CNRS Nantes University UFIP UFIP
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***  ferredoxin  ***

elNémo ID: 22022216550615701

Job options:

ID        	=	 22022216550615701
JOBID     	=	 ferredoxin
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 ferredoxin

HEADER    ELECTRON TRANSPORT                      01-OCT-97   2FDN              
TITLE     2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDI-URICI                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERREDOXIN;                                                
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACIDURICI;                          
SOURCE   3 ORGANISM_TAXID: 1556;                                                
SOURCE   4 ATCC: 7906                                                           
KEYWDS    ELECTRON TRANSPORT, IRON-SULFUR, 4FE-4S                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.DAUTER,K.S.WILSON,L.C.SIEKER,J.MEYER,J.M.MOULIS                     
REVDAT   4   24-MAR-09 2FDN    1       ATOM   CONECT                            
REVDAT   3   24-FEB-09 2FDN    1       VERSN                                    
REVDAT   2   05-JAN-00 2FDN    1       REMARK                                   
REVDAT   1   08-APR-98 2FDN    0                                                
JRNL        AUTH   Z.DAUTER,K.S.WILSON,L.C.SIEKER,J.MEYER,J.M.MOULIS            
JRNL        TITL   ATOMIC RESOLUTION (0.94 A) STRUCTURE OF                      
JRNL        TITL 2 CLOSTRIDIUM ACIDURICI FERREDOXIN. DETAILED                   
JRNL        TITL 3 GEOMETRY OF [4FE-4S] CLUSTERS IN A PROTEIN.                  
JRNL        REF    BIOCHEMISTRY                  V.  36 16065 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9405040                                                      
JRNL        DOI    10.1021/BI972155Y                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.D.DUEE,E.FANCHON,J.VICAT,L.C.SIEKER,J.MEYER,               
REMARK   1  AUTH 2 J.M.MOULIS                                                   
REMARK   1  TITL   REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S]                   
REMARK   1  TITL 2 FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 A              
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 243   683 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.94 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELX                                                
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.94                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.100                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 47452                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.087                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 37200                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 381                                           
REMARK   3   NUCLEIC ACID ATOMS : NULL                                          
REMARK   3   HETEROGEN ATOMS    : 16                                            
REMARK   3   SOLVENT ATOMS      : 96                                            
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 472.00                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 272.00                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 6                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 5145                    
REMARK   3   NUMBER OF RESTRAINTS                     : 5081                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.027                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.038                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.017                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.360                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.033                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.075                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: SHELX SWAT                                            
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NO RESTRAINTS ON [4FE-4S] CLUSTERS        
REMARK   4                                                                      
REMARK   4 2FDN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6-7.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.883                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200   FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48300                            
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: TAKEN FROM PDB ENTRY         
REMARK 200  1FDN                                                                
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 55-60% AMMONIUM SULFATE, 100 MM          
REMARK 280  TRISMALEATE PH 6.6-7.0 MIXED 1:1 WITH 10 MG/ML PROTEIN              
REMARK 280  SOLUTION.                                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.41000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       16.97500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.11500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       16.97500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       18.70500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       16.97500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       56.11500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       16.97500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       18.70500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       37.41000            
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 149  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ILE A   4   C     ASN A   5   N       0.158                       
REMARK 500    SER A  10   CA    SER A  10   CB      0.426                       
REMARK 500    SER A  24   CA    SER A  24   CB      0.150                       
REMARK 500    VAL A  31   CA    VAL A  31   CB      0.167                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A   6   CA  -  C   -  N   ANGL. DEV. =  18.3 DEGREES          
REMARK 500    GLU A   6   O   -  C   -  N   ANGL. DEV. = -23.4 DEGREES          
