CNRS Nantes University UFIP UFIP
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***  3llo  ***

elNémo ID: 19112216345649727

Job options:

ID        	=	 19112216345649727
JOBID     	=	 3llo
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 3llo

HEADER    MOTOR PROTEIN                           29-JAN-10   3LLO              
TITLE     CRYSTAL STRUCTURE OF THE STAS DOMAIN OF MOTOR PROTEIN PRESTIN (ANION  
TITLE    2 TRANSPORTER SLC26A5)                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRESTIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 505-563, 637-718;                             
COMPND   5 SYNONYM: SOLUTE CARRIER FAMILY 26 MEMBER 5;                          
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: SLC26A5, PRES;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STAS DOMAIN, CELL SHAPE, GLYCOPROTEIN, MEMBRANE, MOTOR PROTEIN,       
KEYWDS   2 TRANSMEMBRANE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.PASQUALETTO,R.AIELLO,G.BONETTO,R.BATTISTUTTA                        
REVDAT   3   23-AUG-17 3LLO    1       SOURCE REMARK                            
REVDAT   2   28-JUL-10 3LLO    1       JRNL                                     
REVDAT   1   26-MAY-10 3LLO    0                                                
JRNL        AUTH   E.PASQUALETTO,R.AIELLO,L.GESIOT,G.BONETTO,M.BELLANDA,        
JRNL        AUTH 2 R.BATTISTUTTA                                                
JRNL        TITL   STRUCTURE OF THE CYTOSOLIC PORTION OF THE MOTOR PROTEIN      
JRNL        TITL 2 PRESTIN AND FUNCTIONAL ROLE OF THE STAS DOMAIN IN SLC26/SULP 
JRNL        TITL 3 ANION TRANSPORTERS.                                          
JRNL        REF    J.MOL.BIOL.                   V. 400   448 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20471983                                                     
JRNL        DOI    10.1016/J.JMB.2010.05.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 1.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20831                          
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) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1062                            
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) : 1.57                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.61                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1387                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 92                           
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1031                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 103                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32000                                              
REMARK   3    B22 (A**2) : 0.32000                                              
REMARK   3    B33 (A**2) : -0.47000                                             
REMARK   3    B12 (A**2) : 0.16000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.087         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.076         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.044         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.677         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1082 ; 0.027 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1476 ; 2.108 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   138 ; 5.761 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    50 ;35.989 ;25.600       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   172 ;11.167 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;13.635 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   171 ; 0.165 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   822 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):   668 ; 2.551 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1089 ; 3.902 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   414 ; 5.736 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   383 ; 8.556 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1082 ; 2.949 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.                  
REMARK   3  U VALUES: REFINED INDIVIDUALLY                                      
REMARK   4                                                                      
REMARK   4 3LLO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057430.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93                               
REMARK 200  MONOCHROMATOR                  : DIAMOND (111)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.15                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20860                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.570                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.408                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 11.30                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200   FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.49600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49600                            
REMARK 200   FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER 2.1.4, SHELX, DM 6.1, SHELXD                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 4.5% (V/V) PEG   
REMARK 280  400, 0.1% (W/V) OCTYL-BETA-D-GLUCOPYRANOSIDE, 0.09 M MES, PH 6.5,   
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 293.0K                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       22.37667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.75333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       44.75333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       22.37667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU A   556                                                      
REMARK 465     LYS A   557                                                      
REMARK 465     ARG A   558                                                      
REMARK 465     LYS A   559                                                      
REMARK 465     THR A   560                                                      
REMARK 465     GLY A   561                                                      
REMARK 465     VAL A   562                                                      
REMARK 465     ASN A   563                                                      
REMARK 465     GLY A   635                                                      
REMARK 465     SER A   636                                                      
REMARK 465     GLU A   637                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 522      124.65    -39.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     BOG A  719                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 719                 
DBREF  3LLO A  505   563  UNP    Q9EPH0   S26A5_RAT      505    563             
DBREF  3LLO A  637   718  UNP    Q9EPH0   S26A5_RAT      637    718             
SEQADV 3LLO GLY A  635  UNP  Q9EPH0              LINKER                         
SEQADV 3LLO SER A  636  UNP  Q9EPH0              LINKER                         
SEQRES   1 A  143  SER PRO SER TYR THR VAL LEU GLY GLN LEU PRO ASP THR          
SEQRES   2 A  143  ASP VAL TYR ILE ASP ILE ASP ALA TYR GLU GLU VAL LYS          
SEQRES   3 A  143  GLU ILE PRO GLY ILE LYS ILE PHE GLN ILE ASN ALA PRO          
SEQRES   4 A  143  ILE TYR TYR ALA ASN SER ASP LEU TYR SER SER ALA LEU          
SEQRES   5 A  143  LYS ARG LYS THR GLY VAL ASN GLY SER GLU ASN ILE HIS          
SEQRES   6 A  143  THR VAL ILE LEU ASP PHE THR GLN VAL ASN PHE MET ASP          
SEQRES   7 A  143  SER VAL GLY VAL LYS THR LEU ALA GLY ILE VAL LYS GLU          
SEQRES   8 A  143  TYR GLY ASP VAL GLY ILE TYR VAL TYR LEU ALA GLY CYS          
SEQRES   9 A  143  SER ALA GLN VAL VAL ASN ASP LEU THR SER ASN ARG PHE          
SEQRES  10 A  143  PHE GLU ASN PRO ALA LEU LYS GLU LEU LEU PHE HIS SER          
SEQRES  11 A  143  ILE HIS ASP ALA VAL LEU GLY SER GLN VAL ARG GLU ALA          
HET    BOG  A 719      10                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
FORMUL   2  BOG    C14 H28 O6                                                   
FORMUL   3  HOH   *103(H2 O)                                                    
HELIX    1   1 PRO A  543  ALA A  555  1                                  13    
HELIX    2   2 ASP A  653  ASP A  669  1                                  17    
HELIX    3   3 SER A  680  ASN A  690  1                                  11    
HELIX    4   4 ASN A  695  GLU A  700  5                                   6    
HELIX    5   5 SER A  705  SER A  713  1                                   9    
SHEET    1   A 6 TYR A 520  ASP A 522  0                                        
SHEET    2   A 6 TYR A 508  GLN A 513 -1  N  GLY A 512   O  ILE A 521           
SHEET    3   A 6 ILE A 535  ILE A 540 -1  O  GLN A 539   N  THR A 509           
SHEET    4   A 6 THR A 641  ASP A 645  1  O  ILE A 643   N  LYS A 536           
SHEET    5   A 6 TYR A 673  ALA A 677  1  O  ALA A 677   N  LEU A 644           
SHEET    6   A 6 LEU A 702  PHE A 703  1  O  PHE A 703   N  LEU A 676           
SITE     1 AC1  6 HOH A  88  GLY A 668  TYR A 673  HIS A 704                    
SITE     2 AC1  6 GLU A 717  ALA A 718                                          
CRYST1   61.590   61.590   67.130  90.00  90.00 120.00 P 31 2 1      6          
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      0.016236  0.009374  0.000000        0.00000                         
SCALE2      0.000000  0.018748  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014896        0.00000                         
ATOM      1  N   SER A 505      17.043   5.866   7.905  1.00 44.18           N  
ANISOU    1  N   SER A 505     5408   5697   5681    109    263   -209       N  
ATOM      2  CA  SER A 505      18.407   6.088   8.511  1.00 43.19           C  
ANISOU    2  CA  SER A 505     5502   5511   5394     62    183    -52       C  
ATOM      3  C   SER A 505      19.408   6.560   7.425  1.00 41.28           C  
ANISOU    3  C   SER A 505     5389   5159   5136    -42    129   -272       C  
ATOM      4  O   SER A 505      19.362   6.088   6.290  1.00 42.11           O  
ANISOU    4  O   SER A 505     5548   5377   5071    236     69   -311       O  
ATOM      5  CB  SER A 505      18.941   4.790   9.151  1.00 43.95           C  
ANISOU    5  CB  SER A 505     5684   5560   5455     31    198     11       C  
ATOM      6  OG  SER A 505      20.302   4.908   9.605  1.00 42.84           O  
ANISOU    6  OG  SER A 505     5448   5659   5171    378    802    502       O  
ATOM      7  N   PRO A 506      20.338   7.458   7.782  1.00 39.41           N  
ANISOU    7  N   PRO A 506     5330   4692   4950   -122    151   -366       N  
ATOM      8  CA  PRO A 506      21.310   7.714   6.767  1.00 35.96           C  
ANISOU    8  CA  PRO A 506     4943   4114   4604    -90    232   -575       C  
ATOM      9  C   PRO A 506      22.343   6.593   6.688  1.00 31.78           C  
ANISOU    9  C   PRO A 506     4609   3450   4014    -66    211   -497       C  
ATOM     10  O   PRO A 506      23.098   6.674   5.743  1.00 32.16           O  
ANISOU   10  O   PRO A 506     4855   3273   4089     -3    397   -748       O  
ATOM     11  CB  PRO A 506      22.045   9.018   7.260  1.00 37.46           C  
ANISOU   11  CB  PRO A 506     5189   4311   4731    -48    250   -558       C  
ATOM     12  CG  PRO A 506      22.059   8.780   8.836  1.00 40.71           C  
ANISOU   12  CG  PRO A 506     5427   4925   5113   -294    -13   -428       C  
ATOM     13  CD  PRO A 506      20.628   8.186   9.057  1.00 40.44           C  
ANISOU   13  CD  PRO A 506     5524   4803   5037   -229    201   -421       C  
ATOM     14  N   SER A 507      22.449   5.608   7.623  1.00 26.83           N  
ANISOU   14  N   SER A 507     3969   2671   3553     17    130   -748       N  
ATOM     15  CA  SER A 507      23.677   4.737   7.531  1.00 24.38           C  
ANISOU   15  CA  SER A 507     3619   2636   3007    -57    105   -490       C  
ATOM     16  C   SER A 507      23.406   3.500   6.691  1.00 22.66           C  
ANISOU   16  C   SER A 507     3226   2393   2991    -78     98   -508       C  
ATOM     17  O   SER A 507      24.367   2.818   6.295  1.00 22.25           O  
ANISOU   17  O   SER A 507     3265   2564   2622    -39    162   -264       O  
ATOM     18  CB  SER A 507      24.215   4.236   8.904  1.00 25.65           C  
ANISOU   18  CB  SER A 507     3900   2672   3172   -209    141   -337       C  
ATOM     19  OG  SER A 507      23.310   3.211   9.409  1.00 32.93           O  
ANISOU   19  OG  SER A 507     4823   4336   3352   -193    318   -146       O  
ATOM     20  N   TYR A 508      22.139   3.223   6.396  1.00 22.25           N  
ANISOU   20  N   TYR A 508     3163   2280   3011     24     19   -471       N  
ATOM     21  CA  TYR A 508      21.793   2.070   5.547  1.00 21.79           C  
ANISOU   21  CA  TYR A 508     3099   2232   2946    -50    139   -198       C  
ATOM     22  C   TYR A 508      20.471   2.360   4.901  1.00 20.23           C  
ANISOU   22  C   TYR A 508     2863   1955   2868   -116    239   -287       C  
ATOM     23  O   TYR A 508      19.722   3.291   5.330  1.00 21.83           O  
ANISOU   23  O   TYR A 508     2921   2206   3167    161    352   -375       O  
ATOM     24  CB  TYR A 508      21.745   0.745   6.386  1.00 23.88           C  
ANISOU   24  CB  TYR A 508     3490   2272   3310   -177    169   -233       C  
ATOM     25  CG  TYR A 508      20.504   0.759   7.274  1.00 26.15           C  
ANISOU   25  CG  TYR A 508     3962   2977   2994   -233    290    -51       C  
ATOM     26  CD1 TYR A 508      19.294   0.242   6.825  1.00 30.73           C  
ANISOU   26  CD1 TYR A 508     3949   4015   3709   -126    495    309       C  
ATOM     27  CD2 TYR A 508      20.508   1.464   8.503  1.00 29.82           C  
ANISOU   27  CD2 TYR A 508     4255   3816   3257     56    299   -215       C  
ATOM     28  CE1 TYR A 508      18.109   0.335   7.602  1.00 37.50           C  
ANISOU   28  CE1 TYR A 508     4696   5680   3869   -504    828     16       C  
ATOM     29  CE2 TYR A 508      19.329   1.537   9.287  1.00 36.93           C  
ANISOU   29  CE2 TYR A 508     4574   5411   4044   -290    436   -275       C  
ATOM     30  CZ  TYR A 508      18.155   0.983   8.809  1.00 38.54           C  
ANISOU   30  CZ  TYR A 508     4584   5829   4229   -496    910   -132       C  
ATOM     31  OH  TYR A 508      16.993   1.073   9.552  1.00 43.70           O  
ANISOU   31  OH  TYR A 508     5098   7162   4345    159    928      7       O  
ATOM     32  N   THR A 509      20.176   1.646   3.841  1.00 18.30           N  
ANISOU   32  N   THR A 509     2600   1777   2575    -89    262    -37       N  
ATOM     33  CA  THR A 509      18.912   1.755   3.162  1.00 18.65           C  
ANISOU   33  CA  THR A 509     2432   1866   2787    -61    121   -130       C  
ATOM     34  C   THR A 509      18.370   0.340   2.933  1.00 17.64           C  
ANISOU   34  C   THR A 509     2086   1906   2708    -54     41   -170       C  
ATOM     35  O   THR A 509      19.095  -0.557   2.483  1.00 19.02           O  
ANISOU   35  O   THR A 509     2292   1891   3043     61    360   -202       O  
ATOM     36  CB  THR A 509      19.109   2.455   1.781  1.00 18.68           C  
ANISOU   36  CB  THR A 509     2592   1675   2830   -191    -32    146       C  
ATOM     37  OG1 THR A 509      19.742   3.730   1.975  1.00 21.77           O  
ANISOU   37  OG1 THR A 509     3020   1994   3255   -187    324     42       O  
ATOM     38  CG2 THR A 509      17.790   2.621   1.084  1.00 21.27           C  
ANISOU   38  CG2 THR A 509     2787   1903   3391    344     22   -113       C  
ATOM     39  N   VAL A 510      17.114   0.121   3.295  1.00 17.78           N  
ANISOU   39  N   VAL A 510     2254   1928   2573    -46     92    -64       N  
ATOM     40  CA  VAL A 510      16.516  -1.127   3.015  1.00 17.09           C  
ANISOU   40  CA  VAL A 510     1950   1934   2608    -11    337   -121       C  
ATOM     41  C   VAL A 510      16.121  -1.174   1.532  1.00 16.52           C  
ANISOU   41  C   VAL A 510     2036   1813   2428    238    381     97       C  
ATOM     42  O   VAL A 510      15.482  -0.264   1.015  1.00 18.23           O  
ANISOU   42  O   VAL A 510     1873   2320   2730    300    235    160       O  
ATOM     43  CB  VAL A 510      15.220  -1.292   3.901  1.00 18.21           C  
ANISOU   43  CB  VAL A 510     2107   2270   2541    -65    492    -79       C  
ATOM     44  CG1 VAL A 510      14.445  -2.619   3.483  1.00 19.84           C  
ANISOU   44  CG1 VAL A 510     2302   2046   3188   -362    546   -192       C  
ATOM     45  CG2 VAL A 510      15.596  -1.250   5.371  1.00 22.77           C  
ANISOU   45  CG2 VAL A 510     3091   2738   2821   -158    486     99       C  
ATOM     46  N   LEU A 511      16.493  -2.254   0.849  1.00 16.53           N  
ANISOU   46  N   LEU A 511     2011   1946   2321    119    478    -46       N  
ATOM     47  CA  LEU A 511      16.177  -2.397  -0.560  1.00 16.67           C  
ANISOU   47  CA  LEU A 511     1793   2072   2468     46    233     34       C  
ATOM     48  C   LEU A 511      15.071  -3.425  -0.786  1.00 17.22           C  
ANISOU   48  C   LEU A 511     2103   2022   2415    -80    216    222       C  
ATOM     49  O   LEU A 511      14.947  -4.398  -0.027  1.00 17.07           O  
ANISOU   49  O   LEU A 511     2212   1704   2569   -204    146    448       O  
ATOM     50  CB  LEU A 511      17.422  -2.804  -1.420  1.00 15.92           C  
ANISOU   50  CB  LEU A 511     1503   1875   2668   -131    336    -11       C  
ATOM     51  CG  LEU A 511      18.683  -1.958  -1.222  1.00 14.66           C  
ANISOU   51  CG  LEU A 511     1414   1470   2684   -367    412      1       C  
ATOM     52  CD1 LEU A 511      19.766  -2.512  -2.204  1.00 14.58           C  
ANISOU   52  CD1 LEU A 511     1367   1822   2351     40    353    175       C  
ATOM     53  CD2 LEU A 511      18.466  -0.432  -1.378  1.00 17.56           C  
ANISOU   53  CD2 LEU A 511     2223   1577   2869    393     55    437       C  
ATOM     54  N   GLY A 512      14.315  -3.256  -1.868  1.00 17.19           N  
ANISOU   54  N   GLY A 512     1672   2221   2636     10     80    189       N  
ATOM     55  CA  GLY A 512      13.360  -4.257  -2.343  1.00 18.15           C  
ANISOU   55  CA  GLY A 512     2112   2198   2585   -308    122    184       C  
ATOM     56  C   GLY A 512      13.597  -4.537  -3.804  1.00 17.82           C  
ANISOU   56  C   GLY A 512     2047   2179   2543   -292     29    286       C  
ATOM     57  O   GLY A 512      14.500  -3.905  -4.454  1.00 18.72           O  
ANISOU   57  O   GLY A 512     2141   2228   2742   -244     77    538       O  
ATOM     58  N   GLN A 513      12.881  -5.533  -4.308  1.00 18.77           N  
ANISOU   58  N   GLN A 513     2213   2389   2529    -88   -206    329       N  
ATOM     59  CA  GLN A 513      13.025  -5.947  -5.700  1.00 18.92           C  
ANISOU   59  CA  GLN A 513     2125   2432   2630    -41   -234    352       C  
ATOM     60  C   GLN A 513      11.877  -5.282  -6.537  1.00 20.21           C  
ANISOU   60  C   GLN A 513     2316   2599   2761    -53   -176    449       C  
ATOM     61  O   GLN A 513      10.700  -5.263  -6.116  1.00 21.34           O  
ANISOU   61  O   GLN A 513     2396   2890   2819    187     71    587       O  
ATOM     62  CB  GLN A 513      12.836  -7.454  -5.754  1.00 19.97           C  
ANISOU   62  CB  GLN A 513     2571   2308   2708    -91    -53    289       C  
ATOM     63  CG  GLN A 513      13.176  -8.049  -7.174  1.00 21.05           C  
ANISOU   63  CG  GLN A 513     2507   2489   3002   -516    219      0       C  
ATOM     64  CD  GLN A 513      12.763  -9.473  -7.236  1.00 27.17           C  
ANISOU   64  CD  GLN A 513     3464   2747   4109   -550    607   -126       C  
ATOM     65  OE1 GLN A 513      11.708  -9.837  -6.719  1.00 31.58           O  
ANISOU   65  OE1 GLN A 513     3681   3960   4355   -659    260   -166       O  
ATOM     66  NE2 GLN A 513      13.569 -10.303  -7.837  1.00 34.10           N  
ANISOU   66  NE2 GLN A 513     3899   3381   5677   -880    992    -43       N  
ATOM     67  N   LEU A 514      12.249  -4.733  -7.692  1.00 19.33           N  
ANISOU   67  N   LEU A 514     2476   2226   2643   -138   -290    731       N  
ATOM     68  CA  LEU A 514      11.258  -4.282  -8.665  1.00 21.10           C  
ANISOU   68  CA  LEU A 514     2739   2482   2795   -344   -306    578       C  
ATOM     69  C   LEU A 514      10.684  -5.567  -9.269  1.00 23.86           C  
ANISOU   69  C   LEU A 514     2984   2756   3323   -244   -205    567       C  
ATOM     70  O   LEU A 514      11.432  -6.402  -9.779  1.00 24.31           O  
ANISOU   70  O   LEU A 514     3232   2806   3199   -201   -298    693       O  
ATOM     71  CB  LEU A 514      11.932  -3.373  -9.702  1.00 21.38           C  
ANISOU   71  CB  LEU A 514     2796   2605   2719   -116   -168    806       C  
ATOM     72  CG  LEU A 514      10.924  -2.721 -10.672  1.00 22.76           C  
ANISOU   72  CG  LEU A 514     2740   3013   2895     52   -342    758       C  
ATOM     73  CD1 LEU A 514      10.031  -1.642  -9.949  1.00 25.69           C  
ANISOU   73  CD1 LEU A 514     2229   3619   3913    414   -307    977       C  
ATOM     74  CD2 LEU A 514      11.731  -2.053 -11.811  1.00 23.56           C  
ANISOU   74  CD2 LEU A 514     3165   3070   2716   -322   -624    759       C  
ATOM     75  N   PRO A 515       9.360  -5.729  -9.181  1.00 26.53           N  
ANISOU   75  N   PRO A 515     3135   3142   3800   -393    -68    416       N  
ATOM     76  CA  PRO A 515       8.817  -7.080  -9.498  1.00 28.25           C  
ANISOU   76  CA  PRO A 515     3248   3426   4057   -443   -162    333       C  
ATOM     77  C   PRO A 515       9.181  -7.641 -10.885  1.00 29.09           C  
ANISOU   77  C   PRO A 515     3357   3583   4111   -414   -338    248       C  
ATOM     78  O   PRO A 515       9.131  -6.917 -11.901  1.00 29.24           O  
ANISOU   78  O   PRO A 515     3441   3577   4089   -418   -555    423       O  
ATOM     79  CB  PRO A 515       7.281  -6.880  -9.333  1.00 29.08           C  
ANISOU   79  CB  PRO A 515     3188   3677   4182   -530    120    243       C  
ATOM     80  CG  PRO A 515       7.167  -5.784  -8.285  1.00 31.07           C  
ANISOU   80  CG  PRO A 515     3574   3661   4568   -646    298    283       C  
ATOM     81  CD  PRO A 515       8.319  -4.808  -8.653  1.00 25.73           C  
ANISOU   81  CD  PRO A 515     2883   2932   3959   -517    244    405       C  
ATOM     82  N   ASP A 516       9.554  -8.918 -10.919  1.00 29.61           N  
ANISOU   82  N   ASP A 516     3588   3572   4090   -269   -530    133       N  
ATOM     83  CA  ASP A 516       9.947  -9.642 -12.143  1.00 31.75           C  
ANISOU   83  CA  ASP A 516     3968   3836   4258   -328   -379     76       C  
ATOM     84  C   ASP A 516      11.199  -9.069 -12.823  1.00 29.79           C  
ANISOU   84  C   ASP A 516     3939   3543   3834   -287   -392     97       C  
ATOM     85  O   ASP A 516      11.404  -9.265 -14.024  1.00 30.80           O  
ANISOU   85  O   ASP A 516     4265   3522   3914   -370   -432   -145       O  
ATOM     86  CB  ASP A 516       8.781  -9.791 -13.196  1.00 33.50           C  
ANISOU   86  CB  ASP A 516     4114   4062   4549   -340   -508     97       C  
ATOM     87  CG  ASP A 516       7.419 -10.141 -12.564  1.00 39.57           C  
ANISOU   87  CG  ASP A 516     4983   4610   5441   -385   -272    108       C  
ATOM     88  OD1 ASP A 516       7.284 -11.204 -11.900  1.00 43.50           O  
ANISOU   88  OD1 ASP A 516     5987   4086   6452   -799   -111    232       O  
ATOM     89  OD2 ASP A 516       6.457  -9.348 -12.728  1.00 45.90           O  
ANISOU   89  OD2 ASP A 516     4923   5717   6798   -346   -798    190       O  
ATOM     90  N   THR A 517      12.060  -8.401 -12.032  1.00 26.01           N  
ANISOU   90  N   THR A 517     3511   2820   3551   -423   -367    242       N  
ATOM     91  CA  THR A 517      13.343  -7.971 -12.526  1.00 24.15           C  
ANISOU   91  CA  THR A 517     3210   2792   3171     89   -314    339       C  
ATOM     92  C   THR A 517      14.445  -8.347 -11.552  1.00 23.34           C  
ANISOU   92  C   THR A 517     3339   2742   2788    124   -168    547       C  
ATOM     93  O   THR A 517      14.169  -8.947 -10.483  1.00 24.46           O  
ANISOU   93  O   THR A 517     3741   2790   2762     59   -197    575       O  
ATOM     94  CB  THR A 517      13.375  -6.465 -12.704  1.00 22.70           C  
