100   -109     84       C  
ATOM    324  O   PRO A 447      -3.343  27.349  20.332  1.00 32.37           O  
ANISOU  324  O   PRO A 447     3993   4013   4294   -164   -386    105       O  
ATOM    325  CB  PRO A 447      -3.664  29.592  22.432  1.00 31.96           C  
ANISOU  325  CB  PRO A 447     4137   3863   4141     14      0    157       C  
ATOM    326  CG  PRO A 447      -3.735  30.113  23.818  1.00 32.68           C  
ANISOU  326  CG  PRO A 447     4230   3998   4187     35   -154    130       C  
ATOM    327  CD  PRO A 447      -3.415  28.942  24.766  1.00 31.98           C  
ANISOU  327  CD  PRO A 447     3972   4005   4173    140   -197    121       C  
ATOM    328  N   TRP A 448      -1.751  27.034  21.877  1.00 31.70           N  
ANISOU  328  N   TRP A 448     4019   4024   3998    -37   -169     83       N  
ATOM    329  CA  TRP A 448      -0.730  26.599  20.943  1.00 31.20           C  
ANISOU  329  CA  TRP A 448     3914   3959   3979    -81    -44     49       C  
ATOM    330  C   TRP A 448      -0.606  25.080  20.888  1.00 30.79           C  
ANISOU  330  C   TRP A 448     3865   3940   3892    -87    -62     62       C  
ATOM    331  O   TRP A 448       0.282  24.555  20.217  1.00 30.44           O  
ANISOU  331  O   TRP A 448     3829   3840   3895   -338    237     18       O  
ATOM    332  CB  TRP A 448       0.611  27.256  21.326  1.00 32.13           C  
ANISOU  332  CB  TRP A 448     3966   4096   4144    -90    -91     52       C  
ATOM    333  CG  TRP A 448       0.445  28.724  21.553  1.00 32.25           C  
ANISOU  333  CG  TRP A 448     3902   4244   4107    -49    -58     55       C  
ATOM    334  CD1 TRP A 448       0.315  29.384  22.758  1.00 33.62           C  
ANISOU  334  CD1 TRP A 448     3951   4292   4529   -133    -64     69       C  
ATOM    335  CD2 TRP A 448       0.324  29.720  20.541  1.00 31.60           C  
ANISOU  335  CD2 TRP A 448     3520   4115   4370   -724     11    149       C  
ATOM    336  NE1 TRP A 448       0.075  30.719  22.541  1.00 33.92           N  
ANISOU  336  NE1 TRP A 448     4094   4401   4390   -278    -59     60       N  
ATOM    337  CE2 TRP A 448       0.071  30.954  21.189  1.00 33.71           C  
ANISOU  337  CE2 TRP A 448     4078   4281   4450   -300    247    262       C  
ATOM    338  CE3 TRP A 448       0.347  29.686  19.146  1.00 34.07           C  
ANISOU  338  CE3 TRP A 448     4225   4276   4444   -119    111     89       C  
ATOM    339  CZ2 TRP A 448      -0.112  32.148  20.494  1.00 34.86           C  
ANISOU  339  CZ2 TRP A 448     4480   4308   4456    -17     70     60       C  
ATOM    340  CZ3 TRP A 448       0.172  30.889  18.444  1.00 35.61           C  
ANISOU  340  CZ3 TRP A 448     4691   4404   4432    -54     98     63       C  
ATOM    341  CH2 TRP A 448      -0.037  32.102  19.133  1.00 34.26           C  
ANISOU  341  CH2 TRP A 448     4459   4165   4391    -61    -63     95       C  
ATOM    342  N   HIS A 449      -1.476  24.379  21.613  1.00 29.96           N  
ANISOU  342  N   HIS A 449     3720   3815   3846    -87    -80     75       N  
ATOM    343  CA  HIS A 449      -1.361  22.926  21.742  1.00 29.91           C  
ANISOU  343  CA  HIS A 449     3627   3857   3878   -104    -86     65       C  
ATOM    344  C   HIS A 449      -1.356  22.254  20.372  1.00 30.01           C  
ANISOU  344  C   HIS A 449     3585   3879   3937   -125    -78    122       C  
ATOM    345  O   HIS A 449      -0.619  21.313  20.131  1.00 29.93           O  
ANISOU  345  O   HIS A 449     3324   4002   4043   -466     45    199       O  
ATOM    346  CB  HIS A 449      -2.421  22.332  22.702  1.00 29.00           C  
ANISOU  346  CB  HIS A 449     3544   3676   3798   -140   -143     34       C  
ATOM    347  CG  HIS A 449      -2.367  20.826  22.802  1.00 28.88           C  
ANISOU  347  CG  HIS A 449     3449   3824   3699    -49   -136    216       C  
ATOM    348  ND1 HIS A 449      -1.410  20.168  23.530  1.00 30.44           N  
ANISOU  348  ND1 HIS A 449     3542   4069   3951    -37   -315     93       N  
ATOM    349  CD2 HIS A 449      -3.135  19.861  22.235  1.00 30.97           C  
ANISOU  349  CD2 HIS A 449     3749   4081   3936     14   -218    -47       C  
ATOM    350  CE1 HIS A 449      -1.595  18.862  23.435  1.00 26.92           C  
ANISOU  350  CE1 HIS A 449     3107   3794   3324   -334   -509     37       C  
ATOM    351  NE2 HIS A 449      -2.634  18.642  22.646  1.00 26.97           N  
ANISOU  351  NE2 HIS A 449     2728   3866   3652   -396   -830   -262       N  
ATOM    352  N   GLN A 450      -2.214  22.738  19.478  1.00 31.80           N  
ANISOU  352  N   GLN A 450     3933   4079   4070    -94    -56     91       N  
ATOM    353  CA  GLN A 450      -2.375  22.116  18.171  1.00 32.70           C  
ANISOU  353  CA  GLN A 450     4095   4159   4168    -81    -56     52       C  
ATOM    354  C   GLN A 450      -1.104  22.092  17.297  1.00 31.91           C  
ANISOU  354  C   GLN A 450     4087   3992   4043    -94    -34     85       C  
ATOM    355  O   GLN A 450      -1.006  21.298  16.361  1.00 32.37           O  
ANISOU  355  O   GLN A 450     4209   3943   4145   -252   -189    181       O  
ATOM    356  CB  GLN A 450      -3.507  22.826  17.432  1.00 33.14           C  
ANISOU  356  CB  GLN A 450     4141   4177   4271     -6    -74     58       C  
ATOM    357  CG  GLN A 450      -3.243  24.292  17.129  1.00 35.38           C  
ANISOU  357  CG  GLN A 450     4350   4503   4589    -80      3     14       C  
ATOM    358  CD  GLN A 450      -4.365  24.930  16.308  1.00 35.90           C  
ANISOU  358  CD  GLN A 450     4488   4590   4558    109     19    -66       C  
ATOM    359  OE1 GLN A 450      -4.445  24.748  15.084  1.00 39.59           O  
ANISOU  359  OE1 GLN A 450     4842   5103   5096     93    100   -171       O  
ATOM    360  NE2 GLN A 450      -5.226  25.697  16.978  1.00 40.54           N  
ANISOU  360  NE2 GLN A 450     4790   5329   5281    195    230   -300       N  
ATOM    361  N   PHE A 451      -0.147  22.970  17.591  1.00 31.39           N  
ANISOU  361  N   PHE A 451     4052   3931   3941   -114    -86    129       N  
ATOM    362  CA  PHE A 451       1.079  23.084  16.774  1.00 31.23           C  
ANISOU  362  CA  PHE A 451     3994   3951   3921    -67    -27     44       C  
ATOM    363  C   PHE A 451       2.248  22.229  17.243  1.00 31.65           C  
ANISOU  363  C   PHE A 451     4060   4032   3931    -99    -18     49       C  
ATOM    364  O   PHE A 451       3.245  22.135  16.544  1.00 31.69           O  
ANISOU  364  O   PHE A 451     3929   4325   3786   -133   -134    109       O  
ATOM    365  CB  PHE A 451       1.543  24.554  16.691  1.00 31.65           C  
ANISOU  365  CB  PHE A 451     4020   4012   3994    -51    -21     55       C  
ATOM    366  CG  PHE A 451       0.435  25.500  16.360  1.00 30.17           C  
ANISOU  366  CG  PHE A 451     3765   3730   3967   -191     53    128       C  
ATOM    367  CD1 PHE A 451      -0.083  25.566  15.074  1.00 31.17           C  
ANISOU  367  CD1 PHE A 451     3805   3808   4226   -230    131     25       C  
ATOM    368  CD2 PHE A 451      -0.134  26.266  17.351  1.00 32.82           C  
ANISOU  368  CD2 PHE A 451     4085   4119   4266   -179     36     12       C  
ATOM    369  CE1 PHE A 451      -1.110  26.418  14.777  1.00 30.53           C  
ANISOU  369  CE1 PHE A 451     3968   3718   3914     19    233    115       C  
ATOM    370  CE2 PHE A 451      -1.178  27.127  17.075  1.00 31.77           C  
ANISOU  370  CE2 PHE A 451     4028   4097   3946     45   -121    107       C  
ATOM    371  CZ  PHE A 451      -1.665  27.209  15.784  1.00 33.35           C  
ANISOU  371  CZ  PHE A 451     4233   4219   4218    166   -101     35       C  
ATOM    372  N   VAL A 452       2.125  21.592  18.410  1.00 30.41           N  
ANISOU  372  N   VAL A 452     3919   3898   3737   -147   -122     38       N  
ATOM    373  CA  VAL A 452       3.261  20.938  19.000  1.00 30.26           C  
ANISOU  373  CA  VAL A 452     3953   3776   3766   -163    -57     49       C  
ATOM    374  C   VAL A 452       3.268  19.415  19.019  1.00 29.62           C  
ANISOU  374  C   VAL A 452     3852   3710   3691   -203   -149    -30       C  
ATOM    375  O   VAL A 452       4.045  18.820  19.770  1.00 29.65           O  
ANISOU  375  O   VAL A 452     4049   3597   3618   -247   -214    133       O  
ATOM    376  CB  VAL A 452       3.548  21.528  20.412  1.00 29.83           C  
ANISOU  376  CB  VAL A 452     3890   3734   3707   -164    -90    -49       C  
ATOM    377  CG1 VAL A 452       3.751  23.031  20.295  1.00 29.84           C  
ANISOU  377  CG1 VAL A 452     3799   3734   3804   -348     32     -8       C  
ATOM    378  CG2 VAL A 452       2.438  21.225  21.405  1.00 29.38           C  
ANISOU  378  CG2 VAL A 452     3921   3483   3759   -312   -111    -72       C  
ATOM    379  N   GLU A 453       2.445  18.774  18.179  1.00 29.64           N  
ANISOU  379  N   GLU A 453     3926   3796   3538   -139   -135     28       N  
ATOM    380  CA  GLU A 453       2.565  17.317  17.980  1.00 29.51           C  
ANISOU  380  CA  GLU A 453     3852   3770   3588   -171    -96     31       C  
ATOM    381  C   GLU A 453       2.393  16.577  19.299  1.00 28.88           C  
ANISOU  381  C   GLU A 453     3812   3658   3501   -215    -74     12       C  
ATOM    382  O   GLU A 453       3.077  15.594  19.569  1.00 29.81           O  
ANISOU  382  O   GLU A 453     4116   3703   3506   -280      3     12       O  
ATOM    383  CB  GLU A 453       3.920  16.963  17.382  1.00 29.05           C  
ANISOU  383  CB  GLU A 453     3815   3663   3556   -118     -6     58       C  
ATOM    384  CG  GLU A 453       4.134  17.581  16.005  1.00 31.68           C  
ANISOU  384  CG  GLU A 453     4031   4125   3879   -250      3     -7       C  
ATOM    385  CD  GLU A 453       5.376  17.033  15.341  1.00 32.87           C  
ANISOU  385  CD  GLU A 453     4142   4423   3922   -545    131   -105       C  
ATOM    386  OE1 GLU A 453       6.493  17.361  15.788  1.00 35.79           O  
ANISOU  386  OE1 GLU A 453     4633   4824   4141   -702     89     42       O  
ATOM    387  OE2 GLU A 453       5.222  16.239  14.391  1.00 36.85           O  
ANISOU  387  OE2 GLU A 453     4135   5237   4628  -1367    413   -280       O  
ATOM    388  N   ASN A 454       1.495  17.104  20.119  1.00 28.98           N  
ANISOU  388  N   ASN A 454     3727   3725   3557   -219    -59    -50       N  
ATOM    389  CA  ASN A 454       1.147  16.501  21.394  1.00 29.24           C  
ANISOU  389  CA  ASN A 454     3800   3714   3595   -218     44     27       C  
ATOM    390  C   ASN A 454       2.314  16.355  22.398  1.00 29.38           C  
ANISOU  390  C   ASN A 454     3927   3670   3565   -145     53     43       C  
ATOM    391  O   ASN A 454       2.228  15.581  23.359  1.00 29.42           O  
ANISOU  391  O   ASN A 454     3928   3668   3581   -206    103     47       O  
ATOM    392  CB  ASN A 454       0.450  15.152  21.183  1.00 30.34           C  
ANISOU  392  CB  ASN A 454     4076   3898   3551   -258    115     41       C  
ATOM    393  CG  ASN A 454      -0.347  14.734  22.395  1.00 33.23           C  
ANISOU  393  CG  ASN A 454     4471   4202   3954   -197    186     68       C  
ATOM    394  OD1 ASN A 454      -1.143  15.531  22.922  1.00 36.05           O  
ANISOU  394  OD1 ASN A 454     4663   4821   4213   -408    299    257       O  
ATOM    395  ND2 ASN A 454      -0.132  13.496  22.863  1.00 37.17           N  
ANISOU  395  ND2 ASN A 454     5281   4517   4326   -180    230    169       N  
ATOM    396  N   ASN A 455       3.367  17.166  22.180  1.00 26.47           N  
ANISOU  396  N   ASN A 455     3357   3402   3298   -250    -13     22       N  
ATOM    397  CA  ASN A 455       4.502  17.303  23.081  1.00 26.51           C  
ANISOU  397  CA  ASN A 455     3389   3385   3297   -198     46    -17       C  
ATOM    398  C   ASN A 455       4.184  18.310  24.175  1.00 26.07           C  
ANISOU  398  C   ASN A 455     3304   3333   3266   -100     56     68       C  
ATOM    399  O   ASN A 455       3.616  19.364  23.887  1.00 25.65           O  
ANISOU  399  O   ASN A 455     3077   3397   3271   -408     64     85       O  
ATOM    400  CB  ASN A 455       5.721  17.746  22.296  1.00 27.05           C  
ANISOU  400  CB  ASN A 455     3511   3494   3272   -212    -46    -76       C  
ATOM    401  CG  ASN A 455       6.215  16.660  21.330  1.00 27.69           C  
ANISOU  401  CG  ASN A 455     3480   3718   3323   -266    328   -100       C  
ATOM    402  OD1 ASN A 455       6.475  16.910  20.129  1.00 31.17           O  
ANISOU  402  OD1 ASN A 455     4524   4079   3238   -589     75      0       O  
ATOM    403  ND2 ASN A 455       6.378  15.465  21.861  1.00 25.77           N  
ANISOU  403  ND2 ASN A 455     3506   3244   3040   -468    461     80       N  
ATOM    404  N   LEU A 456       4.556  17.983  25.425  1.00 25.43           N  
ANISOU  404  N   LEU A 456     3187   3199   3275    -74    -46     68       N  
ATOM    405  CA  LEU A 456       4.420  18.915  26.527  1.00 24.26           C  
ANISOU  405  CA  LEU A 456     2917   3221   3079    -65    -48     83       C  
ATOM    406  C   LEU A 456       5.326  20.129  26.270  1.00 24.29           C  
ANISOU  406  C   LEU A 456     2803   3248   3175    -56    -12     37       C  
ATOM    407  O   LEU A 456       6.545  20.002  26.015  1.00 23.74           O  
ANISOU  407  O   LEU A 456     2500   3227   3292    111     94    157       O  
ATOM    408  CB  LEU A 456       4.766  18.279  27.870  1.00 23.82           C  
ANISOU  408  CB  LEU A 456     2777   3179   3094   -111    -69     77       C  
ATOM    409  CG  LEU A 456       4.392  19.092  29.109  1.00 25.29           C  
ANISOU  409  CG  LEU A 456     3048   3195   3364   -230    -64     39       C  
ATOM    410  CD1 LEU A 456       2.938  19.305  29.272  1.00 27.90           C  
ANISOU  410  CD1 LEU A 456     3444   3517   3639    442    108    113       C  
ATOM    411  CD2 LEU A 456       4.999  18.486  30.352  1.00 25.71           C  
ANISOU  411  CD2 LEU A 456     2982   3502   3285    -52    235    -58       C  
ATOM    412  N   ILE A 457       4.732  21.309  26.421  1.00 24.69           N  
ANISOU  412  N   ILE A 457     2704   3307   3369     27    -74     80       N  
ATOM    413  CA  ILE A 457       5.415  22.586  26.280  1.00 25.28           C  
ANISOU  413  CA  ILE A 457     3142   3124   3337     10   -130     -4       C  
ATOM    414  C   ILE A 457       6.106  22.915  27.597  1.00 24.42           C  
ANISOU  414  C   ILE A 457     2966   3149   3163    -36    -66     64       C  
ATOM    415  O   ILE A 457       5.421  23.072  28.631  1.00 26.19           O  
ANISOU  415  O   ILE A 457     3334   3374   3241   -161    -14   -101       O  
ATOM    416  CB  ILE A 457       4.445  23.730  25.912  1.00 24.96           C  
ANISOU  416  CB  ILE A 457     2941   3270   3273     48   -187     97       C  
ATOM    417  CG1 ILE A 457       3.755  23.407  24.587  1.00 24.29           C  
ANISOU  417  CG1 ILE A 457     2755   3112   3361   -195   -307     60       C  
ATOM    418  CG2 ILE A 457       5.194  25.067  25.897  1.00 26.84           C  
ANISOU  418  CG2 ILE A 457     3704   3275   3218    287   -363     35       C  
ATOM    419  CD1 ILE A 457       2.604  24.342  24.185  1.00 24.87           C  
ANISOU  419  CD1 ILE A 457     2991   3235   3223   -141   -134      4       C  
ATOM    420  N   LEU A 458       7.428  23.058  27.545  1.00 23.93           N  
ANISOU  420  N   LEU A 458     2923   3057   3110   -115    -33     64       N  
ATOM    421  CA  LEU A 458       8.290  23.306  28.698  1.00 22.46           C  
ANISOU  421  CA  LEU A 458     2613   2887   3031    -18    -15    172       C  
ATOM    422  C   LEU A 458       8.568  24.801  28.911  1.00 22.13           C  
ANISOU  422  C   LEU A 458     2493   2989   2923     56   -101     65       C  
ATOM    423  O   LEU A 458       8.834  25.264  30.022  1.00 25.17           O  
ANISOU  423  O   LEU A 458     3330   3054   3179    -90    -50    195       O  
ATOM    424  CB  LEU A 458       9.558  22.506  28.553  1.00 23.20           C  
ANISOU  424  CB  LEU A 458     2583   3122   3109   -113     19    111       C  
ATOM    425  CG  LEU A 458       9.353  20.990  28.368  1.00 24.50           C  
ANISOU  425  CG  LEU A 458     2799   3341   3165    270    -12    211       C  
ATOM    426  CD1 LEU A 458      10.682  20.295  28.159  1.00 24.36           C  
ANISOU  426  CD1 LEU A 458     2559   3437   3260    290   -191     82       C  
ATOM    427  CD2 LEU A 458       8.628  20.374  29.516  1.00 27.22           C  
ANISOU  427  CD2 LEU A 458     3381   3322   3638   -117    116    211       C  
ATOM    428  N   LYS A 459       8.637  25.528  27.797  1.00 22.88           N  
ANISOU  428  N   LYS A 459     2886   2939   2866    -76     19    234       N  
ATOM    429  CA  LYS A 459       8.683  26.988  27.868  1.00 22.99           C  
ANISOU  429  CA  LYS A 459     2744   3119   2870    -51   -147    104       C  
ATOM    430  C   LYS A 459       8.067  27.535  26.596  1.00 24.05           C  
ANISOU  430  C   LYS A 459     2972   3110   3056     38    -81    245       C  
ATOM    431  O   LYS A 459       8.303  26.986  25.535  1.00 24.97           O  
ANISOU  431  O   LYS A 459     3299   3373   2815    -77   -176    391       O  
ATOM    432  CB  LYS A 459      10.082  27.513  28.016  1.00 23.33           C  
ANISOU  432  CB  LYS A 459     2631   3190   3040    -98   -246    126       C  
ATOM    433  CG  LYS A 459      10.141  28.999  28.094  1.00 21.91           C  
ANISOU  433  CG  LYS A 459     2243   3349   2730   -378   -403     78       C  
ATOM    434  CD  LYS A 459      11.504  29.409  28.474  1.00 23.00           C  
ANISOU  434  CD  LYS A 459     2310   3681   2745   -248    167   -257       C  
ATOM    435  CE  LYS A 459      11.770  30.948  28.599  1.00 26.33           C  
ANISOU  435  CE  LYS A 459     3270   3559   3174   -191     35    -71       C  
ATOM    436  NZ  LYS A 459      10.992  31.607  29.661  1.00 26.66           N  
ANISOU  436  NZ  LYS A 459     3182   3290   3656   -234    329     83       N  
ATOM    437  N   MET A 460       7.311  28.620  26.708  1.00 21.85           N  
ANISOU  437  N   MET A 460     2087   3181   3032      8   -254    214       N  
ATOM    438  CA  MET A 460       6.889  29.321  25.473  1.00 23.06           C  
ANISOU  438  CA  MET A 460     2573   3022   3166    106    -91    207       C  
ATOM    439  C   MET A 460       6.850  30.820  25.734  1.00 24.38           C  
ANISOU  439  C   MET A 460     2916   3125   3219    -48    -83    183       C  
ATOM    440  O   MET A 460       6.711  31.262  26.894  1.00 22.61           O  
ANISOU  440  O   MET A 460     2378   3138   3074     23     63     38       O  
ATOM    441  CB  MET A 460       5.524  28.835  25.017  1.00 23.45           C  
ANISOU  441  CB  MET A 460     2215   3240   3454     78     99    224       C  
ATOM    442  CG  MET A 460       4.266  29.312  25.841  1.00 21.88           C  
ANISOU  442  CG  MET A 460     1349   3619   3343    225   -398    272       C  
ATOM    443  SD  MET A 460       2.751  28.764  25.247  1.00 26.36           S  
ANISOU  443  SD  MET A 460     2402   3818   3794     98   -195    457       S  
ATOM    444  CE  MET A 460       1.504  29.842  25.993  1.00 28.31           C  
ANISOU  444  CE  MET A 460     2953   3600   4203    652    198    272       C  
ATOM    445  N   GLY A 461       6.858  31.570  24.633  1.00 24.54           N  
ANISOU  445  N   GLY A 461     3255   3088   2980   -167     95    252       N  
ATOM    446  CA  GLY A 461       6.766  33.046  24.730  1.00 24.25           C  
ANISOU  446  CA  GLY A 461     3146   2981   3084    -54     47    299       C  
ATOM    447  C   GLY A 461       6.985  33.653  23.360  1.00 24.40           C  
ANISOU  447  C   GLY A 461     3160   3161   2947    -43    103    141       C  
ATOM    448  O   GLY A 461       7.462  32.977  22.480  1.00 25.13           O  
ANISOU  448  O   GLY A 461     3284   3322   2938     -7     80    349       O  
ATOM    449  N   PRO A 462       6.511  34.875  23.142  1.00 24.33           N  
ANISOU  449  N   PRO A 462     3219   3081   2944    -55     93    189       N  
ATOM    450  CA  PRO A 462       6.760  35.544  21.867  1.00 25.78           C  
ANISOU  450  CA  PRO A 462     3410   3281   3103     42      8    126       C  
ATOM    451  C   PRO A 462       8.177  36.025  21.741  1.00 25.47           C  
ANISOU  451  C   PRO A 462     3258   3360   3058     22    -59    108       C  
ATOM    452  O   PRO A 462       8.837  36.489  22.711  1.00 25.32           O  
ANISOU  452  O   PRO A 462     3085   3503   3033    133   -216    156       O  
ATOM    453  CB  PRO A 462       5.825  36.764  21.900  1.00 26.31           C  
ANISOU  453  CB  PRO A 462     3304   3566   3125     55      8    219       C  
ATOM    454  CG  PRO A 462       5.552  37.003  23.358  1.00 29.15           C  
ANISOU  454  CG  PRO A 462     3878   3560   3638    288    126     43       C  
ATOM    455  CD  PRO A 462       5.669  35.684  24.041  1.00 24.65           C  
ANISOU  455  CD  PRO A 462     3210   3066   3089    -56     14    188       C  
ATOM    456  N   VAL A 463       8.687  35.936  20.517  1.00 24.42           N  
ANISOU  456  N   VAL A 463     3055   3356   2867     40     17     -2       N  
ATOM    457  CA  VAL A 463       9.979  36.490  20.183  1.00 23.89           C  
ANISOU  457  CA  VAL A 463     2968   3092   3014   -100     47     25       C  
ATOM    458  C   VAL A 463       9.865  37.057  18.778  1.00 24.19           C  
ANISOU  458  C   VAL A 463     3054   3162   2975    -34    -65    -27       C  
ATOM    459  O   VAL A 463       8.937  36.713  18.050  1.00 26.20           O  
ANISOU  459  O   VAL A 463     3201   3855   2897   -164    -12    155       O  
ATOM    460  CB  VAL A 463      11.130  35.440  20.158  1.00 24.10           C  
ANISOU  460  CB  VAL A 463     2991   3094   3071    -84    123    158       C  