ANISOU   94  CB  THR A 517     3019   2571   3035    -28   -299    407       C  
ATOM     95  OG1 THR A 517      13.454  -5.841 -11.426  1.00 24.57           O  
ANISOU   95  OG1 THR A 517     3040   2824   3469     13   -638    295       O  
ATOM     96  CG2 THR A 517      12.086  -5.959 -13.392  1.00 23.04           C  
ANISOU   96  CG2 THR A 517     2663   3110   2979    352   -527    282       C  
ATOM     97  N   ASP A 518      15.688  -8.064 -11.963  1.00 21.95           N  
ANISOU   97  N   ASP A 518     3005   2651   2684    212   -211    535       N  
ATOM     98  CA  ASP A 518      16.876  -8.167 -11.137  1.00 23.07           C  
ANISOU   98  CA  ASP A 518     2951   3199   2615    270    -46    381       C  
ATOM     99  C   ASP A 518      17.313  -6.812 -10.604  1.00 21.12           C  
ANISOU   99  C   ASP A 518     2577   2937   2509    122    -45    325       C  
ATOM    100  O   ASP A 518      18.493  -6.575 -10.269  1.00 22.46           O  
ANISOU  100  O   ASP A 518     2600   3463   2468    -29    108    132       O  
ATOM    101  CB  ASP A 518      18.017  -8.870 -11.867  1.00 22.89           C  
ANISOU  101  CB  ASP A 518     2891   3221   2585    211    -42    365       C  
ATOM    102  CG  ASP A 518      18.484  -8.141 -13.104  1.00 28.93           C  
ANISOU  102  CG  ASP A 518     3479   4116   3397    597    341    452       C  
ATOM    103  OD1 ASP A 518      17.899  -7.091 -13.457  1.00 32.76           O  
ANISOU  103  OD1 ASP A 518     4721   4224   3501    666    332    802       O  
ATOM    104  OD2 ASP A 518      19.472  -8.644 -13.745  1.00 35.01           O  
ANISOU  104  OD2 ASP A 518     4488   5347   3465   1332    705    616       O  
ATOM    105  N   VAL A 519      16.360  -5.889 -10.525  1.00 20.19           N  
ANISOU  105  N   VAL A 519     2663   2745   2261    116    -79    319       N  
ATOM    106  CA  VAL A 519      16.656  -4.517 -10.077  1.00 19.67           C  
ANISOU  106  CA  VAL A 519     2638   2688   2147    -24    -91    490       C  
ATOM    107  C   VAL A 519      16.251  -4.407  -8.602  1.00 18.96           C  
ANISOU  107  C   VAL A 519     2371   2520   2310    -65    -52    330       C  
ATOM    108  O   VAL A 519      15.088  -4.682  -8.222  1.00 19.19           O  
ANISOU  108  O   VAL A 519     2103   2648   2538   -272     -2    446       O  
ATOM    109  CB  VAL A 519      15.897  -3.539 -10.961  1.00 21.04           C  
ANISOU  109  CB  VAL A 519     3062   2769   2161     26   -172    499       C  
ATOM    110  CG1 VAL A 519      16.019  -2.113 -10.427  1.00 21.46           C  
ANISOU  110  CG1 VAL A 519     3381   2228   2542   -261   -377    522       C  
ATOM    111  CG2 VAL A 519      16.501  -3.598 -12.392  1.00 25.98           C  
ANISOU  111  CG2 VAL A 519     4256   3199   2415    140     97    949       C  
ATOM    112  N   TYR A 520      17.180  -3.901  -7.804  1.00 17.70           N  
ANISOU  112  N   TYR A 520     2134   2289   2301   -151    -63    527       N  
ATOM    113  CA  TYR A 520      16.972  -3.742  -6.354  1.00 17.20           C  
ANISOU  113  CA  TYR A 520     2075   2068   2390    -73    -92    274       C  
ATOM    114  C   TYR A 520      17.249  -2.326  -5.994  1.00 19.10           C  
ANISOU  114  C   TYR A 520     2320   2123   2812   -128    170    438       C  
ATOM    115  O   TYR A 520      18.370  -1.804  -6.291  1.00 22.59           O  
ANISOU  115  O   TYR A 520     2598   2568   3416   -455    175    242       O  
ATOM    116  CB  TYR A 520      17.917  -4.680  -5.557  1.00 19.11           C  
ANISOU  116  CB  TYR A 520     2192   2359   2707     73    -65    586       C  
ATOM    117  CG  TYR A 520      17.583  -6.117  -5.821  1.00 15.90           C  
ANISOU  117  CG  TYR A 520     1753   2067   2218     -6   -199    529       C  
ATOM    118  CD1 TYR A 520      16.672  -6.843  -4.996  1.00 17.53           C  
ANISOU  118  CD1 TYR A 520     2020   2061   2576    131     15    416       C  
ATOM    119  CD2 TYR A 520      18.072  -6.743  -6.987  1.00 17.58           C  
ANISOU  119  CD2 TYR A 520     1989   2272   2417    184   -228    -40       C  
ATOM    120  CE1 TYR A 520      16.351  -8.179  -5.299  1.00 18.29           C  
ANISOU  120  CE1 TYR A 520     2461   2143   2345    190   -175    383       C  
ATOM    121  CE2 TYR A 520      17.769  -8.067  -7.323  1.00 18.66           C  
ANISOU  121  CE2 TYR A 520     2203   2166   2722     14   -184    471       C  
ATOM    122  CZ  TYR A 520      16.893  -8.784  -6.438  1.00 20.37           C  
ANISOU  122  CZ  TYR A 520     3053   2218   2467   -275   -165    -41       C  
ATOM    123  OH  TYR A 520      16.556 -10.074  -6.696  1.00 20.45           O  
ANISOU  123  OH  TYR A 520     2175   2465   3129    -21   -402    178       O  
ATOM    124  N   ILE A 521      16.238  -1.666  -5.458  1.00 18.45           N  
ANISOU  124  N   ILE A 521     2243   1862   2903    -83    283    421       N  
ATOM    125  CA  ILE A 521      16.439  -0.273  -5.072  1.00 19.39           C  
ANISOU  125  CA  ILE A 521     2467   2038   2860     27    353    548       C  
ATOM    126  C   ILE A 521      15.692   0.069  -3.767  1.00 18.78           C  
ANISOU  126  C   ILE A 521     2335   1964   2836     33    320    403       C  
ATOM    127  O   ILE A 521      14.915  -0.787  -3.236  1.00 18.49           O  
ANISOU  127  O   ILE A 521     2246   1894   2884    -79    432    421       O  
ATOM    128  CB  ILE A 521      15.894   0.669  -6.161  1.00 21.12           C  
ANISOU  128  CB  ILE A 521     2583   2555   2884    168    323    386       C  
ATOM    129  CG1 ILE A 521      14.413   0.391  -6.415  1.00 22.28           C  
ANISOU  129  CG1 ILE A 521     2485   2477   3500   -135    -58    920       C  
ATOM    130  CG2 ILE A 521      16.757   0.578  -7.462  1.00 24.17           C  
ANISOU  130  CG2 ILE A 521     3089   3067   3025   -170    559    847       C  
ATOM    131  CD1 ILE A 521      13.825   1.528  -7.404  1.00 26.47           C  
ANISOU  131  CD1 ILE A 521     2624   3348   4083    741    539   1215       C  
ATOM    132  N   ASP A 522      16.011   1.246  -3.214  1.00 19.27           N  
ANISOU  132  N   ASP A 522     2399   2157   2766    183    254    209       N  
ATOM    133  CA  ASP A 522      15.425   1.746  -1.967  1.00 20.97           C  
ANISOU  133  CA  ASP A 522     2541   2244   3182     11    267    261       C  
ATOM    134  C   ASP A 522      13.900   1.409  -1.923  1.00 20.74           C  
ANISOU  134  C   ASP A 522     2452   2438   2988    -56    232    476       C  
ATOM    135  O   ASP A 522      13.167   1.808  -2.834  1.00 21.50           O  
ANISOU  135  O   ASP A 522     2632   2497   3040     47    322    695       O  
ATOM    136  CB  ASP A 522      15.643   3.262  -1.997  1.00 21.75           C  
ANISOU  136  CB  ASP A 522     2996   2204   3062     70    282    190       C  
ATOM    137  CG  ASP A 522      15.175   3.942  -0.738  1.00 21.59           C  
ANISOU  137  CG  ASP A 522     2849   1848   3504    154    291    -10       C  
ATOM    138  OD1 ASP A 522      14.390   3.401   0.081  1.00 23.78           O  
ANISOU  138  OD1 ASP A 522     2731   2603   3699    127    372    229       O  
ATOM    139  OD2 ASP A 522      15.563   5.107  -0.611  1.00 28.26           O  
ANISOU  139  OD2 ASP A 522     4112   2141   4483   -219    321   -519       O  
ATOM    140  N   ILE A 523      13.432   0.715  -0.859  1.00 21.73           N  
ANISOU  140  N   ILE A 523     2380   2666   3209    -36    402    337       N  
ATOM    141  CA  ILE A 523      12.041   0.313  -0.753  1.00 22.86           C  
ANISOU  141  CA  ILE A 523     2550   2883   3251    100    308    407       C  
ATOM    142  C   ILE A 523      11.083   1.528  -0.890  1.00 24.22           C  
ANISOU  142  C   ILE A 523     2786   2986   3428    218    171    432       C  
ATOM    143  O   ILE A 523       9.931   1.403  -1.371  1.00 26.01           O  
ANISOU  143  O   ILE A 523     2853   3336   3690    172    123    370       O  
ATOM    144  CB  ILE A 523      11.921  -0.455   0.641  1.00 22.66           C  
ANISOU  144  CB  ILE A 523     2578   3125   2906   -295    280    625       C  
ATOM    145  CG1 ILE A 523      10.601  -1.118   0.845  1.00 26.33           C  
ANISOU  145  CG1 ILE A 523     2537   3848   3618   -147    277    267       C  
ATOM    146  CG2 ILE A 523      12.271   0.377   1.813  1.00 22.63           C  
ANISOU  146  CG2 ILE A 523     2698   2794   3106    100    680    298       C  
ATOM    147  CD1 ILE A 523      10.282  -2.138  -0.279  1.00 29.98           C  
ANISOU  147  CD1 ILE A 523     4080   3602   3707     40    392     60       C  
ATOM    148  N   ASP A 524      11.588   2.694  -0.476  1.00 24.60           N  
ANISOU  148  N   ASP A 524     2965   2717   3664    561    381    425       N  
ATOM    149  CA  ASP A 524      10.755   3.951  -0.409  1.00 26.31           C  
ANISOU  149  CA  ASP A 524     3447   2899   3651    712    424    342       C  
ATOM    150  C   ASP A 524      10.847   4.775  -1.684  1.00 27.07           C  
ANISOU  150  C   ASP A 524     3607   2986   3692    760    412    435       C  
ATOM    151  O   ASP A 524      10.123   5.789  -1.836  1.00 28.24           O  
ANISOU  151  O   ASP A 524     3736   3218   3775   1011    797    430       O  
ATOM    152  CB  ASP A 524      11.153   4.805   0.788  1.00 27.30           C  
ANISOU  152  CB  ASP A 524     3649   2900   3821    824    261    213       C  
ATOM    153  CG  ASP A 524      10.814   4.137   2.126  1.00 29.04           C  
ANISOU  153  CG  ASP A 524     3551   3464   4017    593    384     28       C  
ATOM    154  OD1 ASP A 524       9.753   3.454   2.211  1.00 34.87           O  
ANISOU  154  OD1 ASP A 524     4567   4081   4599    244    765    232       O  
ATOM    155  OD2 ASP A 524      11.615   4.296   3.071  1.00 31.89           O  
ANISOU  155  OD2 ASP A 524     4097   4420   3596    741    348   -654       O  
ATOM    156  N   ALA A 525      11.659   4.317  -2.640  1.00 26.27           N  
ANISOU  156  N   ALA A 525     3241   3085   3653    539    533    629       N  
ATOM    157  CA  ALA A 525      11.846   5.089  -3.912  1.00 25.57           C  
ANISOU  157  CA  ALA A 525     3143   3161   3408    593    372    567       C  
ATOM    158  C   ALA A 525      10.712   4.891  -4.925  1.00 24.94           C  
ANISOU  158  C   ALA A 525     2999   2933   3541    443    318    398       C  
ATOM    159  O   ALA A 525      10.493   5.758  -5.814  1.00 26.12           O  
ANISOU  159  O   ALA A 525     3059   3055   3808    561    246    614       O  
ATOM    160  CB  ALA A 525      13.180   4.735  -4.575  1.00 25.44           C  
ANISOU  160  CB  ALA A 525     2840   3169   3657    319    509    545       C  
ATOM    161  N   TYR A 526       9.990   3.785  -4.824  1.00 25.19           N  
ANISOU  161  N   TYR A 526     2939   3073   3556    247    282    435       N  
ATOM    162  CA  TYR A 526       8.967   3.488  -5.838  1.00 24.94           C  
ANISOU  162  CA  TYR A 526     2643   3137   3696    149    314    307       C  
ATOM    163  C   TYR A 526       7.936   2.571  -5.228  1.00 26.35           C  
ANISOU  163  C   TYR A 526     2763   3407   3840    267    341    335       C  
ATOM    164  O   TYR A 526       8.317   1.560  -4.594  1.00 25.25           O  
ANISOU  164  O   TYR A 526     2542   3273   3779    626    300    227       O  
ATOM    165  CB  TYR A 526       9.626   2.835  -7.070  1.00 25.54           C  
ANISOU  165  CB  TYR A 526     2971   3026   3705   -162    442    228       C  
ATOM    166  CG  TYR A 526       8.681   2.671  -8.221  1.00 27.20           C  
ANISOU  166  CG  TYR A 526     3074   3439   3820    331    335    324       C  
ATOM    167  CD1 TYR A 526       8.346   3.748  -9.012  1.00 27.54           C  
ANISOU  167  CD1 TYR A 526     3587   3297   3578    138    422    196       C  
ATOM    168  CD2 TYR A 526       8.177   1.393  -8.547  1.00 27.35           C  
ANISOU  168  CD2 TYR A 526     3206   3703   3481    191    476   -101       C  
ATOM    169  CE1 TYR A 526       7.462   3.599 -10.042  1.00 29.81           C  
ANISOU  169  CE1 TYR A 526     4023   3590   3711    299    199    231       C  
ATOM    170  CE2 TYR A 526       7.254   1.195  -9.580  1.00 27.77           C  
ANISOU  170  CE2 TYR A 526     3584   3750   3217    150    541   1063       C  
ATOM    171  CZ  TYR A 526       6.902   2.334 -10.341  1.00 30.81           C  
ANISOU  171  CZ  TYR A 526     3763   3762   4180    341    166    689       C  
ATOM    172  OH  TYR A 526       6.017   2.205 -11.402  1.00 35.60           O  
ANISOU  172  OH  TYR A 526     4638   4945   3942    671    122    474       O  
ATOM    173  N   GLU A 527       6.630   2.881  -5.437  1.00 28.41           N  
ANISOU  173  N   GLU A 527     2790   3838   4164    352    192    427       N  
ATOM    174  CA  GLU A 527       5.604   2.133  -4.682  1.00 29.33           C  
ANISOU  174  CA  GLU A 527     2664   4129   4351    193    141    451       C  
ATOM    175  C   GLU A 527       5.621   0.607  -4.872  1.00 28.72           C  
ANISOU  175  C   GLU A 527     2659   4112   4140    185     32    430       C  
ATOM    176  O   GLU A 527       5.421  -0.154  -3.881  1.00 30.82           O  
ANISOU  176  O   GLU A 527     3283   4219   4208     99    184    381       O  
ATOM    177  CB  GLU A 527       4.175   2.720  -4.891  1.00 31.48           C  
ANISOU  177  CB  GLU A 527     2824   4501   4635    314    198    502       C  
ATOM    178  CG  GLU A 527       3.136   2.235  -3.836  1.00 39.69           C  
ANISOU  178  CG  GLU A 527     3775   5854   5451    185    217    556       C  
ATOM    179  CD  GLU A 527       1.798   2.955  -4.010  1.00 50.45           C  
ANISOU  179  CD  GLU A 527     5333   7309   6524    868    337    131       C  
ATOM    180  OE1 GLU A 527       1.341   3.106  -5.191  1.00 54.59           O  
ANISOU  180  OE1 GLU A 527     5856   7951   6934   1028     71    166       O  
ATOM    181  OE2 GLU A 527       1.194   3.375  -2.979  1.00 56.43           O  
ANISOU  181  OE2 GLU A 527     6972   7904   6562    422    559    -85       O  
ATOM    182  N   GLU A 528       5.851   0.124  -6.085  1.00 27.09           N  
ANISOU  182  N   GLU A 528     2375   3940   3977    189    -75    416       N  
ATOM    183  CA  GLU A 528       5.764  -1.320  -6.393  1.00 27.10           C  
ANISOU  183  CA  GLU A 528     2473   3881   3943    225   -160    422       C  
ATOM    184  C   GLU A 528       6.976  -2.116  -6.013  1.00 25.29           C  
ANISOU  184  C   GLU A 528     2482   3306   3818    241   -164    421       C  
ATOM    185  O   GLU A 528       6.948  -3.375  -6.071  1.00 26.93           O  
ANISOU  185  O   GLU A 528     2559   3400   4272    301   -141    456       O  
ATOM    186  CB  GLU A 528       5.581  -1.564  -7.893  1.00 30.27           C  
ANISOU  186  CB  GLU A 528     3036   4407   4055    321   -386    447       C  
ATOM    187  CG  GLU A 528       4.158  -1.459  -8.397  1.00 38.19           C  
ANISOU  187  CG  GLU A 528     3676   5632   5201    158   -224    604       C  
ATOM    188  CD  GLU A 528       3.486  -0.220  -7.956  1.00 48.22           C  
ANISOU  188  CD  GLU A 528     5340   6612   6366    125     67    124       C  
ATOM    189  OE1 GLU A 528       4.053   0.898  -8.204  1.00 52.25           O  
ANISOU  189  OE1 GLU A 528     5719   7340   6792     47    401    927       O  
ATOM    190  OE2 GLU A 528       2.395  -0.371  -7.329  1.00 55.12           O  
ANISOU  190  OE2 GLU A 528     5414   8237   7291   -122     67    357       O  
ATOM    191  N   VAL A 529       8.070  -1.422  -5.652  1.00 22.42           N  
ANISOU  191  N   VAL A 529     2234   2790   3493    168   -256    701       N  
ATOM    192  CA  VAL A 529       9.246  -2.187  -5.133  1.00 23.06           C  
ANISOU  192  CA  VAL A 529     2181   3110   3467    150    -56    686       C  
ATOM    193  C   VAL A 529       8.864  -2.960  -3.857  1.00 22.80           C  
ANISOU  193  C   VAL A 529     2333   2953   3377     74     97    548       C  
ATOM    194  O   VAL A 529       8.190  -2.381  -2.964  1.00 25.74           O  
ANISOU  194  O   VAL A 529     2837   3496   3444    135    220    828       O  
ATOM    195  CB  VAL A 529      10.446  -1.234  -4.867  1.00 22.23           C  
ANISOU  195  CB  VAL A 529     2203   2873   3367     75   -281    592       C  
ATOM    196  CG1 VAL A 529      11.563  -1.933  -4.058  1.00 22.54           C  
ANISOU  196  CG1 VAL A 529     2468   3303   2793    238    -48    483       C  
ATOM    197  CG2 VAL A 529      10.983  -0.794  -6.228  1.00 25.52           C  
ANISOU  197  CG2 VAL A 529     2480   3752   3463   -138     -2    745       C  
ATOM    198  N   LYS A 530       9.247  -4.247  -3.752  1.00 21.91           N  
ANISOU  198  N   LYS A 530     2154   2913   3256    -36    121    715       N  
ATOM    199  CA  LYS A 530       8.774  -5.075  -2.626  1.00 22.40           C  
ANISOU  199  CA  LYS A 530     2264   2689   3558   -330    -50    644       C  
ATOM    200  C   LYS A 530       9.927  -5.869  -2.040  1.00 22.07           C  
ANISOU  200  C   LYS A 530     2283   2718   3384   -207    117    512       C  
ATOM    201  O   LYS A 530      10.777  -6.440  -2.785  1.00 21.86           O  
ANISOU  201  O   LYS A 530     2310   2571   3425   -130    327    359       O  
ATOM    202  CB  LYS A 530       7.727  -6.068  -3.131  1.00 24.51           C  
ANISOU  202  CB  LYS A 530     2295   3068   3948   -461    -82    732       C  
ATOM    203  CG  LYS A 530       6.394  -5.363  -3.454  1.00 33.77           C  
ANISOU  203  CG  LYS A 530     3454   4387   4988   -133   -105    739       C  
ATOM    204  CD  LYS A 530       5.919  -4.412  -2.277  1.00 39.76           C  
ANISOU  204  CD  LYS A 530     3656   5841   5609   -126    486    463       C  
ATOM    205  CE  LYS A 530       4.965  -3.332  -2.800  1.00 44.26           C  
ANISOU  205  CE  LYS A 530     4606   6423   5784    -34    172    765       C  
ATOM    206  NZ  LYS A 530       3.797  -3.990  -3.548  1.00 47.91           N  
ANISOU  206  NZ  LYS A 530     4640   6949   6613   -459    -47    573       N  
ATOM    207  N   GLU A 531       9.989  -5.903  -0.712  1.00 21.24           N  
ANISOU  207  N   GLU A 531     2190   2693   3186   -127    159    390       N  
ATOM    208  CA  GLU A 531      10.987  -6.839  -0.090  1.00 19.91           C  
ANISOU  208  CA  GLU A 531     2381   2324   2860    -86    152    147       C  
ATOM    209  C   GLU A 531      10.632  -8.290  -0.445  1.00 20.39           C  
ANISOU  209  C   GLU A 531     2169   2518   3060   -380    227    112       C  
ATOM    210  O   GLU A 531       9.454  -8.622  -0.686  1.00 22.80           O  
ANISOU  210  O   GLU A 531     2360   2746   3557   -514    281    326       O  
ATOM    211  CB  GLU A 531      11.020  -6.652   1.423  1.00 20.91           C  
ANISOU  211  CB  GLU A 531     2463   2579   2903   -207    214     -9       C  
ATOM    212  CG  GLU A 531      11.511  -5.240   1.777  1.00 18.26           C  
ANISOU  212  CG  GLU A 531     2084   2384   2467   -292    262    106       C  
ATOM    213  CD  GLU A 531      11.777  -5.116   3.269  1.00 21.03           C  
ANISOU  213  CD  GLU A 531     2664   2763   2561    -61    688   -229       C  
ATOM    214  OE1 GLU A 531      10.927  -4.483   3.948  1.00 27.59           O  
ANISOU  214  OE1 GLU A 531     2893   4489   3100    471    970   -452       O  
ATOM    215  OE2 GLU A 531      12.786  -5.625   3.774  1.00 22.86           O  
ANISOU  215  OE2 GLU A 531     2745   3153   2787   -503    666    132       O  
ATOM    216  N   ILE A 532      11.636  -9.171  -0.421  1.00 19.43           N  
ANISOU  216  N   ILE A 532     2269   2262   2849   -363    237    142       N  
ATOM    217  CA  ILE A 532      11.405 -10.605  -0.666  1.00 21.10           C  
ANISOU  217  CA  ILE A 532     2453   2456   3105   -188    194    136       C  
ATOM    218  C   ILE A 532      11.254 -11.266   0.676  1.00 20.47           C  
ANISOU  218  C   ILE A 532     2195   2454   3127   -478    383    178       C  
ATOM    219  O   ILE A 532      12.111 -11.162   1.507  1.00 19.41           O  
ANISOU  219  O   ILE A 532     2216   2235   2922   -596    216      4       O  
ATOM    220  CB  ILE A 532      12.615 -11.175  -1.324  1.00 19.87           C  
ANISOU  220  CB  ILE A 532     2619   2267   2661   -166    258    122       C  
ATOM    221  CG1 ILE A 532      12.789 -10.430  -2.669  1.00 20.43           C  
ANISOU  221  CG1 ILE A 532     2375   2579   2806   -307    326    315       C  
ATOM    222  CG2 ILE A 532      12.453 -12.731  -1.546  1.00 20.43           C  
ANISOU  222  CG2 ILE A 532     2558   2132   3069    -48    127   -265       C  
ATOM    223  CD1 ILE A 532      14.143 -10.750  -3.360  1.00 21.67           C  
ANISOU  223  CD1 ILE A 532     2813   2984   2435   -564    722   -222       C  
ATOM    224  N   PRO A 533      10.148 -11.976   0.928  1.00 22.75           N  
ANISOU  224  N   PRO A 533     2291   2777   3574   -664    222    300       N  
ATOM    225  CA  PRO A 533       9.996 -12.677   2.190  1.00 22.17           C  
ANISOU  225  CA  PRO A 533     2171   2644   3606   -610    302    342       C  
ATOM    226  C   PRO A 533      11.177 -13.589   2.455  1.00 21.65           C  
ANISOU  226  C   PRO A 533     2331   2505   3387   -734    484    332       C  
ATOM    227  O   PRO A 533      11.678 -14.268   1.502  1.00 24.00           O  
ANISOU  227  O   PRO A 533     2803   2518   3796   -841    322   -144       O  
ATOM    228  CB  PRO A 533       8.768 -13.545   1.905  1.00 25.45           C  
ANISOU  228  CB  PRO A 533     2579   2873   4217   -722    221    484       C  
ATOM    229  CG  PRO A 533       8.047 -12.867   0.898  1.00 26.79           C  
ANISOU  229  CG  PRO A 533     2443   3694   4041   -917    418    531       C  
ATOM    230  CD  PRO A 533       9.019 -12.226   0.012  1.00 25.27           C  
ANISOU  230  CD  PRO A 533     2650   3042   3910   -811    330    312       C  
ATOM    231  N   GLY A 534      11.628 -13.572   3.702  1.00 19.85           N  
ANISOU  231  N   GLY A 534     2139   2290   3111   -627    518    510       N  
ATOM    232  CA  GLY A 534      12.736 -14.375   4.140  1.00 19.93           C  
ANISOU  232  CA  GLY A 534     2335   2280   2955   -334    566    470       C  
ATOM    233  C   GLY A 534      14.098 -13.724   3.952  1.00 18.23           C  
ANISOU  233  C   GLY A 534     2369   1895   2662   -379    434    400       C  
ATOM    234  O   GLY A 534      15.110 -14.235   4.505  1.00 18.97           O  
ANISOU  234  O   GLY A 534     2410   1787   3011   -373    702    670       O  
ATOM    235  N   ILE A 535      14.148 -12.608   3.208  1.00 18.35           N  
ANISOU  235  N   ILE A 535     2348   1764   2861   -163    718    280       N  
ATOM    236  CA  ILE A 535      15.441 -11.952   2.976  1.00 17.90           C  
ANISOU  236  CA  ILE A 535     2517   1687   2597   -386    506    116       C  
ATOM    237  C   ILE A 535      15.361 -10.525   3.406  1.00 15.87           C  
ANISOU  237  C   ILE A 535     2053   1655   2319   -238    313    317       C  
ATOM    238  O   ILE A 535      14.381  -9.809   3.111  1.00 18.75           O  
ANISOU  238  O   ILE A 535     2451   1717   2956   -352     44    291       O  
ATOM    239  CB  ILE A 535      15.815 -12.035   1.441  1.00 16.79           C  
ANISOU  239  CB  ILE A 535     2280   1661   2438   -339    640    129       C  
ATOM    240  CG1 ILE A 535      15.837 -13.520   0.985  1.00 18.57           C  
ANISOU  240  CG1 ILE A 535     3261   1734   2060    -31    486    128       C  
ATOM    241  CG2 ILE A 535      17.160 -11.358   1.176  1.00 16.89           C  
ANISOU  241  CG2 ILE A 535     1725   2125   2565   -457    733    231       C  
ATOM    242  CD1 ILE A 535      16.143 -13.708  -0.513  1.00 19.67           C  
ANISOU  242  CD1 ILE A 535     2623   2530   2320   -132    305     51       C  
ATOM    243  N   LYS A 536      16.399 -10.065   4.042  1.00 14.29           N  
ANISOU  243  N   LYS A 536     1957   1705   1765   -410    422    339       N  
ATOM    244  CA  LYS A 536      16.574  -8.605   4.304  1.00 15.45           C  
ANISOU  244  CA  LYS A 536     2010   1874   1985   -326    441    479       C  
ATOM    245  C   LYS A 536      17.758  -8.100   3.526  1.00 14.49           C  
ANISOU  245  C   LYS A 536     1880   1584   2041   -157    437    373       C  
ATOM    246  O   LYS A 536      18.866  -8.680   3.648  1.00 16.06           O  
ANISOU  246  O   LYS A 536     1922   1824   2355   -128    356    719       O  
ATOM    247  CB  LYS A 536      16.779  -8.262   5.785  1.00 17.74           C  
ANISOU  247  CB  LYS A 536     2040   2532   2169   -462    253    355       C  
ATOM    248  CG  LYS A 536      15.575  -8.519   6.667  1.00 22.05           C  
ANISOU  248  CG  LYS A 536     3084   2440   2851   -429    398    640       C  
ATOM    249  CD  LYS A 536      14.344  -7.727   6.340  1.00 28.93           C  
ANISOU  249  CD  LYS A 536     3347   4135   3510    277     20    -45       C  
ATOM    250  CE  LYS A 536      14.525  -6.283   6.550  1.00 28.68           C  
ANISOU  250  CE  LYS A 536     3559   3724   3612    549     93    395       C  
ATOM    251  NZ  LYS A 536      13.064  -5.685   6.520  1.00 30.77           N  
ANISOU  251  NZ  LYS A 536     3160   5048   3483    665   1179   -140       N  
ATOM    252  N   ILE A 537      17.556  -7.016   2.753  1.00 13.91           N  
ANISOU  252  N   ILE A 537     1944   1577   1764   -227    545    199       N  
ATOM    253  CA  ILE A 537      18.649  -6.510   1.909  1.00 13.98           C  
ANISOU  253  CA  ILE A 537     2036   1541   1732   -518    464     59       C  
ATOM    254  C   ILE A 537      18.912  -5.097   2.423  1.00 14.71           C  
ANISOU  254  C   ILE A 537     1919   1534   2134   -177    371    115       C  
ATOM    255  O   ILE A 537      18.000  -4.246   2.367  1.00 15.98           O  
ANISOU  255  O   ILE A 537     2258   1443   2368    -11    481    104       O  
ATOM    256  CB  ILE A 537      18.202  -6.471   0.415  1.00 14.26           C  
ANISOU  256  CB  ILE A 537     1953   1528   1937   -308    377    345       C  
ATOM    257  CG1 ILE A 537      17.746  -7.889  -0.052  1.00 14.22           C  
ANISOU  257  CG1 ILE A 537     1735   1540   2129   -538     42     76       C  
ATOM    258  CG2 ILE A 537      19.379  -6.018  -0.470  1.00 14.82           C  
ANISOU  258  CG2 ILE A 537     1841   1716   2072   -163    599    490       C  
ATOM    259  CD1 ILE A 537      17.065  -7.847  -1.426  1.00 17.39           C  
ANISOU  259  CD1 ILE A 537     2234   2511   1862   -400    122    107       C  
ATOM    260  N   PHE A 538      20.146  -4.851   2.897  1.00 13.23           N  
ANISOU  260  N   PHE A 538     1793   1403   1830   -234    382    -42       N  
ATOM    261  CA  PHE A 538      20.524  -3.512   3.361  1.00 14.92           C  
ANISOU  261  CA  PHE A 538     1899   1773   1997   -267    396   -151       C  
ATOM    262  C   PHE A 538      21.706  -2.967   2.544  1.00 14.55           C  
ANISOU  262  C   PHE A 538     1937   1532   2058   -247    312    -68       C  
ATOM    263  O   PHE A 538      22.751  -3.652   2.401  1.00 16.36           O  
ANISOU  263  O   PHE A 538     2169   1540   2505    -99    411    -36       O  
ATOM    264  CB  PHE A 538      20.986  -3.604   4.796  1.00 16.92           C  
ANISOU  264  CB  PHE A 538     2286   2073   2067   -210    409    -67       C  
ATOM    265  CG  PHE A 538      19.942  -4.148   5.729  1.00 15.07           C  
ANISOU  265  CG  PHE A 538     1951   1652   2119    142    310    -73       C  
ATOM    266  CD1 PHE A 538      18.768  -3.414   5.960  1.00 22.99           C  
ANISOU  266  CD1 PHE A 538     3070   3255   2408    343   1228   -130       C  
ATOM    267  CD2 PHE A 538      20.210  -5.300   6.464  1.00 18.32           C  
ANISOU  267  CD2 PHE A 538     2747   1705   2508   -480    754   -286       C  
ATOM    268  CE1 PHE A 538      17.842  -3.892   6.887  1.00 23.89           C  
ANISOU  268  CE1 PHE A 538     2820   3409   2845    212   1069    383       C  
ATOM    269  CE2 PHE A 538      19.256  -5.776   7.388  1.00 20.38           C  
ANISOU  269  CE2 PHE A 538     2177   2349   3217   -459    723      3       C  
ATOM    270  CZ  PHE A 538      18.106  -5.056   7.567  1.00 22.98           C  
ANISOU  270  CZ  PHE A 538     2865   3036   2830    417    744    253       C  
ATOM    271  N   GLN A 539      21.505  -1.768   2.010  1.00 14.83           N  
ANISOU  271  N   GLN A 539     2079   1560   1995   -169    272    154       N  
ATOM    272  CA  GLN A 539      22.598  -1.104   1.380  1.00 15.30           C  
ANISOU  272  CA  GLN A 539     2145   1746   1923   -463    -71     94       C  
ATOM    273  C   GLN A 539      23.396  -0.287   2.391  1.00 15.58           C  
ANISOU  273  C   GLN A 539     2323   1559   2038   -264     67    -61       C  
ATOM    274  O   GLN A 539      22.805   0.477   3.160  1.00 16.77           O  
ANISOU  274  O   GLN A 539     2523   1570   2277    127    242   -217       O  
ATOM    275  CB  GLN A 539      22.068  -0.194   0.290  1.00 15.15           C  
ANISOU  275  CB  GLN A 539     1859   1768   2127   -369   -124    254       C  
ATOM    276  CG  GLN A 539      23.199   0.550  -0.410  1.00 16.17           C  
ANISOU  276  CG  GLN A 539     2243   1725   2175   -459   -366    521       C  
ATOM    277  CD  GLN A 539      22.612   1.445  -1.475  1.00 19.43           C  
ANISOU  277  CD  GLN A 539     2968   2044   2368   -190   -181    593       C  
ATOM    278  OE1 GLN A 539      22.026   2.491  -1.158  1.00 21.67           O  
ANISOU  278  OE1 GLN A 539     3202   2058   2973   -503   -303    328       O  
ATOM    279  NE2 GLN A 539      22.691   1.025  -2.665  1.00 23.21           N  
ANISOU  279  NE2 GLN A 539     3436   2864   2516   -444   -210    253       N  
ATOM    280  N   ILE A 540      24.705  -0.497   2.442  1.00 14.15           N  
ANISOU  280  N   ILE A 540     2182   1551   1643   -465   -107     71       N  
ATOM    281  CA  ILE A 540      25.533   0.218   3.409  1.00 14.45           C  
ANISOU  281  CA  ILE A 540     2107   1460   1920   -477     36   -137       C  
ATOM    282  C   ILE A 540      25.825   1.597   2.840  1.00 14.35           C  
ANISOU  282  C   ILE A 540     2133   1587   1731   -347    -33   -132       C  
ATOM    283  O   ILE A 540      26.363   1.737   1.733  1.00 15.47           O  
ANISOU  283  O   ILE A 540     2123   1830   1922   -417     18     25       O  
ATOM    284  CB  ILE A 540      26.880  -0.558   3.635  1.00 14.54           C  
ANISOU  284  CB  ILE A 540     2230   1486   1807   -386   -173    -79       C  
ATOM    285  CG1 ILE A 540      26.618  -1.938   4.209  1.00 17.62           C  
ANISOU  285  CG1 ILE A 540     2734   1358   2603     72   -452     19       C  
ATOM    286  CG2 ILE A 540      27.775   0.165   4.560  1.00 18.06           C  
ANISOU  286  CG2 ILE A 540     2689   2234   1939   -331   -403   -241       C  
ATOM    287  CD1 ILE A 540      27.777  -2.762   4.369  1.00 23.21           C  
ANISOU  287  CD1 ILE A 540     2801   2385   3631    338    216    -79       C  
ATOM    288  N   ASN A 541      25.489   2.621   3.647  1.00 15.46           N  
ANISOU  288  N   ASN A 541     2452   1278   2143   -172    160   -193       N  
ATOM    289  CA  ASN A 541      25.657   4.037   3.184  1.00 16.06           C  
ANISOU  289  CA  ASN A 541     2618   1181   2300   -410    -27   -183       C  
ATOM    290  C   ASN A 541      26.667   4.845   3.999  1.00 17.03           C  
ANISOU  290  C   ASN A 541     3038   1427   2005   -335    -29   -301       C  
ATOM    291  O   ASN A 541      26.978   6.007   3.661  1.00 20.40           O  
ANISOU  291  O   ASN A 541     3649   1685   2413   -488    164    -39       O  
ATOM    292  CB  ASN A 541      24.304   4.792   3.215  1.00 17.68           C  
ANISOU  292  CB  ASN A 541     2624   1818   2273   -361     94   -215       C  
ATOM    293  CG  ASN A 541      23.232   4.125   2.381  1.00 16.49           C  
ANISOU  293  CG  ASN A 541     2255   1571   2436   -290    517    -41       C  
ATOM    294  OD1 ASN A 541      22.123   3.847   2.883  1.00 24.37           O  
ANISOU  294  OD1 ASN A 541     2725   3213   3322   -564    698    556       O  
ATOM    295  ND2 ASN A 541      23.518   3.877   1.105  1.00 21.97           N  
ANISOU  295  ND2 ASN A 541     3744   2297   2304    -66     56   -297       N  
ATOM    296  N   ALA A 542      27.197   4.233   5.039  1.00 19.33           N  
ANISOU  296  N   ALA A 542     3174   1964   2205   -568   -130   -253       N  
ATOM    297  CA  ALA A 542      28.193   4.882   5.905  1.00 19.95           C  
ANISOU  297  CA  ALA A 542     3318   1924   2337   -467   -178   -307       C  
ATOM    298  C   ALA A 542      29.091   3.768   6.424  1.00 19.70           C  
ANISOU  298  C   ALA A 542     2943   2240   2299   -549   -203   -126       C  
ATOM    299  O   ALA A 542      28.745   2.544   6.294  1.00 19.71           O  
ANISOU  299  O   ALA A 542     3411   2089   1990   -492   -294    -26       O  
ATOM    300  CB  ALA A 542      27.415   5.515   7.110  1.00 21.31           C  
ANISOU  300  CB  ALA A 542     3503   2191   2401   -558    -99   -428       C  
ATOM    301  N   PRO A 543      30.227   4.118   7.022  1.00 22.48           N  
ANISOU  301  N   PRO A 543     3282   2543   2713   -554   -264   -119       N  
ATOM    302  CA  PRO A 543      31.100   3.038   7.548  1.00 22.72           C  
ANISOU  302  CA  PRO A 543     3093   2768   2769   -601   -387   -188       C  
ATOM    303  C   PRO A 543      30.351   2.138   8.507  1.00 23.51           C  
ANISOU  303  C   PRO A 543     3074   3070   2787   -341   -127   -222       C  
ATOM    304  O   PRO A 543      29.369   2.575   9.175  1.00 22.03           O  
ANISOU  304  O   PRO A 543     3146   2704   2518   -304   -144   -485       O  
ATOM    305  CB  PRO A 543      32.261   3.817   8.216  1.00 25.06           C  
ANISOU  305  CB  PRO A 543     3183   3401   2936   -767   -477   -194       C  
ATOM    306  CG  PRO A 543      32.258   5.159   7.481  1.00 26.19           C  
ANISOU  306  CG  PRO A 543     3411   3208   3330   -753   -443   -177       C  
ATOM    307  CD  PRO A 543      30.824   5.476   7.141  1.00 23.12           C  
ANISOU  307  CD  PRO A 543     3180   2589   3013   -611   -285   -206       C  
ATOM    308  N   ILE A 544      30.715   0.863   8.493  1.00 25.65           N  
ANISOU  308  N   ILE A 544     3500   3095   3150   -206    -33   -214       N  
ATOM    309  CA  ILE A 544      29.779  -0.186   9.011  1.00 27.68           C  
ANISOU  309  CA  ILE A 544     3986   3672   2857    -79    448    -69       C  
ATOM    310  C   ILE A 544      29.520  -0.069  10.532  1.00 29.57           C  
ANISOU  310  C   ILE A 544     4137   3939   3156     81    315     21       C  
ATOM    311  O   ILE A 544      28.520  -0.515  11.006  1.00 31.23           O  
ANISOU  311  O   ILE A 544     4544   3942   3380    240    409    213       O  
ATOM    312  CB  ILE A 544      30.121  -1.648   8.563  1.00 29.30           C  
ANISOU  312  CB  ILE A 544     3774   3688   3671    -75    203     95       C  
ATOM    313  CG1 ILE A 544      28.846  -2.552   8.557  1.00 32.71           C  
ANISOU  313  CG1 ILE A 544     4510   3801   4115   -222    747   -247       C  
ATOM    314  CG2 ILE A 544      31.354  -2.184   9.337  1.00 33.47           C  
ANISOU  314  CG2 ILE A 544     4030   4339   4347    548     87     15       C  
ATOM    315  CD1 ILE A 544      29.070  -3.862   7.857  1.00 37.30           C  
ANISOU  315  CD1 ILE A 544     5850   3899   4423    -56    426    198       C  
ATOM    316  N   TYR A 545      30.393   0.575  11.251  1.00 30.78           N  
ANISOU  316  N   TYR A 545     4405   4433   2855    221    163     -2       N  
ATOM    317  CA  TYR A 545      30.061   0.748  12.631  1.00 34.01           C  
ANISOU  317  CA  TYR A 545     4575   4996   3350     82    202    -27       C  
ATOM    318  C   TYR A 545      28.919   1.717  12.885  1.00 32.12           C  
ANISOU  318  C   TYR A 545     4607   4488   3107     99    158    -76       C  
ATOM    319  O   TYR A 545      28.236   1.570  13.908  1.00 30.63           O  
ANISOU  319  O   TYR A 545     4450   4404   2783     12    266    -39       O  
ATOM    320  CB  TYR A 545      31.294   1.017  13.447  1.00 36.63           C  
ANISOU  320  CB  TYR A 545     4839   5365   3714   -103     35   -135       C  
ATOM    321  CG  TYR A 545      32.321   1.743  12.646  1.00 42.22           C  
ANISOU  321  CG  TYR A 545     5752   5697   4591   -254    295    140       C  
ATOM    322  CD1 TYR A 545      32.274   3.157  12.527  1.00 45.46           C  
ANISOU  322  CD1 TYR A 545     6380   5739   5152   -289    -91   -201       C  
ATOM    323  CD2 TYR A 545      33.345   1.013  11.949  1.00 46.74           C  
ANISOU  323  CD2 TYR A 545     6373   5757   5629   -119    471   -344       C  
ATOM    324  CE1 TYR A 545      33.270   3.848  11.741  1.00 46.28           C  
ANISOU  324  CE1 TYR A 545     5949   6646   4989   -228    -36     39       C  
ATOM    325  CE2 TYR A 545      34.303   1.661  11.172  1.00 48.82           C  
ANISOU  325  CE2 TYR A 545     6754   6044   5751   -403    705   -370       C  
ATOM    326  CZ  TYR A 545      34.273   3.076  11.082  1.00 48.80           C  
ANISOU  326  CZ  TYR A 545     6578   6438   5524   -170    257    124       C  
ATOM    327  OH  TYR A 545      35.237   3.731  10.325  1.00 48.52           O  
ANISOU  327  OH  TYR A 545     5487   6915   6032  -1013   -322   -427       O  
ATOM    328  N   TYR A 546      28.616   2.639  11.976  1.00 30.87           N  
ANISOU  328  N   TYR A 546     4489   4313   2926     50    248    -16       N  
ATOM    329  CA  TYR A 546      27.271   3.297  12.019  1.00 31.41           C  
ANISOU  329  CA  TYR A 546     4676   4238   3018     96    135   -184       C  
ATOM    330  C   TYR A 546      26.077   2.372  11.761  1.00 31.24           C  
ANISOU  330  C   TYR A 546     4661   4177   3030    110    164   -422       C  
ATOM    331  O   TYR A 546      25.091   2.399  12.497  1.00 33.78           O  
ANISOU  331  O   TYR A 546     4808   4816   3210    174     32   -368       O  
ATOM    332  CB  TYR A 546      27.177   4.502  11.042  1.00 31.82           C  
ANISOU  332  CB  TYR A 546     4733   4095   3260    -54    300    -76       C  
ATOM    333  CG  TYR A 546      28.170   5.576  11.383  1.00 33.85           C  
ANISOU  333  CG  TYR A 546     4821   4391   3648   -184    124   -492       C  
ATOM    334  CD1 TYR A 546      27.852   6.540  12.342  1.00 34.53           C  
ANISOU  334  CD1 TYR A 546     5096   4342   3682   -253    -62   -604       C  
ATOM    335  CD2 TYR A 546      29.449   5.649  10.716  1.00 36.97           C  
ANISOU  335  CD2 TYR A 546     5086   4642   4317   -381    302   -331       C  
ATOM    336  CE1 TYR A 546      28.795   7.531  12.660  1.00 38.10           C  
ANISOU  336  CE1 TYR A 546     5328   4900   4246   -620   -125   -655       C  
ATOM    337  CE2 TYR A 546      30.379   6.633  11.025  1.00 37.69           C  
ANISOU  337  CE2 TYR A 546     5282   4694   4343   -364    288   -296       C  
ATOM    338  CZ  TYR A 546      30.040   7.586  12.013  1.00 40.22           C  
ANISOU  338  CZ  TYR A 546     5362   5133   4786   -677     44   -874       C  
ATOM    339  OH  TYR A 546      30.932   8.603  12.347  1.00 43.32           O  
ANISOU  339  OH  TYR A 546     5691   5470   5296   -972   -198   -781       O  
ATOM    340  N   ALA A 547      26.088   1.619  10.647  1.00 31.52           N  
ANISOU  340  N   ALA A 547     4864   4120   2992     48     72   -732       N  
ATOM    341  CA  ALA A 547      24.987   0.685  10.450  1.00 32.16           C  
ANISOU  341  CA  ALA A 547     5134   3991   3092    -25     67   -763       C  
ATOM    342  C   ALA A 547      24.856  -0.364  11.575  1.00 32.28           C  
ANISOU  342  C   ALA A 547     5062   3886   3315    -45    109   -798       C  
ATOM    343  O   ALA A 547      23.709  -0.726  11.991  1.00 35.20           O  
ANISOU  343  O   ALA A 547     5346   4257   3769   -196    -13   -748       O  
ATOM    344  CB  ALA A 547      25.133  -0.001   9.040  1.00 33.82           C  
ANISOU  344  CB  ALA A 547     5586   4087   3176    110     89  -1012       C  
ATOM    345  N   ASN A 548      26.000  -0.806  12.111  1.00 31.92           N  
ANISOU  345  N   ASN A 548     5164   3623   3338    -59     87   -724       N  
ATOM    346  CA  ASN A 548      26.043  -1.799  13.191  1.00 32.31           C  
ANISOU  346  CA  ASN A 548     5051   3832   3390    -14    260   -491       C  
ATOM    347  C   ASN A 548      25.434  -1.204  14.456  1.00 33.82           C  
ANISOU  347  C   ASN A 548     5203   3955   3691     16    374   -544       C  
ATOM    348  O   ASN A 548      24.696  -1.902  15.179  1.00 33.76           O  
ANISOU  348  O   ASN A 548     5279   3956   3591     -8    429   -588       O  
ATOM    349  CB  ASN A 548      27.482  -2.150  13.534  1.00 33.75           C  
ANISOU  349  CB  ASN A 548     5292   3953   3579     46    200   -164       C  
ATOM    350  CG  ASN A 548      27.565  -3.239  14.638  1.00 36.08           C  
ANISOU  350  CG  ASN A 548     5502   4503   3704   -320    363     -7       C  
ATOM    351  OD1 ASN A 548      28.152  -3.006  15.701  1.00 43.02           O  
ANISOU  351  OD1 ASN A 548     5836   5976   4531   -236   -184    598       O  
ATOM    352  ND2 ASN A 548      26.958  -4.409  14.384  1.00 37.07           N  
ANISOU  352  ND2 ASN A 548     6211   3971   3903   -294    741     43       N  
ATOM    353  N   SER A 549      25.722   0.086  14.699  1.00 32.26           N  
ANISOU  353  N   SER A 549     4919   3838   3499     34    451   -800       N  
ATOM    354  CA  SER A 549      25.022   0.769  15.822  1.00 34.09           C  
ANISOU  354  CA  SER A 549     5196   4110   3644     85    482   -711       C  
ATOM    355  C   SER A 549      23.470   0.791  15.595  1.00 35.69           C  
ANISOU  355  C   SER A 549     5246   4347   3965    133    425   -531       C  
ATOM    356  O   SER A 549      22.688   0.563  16.526  1.00 36.83           O  
ANISOU  356  O   SER A 549     5522   4467   4003     61    488   -153       O  
ATOM    357  CB  SER A 549      25.587   2.194  16.007  1.00 32.64           C  
ANISOU  357  CB  SER A 549     5177   3911   3310     83    571   -827       C  
ATOM    358  OG  SER A 549      24.850   2.792  17.070  1.00 37.17           O  
ANISOU  358  OG  SER A 549     5968   4091   4062    168    492   -915       O  
ATOM    359  N   ASP A 550      23.002   1.070  14.368  1.00 38.49           N  
ANISOU  359  N   ASP A 550     5496   4775   4350    154    289   -360       N  
ATOM    360  CA  ASP A 550      21.548   0.906  14.042  1.00 41.26           C  
ANISOU  360  CA  ASP A 550     5716   5111   4847    130    139   -223       C  
ATOM    361  C   ASP A 550      20.951  -0.502  14.235  1.00 43.64           C  
ANISOU  361  C   ASP A 550     5866   5500   5216     54    122   -150       C  
ATOM    362  O   ASP A 550      19.771  -0.660  14.612  1.00 43.90           O  
ANISOU  362  O   ASP A 550     5902   5676   5100     64    211   -249       O  
ATOM    363  CB  ASP A 550      21.271   1.380  12.609  1.00 42.13           C  
ANISOU  363  CB  ASP A 550     5939   5246   4820    208    109   -157       C  
ATOM    364  CG  ASP A 550      21.346   2.891  12.488  1.00 43.94           C  
ANISOU  364  CG  ASP A 550     6440   5322   4932    237    145   -203       C  
ATOM    365  OD1 ASP A 550      21.073   3.540  13.526  1.00 45.78           O  
ANISOU  365  OD1 ASP A 550     7195   5508   4689    959    366    -93       O  
ATOM    366  OD2 ASP A 550      21.669   3.432  11.379  1.00 45.78           O  
ANISOU  366  OD2 ASP A 550     6399   6181   4813    387    687   -470       O  
ATOM    367  N   LEU A 551      21.775  -1.509  13.931  1.00 45.08           N  
ANISOU  367  N   LEU A 551     6032   5535   5559     45    131   -194       N  
ATOM    368  CA  LEU A 551      21.397  -2.920  14.063  1.00 47.77           C  
ANISOU  368  CA  LEU A 551     6260   5962   5928    -36     41   -106       C  
ATOM    369  C   LEU A 551      21.096  -3.229  15.530  1.00 49.80           C  
ANISOU  369  C   LEU A 551     6462   6335   6124    -58     51    -55       C  
ATOM    370  O   LEU A 551      20.015  -3.755  15.878  1.00 48.44           O  
ANISOU  370  O   LEU A 551     6312   6203   5888   -220     51    -42       O  
ATOM    371  CB  LEU A 551      22.514  -3.828  13.517  1.00 47.03           C  
ANISOU  371  CB  LEU A 551     6256   5635   5975     43    115   -152       C  
ATOM    372  CG  LEU A 551      22.164  -5.307  13.448  1.00 48.58           C  
ANISOU  372  CG  LEU A 551     6478   5588   6391     75    -13    -19       C  
ATOM    373  CD1 LEU A 551      20.833  -5.539  12.734  1.00 49.41           C  
ANISOU  373  CD1 LEU A 551     6708   5012   7054   -111   -110   -272       C  
ATOM    374  CD2 LEU A 551      23.333  -6.012  12.740  1.00 48.57           C  
ANISOU  374  CD2 LEU A 551     7474   4788   6190    205    317   -337       C  
ATOM    375  N   TYR A 552      22.058  -2.844  16.374  1.00 52.20           N  
ANISOU  375  N   TYR A 552     6697   6731   6403   -141    -33   -184       N  
ATOM    376  CA  TYR A 552      21.953  -2.988  17.804  1.00 55.20           C  
ANISOU  376  CA  TYR A 552     7133   7137   6703    -89     -8   -123       C  
ATOM    377  C   TYR A 552      20.667  -2.288  18.319  1.00 56.16           C  
ANISOU  377  C   TYR A 552     7241   7295   6800    -99     30   -186       C  
ATOM    378  O   TYR A 552      19.862  -2.918  19.026  1.00 55.56           O  
ANISOU  378  O   TYR A 552     7270   7213   6627   -131    120   -258       O  
ATOM    379  CB  TYR A 552      23.233  -2.434  18.448  1.00 56.02           C  
ANISOU  379  CB  TYR A 552     7210   7245   6828   -102    -51   -162       C  
ATOM    380  CG  TYR A 552      23.358  -2.738  19.910  1.00 60.86           C  
ANISOU  380  CG  TYR A 552     7979   7926   7216    -27   -114     90       C  
ATOM    381  CD1 TYR A 552      24.278  -3.702  20.369  1.00 64.85           C  
ANISOU  381  CD1 TYR A 552     8491   8263   7886    231    -32     52       C  
ATOM    382  CD2 TYR A 552      22.565  -2.043  20.851  1.00 65.38           C  
ANISOU  382  CD2 TYR A 552     8370   8603   7868    286     35     47       C  
ATOM    383  CE1 TYR A 552      24.393  -3.984  21.770  1.00 68.61           C  
ANISOU  383  CE1 TYR A 552     8994   8877   8196    388   -235    156       C  
ATOM    384  CE2 TYR A 552      22.658  -2.305  22.244  1.00 68.05           C  
ANISOU  384  CE2 TYR A 552     8939   8844   8074    348    -88     81       C  
ATOM    385  CZ  TYR A 552      23.571  -3.273  22.697  1.00 69.55           C  
ANISOU  385  CZ  TYR A 552     9166   9090   8167    370   -131    138       C  
ATOM    386  OH  TYR A 552      23.646  -3.515  24.054  1.00 70.27           O  
ANISOU  386  OH  TYR A 552     9478   9238   7982    434    -41     53       O  
ATOM    387  N   SER A 553      20.464  -1.023  17.926  1.00 57.68           N  
ANISOU  387  N   SER A 553     7476   7436   7001    -93     24   -171       N  
ATOM    388  CA  SER A 553      19.248  -0.268  18.288  1.00 59.87           C  
ANISOU  388  CA  SER A 553     7724   7746   7276   -108    102   -188       C  
ATOM    389  C   SER A 553      17.905  -0.985  18.047  1.00 61.84           C  
ANISOU  389  C   SER A 553     7955   7972   7566   -148     88   -151       C  
ATOM    390  O   SER A 553      17.088  -1.067  18.974  1.00 62.71           O  
ANISOU  390  O   SER A 553     8151   8123   7553   -163    139   -232       O  
ATOM    391  CB  SER A 553      19.207   1.123  17.638  1.00 59.53           C  
ANISOU  391  CB  SER A 553     7721   7681   7216   -134    143   -197       C  
ATOM    392  OG  SER A 553      20.119   2.000  18.269  1.00 58.99           O  
ANISOU  392  OG  SER A 553     7668   7699   7046   -193    263   -316       O  
ATOM    393  N   SER A 554      17.624  -1.479  16.834  1.00 63.32           N  
ANISOU  393  N   SER A 554     8177   8110   7772   -127     67   -123       N  
ATOM    394  CA  SER A 554      16.288  -2.083  16.663  1.00 64.70           C  
ANISOU  394  CA  SER A 554     8331   8247   8002    -88     37    -79       C  
ATOM    395  C   SER A 554      16.180  -3.482  17.330  1.00 65.32           C  
ANISOU  395  C   SER A 554     8349   8270   8200    -54     17    -48       C  
ATOM    396  O   SER A 554      15.073  -3.905  17.698  1.00 65.40           O  
ANISOU  396  O   SER A 554     8273   8287   8288    -45     64    -29       O  
ATOM    397  CB  SER A 554      15.780  -2.048  15.209  1.00 65.22           C  
ANISOU  397  CB  SER A 554     8457   8302   8019    -48     83    -60       C  
ATOM    398  OG  SER A 554      16.561  -2.886  14.379  1.00 66.36           O  
ANISOU  398  OG  SER A 554     8862   8473   7875    -24    304   -151       O  
ATOM    399  N   ALA A 555      17.336  -4.140  17.540  1.00 65.90           N  
ANISOU  399  N   ALA A 555     8368   8344   8325     -4     14    -49       N  
ATOM    400  CA  ALA A 555      17.423  -5.502  18.114  1.00 66.46           C  
ANISOU  400  CA  ALA A 555     8425   8437   8388     48    -12    -45       C  
ATOM    401  C   ALA A 555      16.878  -5.627  19.540  1.00 66.86           C  