ATOM    461  CG1 VAL A 463      11.364  34.820  21.533  1.00 24.15           C  
ANISOU  461  CG1 VAL A 463     2938   3219   3019   -250   -109    -49       C  
ATOM    462  CG2 VAL A 463      10.874  34.369  19.062  1.00 22.78           C  
ANISOU  462  CG2 VAL A 463     2722   2869   3062   -143    235    254       C  
ATOM    463  N   ASP A 464      10.740  37.988  18.461  1.00 23.37           N  
ANISOU  463  N   ASP A 464     2821   3223   2835   -137    -28    -25       N  
ATOM    464  CA  ASP A 464      10.915  38.478  17.101  1.00 23.60           C  
ANISOU  464  CA  ASP A 464     2872   3116   2977    -70    -42     66       C  
ATOM    465  C   ASP A 464      12.108  37.762  16.504  1.00 24.93           C  
ANISOU  465  C   ASP A 464     3269   3316   2886    -16      0     37       C  
ATOM    466  O   ASP A 464      13.188  37.862  17.052  1.00 26.26           O  
ANISOU  466  O   ASP A 464     3121   3985   2872   -182     86   -125       O  
ATOM    467  CB  ASP A 464      11.137  40.008  17.141  1.00 26.08           C  
ANISOU  467  CB  ASP A 464     3370   3482   3054    -26    -10     39       C  
ATOM    468  CG  ASP A 464       9.965  40.729  17.756  1.00 26.97           C  
ANISOU  468  CG  ASP A 464     3228   3364   3655     84   -426   -112       C  
ATOM    469  OD1 ASP A 464       8.852  40.372  17.412  1.00 29.90           O  
ANISOU  469  OD1 ASP A 464     3334   4359   3665   -260   -450   -322       O  
ATOM    470  OD2 ASP A 464      10.032  41.635  18.620  1.00 35.16           O  
ANISOU  470  OD2 ASP A 464     4329   4598   4432    548   -458   -451       O  
ATOM    471  N   LYS A 465      11.916  37.052  15.395  1.00 25.64           N  
ANISOU  471  N   LYS A 465     3412   3294   3034    -32     -1    -15       N  
ATOM    472  CA  LYS A 465      12.999  36.308  14.738  1.00 24.84           C  
ANISOU  472  CA  LYS A 465     3182   3181   3074    -33     32     17       C  
ATOM    473  C   LYS A 465      13.478  37.116  13.539  1.00 25.75           C  
ANISOU  473  C   LYS A 465     3366   3223   3194    -19     -5     60       C  
ATOM    474  O   LYS A 465      12.716  37.381  12.613  1.00 26.35           O  
ANISOU  474  O   LYS A 465     3839   3295   2877   -231    116    236       O  
ATOM    475  CB  LYS A 465      12.552  34.940  14.250  1.00 26.73           C  
ANISOU  475  CB  LYS A 465     3634   3294   3228     74     61    113       C  
ATOM    476  CG  LYS A 465      13.583  34.194  13.453  1.00 27.60           C  
ANISOU  476  CG  LYS A 465     3618   3381   3487    108     25   -114       C  
ATOM    477  CD  LYS A 465      13.289  32.650  13.402  1.00 25.05           C  
ANISOU  477  CD  LYS A 465     3135   3281   3099    -11     40     65       C  
ATOM    478  CE  LYS A 465      11.894  32.343  12.887  1.00 25.40           C  
ANISOU  478  CE  LYS A 465     3259   3091   3301    116    -89   -136       C  
ATOM    479  NZ  LYS A 465      11.550  32.793  11.488  1.00 26.19           N  
ANISOU  479  NZ  LYS A 465     4100   3239   2612    164    -30    153       N  
ATOM    480  N   ARG A 466      14.723  37.544  13.633  1.00 27.05           N  
ANISOU  480  N   ARG A 466     3482   3368   3427     55    128    106       N  
ATOM    481  CA  ARG A 466      15.351  38.364  12.620  1.00 27.64           C  
ANISOU  481  CA  ARG A 466     3580   3471   3451     40     87     86       C  
ATOM    482  C   ARG A 466      15.772  37.511  11.449  1.00 28.45           C  
ANISOU  482  C   ARG A 466     3781   3472   3553     56    138     71       C  
ATOM    483  O   ARG A 466      16.386  36.456  11.643  1.00 27.82           O  
ANISOU  483  O   ARG A 466     3951   3122   3494    328    240    217       O  
ATOM    484  CB  ARG A 466      16.603  38.999  13.203  1.00 28.76           C  
ANISOU  484  CB  ARG A 466     3751   3557   3618     20      1     48       C  
ATOM    485  CG  ARG A 466      16.296  40.063  14.200  1.00 30.82           C  
ANISOU  485  CG  ARG A 466     3929   3934   3844     30    109     18       C  
ATOM    486  CD  ARG A 466      16.201  41.455  13.581  1.00 33.28           C  
ANISOU  486  CD  ARG A 466     4226   4080   4338    128     -7    -25       C  
ATOM    487  NE  ARG A 466      17.540  41.913  13.242  1.00 34.97           N  
ANISOU  487  NE  ARG A 466     4812   4371   4101    243    228    191       N  
ATOM    488  CZ  ARG A 466      18.030  42.007  12.017  1.00 37.84           C  
ANISOU  488  CZ  ARG A 466     4933   4649   4794     79    130     84       C  
ATOM    489  NH1 ARG A 466      17.285  41.760  10.945  1.00 37.22           N  
ANISOU  489  NH1 ARG A 466     4855   4772   4512    -15   -153    -79       N  
ATOM    490  NH2 ARG A 466      19.273  42.412  11.868  1.00 37.64           N  
ANISOU  490  NH2 ARG A 466     4530   4675   5094     42    -54    156       N  
ATOM    491  N   LYS A 467      15.472  37.974  10.236  1.00 29.38           N  
ANISOU  491  N   LYS A 467     3991   3559   3612     75    155      1       N  
ATOM    492  CA  LYS A 467      15.916  37.300   9.007  1.00 29.97           C  
ANISOU  492  CA  LYS A 467     3895   3749   3741     43    187     23       C  
ATOM    493  C   LYS A 467      15.788  38.380   7.915  1.00 30.08           C  
ANISOU  493  C   LYS A 467     3893   3820   3713     72    239     60       C  
ATOM    494  O   LYS A 467      14.726  39.000   7.737  1.00 29.18           O  
ANISOU  494  O   LYS A 467     3613   3955   3517     85    338    312       O  
ATOM    495  CB  LYS A 467      15.035  36.085   8.707  1.00 30.49           C  
ANISOU  495  CB  LYS A 467     4011   3802   3772     24    185    -14       C  
ATOM    496  CG  LYS A 467      15.560  34.990   7.742  1.00 31.46           C  
ANISOU  496  CG  LYS A 467     4050   3793   4107      8     38    -68       C  
ATOM    497  CD  LYS A 467      17.073  34.819   7.757  1.00 32.47           C  
ANISOU  497  CD  LYS A 467     4099   4078   4160     83     31     14       C  
ATOM    498  CE  LYS A 467      17.523  33.557   7.050  1.00 34.22           C  
ANISOU  498  CE  LYS A 467     4693   4033   4274    -59    -24      9       C  
ATOM    499  NZ  LYS A 467      17.459  33.620   5.549  1.00 36.24           N  
ANISOU  499  NZ  LYS A 467     4812   4362   4596   -253    377     18       N  
ATOM    500  N   GLY A 468      16.873  38.671   7.224  1.00 30.34           N  
ANISOU  500  N   GLY A 468     3936   3782   3808     32    187    -33       N  
ATOM    501  CA  GLY A 468      16.853  39.767   6.291  1.00 28.45           C  
ANISOU  501  CA  GLY A 468     3671   3572   3567     63     89     46       C  
ATOM    502  C   GLY A 468      17.043  41.047   7.066  1.00 26.53           C  
ANISOU  502  C   GLY A 468     3426   3383   3269     46     87     30       C  
ATOM    503  O   GLY A 468      17.704  41.038   8.103  1.00 28.76           O  
ANISOU  503  O   GLY A 468     3976   3336   3613    209    -28    125       O  
ATOM    504  N   LEU A 469      16.568  42.171   6.541  1.00 26.21           N  
ANISOU  504  N   LEU A 469     3246   3375   3338    123     91   -103       N  
ATOM    505  CA  LEU A 469      16.721  43.436   7.247  1.00 25.26           C  
ANISOU  505  CA  LEU A 469     3136   3245   3216    101      1     31       C  
ATOM    506  C   LEU A 469      15.856  43.498   8.483  1.00 24.73           C  
ANISOU  506  C   LEU A 469     3024   3178   3194    123    -13    -14       C  
ATOM    507  O   LEU A 469      16.156  44.258   9.387  1.00 26.32           O  
ANISOU  507  O   LEU A 469     3253   3551   3195    209    -20    -75       O  
ATOM    508  CB  LEU A 469      16.316  44.627   6.358  1.00 25.32           C  
ANISOU  508  CB  LEU A 469     3200   3208   3213     91     27     47       C  
ATOM    509  CG  LEU A 469      17.250  44.963   5.217  1.00 26.75           C  
ANISOU  509  CG  LEU A 469     3362   3591   3211     54    -57     32       C  
ATOM    510  CD1 LEU A 469      16.677  46.156   4.424  1.00 28.75           C  
ANISOU  510  CD1 LEU A 469     3748   3528   3648     71     90     47       C  
ATOM    511  CD2 LEU A 469      18.611  45.270   5.790  1.00 26.88           C  
ANISOU  511  CD2 LEU A 469     3112   3577   3523    -87      0   -175       C  
ATOM    512  N   PHE A 470      14.725  42.801   8.493  1.00 24.19           N  
ANISOU  512  N   PHE A 470     2956   3095   3138     25    -22    -54       N  
ATOM    513  CA  PHE A 470      13.811  42.965   9.621  1.00 24.62           C  
ANISOU  513  CA  PHE A 470     2991   3129   3232    -42    -44    112       C  
ATOM    514  C   PHE A 470      13.523  41.645  10.358  1.00 24.94           C  
ANISOU  514  C   PHE A 470     3052   3153   3270     43      1    197       C  
ATOM    515  O   PHE A 470      14.448  40.854  10.599  1.00 27.19           O  
ANISOU  515  O   PHE A 470     3166   3559   3604   -152    151    389       O  
ATOM    516  CB  PHE A 470      12.590  43.737   9.140  1.00 23.38           C  
ANISOU  516  CB  PHE A 470     2688   3131   3063    -83   -123    -47       C  
ATOM    517  CG  PHE A 470      12.973  45.030   8.456  1.00 22.89           C  
ANISOU  517  CG  PHE A 470     2560   3087   3049     72   -531      7       C  
ATOM    518  CD1 PHE A 470      13.651  46.027   9.164  1.00 25.19           C  
ANISOU  518  CD1 PHE A 470     2852   3683   3035    109   -248   -107       C  
ATOM    519  CD2 PHE A 470      12.789  45.218   7.077  1.00 27.29           C  
ANISOU  519  CD2 PHE A 470     3460   3547   3360    -25   -119    -71       C  
ATOM    520  CE1 PHE A 470      14.049  47.211   8.554  1.00 24.92           C  
ANISOU  520  CE1 PHE A 470     2979   3303   3184    181   -274   -314       C  
ATOM    521  CE2 PHE A 470      13.192  46.402   6.448  1.00 25.01           C  
ANISOU  521  CE2 PHE A 470     2963   3495   3044    300   -153     27       C  
ATOM    522  CZ  PHE A 470      13.838  47.400   7.184  1.00 24.36           C  
ANISOU  522  CZ  PHE A 470     2625   3489   3140    462    166      8       C  
ATOM    523  N   ALA A 471      12.264  41.425  10.705  1.00 25.17           N  
ANISOU  523  N   ALA A 471     3099   3226   3235    -57    112    263       N  
ATOM    524  CA  ALA A 471      11.896  40.280  11.545  1.00 24.89           C  
ANISOU  524  CA  ALA A 471     3088   3222   3144     -8    126     61       C  
ATOM    525  C   ALA A 471      10.415  39.962  11.445  1.00 25.30           C  
ANISOU  525  C   ALA A 471     3235   3324   3053     36    102     70       C  
ATOM    526  O   ALA A 471       9.597  40.721  10.880  1.00 25.61           O  
ANISOU  526  O   ALA A 471     3488   3200   3042    226    337    293       O  
ATOM    527  CB  ALA A 471      12.284  40.554  12.968  1.00 25.90           C  
ANISOU  527  CB  ALA A 471     3178   3412   3251     57     67    313       C  
ATOM    528  N   ARG A 472      10.050  38.862  12.078  1.00 25.46           N  
ANISOU  528  N   ARG A 472     3437   3190   3046     10     27     27       N  
ATOM    529  CA  ARG A 472       8.668  38.445  12.169  1.00 25.51           C  
ANISOU  529  CA  ARG A 472     3333   3315   3044    -21     43     25       C  
ATOM    530  C   ARG A 472       8.426  38.009  13.624  1.00 25.17           C  
ANISOU  530  C   ARG A 472     3386   3183   2994     -5     80     81       C  
ATOM    531  O   ARG A 472       9.306  37.393  14.221  1.00 25.34           O  
ANISOU  531  O   ARG A 472     3567   3300   2758     97    116    128       O  
ATOM    532  CB  ARG A 472       8.394  37.265  11.238  1.00 26.42           C  
ANISOU  532  CB  ARG A 472     3401   3478   3155    104     38     62       C  
ATOM    533  CG  ARG A 472       8.525  37.647   9.762  1.00 25.96           C  
ANISOU  533  CG  ARG A 472     3468   3428   2966    -82    -93   -120       C  
ATOM    534  CD  ARG A 472       7.517  38.663   9.294  1.00 26.39           C  
ANISOU  534  CD  ARG A 472     3628   3278   3118    120     -6     43       C  
ATOM    535  NE  ARG A 472       7.622  38.939   7.846  1.00 27.63           N  
ANISOU  535  NE  ARG A 472     3714   3570   3213    477     84    160       N  
ATOM    536  CZ  ARG A 472       7.023  39.946   7.230  1.00 31.37           C  
ANISOU  536  CZ  ARG A 472     4411   3913   3594    144     79    -12       C  
ATOM    537  NH1 ARG A 472       6.315  40.830   7.921  1.00 31.79           N  
ANISOU  537  NH1 ARG A 472     4329   4200   3547    163    236    -36       N  
ATOM    538  NH2 ARG A 472       7.164  40.107   5.916  1.00 31.09           N  
ANISOU  538  NH2 ARG A 472     4541   3795   3475     92    267   -148       N  
ATOM    539  N   ARG A 473       7.307  38.433  14.201  1.00 24.44           N  
ANISOU  539  N   ARG A 473     3137   3151   2996    -73     66    136       N  
ATOM    540  CA  ARG A 473       6.940  38.020  15.548  1.00 24.98           C  
ANISOU  540  CA  ARG A 473     3259   3160   3073    -73     31      3       C  
ATOM    541  C   ARG A 473       6.392  36.579  15.479  1.00 24.53           C  
ANISOU  541  C   ARG A 473     3230   3170   2917    -79     72      0       C  
ATOM    542  O   ARG A 473       5.425  36.287  14.727  1.00 25.42           O  
ANISOU  542  O   ARG A 473     3579   3123   2954    -96     32     71       O  
ATOM    543  CB  ARG A 473       5.869  38.935  16.098  1.00 24.91           C  
ANISOU  543  CB  ARG A 473     3205   3407   2849   -162     70    -80       C  
ATOM    544  CG  ARG A 473       5.179  38.449  17.361  1.00 28.30           C  
ANISOU  544  CG  ARG A 473     3565   3567   3619   -148     12     59       C  
ATOM    545  CD  ARG A 473       6.078  38.333  18.498  1.00 30.60           C  
ANISOU  545  CD  ARG A 473     3909   3983   3732    -18    186    -87       C  
ATOM    546  NE  ARG A 473       6.783  39.559  18.869  1.00 30.50           N  
ANISOU  546  NE  ARG A 473     3359   4231   3997    -36    384    132       N  
ATOM    547  CZ  ARG A 473       6.358  40.446  19.772  1.00 32.03           C  
ANISOU  547  CZ  ARG A 473     3658   4099   4411   -183     46     -3       C  
ATOM    548  NH1 ARG A 473       5.147  40.343  20.356  1.00 33.41           N  
ANISOU  548  NH1 ARG A 473     3668   4538   4488    -97    217     48       N  
ATOM    549  NH2 ARG A 473       7.125  41.487  20.048  1.00 37.22           N  
ANISOU  549  NH2 ARG A 473     4824   4700   4615   -144   -102   -206       N  
ATOM    550  N   ARG A 474       6.984  35.697  16.292  1.00 25.10           N  
ANISOU  550  N   ARG A 474     3320   3177   3037    -92     15    -29       N  
ATOM    551  CA  ARG A 474       6.527  34.310  16.361  1.00 25.28           C  
ANISOU  551  CA  ARG A 474     3381   3240   2982    -95     48     70       C  
ATOM    552  C   ARG A 474       6.341  33.866  17.821  1.00 26.07           C  
ANISOU  552  C   ARG A 474     3408   3429   3068   -142     51     45       C  
ATOM    553  O   ARG A 474       6.952  34.431  18.723  1.00 26.07           O  
ANISOU  553  O   ARG A 474     3457   3820   2629   -103    -42    120       O  
ATOM    554  CB  ARG A 474       7.541  33.404  15.724  1.00 26.09           C  
ANISOU  554  CB  ARG A 474     3454   3291   3167   -244     89     20       C  
ATOM    555  CG  ARG A 474       7.828  33.738  14.256  1.00 26.91           C  
ANISOU  555  CG  ARG A 474     3637   3443   3143     52    117    111       C  
ATOM    556  CD  ARG A 474       6.752  33.250  13.389  1.00 28.06           C  
ANISOU  556  CD  ARG A 474     3756   3637   3266    125   -110    235       C  
ATOM    557  NE  ARG A 474       6.813  33.656  11.995  1.00 26.70           N  
ANISOU  557  NE  ARG A 474     3452   3452   3240   -309    101    211       N  
ATOM    558  CZ  ARG A 474       6.000  34.553  11.418  1.00 28.85           C  
ANISOU  558  CZ  ARG A 474     3650   3780   3532   -163     70    266       C  
ATOM    559  NH1 ARG A 474       5.076  35.220  12.097  1.00 25.28           N  
ANISOU  559  NH1 ARG A 474     3517   3327   2758   -207    161    134       N  
ATOM    560  NH2 ARG A 474       6.104  34.755  10.120  1.00 29.79           N  
ANISOU  560  NH2 ARG A 474     4031   3959   3327     43     96    274       N  
ATOM    561  N   GLN A 475       5.475  32.890  18.033  1.00 25.97           N  
ANISOU  561  N   GLN A 475     3334   3345   3186   -122     31     54       N  
ATOM    562  CA  GLN A 475       5.358  32.263  19.328  1.00 26.28           C  
ANISOU  562  CA  GLN A 475     3414   3298   3271   -137     74     41       C  
ATOM    563  C   GLN A 475       6.379  31.127  19.277  1.00 26.48           C  
ANISOU  563  C   GLN A 475     3427   3343   3290   -132     49    116       C  
ATOM    564  O   GLN A 475       6.299  30.248  18.378  1.00 26.84           O  
ANISOU  564  O   GLN A 475     3629   3059   3511   -271     14    113       O  
ATOM    565  CB  GLN A 475       3.951  31.736  19.558  1.00 27.52           C  
ANISOU  565  CB  GLN A 475     3574   3476   3405    -54     42    -12       C  
ATOM    566  CG  GLN A 475       3.744  31.048  20.935  1.00 26.60           C  
ANISOU  566  CG  GLN A 475     3479   3340   3287     27    289    116       C  
ATOM    567  CD  GLN A 475       3.728  32.027  22.101  1.00 27.52           C  
ANISOU  567  CD  GLN A 475     3088   3832   3535    111   -130    314       C  
ATOM    568  OE1 GLN A 475       3.821  33.245  21.890  1.00 28.57           O  
ANISOU  568  OE1 GLN A 475     3605   3733   3517    -39    161    512       O  
ATOM    569  NE2 GLN A 475       3.472  31.514  23.313  1.00 29.96           N  
ANISOU  569  NE2 GLN A 475     3483   4747   3150    655   -174    -26       N  
ATOM    570  N   LEU A 476       7.371  31.171  20.177  1.00 26.61           N  
ANISOU  570  N   LEU A 476     3547   3321   3240    -55     23     79       N  
ATOM    571  CA  LEU A 476       8.414  30.146  20.236  1.00 25.36           C  
ANISOU  571  CA  LEU A 476     3268   3271   3095    -55      1    114       C  
ATOM    572  C   LEU A 476       8.031  29.133  21.336  1.00 25.34           C  
ANISOU  572  C   LEU A 476     3281   3218   3128     -5      9    155       C  
ATOM    573  O   LEU A 476       7.708  29.560  22.443  1.00 25.63           O  
ANISOU  573  O   LEU A 476     3455   3253   3028    120    108    302       O  
ATOM    574  CB  LEU A 476       9.727  30.767  20.626  1.00 24.99           C  
ANISOU  574  CB  LEU A 476     3335   3203   2957   -103     52    148       C  
ATOM    575  CG  LEU A 476      10.976  29.887  20.573  1.00 26.99           C  
ANISOU  575  CG  LEU A 476     3519   3390   3343   -112    157    107       C  
ATOM    576  CD1 LEU A 476      11.242  29.276  19.202  1.00 27.18           C  
ANISOU  576  CD1 LEU A 476     3672   3351   3302   -204    217     35       C  
ATOM    577  CD2 LEU A 476      12.159  30.725  21.007  1.00 25.63           C  
ANISOU  577  CD2 LEU A 476     3357   3282   3098     94     24     52       C  
ATOM    578  N   LEU A 477       8.179  27.828  21.042  1.00 24.56           N  
ANISOU  578  N   LEU A 477     3233   3171   2926    -77     -6     23       N  
ATOM    579  CA  LEU A 477       7.723  26.783  21.940  1.00 25.52           C  
ANISOU  579  CA  LEU A 477     3209   3274   3211      1    -41     45       C  
ATOM    580  C   LEU A 477       8.803  25.716  22.077  1.00 25.67           C  
ANISOU  580  C   LEU A 477     3235   3350   3169     17     53     58       C  
ATOM    581  O   LEU A 477       9.149  25.040  21.118  1.00 26.33           O  
ANISOU  581  O   LEU A 477     3555   3509   2938    162   -250    -33       O  
ATOM    582  CB  LEU A 477       6.418  26.161  21.415  1.00 25.72           C  
ANISOU  582  CB  LEU A 477     3103   3451   3218    -98      9     92       C  
ATOM    583  CG  LEU A 477       5.230  27.140  21.228  1.00 27.79           C  
ANISOU  583  CG  LEU A 477     3419   3597   3543    -12    148     71       C  
ATOM    584  CD1 LEU A 477       4.778  27.178  19.766  1.00 30.97           C  
ANISOU  584  CD1 LEU A 477     4020   3717   4030    -14    -19    214       C  
ATOM    585  CD2 LEU A 477       4.045  26.860  22.159  1.00 27.73           C  
ANISOU  585  CD2 LEU A 477     3764   3357   3413    -95    231    129       C  
ATOM    586  N   LEU A 478       9.324  25.604  23.297  1.00 23.96           N  
ANISOU  586  N   LEU A 478     2995   3124   2984      1      0      8       N  
ATOM    587  CA  LEU A 478      10.322  24.592  23.634  1.00 24.53           C  
ANISOU  587  CA  LEU A 478     2923   3294   3102      2    137     79       C  
ATOM    588  C   LEU A 478       9.551  23.454  24.259  1.00 24.18           C  
ANISOU  588  C   LEU A 478     2869   3179   3138    -14      6     30       C  
ATOM    589  O   LEU A 478       8.893  23.724  25.238  1.00 24.46           O  
ANISOU  589  O   LEU A 478     2701   3357   3233   -317    359    131       O  
ATOM    590  CB  LEU A 478      11.299  25.154  24.651  1.00 25.04           C  
ANISOU  590  CB  LEU A 478     2908   3297   3309     17    226     15       C  
ATOM    591  CG  LEU A 478      12.340  24.218  25.279  1.00 25.01           C  
ANISOU  591  CG  LEU A 478     2534   3625   3341    -59   -162    -35       C  
ATOM    592  CD1 LEU A 478      13.278  23.580  24.229  1.00 27.21           C  
ANISOU  592  CD1 LEU A 478     3325   3557   3456    200     37     22       C  
ATOM    593  CD2 LEU A 478      13.195  25.042  26.284  1.00 27.73           C  
ANISOU  593  CD2 LEU A 478     3533   3507   3496   -118    -64     34       C  
ATOM    594  N   THR A 479       9.694  22.223  23.769  1.00 24.01           N  
ANISOU  594  N   THR A 479     2936   3149   3035    -13     86     36       N  
ATOM    595  CA  THR A 479       8.855  21.119  24.205  1.00 24.34           C  
ANISOU  595  CA  THR A 479     3108   3111   3029    -10    -43    -19       C  
ATOM    596  C   THR A 479       9.694  19.871  24.461  1.00 24.36           C  
ANISOU  596  C   THR A 479     2836   3175   3243    -27     30     62       C  
ATOM    597  O   THR A 479      10.887  19.794  24.106  1.00 23.57           O  
ANISOU  597  O   THR A 479     2364   3239   3350   -211   -204     75       O  