ANISOU  401  C   ALA A 555     8459   8551   8393     77    -19    -89       C  
ATOM    402  O   ALA A 555      16.867  -4.651  20.295  1.00 67.49           O  
ANISOU  402  O   ALA A 555     8556   8602   8483     89    -14   -177       O  
ATOM    403  CB  ALA A 555      18.863  -6.026  18.044  1.00 66.26           C  
ANISOU  403  CB  ALA A 555     8377   8385   8411     36     -7     -8       C  
ATOM    404  N   ASN A 638      10.851 -13.718  10.269  1.00 34.51           N  
ANISOU  404  N   ASN A 638     3679   5131   4302   -116   1401    386       N  
ATOM    405  CA  ASN A 638      11.343 -15.037   9.796  1.00 33.37           C  
ANISOU  405  CA  ASN A 638     3879   4701   4099   -441   1162    676       C  
ATOM    406  C   ASN A 638      12.387 -14.942   8.601  1.00 30.94           C  
ANISOU  406  C   ASN A 638     3594   4419   3742   -565   1144    677       C  
ATOM    407  O   ASN A 638      12.125 -15.275   7.426  1.00 31.74           O  
ANISOU  407  O   ASN A 638     3722   4412   3924  -1181   1222    814       O  
ATOM    408  CB  ASN A 638      10.227 -15.856   9.275  1.00 36.58           C  
ANISOU  408  CB  ASN A 638     4420   5038   4439   -488    969    547       C  
ATOM    409  CG  ASN A 638      10.524 -17.354   9.350  1.00 42.81           C  
ANISOU  409  CG  ASN A 638     5160   5484   5622   -376    550    571       C  
ATOM    410  OD1 ASN A 638      11.690 -17.799   9.293  1.00 48.55           O  
ANISOU  410  OD1 ASN A 638     5904   6246   6294    -78    595    388       O  
ATOM    411  ND2 ASN A 638       9.464 -18.143   9.487  1.00 50.36           N  
ANISOU  411  ND2 ASN A 638     5984   6593   6556   -963    744    754       N  
ATOM    412  N   ILE A 639      13.584 -14.628   8.945  1.00 27.90           N  
ANISOU  412  N   ILE A 639     3408   3809   3384   -545   1121    679       N  
ATOM    413  CA  ILE A 639      14.567 -14.295   7.890  1.00 24.43           C  
ANISOU  413  CA  ILE A 639     2927   3202   3151   -522   1137    636       C  
ATOM    414  C   ILE A 639      15.583 -15.406   7.786  1.00 23.24           C  
ANISOU  414  C   ILE A 639     3010   2926   2892   -423    856    565       C  
ATOM    415  O   ILE A 639      16.118 -15.865   8.845  1.00 26.51           O  
ANISOU  415  O   ILE A 639     3237   3446   3388   -342    826    466       O  
ATOM    416  CB  ILE A 639      15.215 -12.942   8.291  1.00 26.48           C  
ANISOU  416  CB  ILE A 639     3094   3317   3648   -434    978    476       C  
ATOM    417  CG1 ILE A 639      14.118 -11.847   8.206  1.00 27.64           C  
ANISOU  417  CG1 ILE A 639     3347   3575   3578    -63    930    283       C  
ATOM    418  CG2 ILE A 639      16.471 -12.606   7.424  1.00 26.50           C  
ANISOU  418  CG2 ILE A 639     3270   3507   3292   -454   1063    711       C  
ATOM    419  CD1 ILE A 639      13.458 -11.588   6.798  1.00 29.09           C  
ANISOU  419  CD1 ILE A 639     3695   3269   4090   -429    822    565       C  
ATOM    420  N   HIS A 640      15.835 -15.903   6.549  1.00 20.36           N  
ANISOU  420  N   HIS A 640     2784   2326   2624   -385    799    508       N  
ATOM    421  CA  HIS A 640      16.904 -16.912   6.360  1.00 19.96           C  
ANISOU  421  CA  HIS A 640     2800   2284   2499   -449    519    407       C  
ATOM    422  C   HIS A 640      18.254 -16.281   5.882  1.00 18.29           C  
ANISOU  422  C   HIS A 640     2636   2052   2258   -326    460    331       C  
ATOM    423  O   HIS A 640      19.331 -16.837   6.122  1.00 17.47           O  
ANISOU  423  O   HIS A 640     2682   2017   1936   -194    384    441       O  
ATOM    424  CB  HIS A 640      16.495 -18.047   5.385  1.00 21.76           C  
ANISOU  424  CB  HIS A 640     3342   1984   2942   -577    628    273       C  
ATOM    425  CG  HIS A 640      16.027 -17.596   4.028  1.00 20.28           C  
ANISOU  425  CG  HIS A 640     2780   1876   3050   -449    108   -103       C  
ATOM    426  ND1 HIS A 640      16.890 -17.166   3.025  1.00 20.64           N  
ANISOU  426  ND1 HIS A 640     2722   2332   2788    -38      3    622       N  
ATOM    427  CD2 HIS A 640      14.766 -17.558   3.488  1.00 22.08           C  
ANISOU  427  CD2 HIS A 640     3058   1875   3455   -357   -110    -16       C  
ATOM    428  CE1 HIS A 640      16.180 -16.888   1.936  1.00 20.70           C  
ANISOU  428  CE1 HIS A 640     2199   2105   3561     68    -67    172       C  
ATOM    429  NE2 HIS A 640      14.883 -17.106   2.198  1.00 22.69           N  
ANISOU  429  NE2 HIS A 640     2902   2097   3621    -22      7   -356       N  
ATOM    430  N   THR A 641      18.187 -15.097   5.239  1.00 17.35           N  
ANISOU  430  N   THR A 641     2528   1982   2082   -364    378    396       N  
ATOM    431  CA  THR A 641      19.380 -14.489   4.649  1.00 15.43           C  
ANISOU  431  CA  THR A 641     2352   1674   1834   -215    470    254       C  
ATOM    432  C   THR A 641      19.349 -12.982   4.837  1.00 15.88           C  
ANISOU  432  C   THR A 641     2266   1735   2033   -164    298    418       C  
ATOM    433  O   THR A 641      18.271 -12.348   4.614  1.00 16.27           O  
ANISOU  433  O   THR A 641     2109   1690   2380   -292    399    414       O  
ATOM    434  CB  THR A 641      19.422 -14.820   3.136  1.00 14.60           C  
ANISOU  434  CB  THR A 641     2250   1489   1807   -308    355    134       C  
ATOM    435  OG1 THR A 641      19.433 -16.235   3.012  1.00 16.14           O  
ANISOU  435  OG1 THR A 641     2895   1395   1842   -230    102    288       O  
ATOM    436  CG2 THR A 641      20.676 -14.246   2.480  1.00 17.47           C  
ANISOU  436  CG2 THR A 641     2286   2143   2206   -632    514    171       C  
ATOM    437  N   VAL A 642      20.509 -12.410   5.190  1.00 14.26           N  
ANISOU  437  N   VAL A 642     2201   1558   1659   -183    489    265       N  
ATOM    438  CA  VAL A 642      20.674 -10.946   5.153  1.00 13.90           C  
ANISOU  438  CA  VAL A 642     1950   1791   1539   -368    477    224       C  
ATOM    439  C   VAL A 642      21.671 -10.659   4.047  1.00 14.23           C  
ANISOU  439  C   VAL A 642     1754   1923   1730   -161    257    279       C  
ATOM    440  O   VAL A 642      22.757 -11.299   4.018  1.00 16.00           O  
ANISOU  440  O   VAL A 642     2067   2262   1748    -39    453    621       O  
ATOM    441  CB  VAL A 642      21.232 -10.442   6.461  1.00 14.83           C  
ANISOU  441  CB  VAL A 642     2270   1780   1585   -274    511     88       C  
ATOM    442  CG1 VAL A 642      21.621  -8.854   6.355  1.00 16.55           C  
ANISOU  442  CG1 VAL A 642     2554   1698   2034   -521     91    130       C  
ATOM    443  CG2 VAL A 642      20.205 -10.679   7.615  1.00 16.03           C  
ANISOU  443  CG2 VAL A 642     2539   2213   1338    -72    938    135       C  
ATOM    444  N   ILE A 643      21.304  -9.788   3.088  1.00 11.73           N  
ANISOU  444  N   ILE A 643     1774   1506   1174   -302    351    294       N  
ATOM    445  CA  ILE A 643      22.239  -9.437   2.000  1.00 11.67           C  
ANISOU  445  CA  ILE A 643     1964   1306   1161   -481    328     26       C  
ATOM    446  C   ILE A 643      22.698  -8.005   2.271  1.00 12.79           C  
ANISOU  446  C   ILE A 643     1726   1374   1757   -364    160    102       C  
ATOM    447  O   ILE A 643      21.843  -7.111   2.352  1.00 14.67           O  
ANISOU  447  O   ILE A 643     2049   1596   1929   -250    209     68       O  
ATOM    448  CB  ILE A 643      21.609  -9.543   0.610  1.00 11.58           C  
ANISOU  448  CB  ILE A 643     1440   1541   1418   -455    236    -48       C  
ATOM    449  CG1 ILE A 643      21.164 -11.007   0.349  1.00 13.55           C  
ANISOU  449  CG1 ILE A 643     1879   1772   1496   -545    -87    358       C  
ATOM    450  CG2 ILE A 643      22.641  -9.058  -0.458  1.00 14.22           C  
ANISOU  450  CG2 ILE A 643     2110   1903   1390   -568    562    427       C  
ATOM    451  CD1 ILE A 643      20.325 -11.193  -0.956  1.00 14.33           C  
ANISOU  451  CD1 ILE A 643     1788   2075   1579   -345   -189    156       C  
ATOM    452  N   LEU A 644      24.009  -7.823   2.395  1.00 12.17           N  
ANISOU  452  N   LEU A 644     1656   1348   1620   -345    205     63       N  
ATOM    453  CA  LEU A 644      24.586  -6.475   2.573  1.00 12.09           C  
ANISOU  453  CA  LEU A 644     1722   1327   1543   -521     58    147       C  
ATOM    454  C   LEU A 644      25.125  -6.023   1.229  1.00 12.08           C  
ANISOU  454  C   LEU A 644     1717   1214   1658   -354    313    167       C  
ATOM    455  O   LEU A 644      26.060  -6.687   0.661  1.00 14.31           O  
ANISOU  455  O   LEU A 644     1981   1672   1783   -376    442    -33       O  
ATOM    456  CB  LEU A 644      25.746  -6.503   3.615  1.00 11.86           C  
ANISOU  456  CB  LEU A 644     1955   1330   1219   -296    -87    208       C  
ATOM    457  CG  LEU A 644      25.246  -7.013   4.971  1.00 13.22           C  
ANISOU  457  CG  LEU A 644     2112   1621   1290   -175    113    133       C  
ATOM    458  CD1 LEU A 644      26.437  -6.911   5.977  1.00 17.03           C  
ANISOU  458  CD1 LEU A 644     2727   2189   1556   -422   -340   -231       C  
ATOM    459  CD2 LEU A 644      24.033  -6.191   5.505  1.00 16.56           C  
ANISOU  459  CD2 LEU A 644     2562   2075   1654    -37    515   -314       C  
ATOM    460  N   ASP A 645      24.557  -4.911   0.696  1.00 12.14           N  
ANISOU  460  N   ASP A 645     1821   1179   1609   -389    266    298       N  
ATOM    461  CA  ASP A 645      25.039  -4.374  -0.593  1.00 12.07           C  
ANISOU  461  CA  ASP A 645     1804   1357   1422   -370    242    110       C  
ATOM    462  C   ASP A 645      26.187  -3.400  -0.294  1.00 12.68           C  
ANISOU  462  C   ASP A 645     2016   1382   1418   -223    220    193       C  
ATOM    463  O   ASP A 645      25.982  -2.388   0.399  1.00 15.02           O  
ANISOU  463  O   ASP A 645     2252   1512   1939   -312    228   -218       O  
ATOM    464  CB  ASP A 645      23.821  -3.695  -1.267  1.00 13.32           C  
ANISOU  464  CB  ASP A 645     1917   1590   1552   -326    157    547       C  
ATOM    465  CG  ASP A 645      24.199  -2.756  -2.422  1.00 14.62           C  
ANISOU  465  CG  ASP A 645     2298   1469   1786   -139    104    206       C  
ATOM    466  OD1 ASP A 645      25.313  -2.942  -2.938  1.00 19.02           O  
ANISOU  466  OD1 ASP A 645     2259   3081   1884   -606    170    524       O  
ATOM    467  OD2 ASP A 645      23.320  -1.937  -2.818  1.00 18.80           O  
ANISOU  467  OD2 ASP A 645     2658   1860   2625   -235    115    458       O  
ATOM    468  N   PHE A 646      27.361  -3.778  -0.763  1.00 13.32           N  
ANISOU  468  N   PHE A 646     1735   1608   1717   -325    105    -24       N  
ATOM    469  CA  PHE A 646      28.603  -3.002  -0.625  1.00 12.83           C  
ANISOU  469  CA  PHE A 646     1621   1536   1715   -204    130     19       C  
ATOM    470  C   PHE A 646      28.932  -2.152  -1.827  1.00 12.76           C  
ANISOU  470  C   PHE A 646     1748   1479   1618   -200    -50    -24       C  
ATOM    471  O   PHE A 646      30.074  -1.636  -1.916  1.00 15.36           O  
ANISOU  471  O   PHE A 646     1991   1903   1942   -295    164      8       O  
ATOM    472  CB  PHE A 646      29.817  -3.932  -0.356  1.00 13.76           C  
ANISOU  472  CB  PHE A 646     2039   1404   1783   -130   -230     33       C  
ATOM    473  CG  PHE A 646      29.962  -4.322   1.123  1.00 15.04           C  
ANISOU  473  CG  PHE A 646     2068   1731   1915   -519   -204    524       C  
ATOM    474  CD1 PHE A 646      29.024  -5.139   1.729  1.00 18.80           C  
ANISOU  474  CD1 PHE A 646     2013   2738   2392   -753   -403    834       C  
ATOM    475  CD2 PHE A 646      31.048  -3.860   1.884  1.00 15.87           C  
ANISOU  475  CD2 PHE A 646     2444   2248   1337   -185   -303    287       C  
ATOM    476  CE1 PHE A 646      29.139  -5.450   3.122  1.00 22.91           C  
ANISOU  476  CE1 PHE A 646     2494   3339   2872   -943   -337   1144       C  
ATOM    477  CE2 PHE A 646      31.198  -4.138   3.245  1.00 19.48           C  
ANISOU  477  CE2 PHE A 646     2572   2758   2072   -117    -69    543       C  
ATOM    478  CZ  PHE A 646      30.246  -4.954   3.896  1.00 20.42           C  
ANISOU  478  CZ  PHE A 646     2346   2757   2655   -652    -97    625       C  
ATOM    479  N   THR A 647      27.968  -1.943  -2.715  1.00 13.43           N  
ANISOU  479  N   THR A 647     2085   1775   1243   -357     27    259       N  
ATOM    480  CA  THR A 647      28.279  -1.164  -3.911  1.00 15.15           C  
ANISOU  480  CA  THR A 647     2539   1739   1479   -595    -97    266       C  
ATOM    481  C   THR A 647      28.793   0.269  -3.615  1.00 14.90           C  
ANISOU  481  C   THR A 647     2383   1835   1440   -674    144    164       C  
ATOM    482  O   THR A 647      29.528   0.830  -4.477  1.00 18.88           O  
ANISOU  482  O   THR A 647     2759   2185   2229  -1022    392    159       O  
ATOM    483  CB  THR A 647      27.103  -1.127  -4.866  1.00 17.11           C  
ANISOU  483  CB  THR A 647     2642   2215   1645   -429    -57    191       C  
ATOM    484  OG1 THR A 647      26.016  -0.522  -4.310  1.00 23.28           O  
ANISOU  484  OG1 THR A 647     3238   3126   2480   -424    174    518       O  
ATOM    485  CG2 THR A 647      26.692  -2.393  -5.387  1.00 17.37           C  
ANISOU  485  CG2 THR A 647     3048   1797   1755   -906   -309     16       C  
ATOM    486  N   GLN A 648      28.402   0.885  -2.473  1.00 13.90           N  
ANISOU  486  N   GLN A 648     2198   1350   1732   -492   -130    103       N  
ATOM    487  CA  GLN A 648      28.893   2.239  -2.162  1.00 16.12           C  
ANISOU  487  CA  GLN A 648     2266   1678   2181   -339     -4     68       C  
ATOM    488  C   GLN A 648      30.169   2.267  -1.397  1.00 16.56           C  
ANISOU  488  C   GLN A 648     2519   1631   2141   -493   -117    113       C  
ATOM    489  O   GLN A 648      30.655   3.346  -1.051  1.00 17.79           O  
ANISOU  489  O   GLN A 648     2716   1744   2299   -817   -330     67       O  
ATOM    490  CB  GLN A 648      27.837   2.949  -1.324  1.00 16.89           C  
ANISOU  490  CB  GLN A 648     2554   1672   2191   -142      9     49       C  
ATOM    491  CG  GLN A 648      26.508   3.005  -2.063  1.00 20.55           C  
ANISOU  491  CG  GLN A 648     2690   2769   2346    -15    -62     35       C  
ATOM    492  CD  GLN A 648      25.627   4.132  -1.437  1.00 27.37           C  
ANISOU  492  CD  GLN A 648     3920   3368   3111     44    189    419       C  
ATOM    493  OE1 GLN A 648      25.809   4.549  -0.243  1.00 32.75           O  
ANISOU  493  OE1 GLN A 648     4225   4639   3579    -11    157   -263       O  
ATOM    494  NE2 GLN A 648      24.728   4.680  -2.262  1.00 31.53           N  
ANISOU  494  NE2 GLN A 648     3915   3659   4405     64   -449    831       N  
ATOM    495  N   VAL A 649      30.689   1.115  -1.038  1.00 14.84           N  
ANISOU  495  N   VAL A 649     2150   1383   2103   -441     22    178       N  
ATOM    496  CA  VAL A 649      31.881   1.028  -0.138  1.00 14.81           C  
ANISOU  496  CA  VAL A 649     2050   1660   1913   -558     48     69       C  
ATOM    497  C   VAL A 649      33.143   0.994  -0.952  1.00 14.45           C  
ANISOU  497  C   VAL A 649     1934   1656   1898   -710      0     -7       C  
ATOM    498  O   VAL A 649      33.294   0.120  -1.837  1.00 16.06           O  
ANISOU  498  O   VAL A 649     2200   1800   2102   -465     57   -106       O  
ATOM    499  CB  VAL A 649      31.794  -0.249   0.792  1.00 14.38           C  
ANISOU  499  CB  VAL A 649     2113   1699   1651   -578    -92    202       C  
ATOM    500  CG1 VAL A 649      33.021  -0.314   1.707  1.00 15.64           C  
ANISOU  500  CG1 VAL A 649     2303   1738   1899   -313   -316     18       C  
ATOM    501  CG2 VAL A 649      30.436  -0.167   1.628  1.00 16.82           C  
ANISOU  501  CG2 VAL A 649     2084   1913   2392   -186    131    272       C  
ATOM    502  N   ASN A 650      34.088   1.889  -0.648  1.00 14.67           N  
ANISOU  502  N   ASN A 650     1937   1559   2076   -676   -145      7       N  
ATOM    503  CA  ASN A 650      35.344   1.934  -1.422  1.00 14.45           C  
ANISOU  503  CA  ASN A 650     1995   1430   2065   -353     61    128       C  
ATOM    504  C   ASN A 650      36.508   1.251  -0.750  1.00 15.88           C  
ANISOU  504  C   ASN A 650     2098   1674   2260   -409      0    356       C  
ATOM    505  O   ASN A 650      37.462   0.788  -1.435  1.00 16.39           O  
ANISOU  505  O   ASN A 650     2174   1824   2227    -48    110    459       O  
ATOM    506  CB  ASN A 650      35.733   3.419  -1.714  1.00 13.88           C  
ANISOU  506  CB  ASN A 650     2067   1142   2061   -467   -237    308       C  
ATOM    507  CG  ASN A 650      34.691   4.048  -2.606  1.00 15.68           C  
ANISOU  507  CG  ASN A 650     2552   1774   1630   -342   -518    182       C  
ATOM    508  OD1 ASN A 650      34.396   3.492  -3.672  1.00 20.12           O  
ANISOU  508  OD1 ASN A 650     3417   2360   1868   -345   -883   -353       O  
ATOM    509  ND2 ASN A 650      34.112   5.197  -2.213  1.00 21.80           N  
ANISOU  509  ND2 ASN A 650     3406   2308   2566    102   -659    -83       N  
ATOM    510  N   PHE A 651      36.455   1.116   0.562  1.00 16.72           N  
ANISOU  510  N   PHE A 651     2063   1974   2315   -361   -262    239       N  
ATOM    511  CA  PHE A 651      37.508   0.343   1.272  1.00 16.21           C  
ANISOU  511  CA  PHE A 651     1893   2029   2236   -477   -188    143       C  
ATOM    512  C   PHE A 651      36.977  -0.013   2.635  1.00 17.60           C  
ANISOU  512  C   PHE A 651     2109   2405   2171   -442   -354     39       C  
ATOM    513  O   PHE A 651      35.986   0.562   3.085  1.00 19.31           O  
ANISOU  513  O   PHE A 651     2379   2513   2442   -544   -321   -215       O  
ATOM    514  CB  PHE A 651      38.873   1.143   1.341  1.00 18.40           C  
ANISOU  514  CB  PHE A 651     2160   2221   2609   -685   -303     62       C  
ATOM    515  CG  PHE A 651      38.867   2.343   2.256  1.00 18.80           C  
ANISOU  515  CG  PHE A 651     2722   1472   2947   -122   -704    213       C  
ATOM    516  CD1 PHE A 651      39.064   2.196   3.663  1.00 24.80           C  
ANISOU  516  CD1 PHE A 651     3605   2349   3468   -176  -1103   -173       C  
ATOM    517  CD2 PHE A 651      38.562   3.652   1.731  1.00 22.50           C  
ANISOU  517  CD2 PHE A 651     2713   1917   3916   -616   -819    399       C  
ATOM    518  CE1 PHE A 651      38.972   3.343   4.593  1.00 27.55           C  
ANISOU  518  CE1 PHE A 651     4129   2796   3541    239  -1630   -219       C  
ATOM    519  CE2 PHE A 651      38.549   4.809   2.656  1.00 23.90           C  
ANISOU  519  CE2 PHE A 651     3497   2024   3559   -300   -902    157       C  
ATOM    520  CZ  PHE A 651      38.715   4.650   4.055  1.00 27.85           C  
ANISOU  520  CZ  PHE A 651     3878   2565   4137   -235  -1067    120       C  
ATOM    521  N   MET A 652      37.713  -0.890   3.313  1.00 17.71           N  
ANISOU  521  N   MET A 652     2261   2472   1992   -553   -460    178       N  
ATOM    522  CA AMET A 652      37.356  -1.110   4.715  0.50 19.52           C  
ANISOU  522  CA AMET A 652     2365   2940   2112   -553   -410     12       C  
ATOM    523  CA BMET A 652      37.370  -1.343   4.668  0.50 18.88           C  
ANISOU  523  CA BMET A 652     2317   2815   2038   -627   -441     56       C  
ATOM    524  C   MET A 652      38.590  -1.089   5.586  1.00 20.90           C  
ANISOU  524  C   MET A 652     2408   3193   2341   -454   -435     28       C  
ATOM    525  O   MET A 652      39.717  -1.453   5.176  1.00 23.36           O  
ANISOU  525  O   MET A 652     2691   3804   2378   -498   -294    -70       O  
ATOM    526  CB AMET A 652      36.562  -2.382   4.942  0.50 19.40           C  
ANISOU  526  CB AMET A 652     2353   2725   2292   -411   -458     59       C  
ATOM    527  CB BMET A 652      37.038  -2.840   4.609  0.50 17.51           C  
ANISOU  527  CB BMET A 652     2075   2481   2095   -698   -465    302       C  
ATOM    528  CG AMET A 652      35.304  -2.410   4.114  0.50 17.98           C  
ANISOU  528  CG AMET A 652     2002   2364   2466   -621   -303     99       C  
ATOM    529  CG BMET A 652      35.581  -3.120   4.132  0.50 16.15           C  
ANISOU  529  CG BMET A 652     1841   2247   2047   -433   -439     32       C  
ATOM    530  SD AMET A 652      34.552  -3.930   4.498  0.50 20.32           S  
ANISOU  530  SD AMET A 652     2953   2308   2457   -441   -211   -228       S  
ATOM    531  SD BMET A 652      34.247  -2.391   5.157  0.50 15.59           S  
ANISOU  531  SD BMET A 652     2386   1795   1742   -308    -94    191       S  
ATOM    532  CE AMET A 652      34.391  -3.825   6.293  0.50 20.37           C  
ANISOU  532  CE AMET A 652     2772   2495   2470    172   -189   -135       C  
ATOM    533  CE BMET A 652      33.970  -3.630   6.460  0.50 16.49           C  
ANISOU  533  CE BMET A 652     2421   2070   1773   -123     78    421       C  
ATOM    534  N   ASP A 653      38.366  -0.489   6.764  1.00 21.65           N  
ANISOU  534  N   ASP A 653     2683   3418   2123   -761   -491    -56       N  
ATOM    535  CA  ASP A 653      39.437  -0.342   7.801  1.00 24.04           C  
ANISOU  535  CA  ASP A 653     3304   3521   2308   -532   -605     -1       C  
ATOM    536  C   ASP A 653      39.395  -1.577   8.730  1.00 23.48           C  
ANISOU  536  C   ASP A 653     3159   3192   2569   -630   -660   -110       C  
ATOM    537  O   ASP A 653      38.396  -2.385   8.726  1.00 22.19           O  
ANISOU  537  O   ASP A 653     2986   3458   1986   -690   -616   -363       O  
ATOM    538  CB  ASP A 653      39.407   1.056   8.554  1.00 25.77           C  
ANISOU  538  CB  ASP A 653     3420   3588   2782   -631   -339    -44       C  
ATOM    539  CG  ASP A 653      38.086   1.381   9.282  1.00 33.30           C  
ANISOU  539  CG  ASP A 653     4596   3984   4072   -257   -244    270       C  
ATOM    540  OD1 ASP A 653      37.729   2.607   9.307  1.00 41.45           O  
ANISOU  540  OD1 ASP A 653     6103   4301   5344   -506   -441    199       O  
ATOM    541  OD2 ASP A 653      37.403   0.520   9.884  1.00 33.60           O  
ANISOU  541  OD2 ASP A 653     4755   2831   5179   -434    139     18       O  
ATOM    542  N   SER A 654      40.407  -1.726   9.581  1.00 24.76           N  
ANISOU  542  N   SER A 654     3330   3388   2690   -539   -826    -92       N  
ATOM    543  CA ASER A 654      40.481  -2.928  10.415  0.50 25.94           C  
ANISOU  543  CA ASER A 654     3441   3564   2847   -390   -826    -26       C  
ATOM    544  CA BSER A 654      40.486  -2.927  10.429  0.50 25.69           C  
ANISOU  544  CA BSER A 654     3425   3434   2898   -439   -858   -106       C  
ATOM    545  C   SER A 654      39.302  -3.025  11.368  1.00 25.96           C  
ANISOU  545  C   SER A 654     3479   3465   2916   -379   -864    -53       C  
ATOM    546  O   SER A 654      38.760  -4.136  11.588  1.00 26.83           O  
ANISOU  546  O   SER A 654     3651   3708   2834   -607   -880    117       O  
ATOM    547  CB ASER A 654      41.802  -2.946  11.187  0.50 27.07           C  
ANISOU  547  CB ASER A 654     3430   3646   3206   -406   -814   -119       C  
ATOM    548  CB BSER A 654      41.785  -2.944  11.250  0.50 26.50           C  
ANISOU  548  CB BSER A 654     3415   3404   3249   -484   -882   -242       C  
ATOM    549  OG ASER A 654      42.883  -3.003  10.269  0.50 29.32           O  
ANISOU  549  OG ASER A 654     3657   4096   3386   -363   -599    250       O  
ATOM    550  OG BSER A 654      42.112  -1.657  11.732  0.50 27.53           O  
ANISOU  550  OG BSER A 654     3510   3165   3783   -769   -902   -411       O  
ATOM    551  N   VAL A 655      38.922  -1.876  11.957  1.00 25.84           N  
ANISOU  551  N   VAL A 655     3435   3673   2709   -531   -801   -382       N  
ATOM    552  CA  VAL A 655      37.771  -1.855  12.821  1.00 27.34           C  
ANISOU  552  CA  VAL A 655     3688   3763   2934   -620   -452   -464       C  
ATOM    553  C   VAL A 655      36.477  -2.288  12.116  1.00 25.65           C  
ANISOU  553  C   VAL A 655     3578   3432   2735   -760   -331   -413       C  
ATOM    554  O   VAL A 655      35.733  -3.109  12.653  1.00 25.90           O  