ATOM    598  CB  THR A 479       7.793  20.767  23.140  1.00 24.71           C  
ANISOU  598  CB  THR A 479     2806   3323   3257      8     39     69       C  
ATOM    599  OG1 THR A 479       8.422  20.081  22.048  1.00 26.35           O  
ANISOU  599  OG1 THR A 479     3541   3455   3013   -165   -124   -189       O  
ATOM    600  CG2 THR A 479       7.130  21.991  22.493  1.00 26.74           C  
ANISOU  600  CG2 THR A 479     3188   3529   3443   -167     57    179       C  
ATOM    601  N   GLU A 480       9.071  18.877  25.091  1.00 25.95           N  
ANISOU  601  N   GLU A 480     3014   3265   3581    -94    -27    109       N  
ATOM    602  CA  GLU A 480       9.702  17.569  25.178  1.00 27.92           C  
ANISOU  602  CA  GLU A 480     3555   3368   3684   -171     71     85       C  
ATOM    603  C   GLU A 480      10.001  17.097  23.784  1.00 28.24           C  
ANISOU  603  C   GLU A 480     3582   3379   3767   -118    -41     -7       C  
ATOM    604  O   GLU A 480       9.403  17.573  22.776  1.00 28.95           O  
ANISOU  604  O   GLU A 480     4050   3091   3855   -258    -45   -113       O  
ATOM    605  CB  GLU A 480       8.808  16.560  25.902  1.00 29.45           C  
ANISOU  605  CB  GLU A 480     3638   3615   3933   -147     14     42       C  
ATOM    606  CG  GLU A 480       7.536  16.223  25.209  1.00 31.89           C  
ANISOU  606  CG  GLU A 480     3986   3949   4180   -271    165    110       C  
ATOM    607  CD  GLU A 480       6.711  15.244  26.034  1.00 30.06           C  
ANISOU  607  CD  GLU A 480     3945   3473   4002   -212    153    294       C  
ATOM    608  OE1 GLU A 480       7.272  14.274  26.596  1.00 35.71           O  
ANISOU  608  OE1 GLU A 480     4652   3750   5166   -224    492    193       O  
ATOM    609  OE2 GLU A 480       5.505  15.478  26.111  1.00 28.15           O  
ANISOU  609  OE2 GLU A 480     3152   3438   4105   -474    146     82       O  
ATOM    610  N   GLY A 481      10.976  16.191  23.711  1.00 27.35           N  
ANISOU  610  N   GLY A 481     3434   3380   3578    -25     19     13       N  
ATOM    611  CA  GLY A 481      11.461  15.744  22.404  1.00 27.66           C  
ANISOU  611  CA  GLY A 481     3640   3353   3515     44     28    -12       C  
ATOM    612  C   GLY A 481      12.964  15.672  22.466  1.00 27.40           C  
ANISOU  612  C   GLY A 481     3674   3326   3411    -25    -62      5       C  
ATOM    613  O   GLY A 481      13.522  14.576  22.462  1.00 29.16           O  
ANISOU  613  O   GLY A 481     4131   3409   3539    -34    177    -79       O  
ATOM    614  N   PRO A 482      13.660  16.815  22.520  1.00 27.91           N  
ANISOU  614  N   PRO A 482     3815   3423   3366     32    -49     67       N  
ATOM    615  CA  PRO A 482      13.043  18.150  22.518  1.00 27.57           C  
ANISOU  615  CA  PRO A 482     3696   3331   3448     30    -13    -46       C  
ATOM    616  C   PRO A 482      12.715  18.677  21.108  1.00 27.39           C  
ANISOU  616  C   PRO A 482     3666   3343   3398     64    -61    -50       C  
ATOM    617  O   PRO A 482      13.197  18.150  20.109  1.00 28.00           O  
ANISOU  617  O   PRO A 482     3829   3382   3426    280     69    -21       O  
ATOM    618  CB  PRO A 482      14.134  19.010  23.119  1.00 26.62           C  
ANISOU  618  CB  PRO A 482     3542   3246   3324    -42    114     97       C  
ATOM    619  CG  PRO A 482      15.392  18.382  22.604  1.00 28.85           C  
ANISOU  619  CG  PRO A 482     3819   3604   3536     94   -127     42       C  
ATOM    620  CD  PRO A 482      15.109  16.890  22.675  1.00 27.70           C  
ANISOU  620  CD  PRO A 482     3852   3412   3260     14    -72    -67       C  
ATOM    621  N   HIS A 483      11.883  19.715  21.067  1.00 27.00           N  
ANISOU  621  N   HIS A 483     3624   3234   3398     75     15   -105       N  
ATOM    622  CA  HIS A 483      11.625  20.523  19.894  1.00 27.22           C  
ANISOU  622  CA  HIS A 483     3584   3308   3449    -19      0    -81       C  
ATOM    623  C   HIS A 483      11.663  22.004  20.277  1.00 26.90           C  
ANISOU  623  C   HIS A 483     3548   3236   3437     10     19    -32       C  
ATOM    624  O   HIS A 483      11.442  22.390  21.427  1.00 26.20           O  
ANISOU  624  O   HIS A 483     3640   3160   3153    -16    -75     36       O  
ATOM    625  CB  HIS A 483      10.240  20.259  19.320  1.00 28.46           C  
ANISOU  625  CB  HIS A 483     3744   3502   3567     50     27    -35       C  
ATOM    626  CG  HIS A 483      10.076  18.876  18.786  1.00 28.17           C  
ANISOU  626  CG  HIS A 483     3869   3441   3392    -62   -168   -317       C  
ATOM    627  ND1 HIS A 483      10.257  18.556  17.456  1.00 31.62           N  
ANISOU  627  ND1 HIS A 483     4621   3324   4067     40   -201   -349       N  
ATOM    628  CD2 HIS A 483       9.754  17.725  19.417  1.00 29.16           C  
ANISOU  628  CD2 HIS A 483     3348   3909   3823    232   -432   -100       C  
ATOM    629  CE1 HIS A 483      10.083  17.250  17.303  1.00 33.06           C  
ANISOU  629  CE1 HIS A 483     4778   4086   3696   -347   -253   -232       C  
ATOM    630  NE2 HIS A 483       9.769  16.726  18.478  1.00 33.26           N  
ANISOU  630  NE2 HIS A 483     4803   3706   4125   -163   -476    -89       N  
ATOM    631  N   LEU A 484      11.897  22.813  19.258  1.00 27.22           N  
ANISOU  631  N   LEU A 484     3635   3343   3364    -43    118      0       N  
ATOM    632  CA  LEU A 484      11.690  24.283  19.352  1.00 26.99           C  
ANISOU  632  CA  LEU A 484     3611   3330   3314    -83     93     11       C  
ATOM    633  C   LEU A 484      10.888  24.623  18.129  1.00 28.04           C  
ANISOU  633  C   LEU A 484     3742   3495   3417   -113    109     -9       C  
ATOM    634  O   LEU A 484      11.455  24.650  17.029  1.00 29.01           O  
ANISOU  634  O   LEU A 484     4110   3768   3143   -194    265     19       O  
ATOM    635  CB  LEU A 484      13.021  25.041  19.321  1.00 26.79           C  
ANISOU  635  CB  LEU A 484     3505   3438   3236    -69     69    -26       C  
ATOM    636  CG  LEU A 484      13.752  25.314  20.634  1.00 28.06           C  
ANISOU  636  CG  LEU A 484     3607   3508   3544   -287      0     81       C  
ATOM    637  CD1 LEU A 484      15.272  25.605  20.574  1.00 27.34           C  
ANISOU  637  CD1 LEU A 484     3283   3614   3488    125     -5   -168       C  
ATOM    638  CD2 LEU A 484      12.999  26.376  21.365  1.00 27.21           C  
ANISOU  638  CD2 LEU A 484     3609   3388   3339   -304    139     29       C  
ATOM    639  N   TYR A 485       9.573  24.750  18.303  1.00 27.25           N  
ANISOU  639  N   TYR A 485     3684   3404   3265    -18    101     55       N  
ATOM    640  CA  TYR A 485       8.652  25.167  17.245  1.00 27.08           C  
ANISOU  640  CA  TYR A 485     3495   3390   3403    -47     -6    -73       C  
ATOM    641  C   TYR A 485       8.504  26.692  17.239  1.00 27.59           C  
ANISOU  641  C   TYR A 485     3665   3440   3377    -35   -108    -14       C  
ATOM    642  O   TYR A 485       8.543  27.332  18.304  1.00 28.30           O  
ANISOU  642  O   TYR A 485     4079   3349   3324     13     48   -121       O  
ATOM    643  CB  TYR A 485       7.268  24.579  17.451  1.00 27.47           C  
ANISOU  643  CB  TYR A 485     3592   3355   3489    -90    -36    -53       C  
ATOM    644  CG  TYR A 485       7.194  23.071  17.552  1.00 25.30           C  
ANISOU  644  CG  TYR A 485     3334   2984   3295   -364    -36    -20       C  
ATOM    645  CD1 TYR A 485       7.010  22.298  16.420  1.00 28.25           C  
ANISOU  645  CD1 TYR A 485     3959   3435   3339      6   -105     17       C  
ATOM    646  CD2 TYR A 485       7.223  22.428  18.793  1.00 26.57           C  
ANISOU  646  CD2 TYR A 485     3425   3228   3442   -200    -93     33       C  
ATOM    647  CE1 TYR A 485       6.883  20.882  16.502  1.00 28.57           C  
ANISOU  647  CE1 TYR A 485     4094   3228   3530   -639   -109   -256       C  
ATOM    648  CE2 TYR A 485       7.092  21.033  18.892  1.00 27.79           C  
ANISOU  648  CE2 TYR A 485     3875   3381   3302   -123    -76      6       C  
ATOM    649  CZ  TYR A 485       6.943  20.253  17.745  1.00 27.47           C  
ANISOU  649  CZ  TYR A 485     3613   3261   3563   -239   -139     24       C  
ATOM    650  OH  TYR A 485       6.824  18.876  17.874  1.00 29.17           O  
ANISOU  650  OH  TYR A 485     3981   3691   3411   -177    -63   -181       O  
ATOM    651  N   TYR A 486       8.305  27.277  16.058  1.00 27.83           N  
ANISOU  651  N   TYR A 486     3798   3445   3331    -98    -26    -70       N  
ATOM    652  CA  TYR A 486       7.829  28.656  16.023  1.00 28.11           C  
ANISOU  652  CA  TYR A 486     3703   3542   3436    -50    -64     21       C  
ATOM    653  C   TYR A 486       6.574  28.789  15.148  1.00 28.37           C  
ANISOU  653  C   TYR A 486     3705   3545   3527   -140    -36     -1       C  
ATOM    654  O   TYR A 486       6.497  28.236  14.059  1.00 29.14           O  
ANISOU  654  O   TYR A 486     3914   3728   3428   -268    -80      9       O  
ATOM    655  CB  TYR A 486       8.943  29.642  15.632  1.00 27.82           C  
ANISOU  655  CB  TYR A 486     3670   3497   3400   -133    -59   -128       C  
ATOM    656  CG  TYR A 486       9.720  29.298  14.393  1.00 28.89           C  
ANISOU  656  CG  TYR A 486     3785   3484   3708   -128    -37    -28       C  
ATOM    657  CD1 TYR A 486      10.919  28.541  14.462  1.00 26.69           C  
ANISOU  657  CD1 TYR A 486     3385   3308   3448    183    -31    -25       C  
ATOM    658  CD2 TYR A 486       9.289  29.734  13.157  1.00 29.77           C  
ANISOU  658  CD2 TYR A 486     3935   3735   3641    -70   -146   -142       C  
ATOM    659  CE1 TYR A 486      11.624  28.217  13.321  1.00 29.16           C  
ANISOU  659  CE1 TYR A 486     3749   3670   3659    -19   -142    -47       C  
ATOM    660  CE2 TYR A 486      10.018  29.435  12.006  1.00 28.03           C  
ANISOU  660  CE2 TYR A 486     3748   3625   3275    -25     85    -33       C  
ATOM    661  CZ  TYR A 486      11.160  28.671  12.091  1.00 26.80           C  
ANISOU  661  CZ  TYR A 486     3719   3196   3265    -89    -66   -109       C  
ATOM    662  OH  TYR A 486      11.836  28.380  10.963  1.00 29.15           O  
ANISOU  662  OH  TYR A 486     3921   3310   3843    -64    123    -23       O  
ATOM    663  N   VAL A 487       5.636  29.586  15.638  1.00 27.86           N  
ANISOU  663  N   VAL A 487     3701   3517   3367   -163    -30     53       N  
ATOM    664  CA  VAL A 487       4.324  29.677  15.092  1.00 28.03           C  
ANISOU  664  CA  VAL A 487     3624   3534   3489    -89    -58     22       C  
ATOM    665  C   VAL A 487       3.957  31.140  14.785  1.00 28.36           C  
ANISOU  665  C   VAL A 487     3726   3537   3513   -144    -48    114       C  
ATOM    666  O   VAL A 487       4.272  32.036  15.541  1.00 26.28           O  
ANISOU  666  O   VAL A 487     3710   3160   3114   -291   -146     66       O  
ATOM    667  CB  VAL A 487       3.329  29.180  16.142  1.00 28.11           C  
ANISOU  667  CB  VAL A 487     3520   3595   3564   -132    -51     70       C  
ATOM    668  CG1 VAL A 487       1.901  29.360  15.647  1.00 30.04           C  
ANISOU  668  CG1 VAL A 487     3628   3896   3888   -131    -74    -67       C  
ATOM    669  CG2 VAL A 487       3.596  27.719  16.511  1.00 29.26           C  
ANISOU  669  CG2 VAL A 487     3504   3939   3673    -87   -217     47       C  
ATOM    670  N   ASP A 488       3.249  31.354  13.685  1.00 28.95           N  
ANISOU  670  N   ASP A 488     3821   3571   3606   -152    -64     96       N  
ATOM    671  CA  ASP A 488       2.655  32.671  13.386  1.00 29.88           C  
ANISOU  671  CA  ASP A 488     3743   3877   3730      0    -74    156       C  
ATOM    672  C   ASP A 488       1.440  32.908  14.268  1.00 30.58           C  
ANISOU  672  C   ASP A 488     3868   3939   3809    -25   -120    146       C  
ATOM    673  O   ASP A 488       0.452  32.191  14.132  1.00 32.49           O  
ANISOU  673  O   ASP A 488     4110   4184   4049   -120    -67    282       O  
ATOM    674  CB  ASP A 488       2.313  32.704  11.899  1.00 30.28           C  
ANISOU  674  CB  ASP A 488     3832   3948   3725    -39    -77     95       C  
ATOM    675  CG  ASP A 488       1.613  33.952  11.476  1.00 30.23           C  
ANISOU  675  CG  ASP A 488     3978   3895   3612     17    -65    250       C  
ATOM    676  OD1 ASP A 488       1.132  34.746  12.336  1.00 31.27           O  
ANISOU  676  OD1 ASP A 488     4250   3613   4018    180   -473    625       O  
ATOM    677  OD2 ASP A 488       1.479  34.206  10.259  1.00 32.95           O  
ANISOU  677  OD2 ASP A 488     4796   4267   3456    239   -173    592       O  
ATOM    678  N   PRO A 489       1.510  33.857  15.202  1.00 31.65           N  
ANISOU  678  N   PRO A 489     3921   4102   4002     13    -69    134       N  
ATOM    679  CA  PRO A 489       0.448  33.992  16.201  1.00 32.90           C  
ANISOU  679  CA  PRO A 489     4079   4231   4188    -42    -24    106       C  
ATOM    680  C   PRO A 489      -0.782  34.702  15.701  1.00 33.73           C  
ANISOU  680  C   PRO A 489     4133   4412   4269    -47    -31    154       C  
ATOM    681  O   PRO A 489      -1.793  34.690  16.396  1.00 34.25           O  
ANISOU  681  O   PRO A 489     4160   4522   4328   -229     72    211       O  
ATOM    682  CB  PRO A 489       1.085  34.862  17.271  1.00 33.39           C  
ANISOU  682  CB  PRO A 489     4225   4289   4171     39    -38     59       C  
ATOM    683  CG  PRO A 489       2.064  35.720  16.508  1.00 32.94           C  
ANISOU  683  CG  PRO A 489     4095   4207   4211    -64    -52     10       C  
ATOM    684  CD  PRO A 489       2.594  34.835  15.427  1.00 32.00           C  
ANISOU  684  CD  PRO A 489     3997   4115   4046     42    -43     68       C  
ATOM    685  N   VAL A 490      -0.695  35.364  14.550  1.00 34.82           N  
ANISOU  685  N   VAL A 490     4285   4509   4433      3    -23    138       N  
ATOM    686  CA  VAL A 490      -1.873  36.055  14.002  1.00 35.11           C  
ANISOU  686  CA  VAL A 490     4399   4489   4449     28    -35     97       C  
ATOM    687  C   VAL A 490      -2.660  35.111  13.114  1.00 35.94           C  
ANISOU  687  C   VAL A 490     4531   4575   4547     10    -34    138       C  
ATOM    688  O   VAL A 490      -3.891  35.005  13.235  1.00 37.24           O  
ANISOU  688  O   VAL A 490     4602   4881   4664     87    -93    193       O  
ATOM    689  CB AVAL A 490      -1.536  37.379  13.256  0.50 35.36           C  
ANISOU  689  CB AVAL A 490     4484   4484   4466     13      8     82       C  
ATOM    690  CG1AVAL A 490      -0.479  38.178  14.004  0.50 33.85           C  
ANISOU  690  CG1AVAL A 490     4216   4312   4332     70    -54    111       C  
ATOM    691  CG2AVAL A 490      -1.127  37.153  11.800  0.50 35.86           C  
ANISOU  691  CG2AVAL A 490     4536   4568   4521      3      8      9       C  
ATOM    692  CB BVAL A 490      -1.449  37.269  13.170  0.50 34.97           C  
ANISOU  692  CB BVAL A 490     4426   4440   4420     23      2     90       C  
ATOM    693  CG1BVAL A 490      -2.666  37.919  12.484  0.50 33.69           C  
ANISOU  693  CG1BVAL A 490     4145   4329   4325     58    -46     99       C  
ATOM    694  CG2BVAL A 490      -0.696  38.272  14.034  0.50 33.52           C  
ANISOU  694  CG2BVAL A 490     4185   4286   4265     64    -90    120       C  
ATOM    695  N   ASN A 491      -1.960  34.431  12.214  1.00 36.14           N  
ANISOU  695  N   ASN A 491     4575   4518   4635      9    -35    137       N  
ATOM    696  CA  ASN A 491      -2.615  33.538  11.282  1.00 36.85           C  
ANISOU  696  CA  ASN A 491     4689   4581   4731    -46    -74    141       C  
ATOM    697  C   ASN A 491      -2.763  32.140  11.856  1.00 36.99           C  
ANISOU  697  C   ASN A 491     4706   4608   4738   -130    -86    108       C  
ATOM    698  O   ASN A 491      -3.477  31.322  11.292  1.00 36.94           O  
ANISOU  698  O   ASN A 491     4674   4559   4800   -241   -235    190       O  
ATOM    699  CB  ASN A 491      -1.847  33.519   9.974  1.00 37.45           C  
ANISOU  699  CB  ASN A 491     4762   4631   4834    -54    -35    127       C  
ATOM    700  CG  ASN A 491      -1.872  34.881   9.286  1.00 38.59           C  
ANISOU  700  CG  ASN A 491     4769   4742   5150    -25    -71    306       C  
ATOM    701  OD1 ASN A 491      -2.945  35.428   9.016  1.00 40.78           O  
ANISOU  701  OD1 ASN A 491     5013   4848   5630    -65     -6    358       O  
ATOM    702  ND2 ASN A 491      -0.695  35.460   9.058  1.00 39.97           N  
ANISOU  702  ND2 ASN A 491     4713   4754   5720     28    -19    534       N  
ATOM    703  N   LYS A 492      -2.109  31.889  12.986  1.00 35.87           N  
ANISOU  703  N   LYS A 492     4485   4514   4629   -154   -117    108       N  
ATOM    704  CA  LYS A 492      -2.259  30.641  13.716  1.00 36.20           C  
ANISOU  704  CA  LYS A 492     4556   4575   4621    -84    -80     36       C  
ATOM    705  C   LYS A 492      -1.842  29.482  12.822  1.00 35.79           C  
ANISOU  705  C   LYS A 492     4543   4514   4540    -91    -89     68       C  
ATOM    706  O   LYS A 492      -2.632  28.565  12.546  1.00 35.61           O  
ANISOU  706  O   LYS A 492     4244   4753   4530   -372   -188    -41       O  
ATOM    707  CB  LYS A 492      -3.703  30.461  14.194  1.00 36.89           C  
ANISOU  707  CB  LYS A 492     4651   4592   4772   -101    -36     37       C  
ATOM    708  CG  LYS A 492      -4.307  31.659  14.905  1.00 38.61           C  
ANISOU  708  CG  LYS A 492     4808   4940   4919    -61     -3     44       C  
ATOM    709  CD  LYS A 492      -3.562  31.997  16.178  1.00 39.59           C  
ANISOU  709  CD  LYS A 492     4951   5156   4932    -16    -74     -8       C  
ATOM    710  CE  LYS A 492      -4.333  32.992  17.030  0.02 40.14           C  
ANISOU  710  CE  LYS A 492     5059   5125   5067    -10    -15      0       C  
ATOM    711  NZ  LYS A 492      -4.562  34.279  16.321  0.02 40.33           N  
ANISOU  711  NZ  LYS A 492     5078   5159   5085     -2    -20     -6       N  
ATOM    712  N   VAL A 493      -0.607  29.548  12.352  1.00 34.01           N  
ANISOU  712  N   VAL A 493     4243   4353   4326    -94   -111     93       N  
ATOM    713  CA  VAL A 493      -0.011  28.494  11.532  1.00 33.60           C  
ANISOU  713  CA  VAL A 493     4259   4312   4192    -45    -83     55       C  
ATOM    714  C   VAL A 493       1.451  28.232  11.970  1.00 33.37           C  
ANISOU  714  C   VAL A 493     4181   4265   4233    -95    -95     21       C  
ATOM    715  O   VAL A 493       2.243  29.176  12.212  1.00 32.87           O  
ANISOU  715  O   VAL A 493     4148   4283   4054   -227   -403    124       O  
ATOM    716  CB AVAL A 493      -0.026  28.888  10.022  0.50 33.97           C  
ANISOU  716  CB AVAL A 493     4288   4336   4282     -2    -51     34       C  
ATOM    717  CG1AVAL A 493       0.047  30.393   9.857  0.50 33.02           C  
ANISOU  717  CG1AVAL A 493     4058   4258   4228    -50    -60     46       C  
ATOM    718  CG2AVAL A 493       1.118  28.224   9.233  0.50 33.70           C  
ANISOU  718  CG2AVAL A 493     4287   4332   4182      1    -31     52       C  
ATOM    719  CB BVAL A 493      -0.122  28.760   9.990  0.50 34.04           C  
ANISOU  719  CB BVAL A 493     4306   4341   4285     -3    -52     35       C  
ATOM    720  CG1BVAL A 493      -1.512  29.303   9.611  0.50 32.80           C  
ANISOU  720  CG1BVAL A 493     4108   4274   4081   -117   -105     16       C  
ATOM    721  CG2BVAL A 493       0.971  29.682   9.491  0.50 33.76           C  
ANISOU  721  CG2BVAL A 493     4319   4266   4239    -64    -67     53       C  
ATOM    722  N   LEU A 494       1.810  26.949  12.048  1.00 32.75           N  
ANISOU  722  N   LEU A 494     4114   4187   4143   -175    -59     54       N  
ATOM    723  CA  LEU A 494       3.187  26.561  12.310  1.00 32.94           C  
ANISOU  723  CA  LEU A 494     4175   4187   4152   -111    -63      0       C  
ATOM    724  C   LEU A 494       4.051  27.055  11.159  1.00 33.19           C  
ANISOU  724  C   LEU A 494     4206   4296   4107   -196    -78    -59       C  
ATOM    725  O   LEU A 494       3.730  26.784   9.997  1.00 34.84           O  
ANISOU  725  O   LEU A 494     4345   4607   4285   -320   -107     23       O  
ATOM    726  CB  LEU A 494       3.321  25.041  12.440  1.00 33.24           C  
ANISOU  726  CB  LEU A 494     4173   4291   4163   -176    -64    -82       C  
ATOM    727  CG  LEU A 494       4.734  24.537  12.686  1.00 33.71           C  
ANISOU  727  CG  LEU A 494     4312   4150   4343   -112   -151    -29       C  
ATOM    728  CD1 LEU A 494       5.209  25.013  14.072  1.00 33.19           C  
ANISOU  728  CD1 LEU A 494     4362   4227   4022    -33    -69    128       C  
ATOM    729  CD2 LEU A 494       4.841  23.022  12.587  1.00 34.31           C  
ANISOU  729  CD2 LEU A 494     4259   4375   4402   -113    -86    -44       C  
ATOM    730  N   LYS A 495       5.139  27.774  11.464  1.00 32.51           N  
ANISOU  730  N   LYS A 495     4097   4237   4018   -108   -109    -46       N  
ATOM    731  CA  LYS A 495       6.050  28.236  10.411  1.00 32.02           C  
ANISOU  731  CA  LYS A 495     4083   4160   3921    -43    -78     -5       C  
ATOM    732  C   LYS A 495       7.324  27.433  10.310  1.00 31.67           C  
ANISOU  732  C   LYS A 495     4144   4082   3805    -11    -62    -23       C  
ATOM    733  O   LYS A 495       7.909  27.341   9.244  1.00 32.29           O  
ANISOU  733  O   LYS A 495     4302   4473   3491     52   -139    125       O  
ATOM    734  CB  LYS A 495       6.399  29.710  10.587  1.00 31.95           C  
ANISOU  734  CB  LYS A 495     4089   4096   3953    -19    -68    -82       C  