ANISOU  554  O   VAL A 655     3780   3685   2376   -990    -16   -396       O  
ATOM    555  CB  VAL A 655      37.613  -0.532  13.550  1.00 29.10           C  
ANISOU  555  CB  VAL A 655     3692   3844   3518   -744   -311   -629       C  
ATOM    556  CG1 VAL A 655      36.286  -0.488  14.363  1.00 31.28           C  
ANISOU  556  CG1 VAL A 655     4479   4224   3180   -531   -150   -979       C  
ATOM    557  CG2 VAL A 655      38.848  -0.423  14.493  1.00 31.95           C  
ANISOU  557  CG2 VAL A 655     4351   4392   3395   -609   -515   -455       C  
ATOM    558  N   GLY A 656      36.269  -1.800  10.903  1.00 23.63           N  
ANISOU  558  N   GLY A 656     3212   3164   2599   -502   -555   -217       N  
ATOM    559  CA  GLY A 656      35.082  -2.167  10.100  1.00 22.10           C  
ANISOU  559  CA  GLY A 656     3301   2678   2414   -508   -501   -411       C  
ATOM    560  C   GLY A 656      35.087  -3.655   9.794  1.00 20.26           C  
ANISOU  560  C   GLY A 656     2952   2438   2307   -232   -352   -236       C  
ATOM    561  O   GLY A 656      34.013  -4.290   9.859  1.00 18.43           O  
ANISOU  561  O   GLY A 656     2985   2412   1605   -256   -205   -407       O  
ATOM    562  N   VAL A 657      36.266  -4.200   9.490  1.00 19.39           N  
ANISOU  562  N   VAL A 657     3130   2267   1970   -129   -403    -98       N  
ATOM    563  CA  VAL A 657      36.297  -5.637   9.166  1.00 17.68           C  
ANISOU  563  CA  VAL A 657     2792   2261   1661   -366   -584      8       C  
ATOM    564  C   VAL A 657      35.920  -6.493  10.415  1.00 19.02           C  
ANISOU  564  C   VAL A 657     2900   2622   1702   -488   -552    -13       C  
ATOM    565  O   VAL A 657      35.167  -7.458  10.310  1.00 19.12           O  
ANISOU  565  O   VAL A 657     2920   2500   1843   -430   -549     73       O  
ATOM    566  CB  VAL A 657      37.641  -6.115   8.535  1.00 17.12           C  
ANISOU  566  CB  VAL A 657     2684   2072   1749   -143   -356     21       C  
ATOM    567  CG1 VAL A 657      37.589  -7.643   8.274  1.00 19.51           C  
ANISOU  567  CG1 VAL A 657     2837   2221   2352   -268   -639     10       C  
ATOM    568  CG2 VAL A 657      37.882  -5.419   7.185  1.00 19.59           C  
ANISOU  568  CG2 VAL A 657     2796   2690   1958   -486   -415    368       C  
ATOM    569  N   LYS A 658      36.444  -6.090  11.603  1.00 22.06           N  
ANISOU  569  N   LYS A 658     3708   3015   1659   -420   -680    212       N  
ATOM    570  CA  LYS A 658      36.130  -6.817  12.835  1.00 22.62           C  
ANISOU  570  CA  LYS A 658     3713   3346   1534   -564   -532    -44       C  
ATOM    571  C   LYS A 658      34.653  -6.732  13.145  1.00 21.48           C  
ANISOU  571  C   LYS A 658     3669   3116   1375   -465   -540   -112       C  
ATOM    572  O   LYS A 658      34.021  -7.745  13.495  1.00 24.03           O  
ANISOU  572  O   LYS A 658     3709   3345   2075   -366   -617   -121       O  
ATOM    573  CB  LYS A 658      37.110  -6.384  13.950  1.00 24.83           C  
ANISOU  573  CB  LYS A 658     3898   3722   1813   -597   -704    -18       C  
ATOM    574  CG  LYS A 658      36.884  -7.125  15.282  1.00 33.34           C  
ANISOU  574  CG  LYS A 658     4926   4862   2877   -722   -555    -30       C  
ATOM    575  CD  LYS A 658      37.753  -6.520  16.424  1.00 42.09           C  
ANISOU  575  CD  LYS A 658     5421   6413   4158   -490   -709   -734       C  
ATOM    576  CE  LYS A 658      36.851  -5.587  17.232  1.00 44.23           C  
ANISOU  576  CE  LYS A 658     5142   6846   4818   -614   -377   -785       C  
ATOM    577  NZ  LYS A 658      35.700  -6.454  17.739  1.00 51.70           N  
ANISOU  577  NZ  LYS A 658     6109   7470   6064   -897    356   -446       N  
ATOM    578  N   THR A 659      34.050  -5.569  12.919  1.00 21.39           N  
ANISOU  578  N   THR A 659     3562   3095   1470   -416   -202   -339       N  
ATOM    579  CA  THR A 659      32.625  -5.374  13.127  1.00 21.88           C  
ANISOU  579  CA  THR A 659     3454   2946   1914   -463    -40   -261       C  
ATOM    580  C   THR A 659      31.795  -6.285  12.192  1.00 19.98           C  
ANISOU  580  C   THR A 659     3235   2722   1630   -516     70   -278       C  
ATOM    581  O   THR A 659      30.874  -7.051  12.614  1.00 20.41           O  
ANISOU  581  O   THR A 659     3377   2543   1835   -308    150   -341       O  
ATOM    582  CB  THR A 659      32.233  -3.906  12.887  1.00 24.67           C  
ANISOU  582  CB  THR A 659     3760   3061   2551   -415     34   -487       C  
ATOM    583  OG1 THR A 659      32.897  -3.112  13.869  1.00 26.44           O  
ANISOU  583  OG1 THR A 659     4160   3004   2881   -743     94   -770       O  
ATOM    584  CG2 THR A 659      30.765  -3.704  13.065  1.00 24.82           C  
ANISOU  584  CG2 THR A 659     3462   3230   2738   -334    303   -399       C  
ATOM    585  N   LEU A 660      32.140  -6.255  10.921  1.00 18.51           N  
ANISOU  585  N   LEU A 660     3038   2547   1446   -361   -198   -158       N  
ATOM    586  CA  LEU A 660      31.476  -7.140   9.970  1.00 16.07           C  
ANISOU  586  CA  LEU A 660     2843   2173   1087   -191    -82    -81       C  
ATOM    587  C   LEU A 660      31.639  -8.640  10.335  1.00 16.03           C  
ANISOU  587  C   LEU A 660     2647   2204   1241   -428    -40     64       C  
ATOM    588  O   LEU A 660      30.677  -9.397  10.203  1.00 17.14           O  
ANISOU  588  O   LEU A 660     2993   2157   1360   -532    -68    151       O  
ATOM    589  CB  LEU A 660      32.049  -6.834   8.533  1.00 14.52           C  
ANISOU  589  CB  LEU A 660     2248   2343    923   -655    -32    -61       C  
ATOM    590  CG  LEU A 660      31.325  -7.659   7.432  1.00 15.14           C  
ANISOU  590  CG  LEU A 660     2511   2222   1019   -296   -101    -70       C  
ATOM    591  CD1 LEU A 660      29.828  -7.258   7.296  1.00 19.66           C  
ANISOU  591  CD1 LEU A 660     2602   2945   1920    -68    225     92       C  
ATOM    592  CD2 LEU A 660      32.176  -7.411   6.145  1.00 18.42           C  
ANISOU  592  CD2 LEU A 660     2875   2861   1262   -462    -97   -171       C  
ATOM    593  N   ALA A 661      32.861  -9.041  10.752  1.00 17.94           N  
ANISOU  593  N   ALA A 661     3047   2399   1370   -165   -234    259       N  
ATOM    594  CA  ALA A 661      33.092 -10.431  11.068  1.00 18.08           C  
ANISOU  594  CA  ALA A 661     2895   2404   1567   -252   -276    390       C  
ATOM    595  C   ALA A 661      32.172 -10.850  12.220  1.00 18.90           C  
ANISOU  595  C   ALA A 661     2920   2574   1688   -165   -180     57       C  
ATOM    596  O   ALA A 661      31.599 -11.952  12.186  1.00 19.03           O  
ANISOU  596  O   ALA A 661     2910   2424   1895   -506   -279    395       O  
ATOM    597  CB  ALA A 661      34.538 -10.659  11.475  1.00 20.49           C  
ANISOU  597  CB  ALA A 661     3022   2778   1982    -83   -349    483       C  
ATOM    598  N   GLY A 662      31.944  -9.948  13.177  1.00 19.87           N  
ANISOU  598  N   GLY A 662     3449   2552   1547   -164     39    103       N  
ATOM    599  CA  GLY A 662      31.026 -10.275  14.284  1.00 20.98           C  
ANISOU  599  CA  GLY A 662     3261   2839   1871   -286    130     45       C  
ATOM    600  C   GLY A 662      29.578 -10.336  13.831  1.00 20.52           C  
ANISOU  600  C   GLY A 662     3604   2457   1734   -331     26    -32       C  
ATOM    601  O   GLY A 662      28.855 -11.224  14.307  1.00 21.33           O  
ANISOU  601  O   GLY A 662     3765   2786   1551   -250     71    198       O  
ATOM    602  N   ILE A 663      29.152  -9.495  12.862  1.00 18.90           N  
ANISOU  602  N   ILE A 663     3198   2358   1625   -112   -111   -127       N  
ATOM    603  CA  ILE A 663      27.797  -9.592  12.387  1.00 18.77           C  
ANISOU  603  CA  ILE A 663     3313   2033   1786   -145    174    -18       C  
ATOM    604  C   ILE A 663      27.642 -10.965  11.716  1.00 17.28           C  
ANISOU  604  C   ILE A 663     3040   1938   1587   -244     84    -67       C  
ATOM    605  O   ILE A 663      26.653 -11.681  11.918  1.00 18.68           O  
ANISOU  605  O   ILE A 663     3064   2256   1775   -312    395   -103       O  
ATOM    606  CB  ILE A 663      27.486  -8.426  11.394  1.00 19.02           C  
ANISOU  606  CB  ILE A 663     3374   1678   2175   -118    -41    -53       C  
ATOM    607  CG1 ILE A 663      27.520  -7.137  12.190  1.00 20.44           C  
ANISOU  607  CG1 ILE A 663     3492   1772   2502   -299    295   -290       C  
ATOM    608  CG2 ILE A 663      26.206  -8.694  10.656  1.00 20.72           C  
ANISOU  608  CG2 ILE A 663     3334   2201   2335   -210   -245     81       C  
ATOM    609  CD1 ILE A 663      27.570  -5.906  11.292  1.00 21.68           C  
ANISOU  609  CD1 ILE A 663     3625   1955   2658   -539    168    335       C  
ATOM    610  N   VAL A 664      28.591 -11.309  10.850  1.00 16.64           N  
ANISOU  610  N   VAL A 664     3069   1961   1289   -187     96     77       N  
ATOM    611  CA  VAL A 664      28.455 -12.586  10.093  1.00 15.26           C  
ANISOU  611  CA  VAL A 664     2889   1586   1321   -181     19    376       C  
ATOM    612  C   VAL A 664      28.448 -13.770  11.046  1.00 15.30           C  
ANISOU  612  C   VAL A 664     2765   1497   1550   -304   -135    180       C  
ATOM    613  O   VAL A 664      27.638 -14.671  10.893  1.00 16.71           O  
ANISOU  613  O   VAL A 664     3121   1915   1311   -574   -115    264       O  
ATOM    614  CB  VAL A 664      29.604 -12.674   9.111  1.00 15.53           C  
ANISOU  614  CB  VAL A 664     2874   1601   1422   -326    205    116       C  
ATOM    615  CG1 VAL A 664      29.715 -14.088   8.521  1.00 16.63           C  
ANISOU  615  CG1 VAL A 664     2805   1890   1624   -162    215   -182       C  
ATOM    616  CG2 VAL A 664      29.391 -11.612   7.987  1.00 15.95           C  
ANISOU  616  CG2 VAL A 664     2651   2283   1124   -261    -98    438       C  
ATOM    617  N   LYS A 665      29.342 -13.744  12.029  1.00 16.83           N  
ANISOU  617  N   LYS A 665     3104   1762   1525    -14   -261    306       N  
ATOM    618  CA  LYS A 665      29.403 -14.809  13.025  1.00 18.59           C  
ANISOU  618  CA  LYS A 665     3163   2262   1635   -160   -210    273       C  
ATOM    619  C   LYS A 665      28.102 -14.934  13.808  1.00 18.28           C  
ANISOU  619  C   LYS A 665     3151   2187   1606   -332   -220    246       C  
ATOM    620  O   LYS A 665      27.514 -16.041  13.942  1.00 21.19           O  
ANISOU  620  O   LYS A 665     3666   2464   1919   -326   -327    426       O  
ATOM    621  CB  LYS A 665      30.640 -14.623  13.955  1.00 18.60           C  
ANISOU  621  CB  LYS A 665     3152   2259   1656   -222   -577    604       C  
ATOM    622  CG  LYS A 665      30.737 -15.821  14.919  1.00 22.15           C  
ANISOU  622  CG  LYS A 665     3739   2426   2249   -146   -426    374       C  
ATOM    623  CD  LYS A 665      31.926 -15.671  15.867  1.00 27.43           C  
ANISOU  623  CD  LYS A 665     3965   3624   2833   -178   -632    808       C  
ATOM    624  CE  LYS A 665      31.911 -16.811  16.928  1.00 29.37           C  
ANISOU  624  CE  LYS A 665     4500   3711   2949    152   -152    929       C  
ATOM    625  NZ  LYS A 665      30.632 -16.840  17.797  1.00 26.24           N  
ANISOU  625  NZ  LYS A 665     3880   3489   2599     49   -300    815       N  
ATOM    626  N   GLU A 666      27.620 -13.803  14.332  1.00 20.05           N  
ANISOU  626  N   GLU A 666     3448   2363   1805   -212    216    177       N  
ATOM    627  CA  GLU A 666      26.459 -13.897  15.222  1.00 21.57           C  
ANISOU  627  CA  GLU A 666     3557   2713   1923   -234    240     61       C  
ATOM    628  C   GLU A 666      25.192 -14.305  14.508  1.00 19.83           C  
ANISOU  628  C   GLU A 666     3219   2654   1661   -357    303    134       C  
ATOM    629  O   GLU A 666      24.381 -15.097  15.089  1.00 21.25           O  
ANISOU  629  O   GLU A 666     3777   2691   1605   -649    160    344       O  
ATOM    630  CB  GLU A 666      26.279 -12.631  16.024  1.00 23.28           C  
ANISOU  630  CB  GLU A 666     3725   2831   2289   -130    278    -66       C  
ATOM    631  CG  GLU A 666      27.543 -12.461  16.869  1.00 28.69           C  
ANISOU  631  CG  GLU A 666     4681   3438   2781   -413   -122    -42       C  
ATOM    632  CD  GLU A 666      27.565 -11.141  17.593  1.00 37.04           C  
ANISOU  632  CD  GLU A 666     5794   4364   3915   -231   -215   -311       C  
ATOM    633  OE1 GLU A 666      28.693 -10.772  18.050  1.00 44.45           O  
ANISOU  633  OE1 GLU A 666     6497   5668   4724   -605   -782   -281       O  
ATOM    634  OE2 GLU A 666      26.493 -10.487  17.689  1.00 38.66           O  
ANISOU  634  OE2 GLU A 666     5719   4778   4188    286   -476  -1340       O  
ATOM    635  N   TYR A 667      24.970 -13.830  13.256  1.00 17.84           N  
ANISOU  635  N   TYR A 667     2879   2422   1475    -22    154    187       N  
ATOM    636  CA  TYR A 667      23.837 -14.375  12.511  1.00 18.12           C  
ANISOU  636  CA  TYR A 667     3330   1993   1560    -83    290    101       C  
ATOM    637  C   TYR A 667      24.082 -15.835  12.199  1.00 17.78           C  
ANISOU  637  C   TYR A 667     3137   2047   1571    -39    345    263       C  
ATOM    638  O   TYR A 667      23.119 -16.644  12.220  1.00 18.88           O  
ANISOU  638  O   TYR A 667     3195   2365   1611   -324    452    142       O  
ATOM    639  CB  TYR A 667      23.649 -13.543  11.172  1.00 17.76           C  
ANISOU  639  CB  TYR A 667     3127   1970   1649    248    387     -9       C  
ATOM    640  CG  TYR A 667      22.831 -12.320  11.407  1.00 20.75           C  
ANISOU  640  CG  TYR A 667     3456   1967   2458     52    518    253       C  
ATOM    641  CD1 TYR A 667      23.370 -11.022  11.196  1.00 23.23           C  
ANISOU  641  CD1 TYR A 667     4111   1805   2911    265    239    196       C  
ATOM    642  CD2 TYR A 667      21.493 -12.440  11.686  1.00 24.18           C  
ANISOU  642  CD2 TYR A 667     3198   3010   2978    141    303    207       C  
ATOM    643  CE1 TYR A 667      22.593  -9.887  11.388  1.00 27.18           C  
ANISOU  643  CE1 TYR A 667     3213   3144   3967    592    333    -18       C  
ATOM    644  CE2 TYR A 667      20.690 -11.270  11.875  1.00 28.71           C  
ANISOU  644  CE2 TYR A 667     3624   3050   4233    102    474    203       C  
ATOM    645  CZ  TYR A 667      21.259 -10.007  11.713  1.00 27.50           C  
ANISOU  645  CZ  TYR A 667     3435   2871   4140    126    375    -20       C  
ATOM    646  OH  TYR A 667      20.516  -8.829  11.888  1.00 35.27           O  
ANISOU  646  OH  TYR A 667     4305   3626   5467    467    800   -303       O  
ATOM    647  N   GLY A 668      25.313 -16.174  11.832  1.00 17.52           N  
ANISOU  647  N   GLY A 668     3161   2051   1441   -102     73    390       N  
ATOM    648  CA  GLY A 668      25.596 -17.568  11.411  1.00 17.64           C  
ANISOU  648  CA  GLY A 668     3284   2009   1408     59    275    503       C  
ATOM    649  C   GLY A 668      25.339 -18.531  12.579  1.00 18.72           C  
ANISOU  649  C   GLY A 668     3654   2026   1430    -85    125    418       C  
ATOM    650  O   GLY A 668      24.875 -19.681  12.360  1.00 19.83           O  
ANISOU  650  O   GLY A 668     3875   1930   1730   -173     -5    431       O  
ATOM    651  N   ASP A 669      25.559 -18.053  13.837  1.00 18.25           N  
ANISOU  651  N   ASP A 669     3394   2053   1484   -139      2    443       N  
ATOM    652  CA  ASP A 669      25.385 -18.933  14.948  1.00 18.88           C  
ANISOU  652  CA  ASP A 669     3397   2216   1559   -276   -120    564       C  
ATOM    653  C   ASP A 669      23.930 -19.278  15.194  1.00 17.72           C  
ANISOU  653  C   ASP A 669     3162   2173   1397    -94    297    628       C  
ATOM    654  O   ASP A 669      23.632 -20.270  15.920  1.00 20.38           O  
ANISOU  654  O   ASP A 669     3370   2178   2195   -265    340    646       O  
ATOM    655  CB  ASP A 669      25.977 -18.223  16.187  1.00 20.11           C  
ANISOU  655  CB  ASP A 669     3770   2496   1374   -432     51    466       C  
ATOM    656  CG  ASP A 669      27.516 -18.234  16.204  1.00 19.82           C  
ANISOU  656  CG  ASP A 669     3792   2203   1535   -128   -134    348       C  
ATOM    657  OD1 ASP A 669      28.181 -19.045  15.496  1.00 24.51           O  
ANISOU  657  OD1 ASP A 669     4111   3040   2159   -354   -526    140       O  
ATOM    658  OD2 ASP A 669      28.111 -17.406  16.979  1.00 26.65           O  
ANISOU  658  OD2 ASP A 669     5340   2778   2008   -583   -577    319       O  
ATOM    659  N   VAL A 670      22.984 -18.472  14.638  1.00 20.43           N  
ANISOU  659  N   VAL A 670     3361   2410   1992    -93    324    461       N  
ATOM    660  CA  VAL A 670      21.550 -18.857  14.561  1.00 20.03           C  
ANISOU  660  CA  VAL A 670     3297   2485   1828     80    407    329       C  
ATOM    661  C   VAL A 670      21.067 -19.318  13.208  1.00 20.11           C  
ANISOU  661  C   VAL A 670     3193   2351   2097    143    208    433       C  
ATOM    662  O   VAL A 670      19.868 -19.364  12.953  1.00 21.90           O  
ANISOU  662  O   VAL A 670     3330   2912   2076   -106    399    220       O  
ATOM    663  CB  VAL A 670      20.564 -17.807  15.190  1.00 20.55           C  
ANISOU  663  CB  VAL A 670     3595   2312   1900    192    197    533       C  
ATOM    664  CG1 VAL A 670      20.837 -17.613  16.684  1.00 23.12           C  
ANISOU  664  CG1 VAL A 670     3563   3097   2122   -107    393    485       C  
ATOM    665  CG2 VAL A 670      20.659 -16.490  14.389  1.00 20.39           C  
ANISOU  665  CG2 VAL A 670     3515   2157   2074    314    597    701       C  
ATOM    666  N   GLY A 671      22.009 -19.752  12.357  1.00 18.92           N  
ANISOU  666  N   GLY A 671     3103   2281   1805    -25    337    236       N  
ATOM    667  CA  GLY A 671      21.652 -20.370  11.061  1.00 19.48           C  
ANISOU  667  CA  GLY A 671     3286   2258   1857    -92    -84    418       C  
ATOM    668  C   GLY A 671      21.299 -19.349   9.935  1.00 18.33           C  
ANISOU  668  C   GLY A 671     3224   2125   1614   -245    161    594       C  
ATOM    669  O   GLY A 671      20.848 -19.748   8.835  1.00 20.53           O  
ANISOU  669  O   GLY A 671     3280   2410   2108   -148   -294    462       O  
ATOM    670  N   ILE A 672      21.512 -18.059  10.190  1.00 17.18           N  
ANISOU  670  N   ILE A 672     2900   1980   1647   -301    298    561       N  
ATOM    671  CA  ILE A 672      21.177 -17.043   9.167  1.00 17.07           C  
ANISOU  671  CA  ILE A 672     2713   1901   1872    -65    307    564       C  
ATOM    672  C   ILE A 672      22.467 -16.651   8.419  1.00 15.54           C  
ANISOU  672  C   ILE A 672     2447   1705   1750   -208     84    499       C  
ATOM    673  O   ILE A 672      23.502 -16.349   9.060  1.00 16.18           O  
ANISOU  673  O   ILE A 672     2367   1996   1783   -176     77    506       O  
ATOM    674  CB  ILE A 672      20.561 -15.784   9.829  1.00 18.82           C  
ANISOU  674  CB  ILE A 672     3101   2054   1994    -93    328    390       C  
ATOM    675  CG1 ILE A 672      19.211 -16.189  10.470  1.00 22.54           C  
ANISOU  675  CG1 ILE A 672     3224   2668   2671    -18    376    265       C  
ATOM    676  CG2 ILE A 672      20.477 -14.650   8.800  1.00 19.15           C  
ANISOU  676  CG2 ILE A 672     3405   2151   1719    -39     54    618       C  
ATOM    677  CD1 ILE A 672      18.516 -15.115  11.346  1.00 24.71           C  
ANISOU  677  CD1 ILE A 672     4144   2342   2900     96    407    132       C  
ATOM    678  N   TYR A 673      22.467 -16.775   7.102  1.00 14.90           N  
ANISOU  678  N   TYR A 673     2272   1811   1577    -67    141    276       N  
ATOM    679  CA  TYR A 673      23.653 -16.405   6.333  1.00 14.45           C  
ANISOU  679  CA  TYR A 673     2522   1651   1316   -391    117    220       C  
ATOM    680  C   TYR A 673      23.611 -14.928   6.031  1.00 14.89           C  
ANISOU  680  C   TYR A 673     2272   1717   1666   -200     27    110       C  
ATOM    681  O   TYR A 673      22.561 -14.366   5.676  1.00 16.21           O  
ANISOU  681  O   TYR A 673     2187   1974   1998    -66     50    268       O  
ATOM    682  CB  TYR A 673      23.611 -17.093   4.966  1.00 15.36           C  
ANISOU  682  CB  TYR A 673     2613   1615   1605   -258     13     49       C  
ATOM    683  CG  TYR A 673      24.012 -18.529   4.922  1.00 15.25           C  
ANISOU  683  CG  TYR A 673     2328   1733   1732   -374    -57     84       C  
ATOM    684  CD1 TYR A 673      25.188 -18.880   4.284  1.00 16.54           C  
ANISOU  684  CD1 TYR A 673     1889   1978   2416    -36     85    -55       C  
ATOM    685  CD2 TYR A 673      23.189 -19.570   5.474  1.00 15.63           C  
ANISOU  685  CD2 TYR A 673     2337   1800   1801   -333    -85    217       C  
ATOM    686  CE1 TYR A 673      25.598 -20.157   4.179  1.00 19.08           C  
ANISOU  686  CE1 TYR A 673     3037   1960   2252   -234     33    378       C  
ATOM    687  CE2 TYR A 673      23.635 -20.916   5.314  1.00 18.61           C  
ANISOU  687  CE2 TYR A 673     2651   2205   2214    142   -123     -9       C  
ATOM    688  CZ  TYR A 673      24.815 -21.165   4.639  1.00 18.91           C  
ANISOU  688  CZ  TYR A 673     2830   1722   2632   -276    131    378       C  
ATOM    689  OH  TYR A 673      25.174 -22.487   4.461  1.00 20.94           O  
ANISOU  689  OH  TYR A 673     3169   2125   2660    -60   -190    206       O  
ATOM    690  N   VAL A 674      24.750 -14.288   6.184  1.00 14.31           N  
ANISOU  690  N   VAL A 674     2405   1604   1425   -386    203    131       N  
ATOM    691  CA  VAL A 674      24.937 -12.864   5.753  1.00 12.71           C  
ANISOU  691  CA  VAL A 674     2350   1350   1127   -208    219     73       C  
ATOM    692  C   VAL A 674      25.759 -12.926   4.472  1.00 13.03           C  
ANISOU  692  C   VAL A 674     2021   1624   1305   -105    153    185       C  
ATOM    693  O   VAL A 674      26.938 -13.367   4.509  1.00 15.29           O  
ANISOU  693  O   VAL A 674     1984   2333   1492     43     22    195       O  
ATOM    694  CB  VAL A 674      25.672 -12.044   6.861  1.00 12.49           C  
ANISOU  694  CB  VAL A 674     2029   1577   1138   -352    247    119       C  
ATOM    695  CG1 VAL A 674      26.007 -10.605   6.385  1.00 15.23           C  
ANISOU  695  CG1 VAL A 674     2950   1400   1435   -300    132    610       C  
ATOM    696  CG2 VAL A 674      24.796 -12.070   8.180  1.00 14.57           C  
ANISOU  696  CG2 VAL A 674     2169   2040   1325   -212    514    189       C  
ATOM    697  N   TYR A 675      25.198 -12.419   3.378  1.00 12.01           N  
ANISOU  697  N   TYR A 675     1901   1484   1176   -270    216    246       N  
ATOM    698  CA  TYR A 675      25.987 -12.399   2.132  1.00 12.28           C  
ANISOU  698  CA  TYR A 675     1916   1638   1111   -351    135    254       C  
ATOM    699  C   TYR A 675      26.485 -10.976   1.857  1.00 13.96           C  
ANISOU  699  C   TYR A 675     2189   1555   1559   -120    164    163       C  
ATOM    700  O   TYR A 675      25.844 -10.009   2.269  1.00 13.24           O  
ANISOU  700  O   TYR A 675     2012   1465   1553   -372    226    285       O  
ATOM    701  CB  TYR A 675      25.070 -12.802   0.986  1.00 12.83           C  
ANISOU  701  CB  TYR A 675     2218   1406   1248   -594    -32   -131       C  
ATOM    702  CG  TYR A 675      24.682 -14.241   0.943  1.00 11.26           C  
ANISOU  702  CG  TYR A 675     1903   1071   1305   -237    209    158       C  
ATOM    703  CD1 TYR A 675      25.430 -15.221   1.577  1.00 13.87           C  
ANISOU  703  CD1 TYR A 675     2507   1145   1617   -109     92    213       C  
ATOM    704  CD2 TYR A 675      23.596 -14.619   0.174  1.00 15.20           C  
ANISOU  704  CD2 TYR A 675     1866   1881   2027   -765    108    289       C  
ATOM    705  CE1 TYR A 675      25.116 -16.619   1.399  1.00 15.29           C  
ANISOU  705  CE1 TYR A 675     2576   1453   1781   -382    173   -174       C  
ATOM    706  CE2 TYR A 675      23.271 -15.966   0.028  1.00 15.03           C  
ANISOU  706  CE2 TYR A 675     2097   1663   1949   -426    191    335       C  
ATOM    707  CZ  TYR A 675      24.018 -16.921   0.645  1.00 16.64           C  
ANISOU  707  CZ  TYR A 675     2754   1350   2215   -468    -45    157       C  
ATOM    708  OH  TYR A 675      23.661 -18.225   0.455  1.00 21.29           O  
ANISOU  708  OH  TYR A 675     3407   1946   2736   -649   -554     65       O  
ATOM    709  N   LEU A 676      27.600 -10.846   1.164  1.00 12.15           N  
ANISOU  709  N   LEU A 676     2117   1408   1088   -222    231    222       N  
ATOM    710  CA  LEU A 676      28.144  -9.541   0.799  1.00 13.57           C  
ANISOU  710  CA  LEU A 676     2289   1575   1289    -49    223    270       C  
ATOM    711  C   LEU A 676      28.059  -9.371  -0.691  1.00 13.51           C  
ANISOU  711  C   LEU A 676     2327   1531   1272    225    158    -20       C  
ATOM    712  O   LEU A 676      28.712 -10.210  -1.425  1.00 14.85           O  
ANISOU  712  O   LEU A 676     2804   1494   1341    193    294    -38       O  
ATOM    713  CB  LEU A 676      29.617  -9.475   1.213  1.00 15.41           C  
ANISOU  713  CB  LEU A 676     2164   2263   1428     11    275    251       C  
ATOM    714  CG  LEU A 676      29.909  -9.999   2.651  1.00 16.87           C  
ANISOU  714  CG  LEU A 676     1995   2365   2047    180    202    173       C  
ATOM    715  CD1 LEU A 676      31.400  -9.779   2.939  1.00 21.17           C  
ANISOU  715  CD1 LEU A 676     2673   3251   2120    240   -125    -40       C  
ATOM    716  CD2 LEU A 676      29.062  -9.256   3.696  1.00 16.59           C  
ANISOU  716  CD2 LEU A 676     2362   2112   1826   -113    -75   -571       C  
ATOM    717  N   ALA A 677      27.286  -8.422  -1.162  1.00 12.35           N  
ANISOU  717  N   ALA A 677     1903   1521   1268   -118    -29    240       N  
ATOM    718  CA  ALA A 677      27.035  -8.261  -2.619  1.00 12.71           C  
ANISOU  718  CA  ALA A 677     2018   1523   1285   -139     64    286       C  
ATOM    719  C   ALA A 677      27.750  -6.995  -3.130  1.00 12.58           C  
ANISOU  719  C   ALA A 677     1892   1464   1424   -299     90    136       C  
ATOM    720  O   ALA A 677      27.730  -5.970  -2.430  1.00 14.01           O  
ANISOU  720  O   ALA A 677     2361   1442   1517   -357    225    -68       O  
ATOM    721  CB  ALA A 677      25.526  -8.137  -2.905  1.00 14.74           C  
ANISOU  721  CB  ALA A 677     1922   2118   1557   -164   -136    278       C  
ATOM    722  N   GLY A 678      28.463  -7.082  -4.232  1.00 12.98           N  
ANISOU  722  N   GLY A 678     1984   1522   1426   -489    215    283       N  
ATOM    723  CA  GLY A 678      29.030  -5.889  -4.824  1.00 14.50           C  
ANISOU  723  CA  GLY A 678     2187   1582   1738   -617    116    387       C  
ATOM    724  C   GLY A 678      30.273  -5.316  -4.166  1.00 13.83           C  
ANISOU  724  C   GLY A 678     2183   1669   1403   -447    201    276       C  
ATOM    725  O   GLY A 678      30.585  -4.132  -4.293  1.00 15.68           O  
ANISOU  725  O   GLY A 678     2362   1693   1900   -515     41    165       O  
ATOM    726  N   CYS A 679      31.057  -6.197  -3.530  1.00 14.44           N  
ANISOU  726  N   CYS A 679     1864   1708   1914   -375    -27    111       N  
ATOM    727  CA  CYS A 679      32.355  -5.714  -3.009  1.00 15.18           C  
ANISOU  727  CA  CYS A 679     1831   1902   2034   -458    116     12       C  
ATOM    728  C   CYS A 679      33.340  -5.517  -4.140  1.00 15.06           C  
ANISOU  728  C   CYS A 679     2058   1778   1885   -757    132    -67       C  
ATOM    729  O   CYS A 679      33.503  -6.463  -5.010  1.00 17.30           O  
ANISOU  729  O   CYS A 679     2414   2063   2096   -422    480     47       O  
ATOM    730  CB  CYS A 679      33.004  -6.755  -2.074  1.00 15.54           C  
ANISOU  730  CB  CYS A 679     1848   1841   2215   -394    264    240       C  
ATOM    731  SG  CYS A 679      32.000  -7.138  -0.599  1.00 18.68           S  
ANISOU  731  SG  CYS A 679     2309   2379   2407   -388    302    452       S  
ATOM    732  N   SER A 680      34.058  -4.397  -4.101  1.00 15.53           N  
ANISOU  732  N   SER A 680     2048   1966   1884   -710    168    319       N  
ATOM    733  CA  SER A 680      35.071  -4.191  -5.131  1.00 16.76           C  
ANISOU  733  CA  SER A 680     2251   2153   1962   -466    318     -3       C  
ATOM    734  C   SER A 680      36.288  -5.047  -4.845  1.00 16.84           C  
ANISOU  734  C   SER A 680     2069   2440   1889   -509    125    136       C  
ATOM    735  O   SER A 680      36.452  -5.635  -3.753  1.00 17.83           O  
ANISOU  735  O   SER A 680     2127   2707   1941   -600    289    280       O  
ATOM    736  CB  SER A 680      35.525  -2.758  -5.086  1.00 17.07           C  
ANISOU  736  CB  SER A 680     2230   2301   1954  -1023    -14    387       C  
ATOM    737  OG  SER A 680      36.220  -2.467  -3.899  1.00 18.48           O  
ANISOU  737  OG  SER A 680     2497   2614   1911   -355     41    141       O  
ATOM    738  N   ALA A 681      37.206  -5.122  -5.805  1.00 19.85           N  
ANISOU  738  N   ALA A 681     2213   2908   2420   -458    508     80       N  
ATOM    739  CA  ALA A 681      38.418  -5.909  -5.539  1.00 19.33           C  
ANISOU  739  CA  ALA A 681     2268   2829   2245   -252    387    -61       C  
ATOM    740  C   ALA A 681      39.195  -5.300  -4.364  1.00 19.19           C  
ANISOU  740  C   ALA A 681     2163   2792   2334   -405    382     84       C  
ATOM    741  O   ALA A 681      39.764  -6.054  -3.534  1.00 20.12           O  
ANISOU  741  O   ALA A 681     2148   2812   2682   -239    380     63       O  
ATOM    742  CB  ALA A 681      39.330  -5.896  -6.776  1.00 23.59           C  
ANISOU  742  CB  ALA A 681     2722   3496   2741   -421    647   -142       C  
ATOM    743  N   GLN A 682      39.202  -3.977  -4.253  1.00 18.91           N  
ANISOU  743  N   GLN A 682     2359   2667   2156   -613    290    177       N  
ATOM    744  CA  GLN A 682      39.869  -3.322  -3.096  1.00 20.27           C  
ANISOU  744  CA  GLN A 682     2704   2552   2442   -674    177    109       C  
ATOM    745  C   GLN A 682      39.235  -3.755  -1.770  1.00 18.66           C  
ANISOU  745  C   GLN A 682     2465   2307   2318   -607     85    -17       C  
ATOM    746  O   GLN A 682      39.954  -4.064  -0.787  1.00 17.83           O  
ANISOU  746  O   GLN A 682     2346   1953   2473   -606     96     31       O  
ATOM    747  CB  GLN A 682      39.819  -1.797  -3.161  1.00 20.28           C  
ANISOU  747  CB  GLN A 682     2859   2534   2310   -686     74    127       C  
ATOM    748  CG  GLN A 682      40.559  -1.106  -1.944  1.00 23.41           C  
ANISOU  748  CG  GLN A 682     2977   3064   2851  -1043     68    149       C  
ATOM    749  CD  GLN A 682      42.070  -1.393  -2.016  1.00 33.08           C  
ANISOU  749  CD  GLN A 682     3817   4948   3801  -1159   -134    337       C  
ATOM    750  OE1 GLN A 682      42.687  -1.075  -3.043  1.00 40.55           O  
ANISOU  750  OE1 GLN A 682     4934   6155   4316  -1792    124     -6       O  
ATOM    751  NE2 GLN A 682      42.665  -2.014  -0.970  1.00 31.17           N  
ANISOU  751  NE2 GLN A 682     3850   4012   3979  -1530   -505     59       N  
ATOM    752  N   VAL A 683      37.903  -3.743  -1.736  1.00 16.75           N  
ANISOU  752  N   VAL A 683     2139   2064   2158   -484    179     -7       N  
ATOM    753  CA  VAL A 683      37.234  -4.167  -0.488  1.00 15.19           C  
ANISOU  753  CA  VAL A 683     1993   1956   1821   -455     47    -58       C  
ATOM    754  C   VAL A 683      37.572  -5.583  -0.150  1.00 15.75           C  
ANISOU  754  C   VAL A 683     2070   1990   1922   -322    111   -255       C  
ATOM    755  O   VAL A 683      37.810  -5.894   1.027  1.00 16.34           O  
ANISOU  755  O   VAL A 683     2262   1849   2094   -255     60   -166       O  
ATOM    756  CB  VAL A 683      35.726  -3.900  -0.548  1.00 14.61           C  
ANISOU  756  CB  VAL A 683     1878   1674   1999   -431     74   -117       C  
ATOM    757  CG1 VAL A 683      34.909  -4.649   0.516  1.00 15.17           C  
ANISOU  757  CG1 VAL A 683     2264   1924   1574   -494    412    249       C  
ATOM    758  CG2 VAL A 683      35.458  -2.406  -0.517  1.00 15.83           C  
ANISOU  758  CG2 VAL A 683     2034   1526   2454   -212   -299   -322       C  
ATOM    759  N   VAL A 684      37.560  -6.503  -1.139  1.00 15.11           N  
ANISOU  759  N   VAL A 684     2272   1700   1766   -431     -5   -106       N  
ATOM    760  CA  VAL A 684      37.906  -7.860  -0.813  1.00 16.67           C  
ANISOU  760  CA  VAL A 684     2444   1845   2043   -275     19   -195       C  
ATOM    761  C   VAL A 684      39.362  -7.960  -0.359  1.00 17.83           C  
ANISOU  761  C   VAL A 684     2605   2022   2144   -204      0    121       C  
ATOM    762  O   VAL A 684      39.669  -8.734   0.578  1.00 18.76           O  
ANISOU  762  O   VAL A 684     2577   2354   2196   -123     24    281       O  
ATOM    763  CB  VAL A 684      37.605  -8.743  -2.059  1.00 17.21           C  
ANISOU  763  CB  VAL A 684     2597   1967   1972   -128   -151   -169       C  
ATOM    764  CG1 VAL A 684      38.154 -10.173  -1.790  1.00 19.77           C  
ANISOU  764  CG1 VAL A 684     3671   1712   2126    -93    137   -341       C  
ATOM    765  CG2 VAL A 684      36.106  -8.810  -2.237  1.00 18.04           C  
ANISOU  765  CG2 VAL A 684     2545   2174   2135   -454     97   -434       C  
ATOM    766  N   ASN A 685      40.249  -7.158  -0.971  1.00 19.14           N  
ANISOU  766  N   ASN A 685     2246   2540   2485   -185    160     28       N  
ATOM    767  CA  ASN A 685      41.645  -7.128  -0.484  1.00 21.69           C  
ANISOU  767  CA  ASN A 685     2570   2593   3077   -223    178    160       C  
ATOM    768  C   ASN A 685      41.687  -6.711   0.990  1.00 20.96           C  
ANISOU  768  C   ASN A 685     2502   2624   2838   -189     87    337       C  
ATOM    769  O   ASN A 685      42.463  -7.270   1.793  1.00 23.57           O  
ANISOU  769  O   ASN A 685     2658   2779   3519   -221    260    270       O  
ATOM    770  CB  ASN A 685      42.517  -6.216  -1.353  1.00 23.08           C  
ANISOU  770  CB  ASN A 685     2640   3178   2951   -228    391    257       C  
ATOM    771  CG  ASN A 685      42.830  -6.839  -2.696  1.00 31.92           C  
ANISOU  771  CG  ASN A 685     4031   4068   4027   -194    279    157       C  
ATOM    772  OD1 ASN A 685      42.631  -8.065  -2.925  1.00 37.41           O  
ANISOU  772  OD1 ASN A 685     4824   4697   4694   -158    571    439       O  
ATOM    773  ND2 ASN A 685      43.312  -6.008  -3.616  1.00 37.50           N  
ANISOU  773  ND2 ASN A 685     4817   4768   4663    153    785    768       N  
ATOM    774  N   ASP A 686      40.880  -5.697   1.359  1.00 19.00           N  
ANISOU  774  N   ASP A 686     2238   2320   2658   -349    121    143       N  
ATOM    775  CA  ASP A 686      40.811  -5.205   2.743  1.00 19.46           C  
ANISOU  775  CA  ASP A 686     2345   2323   2725   -115   -213     88       C  
ATOM    776  C   ASP A 686      40.265  -6.248   3.670  1.00 19.06           C  
ANISOU  776  C   ASP A 686     2524   2258   2460   -224   -280    176       C  
ATOM    777  O   ASP A 686      40.777  -6.413   4.818  1.00 20.74           O  
ANISOU  777  O   ASP A 686     2745   2554   2579   -293   -331    315       O  
ATOM    778  CB  ASP A 686      39.996  -3.906   2.865  1.00 19.82           C  
ANISOU  778  CB  ASP A 686     2742   1840   2947   -327   -305    157       C  
ATOM    779  CG  ASP A 686      40.662  -2.781   2.097  1.00 20.33           C  
ANISOU  779  CG  ASP A 686     2495   1999   3229     24    -95    102       C  
ATOM    780  OD1 ASP A 686      41.920  -2.840   1.837  1.00 25.18           O  
ANISOU  780  OD1 ASP A 686     2664   3034   3868   -423     14   -110       O  
ATOM    781  OD2 ASP A 686      39.941  -1.861   1.764  1.00 20.37           O  
ANISOU  781  OD2 ASP A 686     3207   1732   2800    -50   -320    436       O  
ATOM    782  N   LEU A 687      39.204  -6.946   3.249  1.00 17.01           N  
ANISOU  782  N   LEU A 687     2207   2003   2252   -385   -141     44       N  
ATOM    783  CA  LEU A 687      38.681  -8.024   4.063  1.00 17.32           C  
ANISOU  783  CA  LEU A 687     2264   2083   2232   -149   -111    222       C  
ATOM    784  C   LEU A 687      39.766  -9.074   4.259  1.00 18.14           C  
ANISOU  784  C   LEU A 687     2407   2207   2278    -11   -146    290       C  
ATOM    785  O   LEU A 687      40.002  -9.574   5.373  1.00 20.87           O  
ANISOU  785  O   LEU A 687     2843   2617   2467     64   -205    581       O  
ATOM    786  CB  LEU A 687      37.514  -8.735   3.311  1.00 14.95           C  
ANISOU  786  CB  LEU A 687     2089   1348   2240   -397   -277    -45       C  
ATOM    787  CG  LEU A 687      36.231  -7.874   3.332  1.00 15.45           C  
ANISOU  787  CG  LEU A 687     2011   1953   1907   -300     -6    239       C  
ATOM    788  CD1 LEU A 687      35.138  -8.475   2.396  1.00 17.25           C  
ANISOU  788  CD1 LEU A 687     1826   2458   2270   -410   -299   -345       C  
ATOM    789  CD2 LEU A 687      35.631  -7.575   4.664  1.00 18.44           C  
ANISOU  789  CD2 LEU A 687     2719   2232   2054   -388    363   -252       C  
ATOM    790  N   THR A 688      40.453  -9.416   3.168  1.00 19.78           N  
ANISOU  790  N   THR A 688     2554   2335   2625     87    -76    192       N  
ATOM    791  CA  THR A 688      41.486 -10.471   3.217  1.00 22.67           C  
ANISOU  791  CA  THR A 688     2658   2915   3038    169    -13    204       C  
ATOM    792  C   THR A 688      42.653 -10.071   4.163  1.00 24.33           C  
ANISOU  792  C   THR A 688     2835   3149   3258     67    -78    358       C  
ATOM    793  O   THR A 688      43.124 -10.867   5.047  1.00 25.75           O  
ANISOU  793  O   THR A 688     2876   3288   3618    416    284    446       O  
ATOM    794  CB  THR A 688      41.989 -10.735   1.803  1.00 23.37           C  
ANISOU  794  CB  THR A 688     2742   2938   3197    214    -44     31       C  
ATOM    795  OG1 THR A 688      40.901 -11.209   1.048  1.00 23.12           O  
ANISOU  795  OG1 THR A 688     2985   3158   2641    266     31      1       O  
ATOM    796  CG2 THR A 688      43.126 -11.842   1.810  1.00 26.87           C  
ANISOU  796  CG2 THR A 688     3600   3182   3427    402    119    301       C  
ATOM    797  N   SER A 689      43.153  -8.852   3.993  1.00 24.48           N  
ANISOU  797  N   SER A 689     2843   3126   3332   -135   -198     76       N  
ATOM    798  CA ASER A 689      44.268  -8.370   4.835  0.50 25.97           C  
ANISOU  798  CA ASER A 689     2880   3432   3555   -132   -292    248       C  
ATOM    799  CA BSER A 689      44.299  -8.445   4.818  0.50 25.55           C  
ANISOU  799  CA BSER A 689     2816   3356   3536   -101   -323    326       C  
ATOM    800  C   SER A 689      43.961  -8.371   6.309  1.00 26.71           C  
ANISOU  800  C   SER A 689     3018   3518   3613   -138   -389    299       C  
ATOM    801  O   SER A 689      44.901  -8.487   7.165  1.00 29.63           O  
ANISOU  801  O   SER A 689     3230   4213   3815   -125   -532    365       O  
ATOM    802  CB ASER A 689      44.648  -6.959   4.407  0.50 26.41           C  
ANISOU  802  CB ASER A 689     3027   3383   3622   -167   -169    281       C  
ATOM    803  CB BSER A 689      44.930  -7.143   4.286  0.50 25.70           C  
ANISOU  803  CB BSER A 689     2871   3316   3574   -139   -204    398       C  
ATOM    804  OG ASER A 689      44.921  -6.988   3.039  0.50 28.22           O  
ANISOU  804  OG ASER A 689     2996   3976   3747    -99    -78    121       O  
ATOM    805  OG BSER A 689      44.115  -6.022   4.561  0.50 25.95           O  
ANISOU  805  OG BSER A 689     2693   3492   3673     95   -340    512       O  
ATOM    806  N   ASN A 690      42.669  -8.220   6.659  1.00 26.34           N  
ANISOU  806  N   ASN A 690     2852   3704   3450   -206   -478    323       N  
ATOM    807  CA  ASN A 690      42.187  -8.091   8.057  1.00 26.92           C  
ANISOU  807  CA  ASN A 690     3186   3514   3527   -303   -429    304       C  
ATOM    808  C   ASN A 690      41.592  -9.432   8.546  1.00 27.48           C  
ANISOU  808  C   ASN A 690     3318   3680   3441   -229   -370    379       C  
ATOM    809  O   ASN A 690      40.783  -9.458   9.482  1.00 27.32           O  
ANISOU  809  O   ASN A 690     3279   3727   3371   -209   -447    351       O  
ATOM    810  CB  ASN A 690      41.197  -6.920   8.178  1.00 25.40           C  
ANISOU  810  CB  ASN A 690     2991   3518   3141   -491   -573    338       C  
ATOM    811  CG  ASN A 690      41.900  -5.590   8.061  1.00 29.44           C  
ANISOU  811  CG  ASN A 690     3869   3621   3697   -321   -908    305       C  
ATOM    812  OD1 ASN A 690      41.778  -4.861   7.086  1.00 33.13           O  
ANISOU  812  OD1 ASN A 690     4817   4282   3489   -587   -969    310       O  
ATOM    813  ND2 ASN A 690      42.686  -5.299   9.041  1.00 28.37           N  
ANISOU  813  ND2 ASN A 690     3773   3135   3870   -409  -1481     99       N  
ATOM    814  N   ARG A 691      41.987 -10.515   7.869  1.00 26.97           N  
ANISOU  814  N   ARG A 691     3386   3355   3503   -181   -433    384       N  
ATOM    815  CA  ARG A 691      41.680 -11.911   8.296  1.00 27.81           C  
ANISOU  815  CA  ARG A 691     3570   3581   3414    -26   -411    702       C  
ATOM    816  C   ARG A 691      40.203 -12.310   8.233  1.00 26.77           C  
ANISOU  816  C   ARG A 691     3612   3310   3250    -58   -379    592       C  
ATOM    817  O   ARG A 691      39.770 -13.320   8.830  1.00 27.93           O  
ANISOU  817  O   ARG A 691     3728   3591   3293     11   -407   1030       O  
ATOM    818  CB  ARG A 691      42.335 -12.221   9.692  1.00 29.58           C  
ANISOU  818  CB  ARG A 691     3688   3889   3660     65   -506    631       C  
ATOM    819  CG  ARG A 691      43.854 -12.089   9.585  1.00 36.98           C  
ANISOU  819  CG  ARG A 691     4188   4836   5025     82   -435    650       C  
ATOM    820  CD  ARG A 691      44.637 -12.571  10.803  1.00 47.07           C  
ANISOU  820  CD  ARG A 691     5610   6297   5974    311   -585    545       C  
ATOM    821  NE  ARG A 691      46.121 -12.501  10.596  1.00 52.38           N  
ANISOU  821  NE  ARG A 691     5967   6818   7117    -33    -46    416       N  
ATOM    822  CZ  ARG A 691      46.877 -13.381   9.925  1.00 53.23           C  
ANISOU  822  CZ  ARG A 691     6214   7055   6956    -72    260    418       C  
ATOM    823  NH1 ARG A 691      46.348 -14.457   9.332  1.00 54.75           N  
ANISOU  823  NH1 ARG A 691     6651   7370   6781    -84    432    373       N  
ATOM    824  NH2 ARG A 691      48.189 -13.189   9.852  1.00 54.51           N  
ANISOU  824  NH2 ARG A 691     6169   7049   7491   -467    328    731       N  
ATOM    825  N   PHE A 692      39.393 -11.588   7.483  1.00 24.08           N  
ANISOU  825  N   PHE A 692     3054   3179   2915    -11   -363    531       N  
ATOM    826  CA  PHE A 692      37.993 -12.001   7.362  1.00 22.03           C  
ANISOU  826  CA  PHE A 692     2932   2652   2784     -6   -223    415       C  
ATOM    827  C   PHE A 692      37.842 -13.418   6.775  1.00 22.67           C  
ANISOU  827  C   PHE A 692     3117   2695   2801     79    -33    534       C  
ATOM    828  O   PHE A 692      36.915 -14.127   7.137  1.00 22.78           O  
ANISOU  828  O   PHE A 692     3056   2554   3043     74     42    314       O  
ATOM    829  CB  PHE A 692      37.309 -10.998   6.418  1.00 21.69           C  
ANISOU  829  CB  PHE A 692     2904   2880   2454     72   -321    472       C  
ATOM    830  CG  PHE A 692      35.853 -11.183   6.339  1.00 19.18           C  
ANISOU  830  CG  PHE A 692     2869   2173   2243     28   -120    297       C  
ATOM    831  CD1 PHE A 692      35.027 -10.677   7.343  1.00 20.97           C  
ANISOU  831  CD1 PHE A 692     3600   2003   2363    151    119    398       C  
ATOM    832  CD2 PHE A 692      35.249 -11.881   5.273  1.00 20.67           C  
ANISOU  832  CD2 PHE A 692     3220   2371   2263     60     97    -54       C  
ATOM    833  CE1 PHE A 692      33.671 -10.828   7.283  1.00 21.41           C  
ANISOU  833  CE1 PHE A 692     3053   2680   2402     -2    -58    362       C  
ATOM    834  CE2 PHE A 692      33.842 -12.050   5.186  1.00 20.60           C  
ANISOU  834  CE2 PHE A 692     2917   2303   2606     79    232    150       C  
ATOM    835  CZ  PHE A 692      33.030 -11.544   6.217  1.00 21.23           C  
ANISOU  835  CZ  PHE A 692     3204   2307   2553    220    124    118       C  
ATOM    836  N   PHE A 693      38.763 -13.811   5.883  1.00 24.46           N  
ANISOU  836  N   PHE A 693     3539   2561   3193    305     88    478       N  
ATOM    837  CA  PHE A 693      38.731 -15.138   5.238  1.00 25.50           C  
ANISOU  837  CA  PHE A 693     3807   2550   3329    241     90    498       C  
ATOM    838  C   PHE A 693      39.747 -16.119   5.892  1.00 28.64           C  
ANISOU  838  C   PHE A 693     4025   2954   3902    288     75    534       C  
ATOM    839  O   PHE A 693      40.169 -17.056   5.226  1.00 30.29           O  
ANISOU  839  O   PHE A 693     4392   2649   4464    306    445    674       O  
ATOM    840  CB  PHE A 693      38.944 -15.066   3.699  1.00 25.06           C  
ANISOU  840  CB  PHE A 693     3733   2369   3419     83    350    440       C  
ATOM    841  CG  PHE A 693      37.967 -14.139   2.990  1.00 21.02           C  
ANISOU  841  CG  PHE A 693     3390   1991   2605   -299    256    215       C  
ATOM    842  CD1 PHE A 693      36.597 -14.448   2.853  1.00 23.22           C  
ANISOU  842  CD1 PHE A 693     3490   2852   2481     81    138     35       C  
ATOM    843  CD2 PHE A 693      38.412 -12.881   2.534  1.00 22.93           C  
ANISOU  843  CD2 PHE A 693     3900   2301   2511   -186    441    -78       C  
ATOM    844  CE1 PHE A 693      35.703 -13.589   2.235  1.00 21.76           C  
ANISOU  844  CE1 PHE A 693     3886   2133   2247   -310    344     51       C  
ATOM    845  CE2 PHE A 693      37.517 -11.984   1.895  1.00 21.33           C  
ANISOU  845  CE2 PHE A 693     3118   2716   2267   -157   -228   -162       C  
ATOM    846  CZ  PHE A 693      36.164 -12.324   1.748  1.00 19.86           C  
ANISOU  846  CZ  PHE A 693     3195   2491   1858   -406    369    122       C  
ATOM    847  N   GLU A 694      40.128 -15.903   7.165  1.00 29.32           N  
ANISOU  847  N   GLU A 694     3960   3132   4045    459   -204    874       N  
ATOM    848  CA  GLU A 694      41.012 -16.876   7.906  1.00 32.06           C  
ANISOU  848  CA  GLU A 694     4214   3313   4653    392   -353    863       C  
ATOM    849  C   GLU A 694      40.372 -18.281   7.694  1.00 32.33           C  
ANISOU  849  C   GLU A 694     4095   3418   4767    439   -264    793       C  
ATOM    850  O   GLU A 694      41.054 -19.264   7.373  1.00 33.56           O  
ANISOU  850  O   GLU A 694     4097   3394   5260    343     30    871       O  
ATOM    851  CB  GLU A 694      40.959 -16.446   9.363  1.00 33.38           C  
ANISOU  851  CB  GLU A 694     4430   3601   4651    231   -627    977       C  
ATOM    852  CG  GLU A 694      42.018 -17.073  10.331  1.00 39.29           C  
ANISOU  852  CG  GLU A 694     4755   4926   5246    502   -845   1045       C  
ATOM    853  CD  GLU A 694      43.495 -16.560  10.152  1.00 46.72           C  
ANISOU  853  CD  GLU A 694     5351   6107   6292    215   -602   1057       C  
ATOM    854  OE1 GLU A 694      43.799 -15.689   9.274  1.00 48.26           O  
ANISOU  854  OE1 GLU A 694     5825   6373   6137    312   -360   1065       O  
ATOM    855  OE2 GLU A 694      44.364 -17.073  10.907  1.00 48.18           O  
ANISOU  855  OE2 GLU A 694     5803   6848   5653    410   -669   1385       O  
ATOM    856  N   ASN A 695      39.052 -18.374   7.841  1.00 30.64           N  
ANISOU  856  N   ASN A 695     3772   3221   4649    509   -302    910       N  
ATOM    857  CA  ASN A 695      38.356 -19.549   7.321  1.00 29.87           C  
ANISOU  857  CA  ASN A 695     3698   3525   4125    500   -336    696       C  
ATOM    858  C   ASN A 695      37.922 -19.367   5.845  1.00 29.29           C  
ANISOU  858  C   ASN A 695     3725   3476   3928    632    -65    637       C  
ATOM    859  O   ASN A 695      37.072 -18.497   5.565  1.00 27.71           O  
ANISOU  859  O   ASN A 695     3625   3216   3687    705   -399    964       O  
ATOM    860  CB  ASN A 695      37.148 -19.841   8.201  1.00 29.58           C  
ANISOU  860  CB  ASN A 695     3483   3655   4101    506   -262    787       C  
ATOM    861  CG  ASN A 695      36.351 -21.100   7.743  1.00 30.79           C  