ATOM    735  CG  LYS A 495       5.205  30.650  10.537  1.00 33.37           C  
ANISOU  735  CG  LYS A 495     4197   4231   4251    -66   -125     51       C  
ATOM    736  CD  LYS A 495       4.462  30.619   9.222  1.00 36.21           C  
ANISOU  736  CD  LYS A 495     4636   4525   4595    -57    -24     13       C  
ATOM    737  CE  LYS A 495       5.291  31.058   8.032  1.00 37.96           C  
ANISOU  737  CE  LYS A 495     4882   4838   4702      2    -96     17       C  
ATOM    738  NZ  LYS A 495       4.496  30.825   6.773  1.00 38.93           N  
ANISOU  738  NZ  LYS A 495     5322   4940   4527    -57   -208    200       N  
ATOM    739  N   GLY A 496       7.781  26.852  11.408  1.00 30.59           N  
ANISOU  739  N   GLY A 496     4053   4025   3542    -14    -85    -35       N  
ATOM    740  CA  GLY A 496       8.952  25.979  11.352  1.00 30.67           C  
ANISOU  740  CA  GLY A 496     4055   3956   3642     -9    -17     16       C  
ATOM    741  C   GLY A 496       9.392  25.497  12.726  1.00 30.64           C  
ANISOU  741  C   GLY A 496     4070   3890   3681    -57     15     53       C  
ATOM    742  O   GLY A 496       8.680  25.731  13.712  1.00 29.06           O  
ANISOU  742  O   GLY A 496     3952   3733   3356   -216    158    102       O  
ATOM    743  N   GLU A 497      10.565  24.852  12.743  1.00 30.32           N  
ANISOU  743  N   GLU A 497     4043   3831   3645    -21     44     23       N  
ATOM    744  CA  GLU A 497      11.310  24.472  13.958  1.00 31.11           C  
ANISOU  744  CA  GLU A 497     4142   3932   3746    -58     56    -16       C  
ATOM    745  C   GLU A 497      12.787  24.818  13.839  1.00 30.69           C  
ANISOU  745  C   GLU A 497     4150   3865   3644     13    104    -72       C  
ATOM    746  O   GLU A 497      13.356  24.838  12.736  1.00 31.90           O  
ANISOU  746  O   GLU A 497     4657   4198   3265   -124     68   -189       O  
ATOM    747  CB  GLU A 497      11.266  22.964  14.223  1.00 31.10           C  
ANISOU  747  CB  GLU A 497     4080   3952   3782   -106     99    -16       C  
ATOM    748  CG  GLU A 497       9.923  22.326  14.362  1.00 33.14           C  
ANISOU  748  CG  GLU A 497     4361   4269   3960    -71     17    -66       C  
ATOM    749  CD  GLU A 497      10.069  20.841  14.651  1.00 32.92           C  
ANISOU  749  CD  GLU A 497     4469   4155   3882   -217     18     83       C  
ATOM    750  OE1 GLU A 497      10.822  20.475  15.604  1.00 33.60           O  
ANISOU  750  OE1 GLU A 497     4919   4015   3831   -515   -485    325       O  
ATOM    751  OE2 GLU A 497       9.447  20.053  13.914  1.00 34.83           O  
ANISOU  751  OE2 GLU A 497     4962   4287   3983   -494    140    -96       O  
ATOM    752  N   ILE A 498      13.403  25.078  14.987  1.00 30.17           N  
ANISOU  752  N   ILE A 498     4149   3842   3470    -29    133     -4       N  
ATOM    753  CA  ILE A 498      14.835  25.193  15.107  1.00 28.74           C  
ANISOU  753  CA  ILE A 498     3908   3648   3361     74    155     15       C  
ATOM    754  C   ILE A 498      15.286  23.760  15.330  1.00 29.89           C  
ANISOU  754  C   ILE A 498     4075   3776   3504     92    195    -47       C  
ATOM    755  O   ILE A 498      14.852  23.112  16.294  1.00 29.45           O  
ANISOU  755  O   ILE A 498     4174   3714   3299    312    382    138       O  
ATOM    756  CB  ILE A 498      15.253  26.083  16.305  1.00 29.37           C  
ANISOU  756  CB  ILE A 498     3956   3667   3537     77    164     41       C  
ATOM    757  CG1 ILE A 498      14.703  27.499  16.149  1.00 29.16           C  
ANISOU  757  CG1 ILE A 498     4084   3612   3380    -31    226    107       C  
ATOM    758  CG2 ILE A 498      16.760  26.090  16.481  1.00 29.21           C  
ANISOU  758  CG2 ILE A 498     3903   3487   3708     21    192    164       C  
ATOM    759  CD1 ILE A 498      15.256  28.490  17.199  1.00 29.78           C  
ANISOU  759  CD1 ILE A 498     4150   3670   3495    -29    205   -135       C  
ATOM    760  N   PRO A 499      16.103  23.224  14.431  1.00 30.18           N  
ANISOU  760  N   PRO A 499     3994   3891   3580     97    219    -28       N  
ATOM    761  CA  PRO A 499      16.413  21.804  14.509  1.00 29.91           C  
ANISOU  761  CA  PRO A 499     3977   3802   3586    135    211    -75       C  
ATOM    762  C   PRO A 499      17.351  21.512  15.659  1.00 30.17           C  
ANISOU  762  C   PRO A 499     4017   3768   3678    106    247   -130       C  
ATOM    763  O   PRO A 499      18.355  22.210  15.859  1.00 30.47           O  
ANISOU  763  O   PRO A 499     4312   3588   3677      3    522      2       O  
ATOM    764  CB  PRO A 499      17.077  21.500  13.154  1.00 30.41           C  
ANISOU  764  CB  PRO A 499     4042   3919   3593     98    141   -103       C  
ATOM    765  CG  PRO A 499      17.665  22.781  12.758  1.00 31.17           C  
ANISOU  765  CG  PRO A 499     4098   4027   3718    102    282    -57       C  
ATOM    766  CD  PRO A 499      16.770  23.887  13.299  1.00 31.16           C  
ANISOU  766  CD  PRO A 499     4179   3930   3730     84    164   -129       C  
ATOM    767  N   TRP A 500      16.991  20.506  16.445  1.00 31.04           N  
ANISOU  767  N   TRP A 500     4185   3780   3828     76    139    -74       N  
ATOM    768  CA  TRP A 500      17.851  20.044  17.532  1.00 30.89           C  
ANISOU  768  CA  TRP A 500     4112   3771   3854     56     37    -80       C  
ATOM    769  C   TRP A 500      18.906  19.051  17.069  1.00 32.19           C  
ANISOU  769  C   TRP A 500     4346   3944   3940     66     82    -81       C  
ATOM    770  O   TRP A 500      18.651  18.172  16.228  1.00 32.38           O  
ANISOU  770  O   TRP A 500     4789   3569   3942    140      7   -222       O  
ATOM    771  CB  TRP A 500      17.025  19.385  18.641  1.00 30.17           C  
ANISOU  771  CB  TRP A 500     3956   3771   3735    -31     92    -51       C  
ATOM    772  CG  TRP A 500      16.487  20.360  19.585  1.00 29.36           C  
ANISOU  772  CG  TRP A 500     3912   3685   3558    -61     56     13       C  
ATOM    773  CD1 TRP A 500      15.346  21.069  19.452  1.00 28.98           C  
ANISOU  773  CD1 TRP A 500     3724   3697   3590     -8    -36    -31       C  
ATOM    774  CD2 TRP A 500      17.065  20.774  20.850  1.00 26.55           C  
ANISOU  774  CD2 TRP A 500     3408   3486   3193   -399   -222   -522       C  
ATOM    775  NE1 TRP A 500      15.173  21.911  20.522  1.00 29.45           N  
ANISOU  775  NE1 TRP A 500     3766   3966   3455   -261    127   -117       N  
ATOM    776  CE2 TRP A 500      16.199  21.740  21.405  1.00 29.34           C  
ANISOU  776  CE2 TRP A 500     3820   3776   3550   -229    -25   -137       C  
ATOM    777  CE3 TRP A 500      18.226  20.430  21.558  1.00 28.59           C  
ANISOU  777  CE3 TRP A 500     3738   3497   3625     76     -2   -207       C  
ATOM    778  CZ2 TRP A 500      16.472  22.394  22.630  1.00 29.67           C  
ANISOU  778  CZ2 TRP A 500     3941   3853   3477   -198    -74   -182       C  
ATOM    779  CZ3 TRP A 500      18.479  21.050  22.799  1.00 28.30           C  
ANISOU  779  CZ3 TRP A 500     3438   3632   3683    -71     90    -17       C  
ATOM    780  CH2 TRP A 500      17.616  22.037  23.298  1.00 27.43           C  
ANISOU  780  CH2 TRP A 500     3419   3559   3442    -61    136    -83       C  
ATOM    781  N   SER A 501      20.089  19.230  17.634  1.00 32.65           N  
ANISOU  781  N   SER A 501     4308   4068   4027    130    163   -132       N  
ATOM    782  CA  SER A 501      21.186  18.286  17.554  1.00 33.91           C  
ANISOU  782  CA  SER A 501     4449   4275   4159    102    174    -31       C  
ATOM    783  C   SER A 501      22.091  18.558  18.741  1.00 34.02           C  
ANISOU  783  C   SER A 501     4408   4274   4244    126    156    -71       C  
ATOM    784  O   SER A 501      21.912  19.525  19.459  1.00 33.36           O  
ANISOU  784  O   SER A 501     4562   3974   4138    313    366   -264       O  
ATOM    785  CB  SER A 501      21.981  18.507  16.278  1.00 33.24           C  
ANISOU  785  CB  SER A 501     4299   4331   3998    128    281   -143       C  
ATOM    786  OG  SER A 501      22.818  19.629  16.431  1.00 33.56           O  
ANISOU  786  OG  SER A 501     4568   4462   3719    328    679    -30       O  
ATOM    787  N   GLN A 502      23.081  17.705  18.929  1.00 33.86           N  
ANISOU  787  N   GLN A 502     4407   4194   4264    252    157    -58       N  
ATOM    788  CA  GLN A 502      24.106  17.939  19.924  1.00 34.23           C  
ANISOU  788  CA  GLN A 502     4382   4267   4354    235     25    -41       C  
ATOM    789  C   GLN A 502      24.859  19.263  19.782  1.00 33.71           C  
ANISOU  789  C   GLN A 502     4314   4251   4242    248     65     12       C  
ATOM    790  O   GLN A 502      25.291  19.830  20.773  1.00 34.27           O  
ANISOU  790  O   GLN A 502     4530   4276   4214    288     41     45       O  
ATOM    791  CB  GLN A 502      25.115  16.775  19.925  1.00 35.53           C  
ANISOU  791  CB  GLN A 502     4522   4413   4564    278    -13    -79       C  
ATOM    792  CG  GLN A 502      25.892  16.671  21.199  1.00 36.76           C  
ANISOU  792  CG  GLN A 502     4714   4513   4738    195    -56      4       C  
ATOM    793  CD  GLN A 502      26.383  15.253  21.424  1.00 40.06           C  
ANISOU  793  CD  GLN A 502     4874   4890   5457    237   -192    395       C  
ATOM    794  OE1 GLN A 502      25.586  14.346  21.710  1.00 42.61           O  
ANISOU  794  OE1 GLN A 502     5264   5022   5901    165   -459    475       O  
ATOM    795  NE2 GLN A 502      27.669  15.042  21.246  1.00 40.82           N  
ANISOU  795  NE2 GLN A 502     4709   4887   5910    380   -469    319       N  
ATOM    796  N   GLU A 503      25.028  19.765  18.556  1.00 32.32           N  
ANISOU  796  N   GLU A 503     4063   4142   4076    284    166    -28       N  
ATOM    797  CA  GLU A 503      25.741  21.012  18.326  1.00 31.91           C  
ANISOU  797  CA  GLU A 503     4004   4022   4096    174    130    -41       C  
ATOM    798  C   GLU A 503      24.896  22.248  18.631  1.00 32.03           C  
ANISOU  798  C   GLU A 503     3995   3986   4188    170    161    -13       C  
ATOM    799  O   GLU A 503      25.416  23.379  18.614  1.00 33.92           O  
ANISOU  799  O   GLU A 503     4112   4227   4548    240    253     32       O  
ATOM    800  CB  GLU A 503      26.199  21.087  16.879  0.50 31.48           C  
ANISOU  800  CB  GLU A 503     3949   4025   3986    187    139     -1       C  
ATOM    801  N   LEU A 504      23.606  22.063  18.884  1.00 31.10           N  
ANISOU  801  N   LEU A 504     3883   3879   4052    153    164     45       N  
ATOM    802  CA  LEU A 504      22.749  23.227  19.148  1.00 30.28           C  
ANISOU  802  CA  LEU A 504     3794   3878   3831    113    119    -10       C  
ATOM    803  C   LEU A 504      23.245  23.923  20.408  1.00 29.86           C  
ANISOU  803  C   LEU A 504     3646   3804   3892    134     95    -21       C  
ATOM    804  O   LEU A 504      23.508  23.260  21.440  1.00 29.54           O  
ANISOU  804  O   LEU A 504     3615   3845   3762    311     14    -23       O  
ATOM    805  CB  LEU A 504      21.300  22.804  19.307  1.00 29.94           C  
ANISOU  805  CB  LEU A 504     3818   3742   3813    137     67     -4       C  
ATOM    806  CG  LEU A 504      20.313  23.926  19.662  1.00 27.37           C  
ANISOU  806  CG  LEU A 504     3425   3527   3444     35    214     53       C  
ATOM    807  CD1 LEU A 504      18.947  23.610  19.082  1.00 26.82           C  
ANISOU  807  CD1 LEU A 504     3493   3373   3323    271    245    104       C  
ATOM    808  CD2 LEU A 504      20.243  24.169  21.173  1.00 26.94           C  
ANISOU  808  CD2 LEU A 504     3350   3348   3538    -59     20    101       C  
ATOM    809  N   ARG A 505      23.328  25.244  20.358  1.00 29.81           N  
ANISOU  809  N   ARG A 505     3586   3860   3878    129    132     24       N  
ATOM    810  CA  ARG A 505      23.773  25.995  21.510  1.00 30.78           C  
ANISOU  810  CA  ARG A 505     3826   3876   3991     96     81    -14       C  
ATOM    811  C   ARG A 505      23.117  27.391  21.541  1.00 30.24           C  
ANISOU  811  C   ARG A 505     3742   3785   3961    173    145    -23       C  
ATOM    812  O   ARG A 505      23.232  28.128  20.561  1.00 29.18           O  
ANISOU  812  O   ARG A 505     3458   3717   3910    154    270    -13       O  
ATOM    813  CB  ARG A 505      25.284  26.137  21.400  1.00 30.81           C  
ANISOU  813  CB  ARG A 505     3826   3803   4076    198     29     21       C  
ATOM    814  CG  ARG A 505      25.964  26.827  22.564  1.00 34.19           C  
ANISOU  814  CG  ARG A 505     4272   4301   4418     78    -24      3       C  
ATOM    815  CD  ARG A 505      27.470  26.989  22.406  1.00 36.14           C  
ANISOU  815  CD  ARG A 505     4510   4605   4614     59     16    -27       C  
ATOM    816  NE  ARG A 505      27.759  27.735  21.186  1.00 40.39           N  
ANISOU  816  NE  ARG A 505     5103   4961   5282    -50    -42    191       N  
ATOM    817  CZ  ARG A 505      27.939  29.055  21.100  1.00 43.12           C  
ANISOU  817  CZ  ARG A 505     5403   5463   5517    -61     29    -20       C  
ATOM    818  NH1 ARG A 505      27.940  29.849  22.180  1.00 44.96           N  
ANISOU  818  NH1 ARG A 505     5393   5701   5988     37     23   -181       N  
ATOM    819  NH2 ARG A 505      28.164  29.579  19.906  1.00 43.25           N  
ANISOU  819  NH2 ARG A 505     5440   5345   5646    -48   -231    248       N  
ATOM    820  N   PRO A 506      22.448  27.766  22.642  1.00 30.31           N  
ANISOU  820  N   PRO A 506     3744   3844   3928     63    102    -38       N  
ATOM    821  CA  PRO A 506      21.937  29.143  22.765  1.00 30.20           C  
ANISOU  821  CA  PRO A 506     3707   3867   3897     69     51    -46       C  
ATOM    822  C   PRO A 506      23.013  30.097  23.283  1.00 31.00           C  
ANISOU  822  C   PRO A 506     3823   3921   4032    102     35    -33       C  
ATOM    823  O   PRO A 506      23.896  29.680  24.042  1.00 32.49           O  
ANISOU  823  O   PRO A 506     3860   4166   4316      1    -66    -29       O  
ATOM    824  CB  PRO A 506      20.816  29.002  23.813  1.00 30.73           C  
ANISOU  824  CB  PRO A 506     3859   3911   3904     68     38    -96       C  
ATOM    825  CG  PRO A 506      21.395  27.978  24.762  1.00 30.55           C  
ANISOU  825  CG  PRO A 506     3766   3971   3869     23     75    -66       C  
ATOM    826  CD  PRO A 506      22.143  26.978  23.856  1.00 29.56           C  
ANISOU  826  CD  PRO A 506     3641   3689   3899    210    123   -103       C  
ATOM    827  N   GLU A 507      22.901  31.376  22.951  1.00 31.25           N  
ANISOU  827  N   GLU A 507     3786   4054   4031     23    -13     40       N  
ATOM    828  CA  GLU A 507      23.853  32.372  23.404  1.00 32.42           C  
ANISOU  828  CA  GLU A 507     4046   4109   4161     56     -6      0       C  
ATOM    829  C   GLU A 507      23.151  33.709  23.548  1.00 32.99           C  
ANISOU  829  C   GLU A 507     4093   4194   4246     97    -18    -11       C  
ATOM    830  O   GLU A 507      22.606  34.217  22.570  1.00 32.23           O  
ANISOU  830  O   GLU A 507     4015   4025   4203    383   -131     23       O  
ATOM    831  CB  GLU A 507      24.968  32.496  22.376  1.00 32.20           C  
ANISOU  831  CB  GLU A 507     3860   4214   4158     39     56      7       C  
ATOM    832  CG  GLU A 507      26.021  33.522  22.772  1.00 35.80           C  
ANISOU  832  CG  GLU A 507     4532   4607   4461    -99     95   -130       C  
ATOM    833  CD  GLU A 507      26.810  34.090  21.597  1.00 39.33           C  
ANISOU  833  CD  GLU A 507     5099   5064   4777   -467    215   -170       C  
ATOM    834  OE1 GLU A 507      26.691  33.594  20.443  1.00 46.70           O  
ANISOU  834  OE1 GLU A 507     6019   6114   5608   -400    703     69       O  
ATOM    835  OE2 GLU A 507      27.543  35.065  21.826  1.00 41.92           O  
ANISOU  835  OE2 GLU A 507     4986   5786   5153   -763    405    -16       O  
ATOM    836  N   ALA A 508      23.186  34.275  24.754  1.00 33.39           N  
ANISOU  836  N   ALA A 508     4158   4199   4328     11    -36    -37       N  
ATOM    837  CA  ALA A 508      22.532  35.558  25.043  1.00 34.30           C  
ANISOU  837  CA  ALA A 508     4245   4386   4399    -10      2    -25       C  
ATOM    838  C   ALA A 508      23.512  36.686  24.797  1.00 34.89           C  
ANISOU  838  C   ALA A 508     4288   4454   4515     12    -15    -21       C  
ATOM    839  O   ALA A 508      24.620  36.666  25.333  1.00 35.10           O  
ANISOU  839  O   ALA A 508     4018   4682   4634     14    -36     40       O  
ATOM    840  CB  ALA A 508      22.085  35.604  26.494  1.00 35.08           C  
ANISOU  840  CB  ALA A 508     4351   4440   4537    -93    -21    -27       C  
ATOM    841  N   LYS A 509      23.095  37.659  24.003  1.00 34.98           N  
ANISOU  841  N   LYS A 509     4326   4492   4473     27      8    -26       N  
ATOM    842  CA  LYS A 509      23.867  38.867  23.767  1.00 34.73           C  
ANISOU  842  CA  LYS A 509     4296   4428   4470    -29      4    -56       C  
ATOM    843  C   LYS A 509      23.608  39.936  24.850  1.00 34.31           C  
ANISOU  843  C   LYS A 509     4134   4416   4484    -85     42   -105       C  
ATOM    844  O   LYS A 509      24.512  40.707  25.255  1.00 35.12           O  
ANISOU  844  O   LYS A 509     3927   4688   4728   -192     66   -311       O  
ATOM    845  CB  LYS A 509      23.515  39.406  22.405  1.00 35.71           C  
ANISOU  845  CB  LYS A 509     4434   4571   4563     65    -21    -48       C  
ATOM    846  N   ASN A 510      22.372  40.006  25.299  1.00 32.06           N  
ANISOU  846  N   ASN A 510     3725   4119   4337     28    -53   -159       N  
ATOM    847  CA  ASN A 510      21.983  40.840  26.413  1.00 32.23           C  
ANISOU  847  CA  ASN A 510     3958   4123   4165    -34     -9    -61       C  
ATOM    848  C   ASN A 510      20.655  40.302  26.931  1.00 31.00           C  
ANISOU  848  C   ASN A 510     3735   4001   4040     30    -27   -126       C  
ATOM    849  O   ASN A 510      20.376  39.117  26.747  1.00 31.58           O  
ANISOU  849  O   ASN A 510     3666   4089   4243     13    160   -270       O  
ATOM    850  CB  ASN A 510      21.917  42.333  25.997  1.00 32.76           C  
ANISOU  850  CB  ASN A 510     4082   4102   4260     23    -47    -59       C  
ATOM    851  CG  ASN A 510      21.063  42.573  24.751  1.00 32.39           C  
ANISOU  851  CG  ASN A 510     3984   4114   4205     96    -53     53       C  
ATOM    852  OD1 ASN A 510      19.997  41.971  24.585  1.00 31.26           O  
ANISOU  852  OD1 ASN A 510     3785   4305   3786    154   -780     86       O  
ATOM    853  ND2 ASN A 510      21.544  43.454  23.863  1.00 33.14           N  
ANISOU  853  ND2 ASN A 510     4610   3722   4259    117   -188    -15       N  
ATOM    854  N   PHE A 511      19.843  41.131  27.580  1.00 29.96           N  
ANISOU  854  N   PHE A 511     3663   3834   3884    124    -15   -123       N  
ATOM    855  CA  PHE A 511      18.623  40.615  28.201  1.00 29.39           C  
ANISOU  855  CA  PHE A 511     3641   3770   3754     90    -60   -141       C  
ATOM    856  C   PHE A 511      17.486  40.470  27.196  1.00 28.03           C  
ANISOU  856  C   PHE A 511     3407   3614   3628    121    -29   -202       C  
ATOM    857  O   PHE A 511      16.460  39.887  27.511  1.00 28.11           O  
ANISOU  857  O   PHE A 511     3658   3411   3609    -44     91   -283       O  
ATOM    858  CB  PHE A 511      18.178  41.490  29.396  1.00 30.28           C  
ANISOU  858  CB  PHE A 511     3789   3847   3866    119    -54   -175       C  
ATOM    859  CG  PHE A 511      19.263  41.705  30.433  1.00 31.21           C  
ANISOU  859  CG  PHE A 511     4069   3856   3932    -75   -177   -188       C  
ATOM    860  CD1 PHE A 511      19.888  40.631  31.049  1.00 32.69           C  
ANISOU  860  CD1 PHE A 511     4131   4140   4149   -107   -418   -400       C  
ATOM    861  CD2 PHE A 511      19.644  42.993  30.792  1.00 31.44           C  
ANISOU  861  CD2 PHE A 511     4086   3981   3877    -53   -135   -416       C  
ATOM    862  CE1 PHE A 511      20.905  40.839  32.003  1.00 30.89           C  
ANISOU  862  CE1 PHE A 511     3787   4085   3863     -1   -433   -112       C  
ATOM    863  CE2 PHE A 511      20.649  43.195  31.698  1.00 30.00           C  
ANISOU  863  CE2 PHE A 511     4043   3743   3613     20     30   -294       C  
ATOM    864  CZ  PHE A 511      21.266  42.126  32.322  1.00 30.79           C  
ANISOU  864  CZ  PHE A 511     3782   4094   3822    118   -237   -167       C  
ATOM    865  N   LYS A 512      17.666  41.001  25.994  1.00 28.10           N  
ANISOU  865  N   LYS A 512     3381   3631   3662    132    -38   -143       N  
ATOM    866  CA  LYS A 512      16.587  40.908  24.971  1.00 28.94           C  
ANISOU  866  CA  LYS A 512     3526   3775   3694     35    -47   -153       C  
ATOM    867  C   LYS A 512      17.016  39.966  23.803  1.00 30.45           C  
ANISOU  867  C   LYS A 512     3782   3930   3857   -112    -22   -187       C  
ATOM    868  O   LYS A 512      16.320  39.032  23.384  1.00 32.25           O  
ANISOU  868  O   LYS A 512     3990   4243   4020     -7   -193   -360       O  
ATOM    869  CB  LYS A 512      16.170  42.325  24.562  1.00 29.74           C  
ANISOU  869  CB  LYS A 512     3577   3955   3766    -22    -67   -174       C  
ATOM    870  CG  LYS A 512      15.750  43.167  25.794  1.00 30.23           C  
ANISOU  870  CG  LYS A 512     3806   3926   3753    296    -43    -79       C  
ATOM    871  CD  LYS A 512      15.084  44.527  25.497  1.00 31.39           C  
ANISOU  871  CD  LYS A 512     3992   4049   3884    220     20    -96       C  
ATOM    872  CE  LYS A 512      14.468  45.197  26.744  1.00 32.84           C  