ANISOU  861  CG  ASN A 695     3917   3879   3902    270    -14    657       C  
ATOM    862  OD1 ASN A 695      36.602 -21.721   6.711  1.00 31.75           O  
ANISOU  862  OD1 ASN A 695     4744   3412   3908     95   -401   1004       O  
ATOM    863  ND2 ASN A 695      35.434 -21.502   8.573  1.00 33.57           N  
ANISOU  863  ND2 ASN A 695     3371   4875   4510   -426    316    493       N  
ATOM    864  N   PRO A 696      38.439 -20.196   4.915  1.00 30.56           N  
ANISOU  864  N   PRO A 696     4015   3727   3868    725   -107    499       N  
ATOM    865  CA  PRO A 696      38.145 -19.944   3.491  1.00 32.01           C  
ANISOU  865  CA  PRO A 696     4299   4020   3840    865     50    366       C  
ATOM    866  C   PRO A 696      36.723 -20.200   3.074  1.00 30.79           C  
ANISOU  866  C   PRO A 696     4141   3989   3567    946    146    385       C  
ATOM    867  O   PRO A 696      36.304 -19.728   1.988  1.00 30.38           O  
ANISOU  867  O   PRO A 696     4012   4150   3379   1507    250    484       O  
ATOM    868  CB  PRO A 696      39.088 -20.901   2.724  1.00 33.97           C  
ANISOU  868  CB  PRO A 696     4611   4228   4066    924    159    298       C  
ATOM    869  CG  PRO A 696      39.721 -21.718   3.740  1.00 34.56           C  
ANISOU  869  CG  PRO A 696     4496   4279   4354    985   -123    279       C  
ATOM    870  CD  PRO A 696      39.460 -21.247   5.115  1.00 32.19           C  
ANISOU  870  CD  PRO A 696     4194   3889   4146    997     98    412       C  
ATOM    871  N   ALA A 697      35.972 -20.938   3.884  1.00 28.73           N  
ANISOU  871  N   ALA A 697     3941   3402   3572    650    -36    438       N  
ATOM    872  CA  ALA A 697      34.583 -21.114   3.628  1.00 27.97           C  
ANISOU  872  CA  ALA A 697     4143   3138   3344    512    -64    372       C  
ATOM    873  C   ALA A 697      33.884 -19.736   3.494  1.00 24.36           C  
ANISOU  873  C   ALA A 697     3819   2487   2948    415   -119    426       C  
ATOM    874  O   ALA A 697      32.871 -19.642   2.793  1.00 24.32           O  
ANISOU  874  O   ALA A 697     3943   2315   2983    256   -155    383       O  
ATOM    875  CB  ALA A 697      33.915 -21.959   4.713  1.00 28.53           C  
ANISOU  875  CB  ALA A 697     4200   3179   3458    295   -132    579       C  
ATOM    876  N   LEU A 698      34.406 -18.694   4.164  1.00 21.30           N  
ANISOU  876  N   LEU A 698     3498   2276   2316    401     47    504       N  
ATOM    877  CA  LEU A 698      33.671 -17.378   4.139  1.00 18.34           C  
ANISOU  877  CA  LEU A 698     3299   1811   1856    295    -15    318       C  
ATOM    878  C   LEU A 698      33.744 -16.734   2.746  1.00 17.94           C  
ANISOU  878  C   LEU A 698     2776   2133   1905    307    223    441       C  
ATOM    879  O   LEU A 698      32.912 -15.857   2.451  1.00 15.90           O  
ANISOU  879  O   LEU A 698     2487   1688   1864    278    211    322       O  
ATOM    880  CB  LEU A 698      34.148 -16.374   5.192  1.00 20.22           C  
ANISOU  880  CB  LEU A 698     3543   2312   1825    119     22    278       C  
ATOM    881  CG  LEU A 698      33.423 -16.518   6.578  1.00 22.19           C  
ANISOU  881  CG  LEU A 698     4169   2354   1906     14    178    436       C  
ATOM    882  CD1 LEU A 698      33.932 -17.795   7.219  1.00 29.56           C  
ANISOU  882  CD1 LEU A 698     5306   3162   2761    528    205    550       C  
ATOM    883  CD2 LEU A 698      33.741 -15.329   7.423  1.00 27.80           C  
ANISOU  883  CD2 LEU A 698     4531   3594   2437   -141     38   -114       C  
ATOM    884  N   LYS A 699      34.631 -17.232   1.852  1.00 17.98           N  
ANISOU  884  N   LYS A 699     2726   2361   1742    151    250    258       N  
ATOM    885  CA  LYS A 699      34.595 -16.764   0.456  1.00 18.57           C  
ANISOU  885  CA  LYS A 699     2586   2672   1795    398    442    129       C  
ATOM    886  C   LYS A 699      33.261 -17.100  -0.187  1.00 18.15           C  
ANISOU  886  C   LYS A 699     2831   2213   1851    297    254     67       C  
ATOM    887  O   LYS A 699      32.861 -16.405  -1.169  1.00 18.95           O  
ANISOU  887  O   LYS A 699     2946   2580   1672    461    367    281       O  
ATOM    888  CB  LYS A 699      35.693 -17.455  -0.404  1.00 20.71           C  
ANISOU  888  CB  LYS A 699     2756   3308   1804    505    715    -60       C  
ATOM    889  CG  LYS A 699      37.069 -17.031   0.023  1.00 28.43           C  
ANISOU  889  CG  LYS A 699     3298   4199   3302    663    536   -328       C  
ATOM    890  CD  LYS A 699      38.203 -17.555  -0.905  1.00 37.15           C  
ANISOU  890  CD  LYS A 699     4432   4921   4761   1159   1134   -760       C  
ATOM    891  CE  LYS A 699      38.660 -18.956  -0.577  1.00 43.59           C  
ANISOU  891  CE  LYS A 699     5636   5875   5050   1172    900    292       C  
ATOM    892  NZ  LYS A 699      39.553 -19.559  -1.696  1.00 45.99           N  
ANISOU  892  NZ  LYS A 699     5971   6155   5345   1423    965   -309       N  
ATOM    893  N   GLU A 700      32.522 -18.098   0.345  1.00 18.06           N  
ANISOU  893  N   GLU A 700     2530   2312   2017    361    426   -203       N  
ATOM    894  CA AGLU A 700      31.260 -18.431  -0.278  0.50 18.33           C  
ANISOU  894  CA AGLU A 700     2702   2200   2060    257    230    -57       C  
ATOM    895  CA BGLU A 700      31.231 -18.478  -0.205  0.50 18.61           C  
ANISOU  895  CA BGLU A 700     2737   2206   2125    279    199    -71       C  
ATOM    896  C   GLU A 700      30.132 -17.440   0.073  1.00 16.00           C  
ANISOU  896  C   GLU A 700     2519   1745   1812    202     -2    -55       C  
ATOM    897  O   GLU A 700      29.028 -17.553  -0.464  1.00 18.29           O  
ANISOU  897  O   GLU A 700     2579   2248   2120    224     11   -178       O  
ATOM    898  CB AGLU A 700      30.859 -19.839   0.087  0.50 20.72           C  
ANISOU  898  CB AGLU A 700     3172   2251   2448    230    192   -136       C  
ATOM    899  CB BGLU A 700      30.788 -19.814   0.379  0.50 21.10           C  
ANISOU  899  CB BGLU A 700     3196   2245   2575    263    105   -141       C  
ATOM    900  CG AGLU A 700      31.893 -20.877  -0.316  0.50 23.84           C  
ANISOU  900  CG AGLU A 700     3387   2719   2952    337    485     24       C  
ATOM    901  CG BGLU A 700      31.693 -20.980  -0.027  0.50 25.37           C  
ANISOU  901  CG BGLU A 700     3582   2928   3127    534    283    -90       C  
ATOM    902  CD AGLU A 700      31.590 -22.245   0.267  0.50 29.99           C  
ANISOU  902  CD AGLU A 700     4234   2930   4229    114    386    141       C  
ATOM    903  CD BGLU A 700      32.133 -20.920  -1.474  0.50 30.43           C  
ANISOU  903  CD BGLU A 700     4234   3788   3540    342    264    -78       C  
ATOM    904  OE1AGLU A 700      30.408 -22.502   0.573  0.50 32.66           O  
ANISOU  904  OE1AGLU A 700     4294   3162   4952    193    540    186       O  
ATOM    905  OE1BGLU A 700      31.256 -20.963  -2.365  0.50 33.22           O  
ANISOU  905  OE1BGLU A 700     4937   3988   3697    191    -79   -583       O  
ATOM    906  OE2AGLU A 700      32.538 -23.050   0.413  0.50 34.90           O  
ANISOU  906  OE2AGLU A 700     4703   3446   5109    439    165    208       O  
ATOM    907  OE2BGLU A 700      33.369 -20.834  -1.704  0.50 32.51           O  
ANISOU  907  OE2BGLU A 700     4202   4289   3860    555    313      0       O  
ATOM    908  N   LEU A 701      30.423 -16.457   0.934  1.00 15.31           N  
ANISOU  908  N   LEU A 701     2639   1709   1468    129    239     61       N  
ATOM    909  CA  LEU A 701      29.446 -15.400   1.206  1.00 13.98           C  
ANISOU  909  CA  LEU A 701     2433   1610   1269    -52     59     61       C  
ATOM    910  C   LEU A 701      29.475 -14.230   0.191  1.00 11.75           C  
ANISOU  910  C   LEU A 701     1848   1402   1215   -167     64     22       C  
ATOM    911  O   LEU A 701      28.588 -13.359   0.251  1.00 12.91           O  
ANISOU  911  O   LEU A 701     2242   1464   1200    -32    151    -14       O  
ATOM    912  CB  LEU A 701      29.692 -14.786   2.607  1.00 12.89           C  
ANISOU  912  CB  LEU A 701     2277   1765    854   -109    -21     98       C  
ATOM    913  CG  LEU A 701      29.580 -15.865   3.727  1.00 12.97           C  
ANISOU  913  CG  LEU A 701     2106   1684   1137   -494     96     87       C  
ATOM    914  CD1 LEU A 701      29.926 -15.070   5.086  1.00 17.83           C  
ANISOU  914  CD1 LEU A 701     2645   2550   1579    318   -186   -272       C  
ATOM    915  CD2 LEU A 701      28.271 -16.552   3.757  1.00 15.78           C  
ANISOU  915  CD2 LEU A 701     1820   2355   1819   -543    -34    588       C  
ATOM    916  N   LEU A 702      30.469 -14.223  -0.713  1.00 12.99           N  
ANISOU  916  N   LEU A 702     2310   1357   1265     23    280   -167       N  
ATOM    917  CA  LEU A 702      30.621 -13.097  -1.664  1.00 12.68           C  
ANISOU  917  CA  LEU A 702     1864   1572   1381     24    235    148       C  
ATOM    918  C   LEU A 702      29.828 -13.334  -2.932  1.00 11.66           C  
ANISOU  918  C   LEU A 702     1760   1350   1317    -60    240   -107       C  
ATOM    919  O   LEU A 702      29.907 -14.450  -3.521  1.00 14.12           O  
ANISOU  919  O   LEU A 702     2391   1480   1492    -29    289   -101       O  
ATOM    920  CB  LEU A 702      32.075 -12.909  -2.070  1.00 14.75           C  
ANISOU  920  CB  LEU A 702     1721   2148   1734      9    277   -127       C  
ATOM    921  CG  LEU A 702      33.084 -12.483  -1.038  1.00 19.54           C  
ANISOU  921  CG  LEU A 702     2080   2735   2607    -41     87   -152       C  
ATOM    922  CD1 LEU A 702      34.521 -12.473  -1.633  1.00 21.15           C  
ANISOU  922  CD1 LEU A 702     2069   3090   2875   -537    340   -423       C  
ATOM    923  CD2 LEU A 702      32.754 -11.061  -0.525  1.00 26.41           C  
ANISOU  923  CD2 LEU A 702     3342   2902   3788   -354    342   -954       C  
ATOM    924  N   PHE A 703      29.158 -12.299  -3.420  1.00 12.83           N  
ANISOU  924  N   PHE A 703     1898   1580   1396   -212    190    186       N  
ATOM    925  CA  PHE A 703      28.396 -12.399  -4.723  1.00 13.73           C  
ANISOU  925  CA  PHE A 703     2001   1713   1499   -441     88    244       C  
ATOM    926  C   PHE A 703      28.651 -11.122  -5.446  1.00 13.36           C  
ANISOU  926  C   PHE A 703     2123   1510   1440   -215    154    114       C  
ATOM    927  O   PHE A 703      28.781 -10.039  -4.797  1.00 12.47           O  
ANISOU  927  O   PHE A 703     1915   1460   1360   -355    285    121       O  
ATOM    928  CB  PHE A 703      26.896 -12.524  -4.481  1.00 13.63           C  
ANISOU  928  CB  PHE A 703     1942   1553   1684   -405    405    264       C  
ATOM    929  CG  PHE A 703      26.565 -13.868  -3.891  1.00 12.31           C  
ANISOU  929  CG  PHE A 703     1766   1530   1381   -421    267    139       C  
ATOM    930  CD1 PHE A 703      26.289 -14.979  -4.730  1.00 14.84           C  
ANISOU  930  CD1 PHE A 703     2431   1504   1701   -378    167    206       C  
ATOM    931  CD2 PHE A 703      26.597 -14.050  -2.485  1.00 14.48           C  
ANISOU  931  CD2 PHE A 703     1903   2035   1561   -450    449    333       C  
ATOM    932  CE1 PHE A 703      25.972 -16.242  -4.152  1.00 15.48           C  
ANISOU  932  CE1 PHE A 703     2367   1846   1669   -310    200    371       C  
ATOM    933  CE2 PHE A 703      26.382 -15.320  -1.901  1.00 15.06           C  
ANISOU  933  CE2 PHE A 703     2278   1848   1593   -397      3     75       C  
ATOM    934  CZ  PHE A 703      26.069 -16.401  -2.749  1.00 13.99           C  
ANISOU  934  CZ  PHE A 703     1988   1580   1747   -440    -56     95       C  
ATOM    935  N   HIS A 704      28.670 -11.164  -6.763  1.00 12.68           N  
ANISOU  935  N   HIS A 704     2146   1446   1222   -320    198    204       N  
ATOM    936  CA  HIS A 704      28.888  -9.889  -7.478  1.00 12.33           C  
ANISOU  936  CA  HIS A 704     2004   1456   1221    182    239    213       C  
ATOM    937  C   HIS A 704      27.721  -8.903  -7.408  1.00 13.33           C  
ANISOU  937  C   HIS A 704     2011   1476   1575    -38    105     88       C  
ATOM    938  O   HIS A 704      27.946  -7.684  -7.277  1.00 17.30           O  
ANISOU  938  O   HIS A 704     2199   1965   2410   -269    168   -389       O  
ATOM    939  CB  HIS A 704      29.296 -10.190  -8.952  1.00 13.00           C  
ANISOU  939  CB  HIS A 704     2314   1410   1213    384    363    239       C  
ATOM    940  CG  HIS A 704      29.438  -8.960  -9.783  1.00 16.79           C  
ANISOU  940  CG  HIS A 704     2923   1745   1708    -93    367    190       C  
ATOM    941  ND1 HIS A 704      30.326  -7.936  -9.477  1.00 18.72           N  
ANISOU  941  ND1 HIS A 704     2725   2028   2360    117    709    439       N  
ATOM    942  CD2 HIS A 704      28.800  -8.583 -10.920  1.00 20.50           C  
ANISOU  942  CD2 HIS A 704     3503   2426   1860     76    537     97       C  
ATOM    943  CE1 HIS A 704      30.229  -6.983 -10.399  1.00 19.74           C  
ANISOU  943  CE1 HIS A 704     2747   2440   2311    551    690    390       C  
ATOM    944  NE2 HIS A 704      29.360  -7.383 -11.315  1.00 21.86           N  
ANISOU  944  NE2 HIS A 704     3530   2262   2513   -161    689    161       N  
ATOM    945  N   SER A 705      26.496  -9.399  -7.560  1.00 14.59           N  
ANISOU  945  N   SER A 705     1797   1870   1878   -241    352    124       N  
ATOM    946  CA  SER A 705      25.342  -8.546  -7.543  1.00 15.08           C  
ANISOU  946  CA  SER A 705     1686   2230   1814   -200    174    103       C  
ATOM    947  C   SER A 705      24.346  -9.003  -6.474  1.00 13.96           C  
ANISOU  947  C   SER A 705     1628   1737   1937   -246    206    178       C  
ATOM    948  O   SER A 705      24.405 -10.170  -6.007  1.00 13.77           O  
ANISOU  948  O   SER A 705     1826   1767   1638   -143    326     98       O  
ATOM    949  CB  SER A 705      24.561  -8.540  -8.856  1.00 16.19           C  
ANISOU  949  CB  SER A 705     1806   2529   1817   -339     25    425       C  
ATOM    950  OG  SER A 705      23.981  -9.825  -9.134  1.00 17.88           O  
ANISOU  950  OG  SER A 705     2511   2339   1942   -409     91     62       O  
ATOM    951  N   ILE A 706      23.427  -8.063  -6.122  1.00 13.27           N  
ANISOU  951  N   ILE A 706     1683   1849   1510    -51    232     20       N  
ATOM    952  CA  ILE A 706      22.385  -8.437  -5.188  1.00 12.18           C  
ANISOU  952  CA  ILE A 706     1426   1597   1603   -200    328     47       C  
ATOM    953  C   ILE A 706      21.582  -9.613  -5.773  1.00 12.51           C  
ANISOU  953  C   ILE A 706     1833   1452   1466   -229     79    166       C  
ATOM    954  O   ILE A 706      21.230 -10.576  -5.018  1.00 14.17           O  
ANISOU  954  O   ILE A 706     2237   1573   1574   -407     44    298       O  
ATOM    955  CB  ILE A 706      21.427  -7.254  -4.919  1.00 12.09           C  
ANISOU  955  CB  ILE A 706     1310   1679   1605   -119     53     95       C  
ATOM    956  CG1 ILE A 706      22.222  -6.151  -4.144  1.00 14.51           C  
ANISOU  956  CG1 ILE A 706     1980   1358   2174     79    -12   -340       C  
ATOM    957  CG2 ILE A 706      20.175  -7.721  -4.117  1.00 14.21           C  
ANISOU  957  CG2 ILE A 706     1342   2129   1927     58    155    397       C  
ATOM    958  CD1 ILE A 706      21.516  -4.871  -4.240  1.00 16.23           C  
ANISOU  958  CD1 ILE A 706     2025   1513   2628    146    111     63       C  
ATOM    959  N   HIS A 707      21.235  -9.578  -7.067  1.00 14.34           N  
ANISOU  959  N   HIS A 707     2014   1676   1755   -410    -68     41       N  
ATOM    960  CA  HIS A 707      20.442 -10.699  -7.612  1.00 14.41           C  
ANISOU  960  CA  HIS A 707     2225   1785   1464   -324   -244    140       C  
ATOM    961  C   HIS A 707      21.200 -12.015  -7.481  1.00 14.54           C  
ANISOU  961  C   HIS A 707     2115   1885   1522   -424    -31    100       C  
ATOM    962  O   HIS A 707      20.567 -13.063  -7.211  1.00 15.47           O  
ANISOU  962  O   HIS A 707     2520   1701   1657   -460     88    200       O  
ATOM    963  CB  HIS A 707      20.039 -10.426  -9.070  1.00 16.80           C  
ANISOU  963  CB  HIS A 707     2602   2142   1638   -568   -543    182       C  
ATOM    964  CG  HIS A 707      18.882 -11.297  -9.513  1.00 18.82           C  
ANISOU  964  CG  HIS A 707     2663   2222   2264   -293   -746    388       C  
ATOM    965  ND1 HIS A 707      17.633 -11.196  -8.929  1.00 21.65           N  
ANISOU  965  ND1 HIS A 707     3020   2193   3011   -426   -526    304       N  
ATOM    966  CD2 HIS A 707      18.776 -12.243 -10.477  1.00 25.95           C  
ANISOU  966  CD2 HIS A 707     3709   3076   3075   -181   -345    -73       C  
ATOM    967  CE1 HIS A 707      16.806 -12.063  -9.503  1.00 24.65           C  
ANISOU  967  CE1 HIS A 707     3367   2905   3092   -323   -778   -148       C  
ATOM    968  NE2 HIS A 707      17.468 -12.692 -10.466  1.00 26.13           N  
ANISOU  968  NE2 HIS A 707     3567   3210   3148    -50   -166     94       N  
ATOM    969  N   ASP A 708      22.523 -12.031  -7.738  1.00 13.77           N  
ANISOU  969  N   ASP A 708     2085   1877   1269   -198     32    -32       N  
ATOM    970  CA  ASP A 708      23.273 -13.296  -7.610  1.00 13.80           C  
ANISOU  970  CA  ASP A 708     2084   1887   1270   -186      0    169       C  
ATOM    971  C   ASP A 708      23.158 -13.796  -6.159  1.00 12.84           C  
ANISOU  971  C   ASP A 708     2121   1572   1184   -332    151    -61       C  
ATOM    972  O   ASP A 708      23.029 -14.992  -5.943  1.00 14.16           O  
ANISOU  972  O   ASP A 708     2066   1761   1554   -296    234    194       O  
ATOM    973  CB  ASP A 708      24.767 -13.069  -7.848  1.00 15.56           C  
ANISOU  973  CB  ASP A 708     2276   2252   1382   -294    292    180       C  
ATOM    974  CG  ASP A 708      25.097 -12.688  -9.272  1.00 17.57           C  
ANISOU  974  CG  ASP A 708     2490   2457   1729   -368    -72    411       C  
ATOM    975  OD1 ASP A 708      24.333 -13.049 -10.221  1.00 20.52           O  
ANISOU  975  OD1 ASP A 708     3222   2985   1590   -499     12    129       O  
ATOM    976  OD2 ASP A 708      26.169 -12.008  -9.472  1.00 23.82           O  
ANISOU  976  OD2 ASP A 708     3415   3386   2248   -877    563    238       O  
ATOM    977  N   ALA A 709      23.207 -12.879  -5.160  1.00 12.72           N  
ANISOU  977  N   ALA A 709     1957   1695   1182   -258     86   -132       N  
ATOM    978  CA  ALA A 709      23.090 -13.301  -3.739  1.00 12.14           C  
ANISOU  978  CA  ALA A 709     1820   1457   1335   -422    180    -12       C  
ATOM    979  C   ALA A 709      21.703 -13.847  -3.468  1.00 11.33           C  
ANISOU  979  C   ALA A 709     1687   1309   1306   -294     -1    269       C  
ATOM    980  O   ALA A 709      21.547 -14.853  -2.737  1.00 13.27           O  
ANISOU  980  O   ALA A 709     1983   1236   1820   -556     67    238       O  
ATOM    981  CB  ALA A 709      23.333 -12.071  -2.872  1.00 12.05           C  
ANISOU  981  CB  ALA A 709     1899   1287   1391   -411    242   -112       C  
ATOM    982  N   VAL A 710      20.678 -13.193  -4.029  1.00 12.28           N  
ANISOU  982  N   VAL A 710     1371   1797   1498   -233     10    -13       N  
ATOM    983  CA  VAL A 710      19.265 -13.693  -3.847  1.00 13.59           C  
ANISOU  983  CA  VAL A 710     1696   1763   1702   -244   -103     63       C  
ATOM    984  C   VAL A 710      19.208 -15.118  -4.445  1.00 13.11           C  
ANISOU  984  C   VAL A 710     1815   1731   1434   -350    -41    128       C  
ATOM    985  O   VAL A 710      18.683 -16.062  -3.760  1.00 15.77           O  
ANISOU  985  O   VAL A 710     1952   1911   2125   -494    -49    253       O  
ATOM    986  CB  VAL A 710      18.218 -12.753  -4.534  1.00 13.77           C  
ANISOU  986  CB  VAL A 710     1883   1766   1581   -271    -20     32       C  
ATOM    987  CG1 VAL A 710      16.796 -13.459  -4.611  1.00 17.62           C  
ANISOU  987  CG1 VAL A 710     1931   2325   2436   -705   -134     -3       C  
ATOM    988  CG2 VAL A 710      18.185 -11.413  -3.759  1.00 13.29           C  
ANISOU  988  CG2 VAL A 710     1720   1662   1665    -28    -31   -215       C  
ATOM    989  N   LEU A 711      19.737 -15.334  -5.674  1.00 13.89           N  
ANISOU  989  N   LEU A 711     2201   1555   1522   -513     97   -307       N  
ATOM    990  CA  LEU A 711      19.659 -16.697  -6.268  1.00 15.84           C  
ANISOU  990  CA  LEU A 711     2369   1811   1838   -547    180   -221       C  
ATOM    991  C   LEU A 711      20.498 -17.678  -5.417  1.00 15.80           C  
ANISOU  991  C   LEU A 711     2398   1778   1825   -674     42   -150       C  
ATOM    992  O   LEU A 711      20.121 -18.885  -5.220  1.00 17.39           O  
ANISOU  992  O   LEU A 711     2435   1887   2283   -834    116    -91       O  
ATOM    993  CB  LEU A 711      20.223 -16.667  -7.718  1.00 16.85           C  
ANISOU  993  CB  LEU A 711     2613   2186   1601   -497     82   -162       C  
ATOM    994  CG  LEU A 711      19.348 -15.792  -8.659  1.00 21.97           C  
ANISOU  994  CG  LEU A 711     3087   2782   2475    -99    -43   -144       C  
ATOM    995  CD1 LEU A 711      19.838 -15.877 -10.083  1.00 23.30           C  
ANISOU  995  CD1 LEU A 711     3665   3088   2100    212   -443   -288       C  
ATOM    996  CD2 LEU A 711      17.877 -16.282  -8.611  1.00 28.48           C  
ANISOU  996  CD2 LEU A 711     3790   3790   3238   -323   -437    400       C  
ATOM    997  N   GLY A 712      21.617 -17.197  -4.867  1.00 15.30           N  
ANISOU  997  N   GLY A 712     2239   1907   1665   -436     34    -80       N  
ATOM    998  CA  GLY A 712      22.520 -18.055  -4.088  1.00 15.87           C  
ANISOU  998  CA  GLY A 712     2503   1437   2088   -363    -65     16       C  
ATOM    999  C   GLY A 712      21.878 -18.493  -2.782  1.00 15.57           C  
ANISOU  999  C   GLY A 712     2223   1587   2107   -300    -37    -24       C  
ATOM   1000  O   GLY A 712      22.212 -19.573  -2.264  1.00 19.04           O  
ANISOU 1000  O   GLY A 712     2650   2000   2581   -173     42    260       O  
ATOM   1001  N   SER A 713      20.889 -17.723  -2.296  1.00 13.09           N  
ANISOU 1001  N   SER A 713     1777   1411   1785   -441    -15     20       N  
ATOM   1002  CA  SER A 713      20.209 -18.044  -1.024  1.00 14.35           C  
ANISOU 1002  CA  SER A 713     1909   1738   1805   -412      0     26       C  
ATOM   1003  C   SER A 713      19.169 -19.178  -1.203  1.00 15.80           C  
ANISOU 1003  C   SER A 713     2442   1736   1822   -679    -38    -29       C  
ATOM   1004  O   SER A 713      18.680 -19.710  -0.180  1.00 17.70           O  
ANISOU 1004  O   SER A 713     2677   2252   1795   -867   -168    187       O  
ATOM   1005  CB  SER A 713      19.524 -16.843  -0.379  1.00 15.88           C  
ANISOU 1005  CB  SER A 713     2002   2185   1845    -71   -304    116       C  
ATOM   1006  OG  SER A 713      18.390 -16.519  -1.095  1.00 17.95           O  
ANISOU 1006  OG  SER A 713     2281   2297   2239   -194   -242    252       O  
ATOM   1007  N   GLN A 714      18.860 -19.567  -2.428  1.00 15.80           N  
ANISOU 1007  N   GLN A 714     2285   1745   1973   -721   -255    -30       N  
ATOM   1008  CA  GLN A 714      17.732 -20.506  -2.618  1.00 15.62           C  
ANISOU 1008  CA  GLN A 714     2321   1750   1862   -633   -182    159       C  
ATOM   1009  C   GLN A 714      18.004 -21.875  -2.013  1.00 14.69           C  
ANISOU 1009  C   GLN A 714     1977   1696   1908   -502    -62    203       C  
ATOM   1010  O   GLN A 714      17.085 -22.474  -1.398  1.00 16.92           O  
ANISOU 1010  O   GLN A 714     2270   1703   2455   -703    -12   -123       O  
ATOM   1011  CB  GLN A 714      17.433 -20.682  -4.107  1.00 17.08           C  
ANISOU 1011  CB  GLN A 714     2476   2289   1722   -771   -420   -148       C  
ATOM   1012  CG  GLN A 714      16.157 -21.360  -4.149  1.00 22.67           C  
ANISOU 1012  CG  GLN A 714     3333   2618   2660   -795   -215    -28       C  
ATOM   1013  CD  GLN A 714      15.637 -21.738  -5.445  1.00 27.53           C  
ANISOU 1013  CD  GLN A 714     3872   3134   3451  -1499     52   -228       C  
ATOM   1014  OE1 GLN A 714      15.969 -21.171  -6.468  1.00 25.27           O  
ANISOU 1014  OE1 GLN A 714     3340   4050   2211   -467   -572    293       O  
ATOM   1015  NE2 GLN A 714      14.656 -22.748  -5.381  1.00 33.84           N  
ANISOU 1015  NE2 GLN A 714     3026   4850   4981  -1783    750  -1637       N  
ATOM   1016  N   VAL A 715      19.193 -22.412  -2.259  1.00 17.11           N  
ANISOU 1016  N   VAL A 715     2313   1832   2353   -466   -201    220       N  
ATOM   1017  CA  VAL A 715      19.471 -23.760  -1.783  1.00 16.23           C  
ANISOU 1017  CA  VAL A 715     2262   1823   2081   -409   -201    121       C  
ATOM   1018  C   VAL A 715      20.904 -23.793  -1.310  1.00 18.14           C  
ANISOU 1018  C   VAL A 715     2393   2373   2125   -538   -108    228       C  
ATOM   1019  O   VAL A 715      21.853 -23.416  -2.076  1.00 18.94           O  
ANISOU 1019  O   VAL A 715     2376   2721   2099   -593    125     80       O  
ATOM   1020  CB  VAL A 715      19.326 -24.820  -2.896  1.00 16.80           C  
ANISOU 1020  CB  VAL A 715     2671   1443   2268   -667   -430     61       C  
ATOM   1021  CG1 VAL A 715      19.353 -26.279  -2.265  1.00 19.76           C  
ANISOU 1021  CG1 VAL A 715     3053   1772   2682   -366   -291    131       C  
ATOM   1022  CG2 VAL A 715      17.964 -24.656  -3.629  1.00 16.54           C  
ANISOU 1022  CG2 VAL A 715     2382   1702   2200   -225      0    -54       C  
ATOM   1023  N   ARG A 716      21.101 -24.255  -0.068  1.00 17.66           N  
ANISOU 1023  N   ARG A 716     2356   2257   2097   -475   -445    142       N  
ATOM   1024  CA  ARG A 716      22.502 -24.269   0.474  1.00 18.72           C  
ANISOU 1024  CA  ARG A 716     2723   1926   2460   -810   -487     13       C  
ATOM   1025  C   ARG A 716      22.516 -25.106   1.750  1.00 19.45           C  
ANISOU 1025  C   ARG A 716     2820   2250   2319   -481   -451    159       C  
ATOM   1026  O   ARG A 716      21.444 -25.395   2.302  1.00 19.94           O  
ANISOU 1026  O   ARG A 716     3030   2113   2432   -905   -781    286       O  
ATOM   1027  CB  ARG A 716      22.998 -22.844   0.834  1.00 20.36           C  
ANISOU 1027  CB  ARG A 716     3083   1902   2749   -781    -12   -187       C  
ATOM   1028  CG  ARG A 716      22.134 -22.244   1.920  1.00 19.84           C  
ANISOU 1028  CG  ARG A 716     3167   1815   2553   -403   -279   -360       C  
ATOM   1029  CD  ARG A 716      22.271 -20.791   2.002  1.00 20.36           C  
ANISOU 1029  CD  ARG A 716     3188   2008   2540   -414   -370   -459       C  
ATOM   1030  NE  ARG A 716      21.351 -20.403   3.092  1.00 19.94           N  
ANISOU 1030  NE  ARG A 716     3109   1917   2549   -174   -188   -368       N  
ATOM   1031  CZ  ARG A 716      20.945 -19.142   3.269  1.00 17.28           C  
ANISOU 1031  CZ  ARG A 716     2731   1814   2018   -229   -230     49       C  
ATOM   1032  NH1 ARG A 716      21.319 -18.171   2.369  1.00 18.01           N  
ANISOU 1032  NH1 ARG A 716     3179   1452   2209   -755   -464    -93       N  
ATOM   1033  NH2 ARG A 716      20.101 -18.883   4.253  1.00 20.07           N  
ANISOU 1033  NH2 ARG A 716     2753   2936   1934   -156   -313    -10       N  
ATOM   1034  N   GLU A 717      23.717 -25.394   2.267  1.00 20.83           N  
ANISOU 1034  N   GLU A 717     3223   2183   2506   -245   -604     84       N  
ATOM   1035  CA  GLU A 717      23.782 -26.219   3.491  1.00 21.93           C  
ANISOU 1035  CA  GLU A 717     3129   2577   2627   -152   -559    239       C  
ATOM   1036  C   GLU A 717      23.071 -25.515   4.664  1.00 23.27           C  
ANISOU 1036  C   GLU A 717     3337   2561   2943   -122   -563    187       C  
ATOM   1037  O   GLU A 717      23.325 -24.298   4.936  1.00 23.14           O  
ANISOU 1037  O   GLU A 717     3415   2422   2955   -468   -595     90       O  
ATOM   1038  CB  GLU A 717      25.253 -26.441   3.807  1.00 25.30           C  
ANISOU 1038  CB  GLU A 717     3106   3146   3360   -153   -710    222       C  
ATOM   1039  CG  GLU A 717      25.547 -27.842   4.278  1.00 37.14           C  
ANISOU 1039  CG  GLU A 717     4218   4743   5149    379   -819    608       C  
ATOM   1040  CD  GLU A 717      26.979 -27.913   4.837  1.00 46.88           C  
ANISOU 1040  CD  GLU A 717     4770   6739   6301    642   -834    646       C  
ATOM   1041  OE1 GLU A 717      27.917 -27.538   4.086  1.00 50.38           O  
ANISOU 1041  OE1 GLU A 717     4970   6920   7249    669   -343    723       O  
ATOM   1042  OE2 GLU A 717      27.138 -28.299   6.032  1.00 53.66           O  
ANISOU 1042  OE2 GLU A 717     6173   7666   6549   1078   -851    478       O  
ATOM   1043  N   ALA A 718      22.159 -26.236   5.336  1.00 23.01           N  
ANISOU 1043  N   ALA A 718     3294   2681   2764   -126   -678    238       N  
ATOM   1044  CA  ALA A 718      21.286 -25.637   6.328  1.00 26.43           C  
ANISOU 1044  CA  ALA A 718     3800   3345   2896   -104   -739     31       C  
ATOM   1045  C   ALA A 718      22.007 -25.584   7.732  1.00 27.64           C  
ANISOU 1045  C   ALA A 718     3837   3490   3173    -72   -898   -162       C  
ATOM   1046  O   ALA A 718      21.624 -24.721   8.593  1.00 30.32           O  
ANISOU 1046  O   ALA A 718     4563   3719   3238   -191  -1121   -150       O  
ATOM   1047  CB  ALA A 718      19.979 -26.453   6.473  1.00 26.84           C  
ANISOU 1047  CB  ALA A 718     3736   3288   3173   -109   -697    -83       C  
ATOM   1048  OXT ALA A 718      22.892 -26.396   7.996  1.00 28.46           O  
ANISOU 1048  OXT ALA A 718     4110   3281   3422   -166   -905     45       O  
TER    1049      ALA A 718                                                      
HETATM 1050  C1  BOG A 719      27.455 -25.190   7.484  1.00 40.48           C  
ANISOU 1050  C1  BOG A 719     5363   5415   4600    146     63    116       C  
HETATM 1051  O1  BOG A 719      26.645 -24.225   8.229  1.00 36.54           O  
ANISOU 1051  O1  BOG A 719     4622   4492   4769    157   -707    135       O  
HETATM 1052  C1' BOG A 719      25.299 -23.922   7.739  1.00 31.36           C  
ANISOU 1052  C1' BOG A 719     4444   4156   3316    104   -458    516       C  
HETATM 1053  C2' BOG A 719      24.783 -22.678   8.500  1.00 30.92           C  
ANISOU 1053  C2' BOG A 719     4298   3637   3811   -315    257    668       C  
HETATM 1054  C3' BOG A 719      25.708 -21.533   8.198  1.00 23.48           C  
ANISOU 1054  C3' BOG A 719     3397   2643   2879   -370   -725     -6       C  
HETATM 1055  C4' BOG A 719      25.386 -20.090   8.550  1.00 28.87           C  
ANISOU 1055  C4' BOG A 719     3982   3714   3273    332   -442  -1240       C  
HETATM 1056  C5' BOG A 719      26.822 -19.498   8.563  1.00 25.19           C  
ANISOU 1056  C5' BOG A 719     4203   2782   2585   -274    654   -619       C  
HETATM 1057  C6' BOG A 719      27.306 -18.441   7.639  1.00 32.14           C  
ANISOU 1057  C6' BOG A 719     4945   3471   3795   -203    412   -623       C  
HETATM 1058  C7' BOG A 719      28.563 -17.909   8.290  1.00 34.06           C  
ANISOU 1058  C7' BOG A 719     4824   4429   3686     -8    110    250       C  
HETATM 1059  C8' BOG A 719      29.684 -18.914   8.624  1.00 37.05           C  
ANISOU 1059  C8' BOG A 719     4829   3693   5554   -600    917    748       C  
HETATM 1060  O   HOH A   1      26.117 -15.413   8.601  1.00 16.21           O  
ANISOU 1060  O   HOH A   1     2880   1829   1450   -123   -113    250       O  
HETATM 1061  O   HOH A   2      32.641  -2.343  -2.769  1.00 22.02           O  
ANISOU 1061  O   HOH A   2     2094   2167   4102   -637    389   -971       O  
HETATM 1062  O   HOH A   3      21.173  -7.233  -8.959  1.00 22.45           O  
ANISOU 1062  O   HOH A   3     3075   2628   2825   -517    291   1025       O  
HETATM 1063  O   HOH A   4      23.718  -5.327  -7.386  1.00 28.62           O  
ANISOU 1063  O   HOH A   4     4609   3303   2960   -353   1832   -344       O  
HETATM 1064  O   HOH A   5      28.621 -13.579  -7.981  1.00 22.32           O  
ANISOU 1064  O   HOH A   5     3780   2254   2447   -151    270   -217       O  
HETATM 1065  O   HOH A   6      27.053   0.040  -0.230  1.00 16.88           O  
ANISOU 1065  O   HOH A   6     2396   1629   2387   -253    382     78       O  
HETATM 1066  O   HOH A   7      35.829   0.531   7.973  1.00 40.74           O  
ANISOU 1066  O   HOH A   7     7254   3849   4373   -666    109    777       O  
HETATM 1067  O   HOH A   8      14.910  -6.123   2.124  1.00 17.63           O  
ANISOU 1067  O   HOH A   8     2060   2051   2585     58    484    458       O  
HETATM 1068  O   HOH A   9      41.600 -13.323   5.232  1.00 26.80           O  
ANISOU 1068  O   HOH A   9     3538   2866   3778    550    106    542       O  
HETATM 1069  O   HOH A  10      21.114 -21.480  -4.451  1.00 23.60           O  
ANISOU 1069  O   HOH A  10     3679   2426   2861   -631    225   -148       O  
HETATM 1070  O   HOH A  11      36.975   0.156  -4.051  1.00 21.67           O  
ANISOU 1070  O   HOH A  11     3710   2152   2371   -863      2    234       O  
HETATM 1071  O   HOH A  12      14.120  -8.431   0.714  1.00 19.20           O  
ANISOU 1071  O   HOH A  12     1804   2613   2876   -136    145    208       O  
HETATM 1072  O   HOH A  13      29.464 -17.138  -3.228  1.00 20.82           O  
ANISOU 1072  O   HOH A  13     2785   2661   2464   -166    629   -221       O  
HETATM 1073  O   HOH A  14      38.820  -2.093  -6.500  1.00 28.38           O  
ANISOU 1073  O   HOH A  14     2955   4434   3394   -702    444   1203       O  
HETATM 1074  O   HOH A  15      26.374   6.982   1.065  1.00 27.03           O  
ANISOU 1074  O   HOH A  15     3688   3847   2734   -209    539    623       O  
HETATM 1075  O   HOH A  16      26.553   1.942   7.931  1.00 36.03           O  
ANISOU 1075  O   HOH A  16     5420   4596   3672     49    149   -569       O  
HETATM 1076  O   HOH A  17      19.482 -23.907   3.674  1.00 25.97           O  
ANISOU 1076  O   HOH A  17     3931   3337   2599   -920   -860    272       O  
HETATM 1077  O   HOH A  18      31.000  -9.090  -3.157  1.00 27.50           O  
ANISOU 1077  O   HOH A  18     3006   2462   4977   -925  -1475    835       O  
HETATM 1078  O   HOH A  19      32.980 -14.014  10.919  1.00 31.65           O  
ANISOU 1078  O   HOH A  19     4160   3660   4205    344    531    -60       O  
HETATM 1079  O   HOH A  20      22.755  -1.314  -5.344  1.00 29.22           O  
ANISOU 1079  O   HOH A  20     4740   3020   3342   -496   -407    230       O  
HETATM 1080  O   HOH A  21      20.280 -21.934   5.089  1.00 27.52           O  
ANISOU 1080  O   HOH A  21     4214   2924   3317  -1384   -306    115       O  
HETATM 1081  O   HOH A  22      21.187 -22.275   7.736  1.00 25.91           O  
ANISOU 1081  O   HOH A  22     4378   2428   3037   -261     25    262       O  
HETATM 1082  O   HOH A  23      24.296 -16.896  -7.591  1.00 23.55           O  
ANISOU 1082  O   HOH A  23     3566   2979   2401    135    743   -638       O  
HETATM 1083  O   HOH A  24      26.069 -24.556   0.741  1.00 31.86           O  
ANISOU 1083  O   HOH A  24     3772   3635   4695    190    660    290       O  
HETATM 1084  O   HOH A  25      27.211  -5.367  -8.354  1.00 33.36           O  
ANISOU 1084  O   HOH A  25     5029   2824   4822    109   -369    653       O  
HETATM 1085  O   HOH A  26      15.418   2.304   4.388  1.00 25.98           O  
ANISOU 1085  O   HOH A  26     3127   2930   3814    436    704    129       O  
HETATM 1086  O   HOH A  27      28.952 -18.494  12.652  1.00 29.16           O  
ANISOU 1086  O   HOH A  27     4163   3953   2961    -64    327    421       O  
HETATM 1087  O   HOH A  28      14.220   4.091   2.572  1.00 31.16           O  
ANISOU 1087  O   HOH A  28     4564   2830   4444   1076   1115    506       O  
HETATM 1088  O   HOH A  29      35.339 -13.376   9.635  1.00 30.33           O  
ANISOU 1088  O   HOH A  29     4743   4147   2631    441    846    185       O  
HETATM 1089  O   HOH A  30      28.856   0.001  16.087  1.00 34.47           O  
ANISOU 1089  O   HOH A  30     5457   4597   3040   -327    314     54       O  
HETATM 1090  O   HOH A  31       6.018   5.339  -6.675  1.00 36.92           O  
ANISOU 1090  O   HOH A  31     4349   4025   5654   1799    280    969       O  
HETATM 1091  O   HOH A  32      18.306   2.595  -4.268  1.00 29.31           O  
ANISOU 1091  O   HOH A  32     3757   3591   3788   -660    692    684       O  
HETATM 1092  O   HOH A  33      37.215 -16.425   8.800  1.00 34.39           O  
ANISOU 1092  O   HOH A  33     5085   2960   5020    449    219   1040       O  
HETATM 1093  O   HOH A  34      24.338 -15.181  17.886  1.00 38.34           O  
ANISOU 1093  O   HOH A  34     6996   4113   3457  -1010   1141    467       O  
HETATM 1094  O   HOH A  35      13.894  -3.278   8.168  1.00 48.40           O  
ANISOU 1094  O   HOH A  35     6192   5545   6649  -1251   1362     71       O  
HETATM 1095  O   HOH A  36       7.644   0.111  -1.823  1.00 32.51           O  
ANISOU 1095  O   HOH A  36     3053   3948   5348    227     16    463       O  
HETATM 1096  O   HOH A  37      27.007 -16.024  -8.052  1.00 38.14           O  
ANISOU 1096  O   HOH A  37     4542   5140   4808    476   1621   -741       O  
HETATM 1097  O   HOH A  38      24.257 -19.445  -6.819  1.00 41.12           O  
ANISOU 1097  O   HOH A  38     6635   3786   5203    471   1583   -374       O  
HETATM 1098  O   HOH A  39      11.623  -9.285   4.019  1.00 31.88           O  
ANISOU 1098  O   HOH A  39     4051   4029   4029    679    670    339       O  
HETATM 1099  O   HOH A  40      13.355   1.460   6.077  1.00 36.66           O  
ANISOU 1099  O   HOH A  40     4230   5034   4665    560   1360   -152       O  
HETATM 1100  O   HOH A  41      27.403 -15.679  18.850  1.00 27.10           O  
ANISOU 1100  O   HOH A  41     4957   2926   2412   -254   -335    314       O  
HETATM 1101  O   HOH A  42      30.438 -19.874  16.275  1.00 32.47           O  
ANISOU 1101  O   HOH A  42     5218   4239   2878    273    156   -158       O  
HETATM 1102  O   HOH A  43      22.701   6.568  -1.113  1.00 37.17           O  
ANISOU 1102  O   HOH A  43     4594   4328   5199    665    336     39       O  
HETATM 1103  O   HOH A  44      15.369  -7.619 -15.208  1.00 37.79           O  
ANISOU 1103  O   HOH A  44     5084   4565   4707    864   -323    387       O  
HETATM 1104  O   HOH A  45      19.887   5.721  -0.204  1.00 40.48           O  
ANISOU 1104  O   HOH A  45     6290   3411   5679     81    761    334       O  
HETATM 1105  O   HOH A  46      25.646 -20.014   0.468  1.00 33.53           O  
ANISOU 1105  O   HOH A  46     5965   3808   2964    631    145   -745       O  
HETATM 1106  O   HOH A  47      30.407 -14.376  19.075  1.00 35.97           O  
ANISOU 1106  O   HOH A  47     5406   3660   4600  -1040   1239     88       O  
HETATM 1107  O   HOH A  48       7.790  -4.791   0.785  1.00 28.58           O  
ANISOU 1107  O   HOH A  48     2415   3916   4526    120    721    514       O  
HETATM 1108  O   HOH A  49      24.760 -20.720  -2.248  1.00 33.42           O  
ANISOU 1108  O   HOH A  49     5169   4028   3500    742     21   -312       O  
HETATM 1109  O   HOH A  50      31.624   2.630  -4.634  1.00 29.54           O  
ANISOU 1109  O   HOH A  50     2996   4029   4198  -1104    131   -150       O  
HETATM 1110  O   HOH A  51      30.036  -6.845  15.377  1.00 34.61           O  
ANISOU 1110  O   HOH A  51     5549   4696   2903   -675    540   -241       O  
HETATM 1111  O   HOH A  52      32.910  -0.188   6.817  1.00 33.18           O  
ANISOU 1111  O   HOH A  52     4164   4147   4293   -965   1114    227       O  
HETATM 1112  O   HOH A  53      17.123   3.832   5.900  1.00 37.54           O  
ANISOU 1112  O   HOH A  53     4448   4496   5318    703    232  -2279       O  
HETATM 1113  O   HOH A  54      40.322   0.771  11.878  1.00 39.97           O  
ANISOU 1113  O   HOH A  54     5435   5562   4188   -450   -821    586       O  
HETATM 1114  O   HOH A  55       8.648  -3.560   3.057  1.00 38.08           O  
ANISOU 1114  O   HOH A  55     2947   5821   5700    405   1043   -248       O  
HETATM 1115  O   HOH A  56      24.119 -15.886 -10.195  1.00 39.38           O  
ANISOU 1115  O   HOH A  56     5835   4629   4495   -647   1004    255       O  
HETATM 1116  O   HOH A  57      32.634 -16.767  11.020  1.00 36.87           O  
ANISOU 1116  O   HOH A  57     5795   3657   4555   -321   1019    621       O  
HETATM 1117  O   HOH A  58      10.357 -11.899   5.671  1.00 36.43           O  
ANISOU 1117  O   HOH A  58     4412   5060   4370    353    620   -995       O  
HETATM 1118  O   HOH A  59      34.576  -9.609  15.381  1.00 37.71           O  
ANISOU 1118  O   HOH A  59     5533   5443   3350  -1126   -830     10       O  
HETATM 1119  O   HOH A  60      35.084   1.421  -5.420  1.00 36.38           O  
ANISOU 1119  O   HOH A  60     5917   4404   3499    593   -618   -125       O  
HETATM 1120  O   HOH A  61      19.874  -3.429  -8.866  1.00 34.72           O  
ANISOU 1120  O   HOH A  61     2512   6457   4220   -299   1133    322       O  
HETATM 1121  O   HOH A  62      15.903   6.059   3.656  1.00 38.11           O  
ANISOU 1121  O   HOH A  62     4791   4667   5018    309   -338   -704       O  
HETATM 1122  O   HOH A  63      18.219 -19.680  -7.185  1.00 33.83           O  
ANISOU 1122  O   HOH A  63     6917   2789   3148   -717  -1291    -82       O  
HETATM 1123  O   HOH A  64      13.605 -18.897   7.513  1.00 47.64           O  
ANISOU 1123  O   HOH A  64     4858   6823   6419  -2275     32    216       O  
HETATM 1124  O   HOH A  65      11.952   8.047  -5.889  1.00 43.15           O  
ANISOU 1124  O   HOH A  65     6754   3035   6605    501   -516    455       O  
HETATM 1125  O   HOH A  66      18.123  -4.404 -15.626  1.00 46.28           O  
ANISOU 1125  O   HOH A  66     4894   7914   4775  -1248    331   -348       O  
HETATM 1126  O   HOH A  67      22.631   8.179   3.352  1.00 46.50           O  
ANISOU 1126  O   HOH A  67     6175   7258   4233    650    638   1278       O  
HETATM 1127  O   HOH A  68      35.478 -17.744  10.365  1.00 41.31           O  
ANISOU 1127  O   HOH A  68     6312   5537   3845     50   -520   -150       O  
HETATM 1128  O   HOH A  69       9.207  -8.030  -5.946  1.00 39.68           O  
ANISOU 1128  O   HOH A  69     3052   5588   6433   -796   -255     32       O  
HETATM 1129  O   HOH A  70      42.863  -0.114   9.090  1.00 51.17           O  
ANISOU 1129  O   HOH A  70     6168   5716   7554  -2689  -1704   1753       O  
HETATM 1130  O   HOH A  71      36.340  -4.200  -8.405  1.00 40.42           O  
ANISOU 1130  O   HOH A  71     5539   8023   1793    -70    870    732       O  
HETATM 1131  O   HOH A  72       8.633  -9.696  -3.334  1.00 40.60           O  
ANISOU 1131  O   HOH A  72     4984   6056   4384    -85   -618   -927       O  
HETATM 1132  O   HOH A  73      23.472 -10.108 -11.765  1.00 45.61           O  
ANISOU 1132  O   HOH A  73     7967   6541   2818    120   -599    126       O  
HETATM 1133  O   HOH A  74       9.520 -10.457  -8.547  1.00 41.83           O  
ANISOU 1133  O   HOH A  74     4402   5992   5497  -1232   -933   1747       O  
HETATM 1134  O   HOH A  75      30.088 -19.939   4.661  1.00 42.95           O  
ANISOU 1134  O   HOH A  75     4989   5408   5922    159    724   1212       O  
HETATM 1135  O   HOH A  76      12.726 -16.258   0.408  1.00 34.18           O  
ANISOU 1135  O   HOH A  76     5052   2701   5231    257   -323  -1114       O  
HETATM 1136  O   HOH A  77       7.026  -6.724 -13.657  1.00 39.06           O  
ANISOU 1136  O   HOH A  77     5057   4262   5520   -721   -561    388       O  
HETATM 1137  O   HOH A  78      42.146 -10.639  -1.915  1.00 47.83           O  
ANISOU 1137  O   HOH A  78     6817   4637   6717     33    245    640       O  
HETATM 1138  O   HOH A  79      24.334 -26.979  10.134  1.00 39.04           O  
ANISOU 1138  O   HOH A  79     6208   4657   3968    -75   -864    208       O  
HETATM 1139  O   HOH A  80      43.042  -6.444  11.390  1.00 43.41           O  
ANISOU 1139  O   HOH A  80     6150   5660   4683    344  -1171    485       O  
HETATM 1140  O   HOH A  81       4.573  -4.882  -6.078  1.00 39.36           O  
ANISOU 1140  O   HOH A  81     2709   5853   6393   -614    151    633       O  
HETATM 1141  O   HOH A  82      10.946 -17.100   5.084  1.00 48.82           O  
ANISOU 1141  O   HOH A  82     8868   2264   7417  -2568   -700  -2480       O  
HETATM 1142  O   HOH A  83      33.003  -0.058  -4.925  1.00 45.20           O  
ANISOU 1142  O   HOH A  83     6767   5508   4897   1090    -42   2246       O  
HETATM 1143  O   HOH A  84      19.711   3.542  -2.046  1.00 39.11           O  
ANISOU 1143  O   HOH A  84     5643   4077   5138   1397  -1001     88       O  
HETATM 1144  O   HOH A  85      11.768 -19.286   5.794  1.00 41.05           O  
ANISOU 1144  O   HOH A  85     5960   5086   4548   -690    998  -2333       O  
HETATM 1145  O   HOH A  86      17.460 -21.464   6.288  1.00 40.36           O  
ANISOU 1145  O   HOH A  86     6707   3433   5194    361  -1377    135       O  
HETATM 1146  O   HOH A  87      31.535  -7.174  -6.964  1.00 35.00           O  
ANISOU 1146  O   HOH A  87     3172   4585   5541     77    -40  -2464       O  
HETATM 1147  O   HOH A  88      26.479 -10.725 -11.684  1.00 54.57           O  
ANISOU 1147  O   HOH A  88     8179   7514   5038  -1034    198   -246       O  
HETATM 1148  O   HOH A  89      42.307   0.117   4.123  1.00 50.78           O  
ANISOU 1148  O   HOH A  89     4307   5510   9477    886   -876     24       O  
HETATM 1149  O   HOH A  90      24.228   4.754  13.425  1.00 44.00           O  
ANISOU 1149  O   HOH A  90     6866   4324   5526    812    930  -1337       O  
HETATM 1150  O   HOH A  91       7.293  -8.646   0.953  1.00 45.48           O  
ANISOU 1150  O   HOH A  91     3554   7224   6501    426   1231     -7       O  
HETATM 1151  O   HOH A  92       6.312   2.808  -1.140  1.00 42.31           O  
ANISOU 1151  O   HOH A  92     3987   5329   6760   1018   -702   -542       O  
HETATM 1152  O   HOH A  93      38.225 -10.082  10.918  1.00 41.26           O  
ANISOU 1152  O   HOH A  93     4248   6655   4774    356   -377   2197       O  
HETATM 1153  O   HOH A  94      20.158  -0.019  -5.564  1.00 36.84           O  
ANISOU 1153  O   HOH A  94     4650   4652   4692    268   -533   1086       O  
HETATM 1154  O   HOH A  95      25.040 -23.509  -2.115  1.00 41.74           O  
ANISOU 1154  O   HOH A  95     5752   4916   5190   -427    815   -237       O  
HETATM 1155  O   HOH A  96      37.478 -12.685  11.386  1.00 44.39           O  
ANISOU 1155  O   HOH A  96     6358   5742   4763   -213   -776    579       O  
HETATM 1156  O   HOH A  97      17.459  -9.243  10.552  1.00 47.66           O  
ANISOU 1156  O   HOH A  97     4473   6501   7132    828    414  -1305       O  
HETATM 1157  O   HOH A  98      16.552  -6.739  10.613  1.00 51.78           O  
ANISOU 1157  O   HOH A  98     7173   7311   5187  -1434   2055    254       O  
HETATM 1158  O   HOH A  99      15.081 -12.066 -13.095  1.00 47.39           O  
ANISOU 1158  O   HOH A  99     6468   5750   5787   -700  -1711   -297       O  
HETATM 1159  O   HOH A 100      34.630 -14.154  13.733  1.00 46.52           O  
ANISOU 1159  O   HOH A 100     5808   6578   5288    489   -394   2131       O  
HETATM 1160  O   HOH A 101      33.617 -12.422  15.528  1.00 45.97           O  
ANISOU 1160  O   HOH A 101     5761   5571   6131   -877   -891    806       O  
HETATM 1161  O   HOH A 102      22.806 -16.985 -12.341  1.00 44.71           O  
ANISOU 1161  O   HOH A 102     6517   6225   4243    554    877    379       O  
HETATM 1162  O   HOH A 103      16.554 -14.786 -12.134  1.00 42.39           O  
ANISOU 1162  O   HOH A 103     6278   5019   4807   -525  -1710  -1560       O  
CONECT 1050 1051                                                                
CONECT 1051 1050 1052                                                           
CONECT 1052 1051 1053                                                           
CONECT 1053 1052 1054                                                           
CONECT 1054 1053 1055                                                           
CONECT 1055 1054 1056                                                           
CONECT 1056 1055 1057                                                           
CONECT 1057 1056 1058                                                           
CONECT 1058 1057 1059                                                           
CONECT 1059 1058                                                                
MASTER      293    0    1    5    6    0    2    6 1144    1   10   11          
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.