ANISOU  872  CE  LYS A 512     4390   4031   4054    296     62   -157       C  
ATOM    873  NZ  LYS A 512      14.206  46.684  26.563  1.00 33.02           N  
ANISOU  873  NZ  LYS A 512     4395   3944   4206    796    213    122       N  
ATOM    874  N   THR A 513      18.231  40.126  23.382  1.00 30.07           N  
ANISOU  874  N   THR A 513     3651   3879   3894    -70    -76   -169       N  
ATOM    875  CA  THR A 513      18.735  39.453  22.215  1.00 31.10           C  
ANISOU  875  CA  THR A 513     3873   3966   3975     12      1    -61       C  
ATOM    876  C   THR A 513      19.429  38.148  22.558  1.00 30.91           C  
ANISOU  876  C   THR A 513     3867   3924   3953     19    -57   -131       C  
ATOM    877  O   THR A 513      20.320  38.110  23.453  1.00 30.61           O  
ANISOU  877  O   THR A 513     3618   3971   4038    -65     27   -349       O  
ATOM    878  CB  THR A 513      19.719  40.375  21.559  1.00 32.64           C  
ANISOU  878  CB  THR A 513     4133   4157   4113     45     15     24       C  
ATOM    879  OG1 THR A 513      19.052  41.590  21.200  1.00 34.28           O  
ANISOU  879  OG1 THR A 513     4392   4049   4583    -42    439    424       O  
ATOM    880  CG2 THR A 513      20.234  39.786  20.246  1.00 33.66           C  
ANISOU  880  CG2 THR A 513     4339   4293   4156     83    103    -67       C  
ATOM    881  N   PHE A 514      19.052  37.089  21.832  1.00 30.32           N  
ANISOU  881  N   PHE A 514     3764   3858   3896    -17      0   -118       N  
ATOM    882  CA  PHE A 514      19.769  35.828  21.932  1.00 29.65           C  
ANISOU  882  CA  PHE A 514     3701   3745   3819     23    -13   -111       C  
ATOM    883  C   PHE A 514      19.783  35.041  20.623  1.00 29.87           C  
ANISOU  883  C   PHE A 514     3742   3773   3833      7      8    -93       C  
ATOM    884  O   PHE A 514      18.955  35.228  19.771  1.00 28.56           O  
ANISOU  884  O   PHE A 514     3370   3526   3953    146    -74   -177       O  
ATOM    885  CB  PHE A 514      19.247  34.978  23.063  1.00 29.97           C  
ANISOU  885  CB  PHE A 514     3629   3894   3863    -26     28   -157       C  
ATOM    886  CG  PHE A 514      17.886  34.369  22.831  1.00 30.11           C  
ANISOU  886  CG  PHE A 514     3796   3877   3764   -198    182    -79       C  
ATOM    887  CD1 PHE A 514      17.777  33.024  22.550  1.00 30.39           C  
ANISOU  887  CD1 PHE A 514     3892   3861   3793     24    200     27       C  
ATOM    888  CD2 PHE A 514      16.733  35.129  22.940  1.00 30.24           C  
ANISOU  888  CD2 PHE A 514     3723   3994   3770    -50     54     38       C  
ATOM    889  CE1 PHE A 514      16.556  32.438  22.396  1.00 27.74           C  
ANISOU  889  CE1 PHE A 514     3524   3695   3319   -178   -101    304       C  
ATOM    890  CE2 PHE A 514      15.465  34.555  22.770  1.00 28.24           C  
ANISOU  890  CE2 PHE A 514     3414   4084   3232     86    415   -153       C  
ATOM    891  CZ  PHE A 514      15.367  33.216  22.486  1.00 29.48           C  
ANISOU  891  CZ  PHE A 514     3580   3917   3703   -219    179    146       C  
ATOM    892  N   PHE A 515      20.804  34.218  20.461  1.00 30.20           N  
ANISOU  892  N   PHE A 515     3754   3784   3935     45     17    -50       N  
ATOM    893  CA  PHE A 515      21.012  33.426  19.260  1.00 31.06           C  
ANISOU  893  CA  PHE A 515     3879   3949   3970    108     50    -29       C  
ATOM    894  C   PHE A 515      20.814  31.962  19.588  1.00 29.88           C  
ANISOU  894  C   PHE A 515     3665   3814   3873     82    127    -61       C  
ATOM    895  O   PHE A 515      20.996  31.553  20.730  1.00 28.44           O  
ANISOU  895  O   PHE A 515     3534   3505   3765    440    274    -68       O  
ATOM    896  CB  PHE A 515      22.459  33.577  18.722  1.00 33.10           C  
ANISOU  896  CB  PHE A 515     4111   4134   4328    -35     20     65       C  
ATOM    897  CG  PHE A 515      22.918  34.999  18.550  1.00 35.94           C  
ANISOU  897  CG  PHE A 515     4274   4576   4806     54     43     32       C  
ATOM    898  CD1 PHE A 515      22.008  36.037  18.333  1.00 39.19           C  
ANISOU  898  CD1 PHE A 515     4805   4915   5170    107    -42    236       C  
ATOM    899  CD2 PHE A 515      24.273  35.301  18.574  1.00 39.66           C  
ANISOU  899  CD2 PHE A 515     4876   4938   5253   -175    -91    116       C  
ATOM    900  CE1 PHE A 515      22.435  37.358  18.174  1.00 39.82           C  
ANISOU  900  CE1 PHE A 515     4801   5000   5328    -68     17     66       C  
ATOM    901  CE2 PHE A 515      24.711  36.627  18.404  1.00 42.00           C  
ANISOU  901  CE2 PHE A 515     5163   5290   5502    -13   -108    101       C  
ATOM    902  CZ  PHE A 515      23.787  37.654  18.204  1.00 39.76           C  
ANISOU  902  CZ  PHE A 515     4737   4967   5400     57    -57     10       C  
ATOM    903  N   VAL A 516      20.423  31.154  18.608  1.00 29.41           N  
ANISOU  903  N   VAL A 516     3686   3739   3748    228    187    -42       N  
ATOM    904  CA  VAL A 516      20.484  29.718  18.801  1.00 29.49           C  
ANISOU  904  CA  VAL A 516     3710   3757   3737     76    266   -109       C  
ATOM    905  C   VAL A 516      21.269  29.182  17.623  1.00 29.76           C  
ANISOU  905  C   VAL A 516     3746   3815   3747    146    293    -66       C  
ATOM    906  O   VAL A 516      20.798  29.217  16.488  1.00 29.67           O  
ANISOU  906  O   VAL A 516     3781   3745   3744    163    467    -93       O  
ATOM    907  CB  VAL A 516      19.110  29.070  18.901  1.00 29.95           C  
ANISOU  907  CB  VAL A 516     3831   3771   3774     78    183    -29       C  
ATOM    908  CG1 VAL A 516      19.225  27.538  19.078  1.00 31.09           C  
ANISOU  908  CG1 VAL A 516     3831   4024   3955    199    254   -261       C  
ATOM    909  CG2 VAL A 516      18.413  29.634  20.098  1.00 30.58           C  
ANISOU  909  CG2 VAL A 516     3785   3843   3991    110    417   -114       C  
ATOM    910  N   HIS A 517      22.455  28.695  17.926  1.00 31.10           N  
ANISOU  910  N   HIS A 517     3944   4003   3870    142    239    -35       N  
ATOM    911  CA  HIS A 517      23.362  28.183  16.898  1.00 32.03           C  
ANISOU  911  CA  HIS A 517     4071   4099   3998     64    246      4       C  
ATOM    912  C   HIS A 517      22.994  26.766  16.519  1.00 32.02           C  
ANISOU  912  C   HIS A 517     4032   4185   3948    107    245    -12       C  
ATOM    913  O   HIS A 517      22.853  25.897  17.380  1.00 31.39           O  
ANISOU  913  O   HIS A 517     4030   4021   3873     11    400     82       O  
ATOM    914  CB  HIS A 517      24.777  28.196  17.445  1.00 33.64           C  
ANISOU  914  CB  HIS A 517     4386   4253   4143     43    155      0       C  
ATOM    915  CG  HIS A 517      25.238  29.545  17.885  1.00 36.38           C  
ANISOU  915  CG  HIS A 517     4661   4658   4503    -77    185    -11       C  
ATOM    916  ND1 HIS A 517      25.862  30.433  17.035  1.00 39.61           N  
ANISOU  916  ND1 HIS A 517     5239   4781   5030   -171    -20     93       N  
ATOM    917  CD2 HIS A 517      25.168  30.160  19.090  1.00 38.15           C  
ANISOU  917  CD2 HIS A 517     4963   4893   4637    -69    208   -125       C  
ATOM    918  CE1 HIS A 517      26.157  31.537  17.704  1.00 39.95           C  
ANISOU  918  CE1 HIS A 517     5446   4806   4927   -146    122    191       C  
ATOM    919  NE2 HIS A 517      25.740  31.401  18.948  1.00 40.31           N  
ANISOU  919  NE2 HIS A 517     5297   5138   4879   -151    349    110       N  
ATOM    920  N   THR A 518      22.849  26.505  15.225  1.00 32.17           N  
ANISOU  920  N   THR A 518     4128   4180   3913    117    290    111       N  
ATOM    921  CA  THR A 518      22.833  25.146  14.739  1.00 32.80           C  
ANISOU  921  CA  THR A 518     4216   4274   3973     73    261     28       C  
ATOM    922  C   THR A 518      23.877  25.068  13.603  1.00 33.24           C  
ANISOU  922  C   THR A 518     4245   4267   4116    169    342     -4       C  
ATOM    923  O   THR A 518      24.321  26.099  13.103  1.00 32.43           O  
ANISOU  923  O   THR A 518     4126   4280   3914    302    721      0       O  
ATOM    924  CB  THR A 518      21.440  24.726  14.276  1.00 32.82           C  
ANISOU  924  CB  THR A 518     4109   4290   4071    204    295     33       C  
ATOM    925  OG1 THR A 518      21.106  25.410  13.061  1.00 33.42           O  
ANISOU  925  OG1 THR A 518     4468   4462   3767    393    298     48       O  
ATOM    926  CG2 THR A 518      20.329  25.084  15.351  1.00 32.15           C  
ANISOU  926  CG2 THR A 518     4147   4210   3858     99    220    170       C  
ATOM    927  N   PRO A 519      24.273  23.859  13.227  1.00 33.82           N  
ANISOU  927  N   PRO A 519     4346   4343   4159    122    247    -25       N  
ATOM    928  CA  PRO A 519      25.415  23.700  12.347  1.00 34.57           C  
ANISOU  928  CA  PRO A 519     4398   4413   4322    117    194     -6       C  
ATOM    929  C   PRO A 519      25.331  24.516  11.060  1.00 35.17           C  
ANISOU  929  C   PRO A 519     4514   4430   4417    157    168    -20       C  
ATOM    930  O   PRO A 519      26.320  25.140  10.700  1.00 35.40           O  
ANISOU  930  O   PRO A 519     4448   4544   4456    380    277    -75       O  
ATOM    931  CB  PRO A 519      25.442  22.205  12.065  1.00 34.62           C  
ANISOU  931  CB  PRO A 519     4439   4381   4332     64    168      3       C  
ATOM    932  CG  PRO A 519      24.771  21.595  13.277  1.00 33.66           C  
ANISOU  932  CG  PRO A 519     4265   4285   4240     66    177     28       C  
ATOM    933  CD  PRO A 519      23.678  22.565  13.607  1.00 33.58           C  
ANISOU  933  CD  PRO A 519     4347   4247   4165     99    236    -92       C  
ATOM    934  N   ASN A 520      24.180  24.522  10.390  1.00 35.99           N  
ANISOU  934  N   ASN A 520     4608   4579   4486    125    181    -38       N  
ATOM    935  CA  ASN A 520      24.043  25.231   9.110  1.00 37.10           C  
ANISOU  935  CA  ASN A 520     4734   4705   4656    111     57    -43       C  
ATOM    936  C   ASN A 520      23.216  26.510   9.167  1.00 37.20           C  
ANISOU  936  C   ASN A 520     4814   4740   4581    139     73    -45       C  
ATOM    937  O   ASN A 520      22.935  27.125   8.136  1.00 37.69           O  
ANISOU  937  O   ASN A 520     4932   4833   4556    178     95    -62       O  
ATOM    938  CB  ASN A 520      23.468  24.288   8.071  1.00 37.67           C  
ANISOU  938  CB  ASN A 520     4769   4814   4727     81     57    -50       C  
ATOM    939  CG  ASN A 520      24.323  23.057   7.896  1.00 39.09           C  
ANISOU  939  CG  ASN A 520     4743   5038   5069    123    -26   -206       C  
ATOM    940  OD1 ASN A 520      25.545  23.128   8.021  1.00 41.53           O  
ANISOU  940  OD1 ASN A 520     4461   5935   5383    159    200   -533       O  
ATOM    941  ND2 ASN A 520      23.695  21.917   7.639  1.00 43.12           N  
ANISOU  941  ND2 ASN A 520     5036   5518   5829    136   -359    -65       N  
ATOM    942  N   ARG A 521      22.853  26.941  10.372  1.00 36.79           N  
ANISOU  942  N   ARG A 521     4732   4721   4523    172    100     -7       N  
ATOM    943  CA  ARG A 521      22.169  28.216  10.520  1.00 36.01           C  
ANISOU  943  CA  ARG A 521     4644   4609   4426    149     73     -6       C  
ATOM    944  C   ARG A 521      22.155  28.655  11.972  1.00 35.65           C  
ANISOU  944  C   ARG A 521     4605   4526   4414    190    159    -12       C  
ATOM    945  O   ARG A 521      21.988  27.829  12.884  1.00 35.23           O  
ANISOU  945  O   ARG A 521     4833   4416   4136    359    298     92       O  
ATOM    946  CB  ARG A 521      20.733  28.096  10.036  1.00 35.37           C  
ANISOU  946  CB  ARG A 521     4547   4539   4351    147    125    -24       C  
ATOM    947  CG  ARG A 521      19.932  29.340  10.317  1.00 34.55           C  
ANISOU  947  CG  ARG A 521     4307   4652   4168     86    107     88       C  
ATOM    948  CD  ARG A 521      18.660  29.393   9.570  1.00 35.60           C  
ANISOU  948  CD  ARG A 521     4688   4816   4022    102    221    101       C  
ATOM    949  NE  ARG A 521      17.868  30.525  10.012  1.00 34.52           N  
ANISOU  949  NE  ARG A 521     4390   4683   4041    327    376    632       N  
ATOM    950  CZ  ARG A 521      16.581  30.667   9.733  1.00 34.33           C  
ANISOU  950  CZ  ARG A 521     4466   4513   4064    -34    181    432       C  
ATOM    951  NH1 ARG A 521      15.950  29.771   8.974  1.00 34.74           N  
ANISOU  951  NH1 ARG A 521     4555   4719   3923    116    465    219       N  
ATOM    952  NH2 ARG A 521      15.934  31.706  10.219  1.00 32.92           N  
ANISOU  952  NH2 ARG A 521     4340   4173   3993    330    422    239       N  
ATOM    953  N   THR A 522      22.320  29.957  12.175  1.00 34.94           N  
ANISOU  953  N   THR A 522     4529   4393   4353    145    155     88       N  
ATOM    954  CA  THR A 522      22.087  30.553  13.478  1.00 34.67           C  
ANISOU  954  CA  THR A 522     4412   4388   4372    160    130    105       C  
ATOM    955  C   THR A 522      20.767  31.334  13.451  1.00 33.87           C  
ANISOU  955  C   THR A 522     4261   4343   4262    163    162    141       C  
ATOM    956  O   THR A 522      20.503  32.120  12.537  1.00 33.63           O  
ANISOU  956  O   THR A 522     4117   4429   4229    397    283    347       O  
ATOM    957  CB  THR A 522      23.276  31.443  13.832  1.00 35.19           C  
ANISOU  957  CB  THR A 522     4419   4506   4443    138    127     72       C  
ATOM    958  OG1 THR A 522      24.453  30.627  13.966  1.00 35.30           O  
ANISOU  958  OG1 THR A 522     4295   4610   4505    242    438    193       O  
ATOM    959  CG2 THR A 522      23.099  32.116  15.204  1.00 37.00           C  
ANISOU  959  CG2 THR A 522     4753   4716   4588    100    122     50       C  
ATOM    960  N   TYR A 523      19.947  31.123  14.467  1.00 30.77           N  
ANISOU  960  N   TYR A 523     3916   3968   3807    163    244    111       N  
ATOM    961  CA  TYR A 523      18.657  31.811  14.571  1.00 30.19           C  
ANISOU  961  CA  TYR A 523     3832   3780   3860    110     80     29       C  
ATOM    962  C   TYR A 523      18.838  33.028  15.479  1.00 29.78           C  
ANISOU  962  C   TYR A 523     3814   3733   3769    231     87    -17       C  
ATOM    963  O   TYR A 523      19.451  32.940  16.534  1.00 29.39           O  
ANISOU  963  O   TYR A 523     3940   3553   3673    578     12   -117       O  
ATOM    964  CB  TYR A 523      17.566  30.856  15.107  1.00 29.83           C  
ANISOU  964  CB  TYR A 523     3941   3669   3722    138    173     50       C  
ATOM    965  CG  TYR A 523      17.225  29.734  14.118  1.00 28.22           C  
ANISOU  965  CG  TYR A 523     3982   3367   3374    224    247    117       C  
ATOM    966  CD1 TYR A 523      18.076  28.642  13.936  1.00 28.02           C  
ANISOU  966  CD1 TYR A 523     3737   3315   3594    160    329    252       C  
ATOM    967  CD2 TYR A 523      16.061  29.762  13.374  1.00 27.97           C  
ANISOU  967  CD2 TYR A 523     3837   3326   3464     47    385    -40       C  
ATOM    968  CE1 TYR A 523      17.752  27.628  13.035  1.00 27.07           C  
ANISOU  968  CE1 TYR A 523     3374   3389   3520    539    213    157       C  
ATOM    969  CE2 TYR A 523      15.741  28.743  12.468  1.00 29.54           C  
ANISOU  969  CE2 TYR A 523     3911   3582   3728     34    554    209       C  
ATOM    970  CZ  TYR A 523      16.596  27.673  12.318  1.00 29.06           C  
ANISOU  970  CZ  TYR A 523     4177   3461   3401     54    268    166       C  
ATOM    971  OH  TYR A 523      16.300  26.657  11.423  1.00 30.47           O  
ANISOU  971  OH  TYR A 523     4649   3359   3569    247    365     49       O  
ATOM    972  N   TYR A 524      18.308  34.163  15.071  1.00 29.87           N  
ANISOU  972  N   TYR A 524     3792   3828   3730    100     61     42       N  
ATOM    973  CA  TYR A 524      18.592  35.421  15.753  1.00 29.41           C  
ANISOU  973  CA  TYR A 524     3732   3741   3699     76    132     38       C  
ATOM    974  C   TYR A 524      17.278  35.846  16.330  1.00 27.44           C  
ANISOU  974  C   TYR A 524     3380   3611   3435     74    136     24       C  
ATOM    975  O   TYR A 524      16.363  36.177  15.589  1.00 27.80           O  
ANISOU  975  O   TYR A 524     3811   3510   3238     72    325    145       O  
ATOM    976  CB  TYR A 524      19.161  36.463  14.757  1.00 31.72           C  
ANISOU  976  CB  TYR A 524     3966   4092   3991     31     99     81       C  
ATOM    977  CG  TYR A 524      20.527  36.063  14.264  1.00 34.22           C  
ANISOU  977  CG  TYR A 524     4311   4373   4315     28      0    -71       C  
ATOM    978  CD1 TYR A 524      21.639  36.170  15.087  1.00 37.80           C  
ANISOU  978  CD1 TYR A 524     4667   4782   4911     -9    -10    -68       C  
ATOM    979  CD2 TYR A 524      20.711  35.512  12.999  1.00 37.43           C  
ANISOU  979  CD2 TYR A 524     4506   4982   4730    -56    213    -54       C  
ATOM    980  CE1 TYR A 524      22.896  35.754  14.660  1.00 37.76           C  
ANISOU  980  CE1 TYR A 524     4699   4873   4775      1    210   -100       C  
ATOM    981  CE2 TYR A 524      21.965  35.103  12.568  1.00 37.54           C  
ANISOU  981  CE2 TYR A 524     4411   5077   4774     35    330   -127       C  
ATOM    982  CZ  TYR A 524      23.047  35.226  13.397  1.00 36.71           C  
ANISOU  982  CZ  TYR A 524     4438   4938   4570    194    271    -93       C  
ATOM    983  OH  TYR A 524      24.307  34.811  12.957  1.00 41.06           O  
ANISOU  983  OH  TYR A 524     5083   5389   5127    -58     54    -65       O  
ATOM    984  N   LEU A 525      17.172  35.777  17.655  1.00 28.29           N  
ANISOU  984  N   LEU A 525     3469   3656   3621    -33     22    -20       N  
ATOM    985  CA  LEU A 525      15.911  36.088  18.327  1.00 27.81           C  
ANISOU  985  CA  LEU A 525     3492   3539   3533     60     10   -116       C  
ATOM    986  C   LEU A 525      16.010  37.283  19.260  1.00 27.76           C  
ANISOU  986  C   LEU A 525     3463   3559   3526     45    -77   -155       C  
ATOM    987  O   LEU A 525      17.076  37.574  19.818  1.00 28.56           O  
ANISOU  987  O   LEU A 525     3436   3503   3911    266   -150   -331       O  
ATOM    988  CB  LEU A 525      15.452  34.928  19.176  1.00 28.35           C  
ANISOU  988  CB  LEU A 525     3598   3599   3573    -69    -25    -86       C  
ATOM    989  CG  LEU A 525      15.094  33.611  18.487  1.00 29.19           C  
ANISOU  989  CG  LEU A 525     3751   3648   3691     27     24    -25       C  
ATOM    990  CD1 LEU A 525      14.469  33.730  17.094  1.00 28.72           C  
ANISOU  990  CD1 LEU A 525     3597   3691   3624     69      6   -310       C  
ATOM    991  CD2 LEU A 525      16.258  32.811  18.407  1.00 32.17           C  
ANISOU  991  CD2 LEU A 525     3980   4191   4052    118   -320   -316       C  
ATOM    992  N   MET A 526      14.874  37.962  19.401  1.00 27.45           N  
ANISOU  992  N   MET A 526     3363   3608   3456     55    -33   -145       N  
ATOM    993  CA  MET A 526      14.770  39.122  20.292  1.00 28.46           C  
ANISOU  993  CA  MET A 526     3462   3696   3655     51      2    -71       C  
ATOM    994  C   MET A 526      13.532  38.930  21.190  1.00 26.82           C  
ANISOU  994  C   MET A 526     3107   3669   3411      7    -77   -116       C  
ATOM    995  O   MET A 526      12.466  38.545  20.738  1.00 25.53           O  
ANISOU  995  O   MET A 526     2688   3588   3424     96   -306   -136       O  
ATOM    996  CB AMET A 526      14.721  40.442  19.522  0.50 28.69           C  
ANISOU  996  CB AMET A 526     3442   3741   3715      0      9    -86       C  
ATOM    997  CG AMET A 526      15.010  41.669  20.404  0.50 30.99           C  
ANISOU  997  CG AMET A 526     3820   4044   3909     51     37    -83       C  
ATOM    998  SD AMET A 526      13.630  42.235  21.425  0.50 35.02           S  
ANISOU  998  SD AMET A 526     4228   4885   4192   -145    -75     51       S  
ATOM    999  CE AMET A 526      14.171  43.870  21.799  0.50 31.85           C  
ANISOU  999  CE AMET A 526     4067   4103   3929    177     58    -88       C  
ATOM   1000  CB BMET A 526      14.695  40.426  19.471  0.50 28.14           C  
ANISOU 1000  CB BMET A 526     3370   3661   3659     -9     16    -97       C  
ATOM   1001  CG BMET A 526      15.893  40.711  18.533  0.50 29.10           C  
ANISOU 1001  CG BMET A 526     3731   3680   3643      5     23   -120       C  
ATOM   1002  SD BMET A 526      15.785  42.274  17.612  0.50 32.28           S  
ANISOU 1002  SD BMET A 526     3855   4210   4200      5    241   -278       S  
ATOM   1003  CE BMET A 526      14.135  42.137  16.963  0.50 30.45           C  
ANISOU 1003  CE BMET A 526     3931   3860   3776   -113     26      1       C  
ATOM   1004  N   ASP A 527      13.713  39.113  22.487  1.00 29.04           N  
ANISOU 1004  N   ASP A 527     3379   3917   3738     50   -116   -130       N  
ATOM   1005  CA  ASP A 527      12.687  38.990  23.496  1.00 28.93           C  
ANISOU 1005  CA  ASP A 527     3618   3759   3615     81    -37    -92       C  
ATOM   1006  C   ASP A 527      12.507  40.375  24.127  1.00 30.07           C  
ANISOU 1006  C   ASP A 527     3813   3868   3742    164    -70    -58       C  
ATOM   1007  O   ASP A 527      13.259  40.755  24.998  1.00 29.40           O  
ANISOU 1007  O   ASP A 527     3523   3776   3871    206    -24   -133       O  
ATOM   1008  CB  ASP A 527      13.119  37.954  24.531  1.00 29.05           C  
ANISOU 1008  CB  ASP A 527     3577   3742   3717    178    -42   -212       C  
ATOM   1009  CG  ASP A 527      12.210  37.873  25.725  1.00 29.34           C  
ANISOU 1009  CG  ASP A 527     3957   3812   3378    260   -128   -181       C  
ATOM   1010  OD1 ASP A 527      11.111  38.479  25.693  1.00 30.00           O  
ANISOU 1010  OD1 ASP A 527     3482   4777   3137    452   -205   -282       O  
ATOM   1011  OD2 ASP A 527      12.499  37.208  26.752  1.00 30.28           O  
ANISOU 1011  OD2 ASP A 527     4470   3937   3096    155   -288   -442       O  
ATOM   1012  N   PRO A 528      11.537  41.169  23.676  1.00 30.22           N  
ANISOU 1012  N   PRO A 528     3707   3987   3789    131   -118    -74       N  
ATOM   1013  CA  PRO A 528      11.394  42.523  24.221  1.00 30.56           C  
ANISOU 1013  CA  PRO A 528     3757   3959   3895     70   -100      9       C  
ATOM   1014  C   PRO A 528      11.071  42.560  25.703  1.00 28.71           C  
ANISOU 1014  C   PRO A 528     3671   3696   3538     33    -66    -23       C  
ATOM   1015  O   PRO A 528      11.119  43.653  26.302  1.00 30.54           O  
ANISOU 1015  O   PRO A 528     3994   3653   3954    115      2    251       O  
ATOM   1016  CB  PRO A 528      10.225  43.136  23.434  1.00 30.73           C  
ANISOU 1016  CB  PRO A 528     3813   3941   3922     71    -73     84       C  
ATOM   1017  CG  PRO A 528       9.735  42.127  22.523  1.00 33.20           C  
ANISOU 1017  CG  PRO A 528     4171   4302   4141    149   -103    -40       C  
ATOM   1018  CD  PRO A 528      10.607  40.916  22.559  1.00 31.93           C  
ANISOU 1018  CD  PRO A 528     3967   4098   4067    150   -214      2       C  
ATOM   1019  N   SER A 529      10.735  41.412  26.306  1.00 28.12           N  
ANISOU 1019  N   SER A 529     3523   3662   3499     47    -30    -67       N  
ATOM   1020  CA  SER A 529      10.359  41.389  27.732  1.00 28.06           C  
ANISOU 1020  CA  SER A 529     3509   3646   3504      8   -101    -55       C  
ATOM   1021  C   SER A 529      11.592  41.450  28.639  1.00 27.78           C  
ANISOU 1021  C   SER A 529     3503   3575   3475     32   -168    -81       C  
ATOM   1022  O   SER A 529      11.453  41.603  29.854  1.00 28.47           O  
ANISOU 1022  O   SER A 529     3469   3810   3537     62   -253      3       O  
ATOM   1023  CB  SER A 529       9.549  40.136  28.068  1.00 28.12           C  
ANISOU 1023  CB  SER A 529     3575   3718   3390      3    -38    -34       C  
ATOM   1024  OG  SER A 529      10.386  38.977  28.110  1.00 30.46           O  
ANISOU 1024  OG  SER A 529     3922   3842   3807    160    122     41       O  
ATOM   1025  N   GLY A 530      12.758  41.307  28.032  1.00 27.31           N  
ANISOU 1025  N   GLY A 530     3502   3429   3443     50   -101    -49       N  
ATOM   1026  CA  GLY A 530      14.050  41.283  28.768  1.00 26.45           C  
ANISOU 1026  CA  GLY A 530     3298   3300   3451     31    -61    -80       C  
ATOM   1027  C   GLY A 530      14.411  39.971  29.476  1.00 26.80           C  
ANISOU 1027  C   GLY A 530     3380   3364   3438      0   -185    -72       C  
ATOM   1028  O   GLY A 530      15.231  39.944  30.438  1.00 26.73           O  
ANISOU 1028  O   GLY A 530     3294   3314   3547    141   -269   -237       O  
ATOM   1029  N   ASN A 531      13.860  38.872  28.960  1.00 26.79           N  
ANISOU 1029  N   ASN A 531     3270   3409   3497     35   -111   -107       N  
ATOM   1030  CA  ASN A 531      14.026  37.586  29.571  1.00 26.03           C  
ANISOU 1030  CA  ASN A 531     3237   3364   3288    -66    -60   -115       C  
ATOM   1031  C   ASN A 531      14.839  36.638  28.677  1.00 26.00           C  
ANISOU 1031  C   ASN A 531     3158   3461   3259     10    -72    -76       C  
ATOM   1032  O   ASN A 531      14.690  35.418  28.773  1.00 27.23           O  
ANISOU 1032  O   ASN A 531     3257   3829   3257   -285    115   -174       O  
ATOM   1033  CB  ASN A 531      12.659  37.005  29.884  1.00 27.29           C  
ANISOU 1033  CB  ASN A 531     3532   3423   3413    -22     50    -87       C  
ATOM   1034  CG  ASN A 531      12.017  37.691  31.092  1.00 27.02           C  
ANISOU 1034  CG  ASN A 531     3636   3391   3238     20   -147   -391       C  
ATOM   1035  OD1 ASN A 531      12.532  37.562  32.224  1.00 27.27           O  
ANISOU 1035  OD1 ASN A 531     3566   3400   3395    152   -376   -154       O  
ATOM   1036  ND2 ASN A 531      10.921  38.433  30.866  1.00 29.81           N  
ANISOU 1036  ND2 ASN A 531     3862   3854   3609     12    155   -333       N  
ATOM   1037  N   ALA A 532      15.680  37.198  27.799  1.00 26.76           N  
ANISOU 1037  N   ALA A 532     3352   3467   3349    -63    -40    -64       N  
ATOM   1038  CA  ALA A 532      16.525  36.348  26.927  1.00 27.04           C  
ANISOU 1038  CA  ALA A 532     3411   3484   3377    -73    -25    -67       C  
ATOM   1039  C   ALA A 532      17.350  35.312  27.698  1.00 27.04           C  
ANISOU 1039  C   ALA A 532     3343   3505   3424    -86    -87   -144       C  
ATOM   1040  O   ALA A 532      17.529  34.177  27.230  1.00 26.67           O  
ANISOU 1040  O   ALA A 532     3031   3618   3482   -187   -306   -216       O  
ATOM   1041  CB  ALA A 532      17.433  37.185  26.011  1.00 27.80           C  
ANISOU 1041  CB  ALA A 532     3550   3547   3466   -133     -8   -127       C  
ATOM   1042  N   HIS A 533      17.832  35.689  28.899  1.00 26.15           N  
ANISOU 1042  N   HIS A 533     3223   3369   3341   -146   -175   -177       N  
ATOM   1043  CA  HIS A 533      18.651  34.772  29.703  1.00 27.63           C  
ANISOU 1043  CA  HIS A 533     3415   3571   3511    -37    -61   -155       C  
ATOM   1044  C   HIS A 533      17.814  33.572  30.178  1.00 25.80           C  
ANISOU 1044  C   HIS A 533     3188   3340   3274   -120   -153   -196       C  
ATOM   1045  O   HIS A 533      18.321  32.438  30.340  1.00 26.53           O  
ANISOU 1045  O   HIS A 533     3006   3474   3599   -151     97   -312       O  
ATOM   1046  CB  HIS A 533      19.262  35.487  30.911  1.00 27.84           C  
ANISOU 1046  CB  HIS A 533     3335   3672   3572     12   -192    -99       C  
ATOM   1047  CG  HIS A 533      20.406  36.400  30.571  1.00 30.78           C  
ANISOU 1047  CG  HIS A 533     3807   4061   3826    -27   -112   -132       C  
ATOM   1048  ND1 HIS A 533      20.622  36.896  29.307  1.00 35.69           N  
ANISOU 1048  ND1 HIS A 533     4298   4451   4810   -299     -8    -21       N  
ATOM   1049  CD2 HIS A 533      21.383  36.926  31.344  1.00 34.85           C  
ANISOU 1049  CD2 HIS A 533     4281   4485   4473   -366     61    -92       C  
ATOM   1050  CE1 HIS A 533      21.691  37.669  29.307  1.00 35.52           C  
ANISOU 1050  CE1 HIS A 533     4377   4632   4485   -108    120    -52       C  
ATOM   1051  NE2 HIS A 533      22.178  37.695  30.527  1.00 36.28           N  
ANISOU 1051  NE2 HIS A 533     4482   4547   4753   -362    -29   -137       N  
ATOM   1052  N   LYS A 534      16.536  33.815  30.443  1.00 26.25           N  
ANISOU 1052  N   LYS A 534     3273   3331   3369     77    -84   -145       N  
ATOM   1053  CA  LYS A 534      15.656  32.690  30.843  1.00 25.77           C  
ANISOU 1053  CA  LYS A 534     3100   3346   3345      0     13    -91       C  
ATOM   1054  C   LYS A 534      15.501  31.700  29.665  1.00 24.91           C  
ANISOU 1054  C   LYS A 534     2974   3263   3224     13   -106    -70       C  
ATOM   1055  O   LYS A 534      15.539  30.489  29.859  1.00 24.53           O  
ANISOU 1055  O   LYS A 534     2864   3404   3053    -58   -275      4       O  
ATOM   1056  CB  LYS A 534      14.292  33.133  31.358  1.00 27.45           C  
ANISOU 1056  CB  LYS A 534     3281   3521   3625     35      6    -40       C  
ATOM   1057  CG  LYS A 534      14.402  34.039  32.574  1.00 28.38           C  
ANISOU 1057  CG  LYS A 534     3389   3639   3753     -6    140    -14       C  
ATOM   1058  CD  LYS A 534      13.007  34.348  33.129  1.00 30.05           C  
ANISOU 1058  CD  LYS A 534     3646   3953   3816    141    100    -84       C  
ATOM   1059  CE  LYS A 534      12.739  33.578  34.384  1.00 37.77           C  
ANISOU 1059  CE  LYS A 534     4658   4871   4821     86   -111   -106       C  
ATOM   1060  NZ  LYS A 534      13.762  33.927  35.466  1.00 38.77           N  
ANISOU 1060  NZ  LYS A 534     4444   5519   4765     33   -244    -49       N  
ATOM   1061  N   TRP A 535      15.363  32.231  28.448  1.00 23.92           N  
ANISOU 1061  N   TRP A 535     2944   3128   3014    -78   -135    -77       N  
ATOM   1062  CA  TRP A 535      15.329  31.394  27.260  1.00 24.02           C  
ANISOU 1062  CA  TRP A 535     2917   3094   3114     18    -58    -69       C  
ATOM   1063  C   TRP A 535      16.608  30.572  27.165  1.00 24.14           C  
ANISOU 1063  C   TRP A 535     2819   3177   3173    -29    -96    -74       C  
ATOM   1064  O   TRP A 535      16.597  29.371  26.940  1.00 25.19           O  
ANISOU 1064  O   TRP A 535     2695   3286   3588   -228   -186   -135       O  
ATOM   1065  CB  TRP A 535      15.119  32.202  25.988  1.00 22.65           C  
ANISOU 1065  CB  TRP A 535     2632   2958   3014    -32     77    -50       C  
ATOM   1066  CG  TRP A 535      13.675  32.385  25.640  1.00 23.83           C  
ANISOU 1066  CG  TRP A 535     2832   3133   3089    -29     88   -149       C  
ATOM   1067  CD1 TRP A 535      12.924  33.546  25.689  1.00 24.10           C  
ANISOU 1067  CD1 TRP A 535     2341   3416   3398   -198    150    -47       C  
ATOM   1068  CD2 TRP A 535      12.806  31.366  25.191  1.00 26.10           C  
ANISOU 1068  CD2 TRP A 535     2968   3460   3487   -127    229    128       C  
ATOM   1069  NE1 TRP A 535      11.648  33.290  25.245  1.00 24.48           N  
ANISOU 1069  NE1 TRP A 535     2523   3363   3414   -173   -222   -110       N  
ATOM   1070  CE2 TRP A 535      11.550  31.949  24.954  1.00 22.37           C  
ANISOU 1070  CE2 TRP A 535     2696   3022   2780    -82   -260    -19       C  
ATOM   1071  CE3 TRP A 535      12.972  30.005  24.926  1.00 24.97           C  
ANISOU 1071  CE3 TRP A 535     3162   3239   3084   -241     83     17       C  
ATOM   1072  CZ2 TRP A 535      10.458  31.199  24.520  1.00 24.57           C  
ANISOU 1072  CZ2 TRP A 535     2845   3388   3100   -205    108     80       C  
ATOM   1073  CZ3 TRP A 535      11.882  29.261  24.524  1.00 21.11           C  
ANISOU 1073  CZ3 TRP A 535     2100   2716   3201      4    113    -51       C  
ATOM   1074  CH2 TRP A 535      10.662  29.867  24.273  1.00 23.63           C  
ANISOU 1074  CH2 TRP A 535     2442   3229   3305    -69   -159     47       C  
ATOM   1075  N   CYS A 536      17.745  31.242  27.316  1.00 24.94           N  
ANISOU 1075  N   CYS A 536     2889   3169   3416   -113    -98    -34       N  
ATOM   1076  CA  CYS A 536      19.032  30.550  27.130  1.00 26.16           C  
ANISOU 1076  CA  CYS A 536     3215   3310   3414     40     28    -54       C  
ATOM   1077  C   CYS A 536      19.214  29.486  28.189  1.00 26.14           C  
ANISOU 1077  C   CYS A 536     3124   3411   3396     -3    -12    -55       C  
ATOM   1078  O   CYS A 536      19.566  28.350  27.885  1.00 26.77           O  
ANISOU 1078  O   CYS A 536     3311   3383   3476    163     25    -98       O  
ATOM   1079  CB  CYS A 536      20.176  31.514  27.156  1.00 27.07           C  
ANISOU 1079  CB  CYS A 536     3302   3505   3479     98    124    -11       C  
ATOM   1080  SG  CYS A 536      20.150  32.544  25.670  1.00 30.22           S  
ANISOU 1080  SG  CYS A 536     3590   3872   4018    193    346     42       S  
ATOM   1081  N   ARG A 537      18.910  29.856  29.418  1.00 25.04           N  
ANISOU 1081  N   ARG A 537     2994   3279   3238      4     42   -144       N  
ATOM   1082  CA  ARG A 537      19.013  28.935  30.539  1.00 27.08           C  
ANISOU 1082  CA  ARG A 537     3321   3586   3380     14     12    -88       C  
ATOM   1083  C   ARG A 537      18.163  27.655  30.352  1.00 25.53           C  
ANISOU 1083  C   ARG A 537     3177   3382   3140     58     14   -108       C  
ATOM   1084  O   ARG A 537      18.661  26.522  30.530  1.00 27.19           O  
ANISOU 1084  O   ARG A 537     3196   3711   3422    119   -153    -18       O  
ATOM   1085  CB  ARG A 537      18.560  29.649  31.811  1.00 27.78           C  
ANISOU 1085  CB  ARG A 537     3651   3587   3315     39    -67   -183       C  
ATOM   1086  CG  ARG A 537      19.530  30.632  32.382  1.00 29.15           C  
ANISOU 1086  CG  ARG A 537     3545   3712   3819      0   -135   -125       C  
ATOM   1087  CD  ARG A 537      18.932  31.526  33.610  1.00 32.71           C  
ANISOU 1087  CD  ARG A 537     4117   4226   4085   -116    -30    -89       C  
ATOM   1088  NE  ARG A 537      19.671  32.786  33.824  1.00 37.13           N  
ANISOU 1088  NE  ARG A 537     5018   4604   4486    156   -266   -293       N  
ATOM   1089  CZ  ARG A 537      19.131  34.004  34.006  1.00 39.17           C  
ANISOU 1089  CZ  ARG A 537     4969   5029   4884     47   -228    -99       C  
ATOM   1090  NH1 ARG A 537      17.802  34.193  34.044  1.00 41.54           N  
ANISOU 1090  NH1 ARG A 537     5320   5323   5139    213   -227     23       N  
ATOM   1091  NH2 ARG A 537      19.946  35.052  34.154  1.00 40.66           N  
ANISOU 1091  NH2 ARG A 537     5408   5148   4890    340   -132     90       N  
ATOM   1092  N   LYS A 538      16.905  27.820  29.950  1.00 24.68           N  
ANISOU 1092  N   LYS A 538     3127   3187   3061     57     -5   -158       N  
ATOM   1093  CA  LYS A 538      15.986  26.695  29.831  1.00 24.24           C  
ANISOU 1093  CA  LYS A 538     2847   3255   3106     40    -44    -42       C  
ATOM   1094  C   LYS A 538      16.370  25.812  28.648  1.00 22.92           C  
ANISOU 1094  C   LYS A 538     2588   3185   2935     40    -36     -6       C  
ATOM   1095  O   LYS A 538      16.315  24.563  28.742  1.00 23.78           O  
ANISOU 1095  O   LYS A 538     2546   3336   3153   -197    172    125       O  
ATOM   1096  CB  LYS A 538      14.563  27.175  29.638  1.00 25.77           C  
ANISOU 1096  CB  LYS A 538     2989   3603   3199      9   -108    -49       C  
ATOM   1097  CG  LYS A 538      13.516  26.119  29.954  1.00 27.58           C  
ANISOU 1097  CG  LYS A 538     3413   3685   3380    168   -127     42       C  
ATOM   1098  CD  LYS A 538      13.819  25.533  31.358  1.00 32.88           C  
ANISOU 1098  CD  LYS A 538     4050   4280   4162    -65     85    212       C  
ATOM   1099  CE  LYS A 538      12.629  25.146  32.166  1.00 35.47           C  
ANISOU 1099  CE  LYS A 538     4233   4442   4800     43     67    204       C  
ATOM   1100  NZ  LYS A 538      13.071  24.963  33.624  1.00 29.51           N  
ANISOU 1100  NZ  LYS A 538     3540   4107   3562    154    -63    614       N  
ATOM   1101  N   ILE A 539      16.750  26.448  27.528  1.00 22.84           N  
ANISOU 1101  N   ILE A 539     2640   2973   3062     34     57     59       N  
ATOM   1102  CA  ILE A 539      17.220  25.674  26.366  1.00 22.73           C  
ANISOU 1102  CA  ILE A 539     2468   3189   2979    -25    -55     74       C  
ATOM   1103  C   ILE A 539      18.488  24.907  26.786  1.00 22.83           C  
ANISOU 1103  C   ILE A 539     2386   3214   3072     32   -138      0       C  
ATOM   1104  O   ILE A 539      18.638  23.724  26.409  1.00 23.41           O  
ANISOU 1104  O   ILE A 539     1443   3865   3587    -31   -759   -135       O  
ATOM   1105  CB  ILE A 539      17.532  26.609  25.161  1.00 23.59           C  
ANISOU 1105  CB  ILE A 539     2730   3276   2956    -21   -108    134       C  
ATOM   1106  CG1 ILE A 539      16.260  27.178  24.593  1.00 23.54           C  
ANISOU 1106  CG1 ILE A 539     2534   3391   3018     97     75     68       C  
ATOM   1107  CG2 ILE A 539      18.372  25.874  24.096  1.00 25.51           C  
ANISOU 1107  CG2 ILE A 539     3076   3271   3346     35     10    112       C  
ATOM   1108  CD1 ILE A 539      16.473  28.364  23.628  1.00 25.12           C  
ANISOU 1108  CD1 ILE A 539     2740   3421   3381    112   -101     49       C  
ATOM   1109  N   GLN A 540      19.405  25.528  27.549  1.00 24.48           N  
ANISOU 1109  N   GLN A 540     3093   3076   3131     13   -109    -41       N  
ATOM   1110  CA  GLN A 540      20.620  24.839  27.997  1.00 25.98           C  
ANISOU 1110  CA  GLN A 540     3297   3337   3236    -28     83    -23       C  
ATOM   1111  C   GLN A 540      20.281  23.663  28.949  1.00 26.56           C  
ANISOU 1111  C   GLN A 540     3409   3391   3292     69     22     -1       C  
ATOM   1112  O   GLN A 540      20.873  22.573  28.847  1.00 27.01           O  
ANISOU 1112  O   GLN A 540     3350   3458   3453    128    268   -142       O  
ATOM   1113  CB  GLN A 540      21.609  25.767  28.626  1.00 26.49           C  
ANISOU 1113  CB  GLN A 540     3399   3396   3270    110    165     20       C  
ATOM   1114  CG  GLN A 540      22.887  25.099  28.821  1.00 28.58           C  
ANISOU 1114  CG  GLN A 540     3495   3802   3560    109   -177     63       C  
ATOM   1115  CD  GLN A 540      23.570  24.578  27.516  1.00 34.13           C  
ANISOU 1115  CD  GLN A 540     3826   4712   4428    376     -4    288       C  
ATOM   1116  OE1 GLN A 540      23.402  25.156  26.433  1.00 35.95           O  
ANISOU 1116  OE1 GLN A 540     3076   5580   5000    373   -321    272       O  
ATOM   1117  NE2 GLN A 540      24.385  23.513  27.648  1.00 38.01           N  
ANISOU 1117  NE2 GLN A 540     4771   4766   4904    288    -95    386       N  
ATOM   1118  N   GLU A 541      19.311  23.891  29.823  1.00 26.51           N  
ANISOU 1118  N   GLU A 541     3314   3368   3391    -29     54    -15       N  
ATOM   1119  CA  GLU A 541      18.839  22.842  30.736  1.00 27.20           C  
ANISOU 1119  CA  GLU A 541     3380   3496   3459      7    130     24       C  
ATOM   1120  C   GLU A 541      18.360  21.615  29.954  1.00 26.37           C  
ANISOU 1120  C   GLU A 541     3149   3459   3411     43     99     47       C  
ATOM   1121  O   GLU A 541      18.736  20.452  30.254  1.00 27.75           O  
ANISOU 1121  O   GLU A 541     3334   3750   3459    226   -116     59       O  
ATOM   1122  CB  GLU A 541      17.775  23.394  31.661  1.00 27.48           C  
ANISOU 1122  CB  GLU A 541     3300   3544   3594    -48    239     90       C  
ATOM   1123  CG  GLU A 541      17.372  22.398  32.740  1.00 30.64           C  
ANISOU 1123  CG  GLU A 541     3844   3919   3877     61    225    104       C  
ATOM   1124  CD  GLU A 541      16.176  22.802  33.590  1.00 30.37           C  
ANISOU 1124  CD  GLU A 541     3793   3905   3839     59    309     85       C  
ATOM   1125  OE1 GLU A 541      15.511  23.847  33.343  1.00 32.89           O  
ANISOU 1125  OE1 GLU A 541     3799   4367   4328     31    993    -45       O  
ATOM   1126  OE2 GLU A 541      15.890  22.008  34.506  1.00 32.11           O  
ANISOU 1126  OE2 GLU A 541     4327   3901   3969     59    926    269       O  
ATOM   1127  N   VAL A 542      17.530  21.877  28.951  1.00 25.08           N  
ANISOU 1127  N   VAL A 542     3022   3203   3303     25      0     19       N  
ATOM   1128  CA  VAL A 542      16.971  20.829  28.084  1.00 24.84           C  
ANISOU 1128  CA  VAL A 542     2741   3339   3356     39     95     19       C  
ATOM   1129  C   VAL A 542      18.137  20.123  27.336  1.00 24.23           C  
ANISOU 1129  C   VAL A 542     2578   3344   3284     25     18    -29       C  
ATOM   1130  O   VAL A 542      18.155  18.858  27.203  1.00 22.47           O  
ANISOU 1130  O   VAL A 542     1275   3498   3761   -130    267    121       O  
ATOM   1131  CB  VAL A 542      15.877  21.429  27.154  1.00 24.99           C  
ANISOU 1131  CB  VAL A 542     2906   3306   3282    -18     79     46       C  
ATOM   1132  CG1 VAL A 542      15.522  20.459  25.982  1.00 26.19           C  
ANISOU 1132  CG1 VAL A 542     3085   3667   3199    -69     82    163       C  
ATOM   1133  CG2 VAL A 542      14.630  21.897  27.992  1.00 23.92           C  
ANISOU 1133  CG2 VAL A 542     2443   3284   3359   -251    172    155       C  
ATOM   1134  N   TRP A 543      19.052  20.935  26.819  1.00 24.23           N  
ANISOU 1134  N   TRP A 543     2717   3176   3310    -38    213    -46       N  
ATOM   1135  CA  TRP A 543      20.257  20.409  26.123  1.00 23.59           C  
ANISOU 1135  CA  TRP A 543     2525   3230   3207   -126    135      9       C  
ATOM   1136  C   TRP A 543      21.004  19.405  27.015  1.00 22.35           C  
ANISOU 1136  C   TRP A 543     1941   3160   3389   -134    235    -61       C  
ATOM   1137  O   TRP A 543      21.248  18.246  26.628  1.00 22.55           O  
ANISOU 1137  O   TRP A 543     1297   3626   3643    -54    -30     19       O  
ATOM   1138  CB  TRP A 543      21.189  21.530  25.671  1.00 24.37           C  
ANISOU 1138  CB  TRP A 543     2760   3214   3282    -63     70     79       C  
ATOM   1139  CG  TRP A 543      22.306  20.993  24.857  1.00 26.74           C  
ANISOU 1139  CG  TRP A 543     3320   3428   3413    -74    128    -45       C  
ATOM   1140  CD1 TRP A 543      22.369  20.919  23.490  1.00 26.64           C  
ANISOU 1140  CD1 TRP A 543     3340   3302   3480    -79    172     64       C  
ATOM   1141  CD2 TRP A 543      23.506  20.394  25.342  1.00 26.02           C  
ANISOU 1141  CD2 TRP A 543     3136   3327   3420   -209    299   -123       C  
ATOM   1142  NE1 TRP A 543      23.553  20.343  23.108  1.00 27.19           N  
ANISOU 1142  NE1 TRP A 543     3177   3640   3514    197    -20    -16       N  
ATOM   1143  CE2 TRP A 543      24.264  20.003  24.227  1.00 26.25           C  
ANISOU 1143  CE2 TRP A 543     3195   3481   3295     23     92   -115       C  
ATOM   1144  CE3 TRP A 543      24.034  20.159  26.617  1.00 23.52           C  
ANISOU 1144  CE3 TRP A 543     2424   3170   3343   -308      4    105       C  
ATOM   1145  CZ2 TRP A 543      25.491  19.384  24.361  1.00 23.31           C  
ANISOU 1145  CZ2 TRP A 543     2134   3398   3322   -163    127   -104       C  
ATOM   1146  CZ3 TRP A 543      25.262  19.563  26.737  1.00 27.32           C  
ANISOU 1146  CZ3 TRP A 543     3414   3556   3410   -127     83    -41       C  
ATOM   1147  CH2 TRP A 543      25.963  19.172  25.627  1.00 25.19           C  
ANISOU 1147  CH2 TRP A 543     2703   3333   3532   -164    230    -21       C  
ATOM   1148  N   ARG A 544      21.167  19.758  28.273  1.00 24.96           N  
ANISOU 1148  N   ARG A 544     2717   3271   3493   -161     -5     44       N  
ATOM   1149  CA  ARG A 544      21.892  18.907  29.222  1.00 26.99           C  
ANISOU 1149  CA  ARG A 544     3225   3431   3596    -18      6    -51       C  
ATOM   1150  C   ARG A 544      21.138  17.608  29.489  1.00 26.70           C  
ANISOU 1150  C   ARG A 544     3128   3403   3612   -128    107      3       C  
ATOM   1151  O   ARG A 544      21.752  16.529  29.537  1.00 27.44           O  
ANISOU 1151  O   ARG A 544     3069   3444   3911   -154    157    -30       O  
ATOM   1152  CB  ARG A 544      22.099  19.607  30.547  1.00 28.71           C  
ANISOU 1152  CB  ARG A 544     3564   3512   3830   -195     46    -69       C  
ATOM   1153  CG  ARG A 544      23.191  20.697  30.517  1.00 31.08           C  
ANISOU 1153  CG  ARG A 544     3694   4021   4092   -103    -78   -213       C  
ATOM   1154  CD  ARG A 544      23.719  21.020  31.896  1.00 37.75           C  
ANISOU 1154  CD  ARG A 544     4692   4828   4823    -49   -110    -86       C  
ATOM   1155  NE  ARG A 544      22.644  21.516  32.765  1.00 40.25           N  
ANISOU 1155  NE  ARG A 544     5149   5054   5087    181      2   -204       N  
ATOM   1156  CZ  ARG A 544      22.181  22.771  32.764  1.00 42.58           C  
ANISOU 1156  CZ  ARG A 544     5424   5463   5289     44    -24   -229       C  
ATOM   1157  NH1 ARG A 544      22.696  23.684  31.947  1.00 42.02           N  
ANISOU 1157  NH1 ARG A 544     5674   5076   5213     60   -114   -209       N  
ATOM   1158  NH2 ARG A 544      21.198  23.113  33.595  1.00 44.20           N  
ANISOU 1158  NH2 ARG A 544     5665   5787   5341    205    130   -309       N  
ATOM   1159  N   GLN A 545      19.815  17.699  29.644  1.00 26.89           N  
ANISOU 1159  N   GLN A 545     3279   3382   3554    -78     94    -59       N  
ATOM   1160  CA  GLN A 545      18.988  16.497  29.940  1.00 27.54           C  
ANISOU 1160  CA  GLN A 545     3401   3456   3604    -30     86    -49       C  
ATOM   1161  C   GLN A 545      18.923  15.617  28.720  1.00 26.26           C  
ANISOU 1161  C   GLN A 545     3076   3372   3528    -86     67     -2       C  
ATOM   1162  O   GLN A 545      18.858  14.379  28.855  1.00 27.27           O  
ANISOU 1162  O   GLN A 545     3566   3355   3438   -123     66   -103       O  
ATOM   1163  CB  GLN A 545      17.574  16.862  30.408  1.00 28.41           C  
ANISOU 1163  CB  GLN A 545     3596   3527   3670    -31     21     38       C  
ATOM   1164  CG  GLN A 545      17.525  17.687  31.685  1.00 32.05           C  
ANISOU 1164  CG  GLN A 545     4198   4095   3884    221     90    -31       C  
ATOM   1165  CD  GLN A 545      16.268  17.463  32.588  1.00 34.45           C  
ANISOU 1165  CD  GLN A 545     4425   4278   4385    -84     70   -177       C  
ATOM   1166  OE1 GLN A 545      16.050  18.230  33.554  1.00 45.40           O  
ANISOU 1166  OE1 GLN A 545     5884   5955   5409    -13    235   -158       O  
ATOM   1167  NE2 GLN A 545      15.490  16.426  32.315  1.00 39.29           N  
ANISOU 1167  NE2 GLN A 545     5143   4990   4793   -180   -204     26       N  
ATOM   1168  N   ARG A 546      18.983  16.228  27.529  1.00 25.05           N  
ANISOU 1168  N   ARG A 546     3121   3047   3347    -65     24    -14       N  
ATOM   1169  CA  ARG A 546      18.923  15.461  26.297  1.00 26.72           C  
ANISOU 1169  CA  ARG A 546     3379   3415   3357     35    113     33       C  
ATOM   1170  C   ARG A 546      20.223  14.717  26.004  1.00 27.14           C  
ANISOU 1170  C   ARG A 546     3440   3405   3465     86     83    -22       C  
ATOM   1171  O   ARG A 546      20.176  13.550  25.574  1.00 27.24           O  
ANISOU 1171  O   ARG A 546     3588   3301   3459     83    181     84       O  
ATOM   1172  CB  ARG A 546      18.506  16.347  25.110  1.00 27.07           C  
ANISOU 1172  CB  ARG A 546     3369   3463   3450     20    128     34       C  
ATOM   1173  CG  ARG A 546      18.545  15.666  23.732  1.00 28.55           C  
ANISOU 1173  CG  ARG A 546     3867   3485   3496    -65   -138    -91       C  
ATOM   1174  CD  ARG A 546      17.693  14.404  23.543  1.00 29.68           C  
ANISOU 1174  CD  ARG A 546     3705   3964   3608    -28    288   -106       C  
ATOM   1175  NE  ARG A 546      17.956  13.853  22.194  1.00 30.26           N  
ANISOU 1175  NE  ARG A 546     4125   3704   3669   -145    101    -94       N  
ATOM   1176  CZ  ARG A 546      19.003  13.110  21.875  1.00 29.62           C  
ANISOU 1176  CZ  ARG A 546     3932   3525   3796   -433      0    -25       C  
ATOM   1177  NH1 ARG A 546      19.918  12.765  22.790  1.00 27.91           N  
ANISOU 1177  NH1 ARG A 546     3646   3674   3281    144   -181    -72       N  
ATOM   1178  NH2 ARG A 546      19.147  12.699  20.611  1.00 30.39           N  
ANISOU 1178  NH2 ARG A 546     4347   3528   3671   -115    332     21       N  
ATOM   1179  N   TYR A 547      21.358  15.411  26.173  1.00 27.74           N  
ANISOU 1179  N   TYR A 547     3497   3415   3626    139     95    -96       N  
ATOM   1180  CA  TYR A 547      22.655  14.929  25.631  1.00 29.29           C  
ANISOU 1180  CA  TYR A 547     3676   3703   3747     -3     10    -26       C  
ATOM   1181  C   TYR A 547      23.628  14.468  26.698  1.00 30.36           C  
ANISOU 1181  C   TYR A 547     3805   3804   3926     69     29     19       C  
ATOM   1182  O   TYR A 547      24.606  13.809  26.377  1.00 31.76           O  
ANISOU 1182  O   TYR A 547     4079   3844   4141     97    218   -174       O  
ATOM   1183  CB  TYR A 547      23.320  16.010  24.743  1.00 29.38           C  
ANISOU 1183  CB  TYR A 547     3724   3687   3751     -8    -30    -39       C  
ATOM   1184  CG  TYR A 547      22.492  16.339  23.534  1.00 30.67           C  
ANISOU 1184  CG  TYR A 547     3976   3803   3874     66      7    -86       C  
ATOM   1185  CD1 TYR A 547      22.299  15.403  22.540  1.00 29.72           C  
ANISOU 1185  CD1 TYR A 547     4006   3560   3724    232    142   -100       C  
ATOM   1186  CD2 TYR A 547      21.871  17.590  23.387  1.00 29.32           C  
ANISOU 1186  CD2 TYR A 547     3906   3528   3706    320      3     54       C  
ATOM   1187  CE1 TYR A 547      21.510  15.673  21.473  1.00 32.70           C  
ANISOU 1187  CE1 TYR A 547     4610   4000   3811    190    -35   -408       C  
ATOM   1188  CE2 TYR A 547      21.052  17.852  22.343  1.00 31.01           C  
ANISOU 1188  CE2 TYR A 547     4483   3507   3792    157    125   -217       C  
ATOM   1189  CZ  TYR A 547      20.898  16.909  21.348  1.00 31.93           C  
ANISOU 1189  CZ  TYR A 547     4399   3820   3911    115   -390   -100       C  
ATOM   1190  OH  TYR A 547      20.090  17.174  20.256  1.00 34.70           O  
ANISOU 1190  OH  TYR A 547     4721   4301   4162   -104   -203    -36       O  
ATOM   1191  N   GLN A 548      23.381  14.814  27.959  1.00 31.35           N  
ANISOU 1191  N   GLN A 548     3772   4029   4108     17    108    -16       N  
ATOM   1192  CA  GLN A 548      24.244  14.367  29.057  1.00 32.94           C  
ANISOU 1192  CA  GLN A 548     4109   4210   4195    -82     53     78       C  
ATOM   1193  C   GLN A 548      23.419  13.531  30.053  1.00 35.87           C  
ANISOU 1193  C   GLN A 548     4419   4716   4494   -119     16     69       C  
ATOM   1194  O   GLN A 548      22.341  13.060  29.707  1.00 32.81           O  
ANISOU 1194  O   GLN A 548     3914   4456   4096   -372    -95     -9       O  
ATOM   1195  CB  GLN A 548      25.004  15.550  29.668  1.00 32.42           C  
ANISOU 1195  CB  GLN A 548     3931   4271   4116     35     24     20       C  
ATOM   1196  CG  GLN A 548      25.799  16.264  28.564  1.00 32.09           C  
ANISOU 1196  CG  GLN A 548     3870   4142   4180   -117    -72    149       C  
ATOM   1197  CD  GLN A 548      26.716  17.388  29.042  1.00 32.07           C  
ANISOU 1197  CD  GLN A 548     3884   4068   4232    -71     -3    150       C  
ATOM   1198  OE1 GLN A 548      27.793  17.659  28.432  1.00 33.19           O  
ANISOU 1198  OE1 GLN A 548     3545   4479   4587    118    -56    267       O  
ATOM   1199  NE2 GLN A 548      26.281  18.083  30.086  1.00 26.66           N  
ANISOU 1199  NE2 GLN A 548     3076   3728   3324   -116    -66    265       N  
ATOM   1200  N   SER A 549      23.956  13.348  31.255  1.00 40.52           N  
ANISOU 1200  N   SER A 549     5152   5254   4986   -146     62    133       N  
ATOM   1201  CA  SER A 549      23.450  12.380  32.257  1.00 43.27           C  
ANISOU 1201  CA  SER A 549     5567   5527   5345    -87     21     52       C  
ATOM   1202  C   SER A 549      23.676  10.949  31.778  1.00 44.50           C  
ANISOU 1202  C   SER A 549     5805   5706   5397   -102      3    103       C  
ATOM   1203  O   SER A 549      23.773  10.688  30.572  1.00 47.09           O  
ANISOU 1203  O   SER A 549     6141   6072   5676   -111    -77    119       O  
ATOM   1204  CB  SER A 549      21.990  12.669  32.587  1.00 43.86           C  
ANISOU 1204  CB  SER A 549     5667   5640   5356    -67     -1     78       C  
ATOM   1205  OG  SER A 549      21.766  14.085  32.648  1.00 46.44           O  
ANISOU 1205  OG  SER A 549     6169   5857   5618   -226    -70   -234       O  
ATOM   1206  N   HIS A 550      23.828  10.001  32.566  1.00 46.83           N  
ANISOU 1206  N   HIS A 550     6116   6003   5674    -69    -13     28       N  
TER    1207      HIS A 550                                                      
HETATM 1208  O0F 4PT A1550      11.531  38.493   0.495  1.00 56.22           O  
ANISOU 1208  O0F 4PT A1550     6723   7164   7471   -404    -29   -216       O  
HETATM 1209  C0E 4PT A1550      10.678  37.403   0.072  1.00 54.01           C  
ANISOU 1209  C0E 4PT A1550     6793   6822   6903   -149     47   -115       C  
HETATM 1210  C0C 4PT A1550       9.676  37.103   1.187  1.00 49.98           C  
ANISOU 1210  C0C 4PT A1550     6298   6378   6313   -235     66    -37       C  
HETATM 1211  O0D 4PT A1550       8.963  35.904   0.903  1.00 52.55           O  
ANISOU 1211  O0D 4PT A1550     6423   6897   6647   -375    257   -110       O  
HETATM 1212  C0B 4PT A1550      10.379  36.895   2.541  1.00 48.16           C  
ANISOU 1212  C0B 4PT A1550     6232   6081   5985   -125      5     22       C  
HETATM 1213  OP1 4PT A1550       9.387  36.736   3.572  1.00 42.13           O  
ANISOU 1213  OP1 4PT A1550     5841   5194   4971    -59   -202    101       O  
HETATM 1214  P1  4PT A1550       9.630  37.419   4.969  1.00 39.13           P  
ANISOU 1214  P1  4PT A1550     5576   4803   4488     28    -69    146       P  
HETATM 1215  OP3 4PT A1550       8.320  37.029   5.836  1.00 38.15           O  
ANISOU 1215  OP3 4PT A1550     5437   4859   4198     14   -287    -29       O  
HETATM 1216  OP2 4PT A1550       9.857  38.891   4.868  1.00 37.83           O  
ANISOU 1216  OP2 4PT A1550     5874   4409   4087    -52   -351    204       O  
HETATM 1217  O1  4PT A1550      10.932  36.772   5.569  1.00 34.57           O  
ANISOU 1217  O1  4PT A1550     5181   4453   3498    145     58    183       O  
HETATM 1218  C1  4PT A1550      10.878  35.357   5.841  1.00 31.01           C  
ANISOU 1218  C1  4PT A1550     4755   3561   3463     82    170    347       C  
HETATM 1219  C2  4PT A1550      10.537  35.066   7.325  1.00 28.28           C  
ANISOU 1219  C2  4PT A1550     4100   3620   3026    103    385    -83       C  
HETATM 1220  O2  4PT A1550      11.522  35.649   8.194  1.00 28.48           O  
ANISOU 1220  O2  4PT A1550     4520   3255   3044   -345    112    -67       O  
HETATM 1221  C3  4PT A1550      10.586  33.528   7.549  1.00 28.24           C  
ANISOU 1221  C3  4PT A1550     4087   3476   3166    -43    436    272       C  
HETATM 1222  O3  4PT A1550      10.329  33.236   8.932  1.00 28.10           O  
ANISOU 1222  O3  4PT A1550     4572   3481   2623    -77    480    -52       O  
HETATM 1223  P3  4PT A1550       8.999  32.356   9.171  1.00 32.26           P  
ANISOU 1223  P3  4PT A1550     4592   4063   3601   -221    117     83       P  
HETATM 1224  O11 4PT A1550       7.763  33.127   8.619  1.00 29.64           O  
ANISOU 1224  O11 4PT A1550     4512   4101   2648   -396    524    303       O  
HETATM 1225  O10 4PT A1550       8.908  32.304  10.782  1.00 29.88           O  
ANISOU 1225  O10 4PT A1550     4241   3731   3379     86    208     81       O  
HETATM 1226  O12 4PT A1550       9.077  31.010   8.485  1.00 32.07           O  
ANISOU 1226  O12 4PT A1550     5092   3930   3162   -280   -143   -132       O  
HETATM 1227  C4  4PT A1550      11.958  32.933   7.207  1.00 31.09           C  
ANISOU 1227  C4  4PT A1550     4841   3802   3169    157    576    294       C  
HETATM 1228  O4  4PT A1550      11.907  31.500   7.265  1.00 31.44           O  
ANISOU 1228  O4  4PT A1550     4830   3658   3457    311    101    -84       O  
HETATM 1229  P4  4PT A1550      12.465  30.732   8.607  1.00 32.36           P  
ANISOU 1229  P4  4PT A1550     4317   4400   3576     65    267   -230       P  
HETATM 1230  OP5 4PT A1550      11.127  29.989   9.033  1.00 34.28           O  
ANISOU 1230  OP5 4PT A1550     4947   4426   3651   -196     75   -336       O  
HETATM 1231  OP6 4PT A1550      13.552  29.777   8.017  1.00 32.93           O  
ANISOU 1231  OP6 4PT A1550     4970   3952   3587    406    522    -40       O  
HETATM 1232  OP4 4PT A1550      13.151  31.688   9.573  1.00 29.73           O  
ANISOU 1232  OP4 4PT A1550     4299   3488   3505   -211    -60    280       O  
HETATM 1233  C5  4PT A1550      12.374  33.301   5.753  1.00 31.86           C  
ANISOU 1233  C5  4PT A1550     4918   3867   3320    149    504    383       C  
HETATM 1234  O5  4PT A1550      13.736  32.965   5.654  1.00 35.48           O  
ANISOU 1234  O5  4PT A1550     5994   3963   3521    781    910    197       O  
HETATM 1235  P5  4PT A1550      14.158  31.588   4.863  1.00 41.26           P  
ANISOU 1235  P5  4PT A1550     6667   4704   4303   1035    488    -97       P  
HETATM 1236  OP8 4PT A1550      14.947  30.779   5.997  1.00 39.76           O  
ANISOU 1236  OP8 4PT A1550     6620   4239   4245   1683    717   -281       O  
HETATM 1237  OP7 4PT A1550      15.304  31.952   3.862  1.00 42.07           O  
ANISOU 1237  OP7 4PT A1550     6231   4930   4824   1273    656    262       O  
HETATM 1238  OP9 4PT A1550      12.941  30.862   4.387  1.00 37.38           O  
ANISOU 1238  OP9 4PT A1550     6228   4132   3839   1208    469   -134       O  
HETATM 1239  C6  4PT A1550      12.234  34.792   5.492  1.00 32.72           C  
ANISOU 1239  C6  4PT A1550     4963   4009   3458    209    500    259       C  
HETATM 1240  O6  4PT A1550      12.483  35.013   4.090  1.00 34.96           O  
ANISOU 1240  O6  4PT A1550     5888   4231   3164    430    609    297       O  
HETATM 1241  O   HOH A2001       0.117  22.567  12.782  1.00 44.56           O  
ANISOU 1241  O   HOH A2001     3365   6926   6639    496   -398   1103       O  
HETATM 1242  O   HOH A2002      17.627  39.668   2.743  1.00 52.17           O  
ANISOU 1242  O   HOH A2002     6638   7237   5945   1748    987   -461       O  
HETATM 1243  O   HOH A2003       1.472  39.232  18.084  1.00 49.25           O  
ANISOU 1243  O   HOH A2003     4472   7145   7094   1760    861   1821       O  
HETATM 1244  O   HOH A2004       2.154  39.906  15.785  1.00 37.97           O  
ANISOU 1244  O   HOH A2004     3333   6067   5025   -184    316   1366       O  
HETATM 1245  O   HOH A2005      -0.285  35.598  21.037  1.00 49.40           O  
ANISOU 1245  O   HOH A2005     3483   5366   9920    -68   -235    983       O  
HETATM 1246  O   HOH A2006      15.564  15.696  18.329  1.00 50.10           O  
ANISOU 1246  O   HOH A2006     4720   7929   6386  -1703  -1924   2726       O  
HETATM 1247  O   HOH A2007       0.788  39.295  10.572  1.00 46.76           O  
ANISOU 1247  O   HOH A2007     5117   6182   6466   -756   -624   3136       O  
HETATM 1248  O   HOH A2008      -5.949  38.412  11.590  1.00 55.43           O  
ANISOU 1248  O   HOH A2008     5131   8451   7475   -227   -291   1231       O  
HETATM 1249  O   HOH A2009      -3.563  25.750   8.498  1.00 80.37           O  
ANISOU 1249  O   HOH A2009     9321  16542   4671    102  -4405   1000       O  
HETATM 1250  O   HOH A2010      14.237  19.437  12.860  1.00 49.45           O  
ANISOU 1250  O   HOH A2010     6498   5818   6472    290   1582  -1528       O  
HETATM 1251  O   HOH A2011      16.283  22.677   9.699  1.00 49.32           O  
ANISOU 1251  O   HOH A2011     7435   5039   6266    307   1621  -1141       O  
HETATM 1252  O   HOH A2012      12.320  45.762  22.715  1.00 70.08           O  
ANISOU 1252  O   HOH A2012    15591   5721   5312   2881    120    737       O  
HETATM 1253  O   HOH A2013      25.695  35.713  29.710  1.00 63.74           O  
ANISOU 1253  O   HOH A2013     6206   9009   9001    -96   -993  -1887       O  
HETATM 1254  O   HOH A2014      22.728  27.901  31.646  1.00 48.20           O  
ANISOU 1254  O   HOH A2014     2906   8236   7171   -719    243  -1448       O  
HETATM 1255  O   HOH A2015       8.771  33.017   4.164  1.00 55.14           O  
ANISOU 1255  O   HOH A2015     7296   6403   7250   2306   -744   1614       O  
HETATM 1256  O   HOH A2016      -0.999  38.061  18.735  1.00 49.89           O  
ANISOU 1256  O   HOH A2016     3512   6601   8843  -1832   -504   2161       O  
HETATM 1257  O   HOH A2017       0.866  16.113  46.274  1.00 35.29           O  
ANISOU 1257  O   HOH A2017     4489   4230   4690     56    225   -704       O  
HETATM 1258  O   HOH A2018      -3.344  19.254  40.504  1.00 44.17           O  
ANISOU 1258  O   HOH A2018     4722   5535   6524    370    992   1346       O  
HETATM 1259  O   HOH A2019       1.715  22.512  45.795  1.00 40.50           O  
ANISOU 1259  O   HOH A2019     5316   5004   5069    737     30   -129       O  
HETATM 1260  O   HOH A2020      -4.488  23.141  44.312  1.00 51.76           O  
ANISOU 1260  O   HOH A2020     4569   8871   6225    107    679    980       O  
HETATM 1261  O   HOH A2021      -1.733  26.685  42.525  1.00 54.05           O  
ANISOU 1261  O   HOH A2021    10499   5155   4880   1030  -1733   -728       O  
HETATM 1262  O   HOH A2022      -4.575  21.950  41.173  1.00 56.84           O  
ANISOU 1262  O   HOH A2022     6082   8114   7398   -290   2239   2162       O  
HETATM 1263  O   HOH A2023       2.873  18.119  45.577  1.00 41.11           O  
ANISOU 1263  O   HOH A2023     7738   4628   3253   -951     28    114       O  
HETATM 1264  O   HOH A2024       7.288  21.512  43.269  1.00 46.16           O  
ANISOU 1264  O   HOH A2024     7814   5625   4100   -389   1112   -786       O  
HETATM 1265  O   HOH A2025       4.102  21.708  45.905  1.00 45.29           O  
ANISOU 1265  O   HOH A2025     6445   5783   4977   -720   1970   -881       O  
HETATM 1266  O   HOH A2026       8.642  17.068  42.553  1.00 58.17           O  
ANISOU 1266  O   HOH A2026     6071   6236   9792     11  -2628  -3387       O  
HETATM 1267  O   HOH A2027       4.052  27.842  40.417  1.00 54.12           O  
ANISOU 1267  O   HOH A2027     9507   7286   3768   1539   1602    912       O  
HETATM 1268  O   HOH A2028       1.654  28.290  38.421  1.00 54.52           O  
ANISOU 1268  O   HOH A2028     6666   7939   6110  -1991   3952  -2968       O  
HETATM 1269  O   HOH A2029       3.195  31.402  37.933  1.00 45.87           O  
ANISOU 1269  O   HOH A2029     6876   7266   3287   3589   1042    737       O  
HETATM 1270  O   HOH A2030       1.099  32.152  31.132  1.00 44.58           O  
ANISOU 1270  O   HOH A2030     5361   5824   5752   -479   1299    349       O  
HETATM 1271  O   HOH A2031       0.002  28.717  33.073  1.00 50.91           O  
ANISOU 1271  O   HOH A2031     5257   4508   9576    471    591   1682       O  
HETATM 1272  O   HOH A2032       7.373  38.664  30.628  1.00 37.57           O  
ANISOU 1272  O   HOH A2032     3375   5286   5613    131    245   -684       O  
HETATM 1273  O   HOH A2033       5.872  40.679  29.275  1.00 48.86           O  
ANISOU 1273  O   HOH A2033     5507   4026   9032   -290    220  -1667       O  
HETATM 1274  O   HOH A2034       4.036  38.601  26.296  1.00 48.85           O  
ANISOU 1274  O   HOH A2034     6558   4840   7160  -1516   2724   -197       O  
HETATM 1275  O   HOH A2035       2.705  39.178  22.635  1.00 41.44           O  
ANISOU 1275  O   HOH A2035     4868   5338   5537    703   -681    298       O  
HETATM 1276  O   HOH A2036       7.862  36.832  28.658  1.00 33.12           O  
ANISOU 1276  O   HOH A2036     3768   4189   4624    385    593    135       O  
HETATM 1277  O   HOH A2037       8.649  32.283  28.585  1.00 31.30           O  
ANISOU 1277  O   HOH A2037     4095   4249   3547    323   -348   -452       O  
HETATM 1278  O   HOH A2038       6.615  38.097  26.759  1.00 47.11           O  
ANISOU 1278  O   HOH A2038     5641   5641   6615   -822    915   1783       O  
HETATM 1279  O   HOH A2039      14.583  29.827  32.418  1.00 30.69           O  
ANISOU 1279  O   HOH A2039     2962   4412   4287   -606     12    -11       O  
HETATM 1280  O   HOH A2040      13.388  24.996  37.107  1.00 45.90           O  
ANISOU 1280  O   HOH A2040     5945   4279   7212   -187   -426  -1487       O  
HETATM 1281  O   HOH A2041      13.584  20.501  38.068  1.00 46.06           O  
ANISOU 1281  O   HOH A2041     6230   4838   6432   -691  -2623   1170       O  
HETATM 1282  O   HOH A2042       9.079  22.523  41.277  1.00 39.16           O  
ANISOU 1282  O   HOH A2042     5342   5489   4048   -144   1268   -481       O  
HETATM 1283  O   HOH A2043      10.824  14.677  34.678  1.00 49.83           O  
ANISOU 1283  O   HOH A2043     6597   4962   7372   -721   2870  -2654       O  
HETATM 1284  O   HOH A2044       8.590  13.509  33.214  1.00 55.84           O  
ANISOU 1284  O   HOH A2044     4202  11295   5717  -1550   -636   2118       O  
HETATM 1285  O   HOH A2045       4.361   8.836  29.677  1.00 51.10           O  
ANISOU 1285  O   HOH A2045     9340   4527   5546   1851   2020    931       O  
HETATM 1286  O   HOH A2046       8.005   6.434  29.962  1.00 55.21           O  
ANISOU 1286  O   HOH A2046     7279   7899   5796   1550   2716    -30       O  
HETATM 1287  O   HOH A2047       2.733  10.554  31.008  1.00 31.34           O  
ANISOU 1287  O   HOH A2047     3660   4117   4131   -290   -559    -18       O  
HETATM 1288  O   HOH A2048       4.746   8.564  37.534  1.00 34.59           O  
ANISOU 1288  O   HOH A2048     5213   3900   4028    197   -304   -625       O  
HETATM 1289  O   HOH A2049       2.414   8.582  40.651  1.00 29.63           O  
ANISOU 1289  O   HOH A2049     2496   4005   4755    433   -741    381       O  
HETATM 1290  O   HOH A2050       7.434  15.136  41.451  1.00 39.71           O  
ANISOU 1290  O   HOH A2050     5804   5280   4003  -1206   -764   -162       O  
HETATM 1291  O   HOH A2051       1.667  16.169  42.225  1.00 36.57           O  
ANISOU 1291  O   HOH A2051     4779   5013   4100    402    715    778       O  
HETATM 1292  O   HOH A2052       0.928   8.160  31.545  1.00 46.72           O  
ANISOU 1292  O   HOH A2052     6298   5189   6262    -50  -1174     12       O  
HETATM 1293  O   HOH A2053      -2.359  13.566  29.108  1.00 33.74           O  
ANISOU 1293  O   HOH A2053     3671   4445   4703    209   -630    106       O  
HETATM 1294  O   HOH A2054      -4.761  18.702  34.176  1.00 45.09           O  
ANISOU 1294  O   HOH A2054     4923   5269   6941    -49     76    744       O  
HETATM 1295  O   HOH A2055       0.806  22.282  31.218  1.00 29.02           O  
ANISOU 1295  O   HOH A2055     3139   3731   4154    -31    703      1       O  
HETATM 1296  O   HOH A2056      -7.234  13.306  27.846  1.00 51.57           O  
ANISOU 1296  O   HOH A2056     6130   4286   9176   -300   -972   -447       O  
HETATM 1297  O   HOH A2057      -4.697  11.923  29.555  1.00 38.43           O  
ANISOU 1297  O   HOH A2057     4397   4564   5640  -1490   -585    169       O  
HETATM 1298  O   HOH A2058      -3.759  15.217  27.187  1.00 40.22           O  
ANISOU 1298  O   HOH A2058     4174   6390   4716   -244    123    576       O  
HETATM 1299  O   HOH A2059      -6.930  16.852  33.733  1.00 43.91           O  
ANISOU 1299  O   HOH A2059     5672   5806   5205  -1366   -419   1119       O  
HETATM 1300  O   HOH A2060      -5.485  25.596  31.440  1.00 63.16           O  
ANISOU 1300  O   HOH A2060     7166  11545   5285   3873    557   -821       O  
HETATM 1301  O   HOH A2061       2.617  22.821  29.052  1.00 25.92           O  
ANISOU 1301  O   HOH A2061     1997   4071   3777    146    -63    264       O  
HETATM 1302  O   HOH A2062      -6.805  20.324  22.376  1.00 45.03           O  
ANISOU 1302  O   HOH A2062     4357   7190   5559   -477    666    -46       O  
HETATM 1303  O   HOH A2063      -8.428  22.636  23.112  1.00 43.68           O  
ANISOU 1303  O   HOH A2063     4153   5525   6916      9    894   1624       O  
HETATM 1304  O   HOH A2064      -7.246  28.221  25.721  1.00 71.87           O  
ANISOU 1304  O   HOH A2064     2645  14103  10559   3653  -2590    365       O  
HETATM 1305  O   HOH A2065       0.411  24.657  28.585  1.00 31.63           O  
ANISOU 1305  O   HOH A2065     3683   3683   4651    461   -495    911       O  
HETATM 1306  O   HOH A2066      -5.703  23.868  23.384  1.00 48.77           O  
ANISOU 1306  O   HOH A2066     4511   5130   8888  -2565   -352    799       O  
HETATM 1307  O   HOH A2067      -4.163  29.256  18.472  1.00 55.43           O  
ANISOU 1307  O   HOH A2067     7936   7368   5756    301   1066   2026       O  
HETATM 1308  O   HOH A2068      -0.909  32.467  24.717  1.00 46.05           O  
ANISOU 1308  O   HOH A2068     3967   7192   6338   -730   -858  -1378       O  
HETATM 1309  O   HOH A2069      -0.715  18.729  19.427  1.00 39.49           O  
ANISOU 1309  O   HOH A2069     4624   4817   5563  -1629  -1080   -493       O  
HETATM 1310  O   HOH A2070      -4.614  16.457  22.248  1.00 53.74           O  
ANISOU 1310  O   HOH A2070     6319   5584   8515   -880   1438  -2564       O  
HETATM 1311  O   HOH A2071      -3.172  23.366  13.374  1.00 55.24           O  
ANISOU 1311  O   HOH A2071     5770  10475   4744    157    393    358       O  
HETATM 1312  O   HOH A2072      -7.324  22.544  14.708  1.00 61.17           O  
ANISOU 1312  O   HOH A2072     5499  10061   7679  -1762    872   3076       O  
HETATM 1313  O   HOH A2073       4.014  20.426  14.070  1.00 56.11           O  
ANISOU 1313  O   HOH A2073     9028   4830   7461   1148    788   1391       O  
HETATM 1314  O   HOH A2074       8.726  17.565  14.507  1.00 54.07           O  
ANISOU 1314  O   HOH A2074    11978   4299   4265    711  -1606   -642       O  
HETATM 1315  O   HOH A2075       0.961  19.349  15.881  1.00 44.37           O  
ANISOU 1315  O   HOH A2075     7429   6014   3413  -2635  -1904    985       O  
HETATM 1316  O   HOH A2076      -0.650  11.727  25.367  1.00 54.36           O  
ANISOU 1316  O   HOH A2076    11271   4924   4456  -2041   1253    482       O  
HETATM 1317  O   HOH A2077      -3.049  14.970  24.631  1.00 42.34           O  
ANISOU 1317  O   HOH A2077     6014   5667   4404   -804   -417    256       O  
HETATM 1318  O   HOH A2078       7.149  15.182  17.884  1.00 41.34           O  
ANISOU 1318  O   HOH A2078     6118   5746   3843    141   1197   -874       O  
HETATM 1319  O   HOH A2079      11.774  34.112  28.842  1.00 31.25           O  
ANISOU 1319  O   HOH A2079     2336   4295   5242    111  -1188   -163       O  
HETATM 1320  O   HOH A2080       9.427  35.113  24.999  1.00 27.26           O  
ANISOU 1320  O   HOH A2080     2877   4167   3311   -297    598     78       O  
HETATM 1321  O   HOH A2081       8.573  38.654  24.263  1.00 36.29           O  
ANISOU 1321  O   HOH A2081     4819   3768   5201    487   -861  -1313       O  
HETATM 1322  O   HOH A2082      12.068  43.122  19.483  1.00 42.40           O  
ANISOU 1322  O   HOH A2082     4197   5692   6220   -266    565   -238       O  
HETATM 1323  O   HOH A2083       8.668  43.730  19.124  1.00 47.22           O  
ANISOU 1323  O   HOH A2083     4823   5623   7495    325    948   1705       O  
HETATM 1324  O   HOH A2084      11.517  35.452  10.942  1.00 29.44           O  
ANISOU 1324  O   HOH A2084     4262   3219   3706    -51    863      7       O  
HETATM 1325  O   HOH A2085      19.063  43.474  15.013  1.00 45.19           O  
ANISOU 1325  O   HOH A2085     7364   6024   3779    110   -803    114       O  
HETATM 1326  O   HOH A2086      17.011  33.988  12.420  1.00 31.34           O  
ANISOU 1326  O   HOH A2086     4766   2751   4390    450    411    122       O  
HETATM 1327  O   HOH A2087      19.252  37.422   8.036  1.00 40.47           O  
ANISOU 1327  O   HOH A2087     3780   5601   5995    392    822     85       O  
HETATM 1328  O   HOH A2088      19.354  39.298  10.017  1.00 51.87           O  
ANISOU 1328  O   HOH A2088     7105   5835   6767   1620   -252    534       O  
HETATM 1329  O   HOH A2089      15.065  41.609   4.131  1.00 44.61           O  
ANISOU 1329  O   HOH A2089     7248   6324   3376  -2141   -546    909       O  
HETATM 1330  O   HOH A2090      13.459  41.393   6.441  1.00 35.57           O  
ANISOU 1330  O   HOH A2090     3930   5035   4549   -775    775   -777       O  
HETATM 1331  O   HOH A2091       3.063  37.810  14.160  1.00 35.96           O  
ANISOU 1331  O   HOH A2091     2974   4924   5763    464    -30    464       O  
HETATM 1332  O   HOH A2092       3.023  37.911  20.123  1.00 39.21           O  
ANISOU 1332  O   HOH A2092     3951   5643   5302    387    218   1952       O  
HETATM 1333  O   HOH A2093       4.221  37.270  10.299  1.00 43.45           O  
ANISOU 1333  O   HOH A2093     4676   4756   7078   1056   -366   2149       O  
HETATM 1334  O   HOH A2094       2.395  35.198  20.420  1.00 31.87           O  
ANISOU 1334  O   HOH A2094     2727   5151   4230    922   -415    619       O  
HETATM 1335  O   HOH A2095       3.834  13.800  25.077  1.00 39.15           O  
ANISOU 1335  O   HOH A2095     6933   3580   4360     46    112    265       O  
HETATM 1336  O   HOH A2096      15.432  13.853  20.363  1.00 48.83           O  
ANISOU 1336  O   HOH A2096     8364   5187   4999   1661   1205     68       O  
HETATM 1337  O   HOH A2097       1.941  37.176  11.745  1.00 36.21           O  
ANISOU 1337  O   HOH A2097     4116   4381   5260  -1203   -264   1507       O  
HETATM 1338  O   HOH A2098      -0.552  38.120   7.930  1.00 54.82           O  
ANISOU 1338  O   HOH A2098     7297   5591   7937  -2145  -2834   2440       O  
HETATM 1339  O   HOH A2099      -4.212  37.760   9.327  1.00 54.52           O  
ANISOU 1339  O   HOH A2099     8720   4587   7406   1915  -2486    330       O  
HETATM 1340  O   HOH A2100      -2.616  25.945  11.076  1.00 41.98           O  
ANISOU 1340  O   HOH A2100     4706   5977   5267  -1135    146   -121       O  
HETATM 1341  O   HOH A2101      -5.079  36.637  15.071  1.00 74.00           O  
ANISOU 1341  O   HOH A2101     5520   7454  15141  -1496  -1577    -68       O  
HETATM 1342  O   HOH A2102       0.041  24.877  11.250  1.00 41.72           O  
ANISOU 1342  O   HOH A2102     4765   4498   6589  -1146   -494    -85       O  
HETATM 1343  O   HOH A2103       9.798  26.023   8.143  1.00 41.00           O  
ANISOU 1343  O   HOH A2103     7058   4472   4048    423    583   1471       O  
HETATM 1344  O   HOH A2104       7.362  29.000   6.816  1.00 63.97           O  
ANISOU 1344  O   HOH A2104    10303   8681   5320   4659  -2876  -2614       O  
HETATM 1345  O   HOH A2105      11.454  24.526  10.013  1.00 38.73           O  
ANISOU 1345  O   HOH A2105     7019   4777   2920    163    557    105       O  
HETATM 1346  O   HOH A2106      14.105  21.723  11.614  1.00 53.92           O  
ANISOU 1346  O   HOH A2106     6026   8318   6141   2601   2008   -332       O  
HETATM 1347  O   HOH A2107      12.862  21.357  16.984  1.00 34.73           O  
ANISOU 1347  O   HOH A2107     5798   3768   3630   -100   1175     14       O  
HETATM 1348  O   HOH A2108      10.565  20.300  11.100  1.00 39.56           O  
ANISOU 1348  O   HOH A2108     3314   4663   7052   -163   1237   -721       O  
HETATM 1349  O   HOH A2109       6.980  20.017  12.605  1.00 56.53           O  
ANISOU 1349  O   HOH A2109     6046   8975   6456   3689  -2898  -2129       O  
HETATM 1350  O   HOH A2110      20.919  21.449  15.329  1.00 36.67           O  
ANISOU 1350  O   HOH A2110     4378   4973   4582   1538    349   -174       O  
HETATM 1351  O   HOH A2111      14.482  19.188  15.945  1.00 44.20           O  
ANISOU 1351  O   HOH A2111     7329   4103   5360  -1220     23   -153       O  
HETATM 1352  O   HOH A2112      28.781  18.018  22.290  1.00 53.04           O  
ANISOU 1352  O   HOH A2112     5247   8696   6208   -675  -1890   -863       O  
HETATM 1353  O   HOH A2113      23.286  12.445  20.398  1.00 58.71           O  
ANISOU 1353  O   HOH A2113     6612   5518  10178     31    513  -3009       O  
HETATM 1354  O   HOH A2114      25.780  24.894  15.946  1.00 56.41           O  
ANISOU 1354  O   HOH A2114     5413   7506   8514    634   -360   3441       O  
HETATM 1355  O   HOH A2115      23.608  30.142  27.148  1.00 46.34           O  
ANISOU 1355  O   HOH A2115     4112   7185   6309   1251    259   -671       O  
HETATM 1356  O   HOH A2116      24.861  33.095  26.827  1.00 50.08           O  
ANISOU 1356  O   HOH A2116     7252   6301   5472    897  -2138   -302       O  
HETATM 1357  O   HOH A2117      19.339  43.920  27.145  1.00 35.17           O  
ANISOU 1357  O   HOH A2117     4983   4610   3770   -213    -94   -133       O  
HETATM 1358  O   HOH A2118      12.007  46.108  25.332  1.00 50.70           O  
ANISOU 1358  O   HOH A2118     6402   7015   5845   1518   -301  -1555       O  
HETATM 1359  O   HOH A2119      27.669  29.390  15.219  1.00 53.27           O  
ANISOU 1359  O   HOH A2119     3881   7916   8441    119   1476    359       O  
HETATM 1360  O   HOH A2120      25.406  28.421  12.450  1.00 56.73           O  
ANISOU 1360  O   HOH A2120     6901   7056   7597   2059   3193   2711       O  
HETATM 1361  O   HOH A2121      21.165  23.864  10.796  1.00 54.97           O  
ANISOU 1361  O   HOH A2121     8476   8812   3598   -981    282  -1074       O  
HETATM 1362  O   HOH A2122      28.512  25.634  11.906  1.00 80.69           O  
ANISOU 1362  O   HOH A2122     6484  11396  12779   1421   2546   6899       O  
HETATM 1363  O   HOH A2123      17.205  27.333   7.564  1.00 46.53           O  
ANISOU 1363  O   HOH A2123     6857   5770   5053   1544   1649    928       O  
HETATM 1364  O   HOH A2124      18.809  33.109  10.837  1.00 47.27           O  
ANISOU 1364  O   HOH A2124     6136   7111   4713   2037   1272    377       O  
HETATM 1365  O   HOH A2125      22.997  31.662   9.857  1.00 42.58           O  
ANISOU 1365  O   HOH A2125     5318   5585   5274   -228   1040   1002       O  
HETATM 1366  O   HOH A2126      26.230  32.005  14.907  1.00 96.37           O  
ANISOU 1366  O   HOH A2126    10180  18810   7623  -1233   6347  -2041       O  
HETATM 1367  O   HOH A2127      13.874  26.692  10.303  1.00 39.83           O  
ANISOU 1367  O   HOH A2127     6330   4527   4276     78   1313   -521       O  
HETATM 1368  O   HOH A2128      17.729  25.151   9.587  1.00 38.98           O  
ANISOU 1368  O   HOH A2128     4702   6370   3739   1052    228   -893       O  
HETATM 1369  O   HOH A2129      10.240  35.892  27.525  1.00 33.77           O  
ANISOU 1369  O   HOH A2129     3285   5198   4346     48   -729  -1721       O  
HETATM 1370  O   HOH A2130       9.752  42.274  31.785  1.00 51.49           O  
ANISOU 1370  O   HOH A2130     5323   6857   7382    667   1480   2819       O  
HETATM 1371  O   HOH A2131       9.441  39.862  32.895  1.00 38.49           O  
ANISOU 1371  O   HOH A2131     4211   5052   5360   -444   -158   -690       O  
HETATM 1372  O   HOH A2132      11.597  38.331  34.724  1.00 33.00           O  
ANISOU 1372  O   HOH A2132     4832   4003   3701   -330   -288    122       O  
HETATM 1373  O   HOH A2133      24.230  38.699  28.249  1.00 53.78           O  
ANISOU 1373  O   HOH A2133     6526   7214   6692  -2824    518   -263       O  
HETATM 1374  O   HOH A2134      22.109  33.076  29.855  1.00 55.92           O  
ANISOU 1374  O   HOH A2134     7642   7020   6585   2334  -1516  -2538       O  
HETATM 1375  O   HOH A2135      13.441  31.267  35.843  1.00 58.93           O  
ANISOU 1375  O   HOH A2135     8696   7119   6572  -1097  -2906  -1035       O  
HETATM 1376  O   HOH A2136      20.692  26.201  32.253  1.00 36.24           O  
ANISOU 1376  O   HOH A2136     3480   5233   5056   -995     20   -241       O  
HETATM 1377  O   HOH A2137      12.774  27.110  34.998  1.00 44.14           O  
ANISOU 1377  O   HOH A2137     5424   4956   6390   -272   1476    876       O  
HETATM 1378  O   HOH A2138      24.699  23.755  24.176  1.00 53.89           O  
ANISOU 1378  O   HOH A2138     5879   4381  10214   1151   1464    753       O  
HETATM 1379  O   HOH A2139      19.716  19.864  33.042  1.00 52.03           O  
ANISOU 1379  O   HOH A2139     7808   5890   6070   2287   1456    211       O  
HETATM 1380  O   HOH A2140      17.058  26.122  34.158  1.00 55.26           O  
ANISOU 1380  O   HOH A2140     2656   6663  11676  -1511    538  -2640       O  
HETATM 1381  O   HOH A2141      13.767  22.635  35.936  1.00 31.25           O  
ANISOU 1381  O   HOH A2141     3795   4231   3844    644    592   -393       O  
HETATM 1382  O   HOH A2142       1.549  15.476  48.767  1.00 40.79           O  
ANISOU 1382  O   HOH A2142     6437   4995   4066   -190   -161   -533       O  
HETATM 1383  O   HOH A2143      17.797  15.295  32.867  1.00 68.33           O  
ANISOU 1383  O   HOH A2143     5211  13390   7360    780   -601   3044       O  
HETATM 1384  O   HOH A2144      17.153  19.874  34.801  1.00 52.46           O  
ANISOU 1384  O   HOH A2144     6981   6549   6402   2819    -91   -178       O  
HETATM 1385  O   HOH A2145      17.800  12.391  27.249  1.00 31.65           O  
ANISOU 1385  O   HOH A2145     4928   3875   3222    553    595   -315       O  
HETATM 1386  O   HOH A2146      -5.101  19.191  37.718  1.00 55.82           O  
ANISOU 1386  O   HOH A2146     7289   5691   8227   -623  -2132   2348       O  
HETATM 1387  O   HOH A2147       0.230  28.550  40.399  1.00 53.77           O  
ANISOU 1387  O   HOH A2147     6866   6967   6594   1307   1554  -1625       O  
HETATM 1388  O   HOH A2148      22.168  10.943  22.613  1.00 41.71           O  
ANISOU 1388  O   HOH A2148     3926   5659   6261    473    -30  -3225       O  
HETATM 1389  O   HOH A2149       0.527  26.831  31.556  1.00 59.01           O  
ANISOU 1389  O   HOH A2149     8539   4686   9194    697  -2294   -478       O  
HETATM 1390  O   HOH A2150      26.777  20.747  30.568  1.00 42.13           O  
ANISOU 1390  O   HOH A2150     4898   4560   6548  -1460   1457   -145       O  
HETATM 1391  O   HOH A2151      24.509  16.860  32.774  1.00 67.57           O  
ANISOU 1391  O   HOH A2151     9705   8236   7730   4051  -4312   -896       O  
HETATM 1392  O   HOH A2152      29.033  15.665  26.778  1.00 43.65           O  
ANISOU 1392  O   HOH A2152     5343   6548   4694    762   -493   -166       O  
HETATM 1393  O   HOH A2153       4.414  40.197  24.104  1.00 56.48           O  
ANISOU 1393  O   HOH A2153     6157   5292  10011   -169   1090    415       O  
HETATM 1394  O   HOH A2154       6.823  40.582  24.687  1.00 40.12           O  
ANISOU 1394  O   HOH A2154     3407   5195   6639    635   -894  -1077       O  
HETATM 1395  O   HOH A2155      12.100  38.255   8.553  1.00 32.35           O  
ANISOU 1395  O   HOH A2155     4483   4301   3507    268    721    439       O  
HETATM 1396  O   HOH A2156      11.016  40.042   6.920  1.00 33.87           O  
ANISOU 1396  O   HOH A2156     4196   4506   4164    -82    260    -54       O  
HETATM 1397  O   HOH A2157       7.093  34.393   6.230  1.00 56.09           O  
ANISOU 1397  O   HOH A2157     7580  10394   3337   1031    612    379       O  
HETATM 1398  O   HOH A2158       8.034  11.312  31.547  1.00 55.12           O  
ANISOU 1398  O   HOH A2158     3868   9842   7234  -2276    396    962       O  
HETATM 1399  O   HOH A2159       1.701  12.180  29.011  1.00 34.07           O  
ANISOU 1399  O   HOH A2159     4421   4343   4179    393   -290    -15       O  
HETATM 1400  O   HOH A2160      -0.609  11.651  28.046  1.00 35.92           O  
ANISOU 1400  O   HOH A2160     5189   4263   4196     39  -1100   -285       O  
HETATM 1401  O   HOH A2161      -0.870  24.568  31.309  1.00 38.55           O  
ANISOU 1401  O   HOH A2161     4942   3509   6194   1237   -566   -148       O  
HETATM 1402  O   HOH A2162      -5.851  21.431  20.130  1.00 45.96           O  
ANISOU 1402  O   HOH A2162     3148   8582   5732    368   -905    720       O  
HETATM 1403  O   HOH A2163      -4.022  32.460  20.513  1.00 64.42           O  
ANISOU 1403  O   HOH A2163     5613   6571  12292    717    285   1972       O  
CONECT 1208 1209                                                                
CONECT 1209 1208 1210                                                           
CONECT 1210 1209 1211 1212                                                      
CONECT 1211 1210                                                                
CONECT 1212 1210 1213                                                           
CONECT 1213 1212 1214                                                           
CONECT 1214 1213 1215 1216 1217                                                 
CONECT 1215 1214                                                                
CONECT 1216 1214                                                                
CONECT 1217 1214 1218                                                           
CONECT 1218 1217 1219 1239                                                      
CONECT 1219 1218 1220 1221                                                      
CONECT 1220 1219                                                                
CONECT 1221 1219 1222 1227                                                      
CONECT 1222 1221 1223                                                           
CONECT 1223 1222 1224 1225 1226                                                 
CONECT 1224 1223                                                                
CONECT 1225 1223                                                                
CONECT 1226 1223                                                                
CONECT 1227 1221 1228 1233                                                      
CONECT 1228 1227 1229                                                           
CONECT 1229 1228 1230 1231 1232                                                 
CONECT 1230 1229                                                                
CONECT 1231 1229                                                                
CONECT 1232 1229                                                                
CONECT 1233 1227 1234 1239                                                      
CONECT 1234 1233 1235                                                           
CONECT 1235 1234 1236 1237 1238                                                 
CONECT 1236 1235                                                                
CONECT 1237 1235                                                                
CONECT 1238 1235                                                                
CONECT 1239 1218 1233 1240                                                      
CONECT 1240 1239                                                                
MASTER      400    0    1    4   12    0    4    6 1402    1   33   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.