REMARK 500    ALA A   7   C   -  N   -  CA  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    SER A  10   CB  -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    SER A  24   CB  -  CA  -  C   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    SER A  24   N   -  CA  -  CB  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ASP A  27   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A  28   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ARG A  29   CD  -  NE  -  CZ  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    TYR A  30   C   -  N   -  CA  ANGL. DEV. = -17.9 DEGREES          
REMARK 500    VAL A  31   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    VAL A  31   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    VAL A  31   CA  -  CB  -  CG2 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  27      -70.17    -57.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 61                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 62                  
DBREF  2FDN A    1    55  UNP    P00198   FER_CLOAC        1     55             
SEQRES   1 A   55  ALA TYR VAL ILE ASN GLU ALA CYS ILE SER CYS GLY ALA          
SEQRES   2 A   55  CYS GLU PRO GLU CYS PRO VAL ASN ALA ILE SER SER GLY          
SEQRES   3 A   55  ASP ASP ARG TYR VAL ILE ASP ALA ASP THR CYS ILE ASP          
SEQRES   4 A   55  CYS GLY ALA CYS ALA GLY VAL CYS PRO VAL ASP ALA PRO          
SEQRES   5 A   55  VAL GLN ALA                                                  
HET    SF4  A  61       8                                                       
HET    SF4  A  62       8                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
FORMUL   2  SF4    2(FE4 S4)                                                    
FORMUL   4  HOH   *94(H2 O)                                                     
HELIX    1   1 GLU A   15  GLU A   17  5                                   3    
HELIX    2   2 ALA A   42  VAL A   46  1                                   5    
SHEET    1   A 2 TYR A   2  ILE A   4  0                                        
SHEET    2   A 2 PRO A  52  GLN A  54 -1  N  VAL A  53   O  VAL A   3           
LINK        FE1  SF4 A  61                 SG  CYS A   8     1555   1555  2.26  
LINK        FE2  SF4 A  61                 SG  CYS A  11     1555   1555  2.27  
LINK        FE3  SF4 A  61                 SG  CYS A  14     1555   1555  2.23  
LINK        FE4  SF4 A  61                 SG  CYS A  47     1555   1555  2.25  
LINK        FE1  SF4 A  62                 SG  CYS A  37     1555   1555  2.28  
LINK        FE2  SF4 A  62                 SG  CYS A  40     1555   1555  2.28  
LINK        FE3  SF4 A  62                 SG  CYS A  43     1555   1555  2.26  
LINK        FE4  SF4 A  62                 SG  CYS A  18     1555   1555  2.28  
SITE     1 AC1  7 CYS A   8  ILE A   9  CYS A  11  GLY A  12                    
SITE     2 AC1  7 CYS A  14  TYR A  30  CYS A  47                               
SITE     1 AC2  8 CYS A  18  VAL A  20  ILE A  32  CYS A  37                    
SITE     2 AC2  8 ILE A  38  CYS A  40  GLY A  41  CYS A  43                    
CRYST1   33.950   33.950   74.820  90.00  90.00  90.00 P 43 21 2     8          
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      0.029455  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.029455  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013365        0.00000                         
ATOM      1  N   ALA A   1       9.251  24.410  64.133  1.00  7.34           N  
ANISOU    1  N   ALA A   1      972    917    833    -95    -41    211       N  
ATOM      2  CA  ALA A   1       8.069  23.677  64.576  1.00  6.49           C  
ANISOU    2  CA  ALA A   1     1140    752    513   -162   -141     42       C  
ATOM      3  C   ALA A   1       8.390  22.270  65.061  1.00  5.92           C  
ANISOU    3  C   ALA A   1      881    769    545    -25    -20     59       C  
ATOM      4  O   ALA A   1       9.055  21.505  64.383  1.00  7.19           O  
ANISOU    4  O   ALA A   1     1105    873    687     -4    227     60       O  
ATOM      5  CB  ALA A   1       7.045  23.569  63.447  1.00  8.54           C  
ANISOU    5  CB  ALA A   1     1367    715   1083    -97   -484     34       C  
ATOM      6  H1  ALA A   1       9.833  24.468  64.804  1.00 11.02           H  
ANISOU    6  H1  ALA A   1     1396   1396   1396      0      0      0       H  
ATOM      7  H2  ALA A   1       9.627  23.981  63.450  1.00 11.02           H  
ANISOU    7  H2  ALA A   1     1396   1396   1396      0      0      0       H  
ATOM      8  H3  ALA A   1       9.013  25.228  63.875  1.00 11.02           H  
ANISOU    8  H3  ALA A   1     1396   1396   1396      0      0      0       H  
ATOM      9  HA  ALA A   1       7.660  24.172  65.316  1.00  7.79           H  
ANISOU    9  HA  ALA A   1      987    987    987      0      0      0       H  
ATOM     10  HB1 ALA A   1       6.828  24.448  63.126  1.00 12.81           H  
ANISOU   10  HB1 ALA A   1     1622   1622   1622      0      0      0       H  
ATOM     11  HB2 ALA A   1       7.413  23.048  62.729  1.00 12.81           H  
ANISOU   11  HB2 ALA A   1     1622   1622   1622      0      0      0       H  
ATOM     12  HB3 ALA A   1       6.249  23.144  63.776  1.00 12.81           H  
ANISOU   12  HB3 ALA A   1     1622   1622   1622      0      0      0       H  
ATOM     13  N   TYR A   2       7.838  21.933  66.245  1.00  6.09           N  
ANISOU   13  N   TYR A   2      889    777    591    -87     -7     39       N  
ATOM     14  CA  TYR A   2       7.623  20.562  66.650  1.00  5.40           C  
ANISOU   14  CA  TYR A   2      765    734    501    -77     49     23       C  
ATOM     15  C   TYR A   2       6.330  20.099  65.992  1.00  5.69           C  
ANISOU   15  C   TYR A   2      751    828    531    -80      7     38       C  
ATOM     16  O   TYR A   2       5.482  20.919  65.598  1.00  6.18           O  
ANISOU   16  O   TYR A   2      829    831    631     66    -52     69       O  
ATOM     17  CB  TYR A   2       7.487  20.490  68.189  1.00  6.25           C  
ANISOU   17  CB  TYR A   2      887    923    505   -142    -97     15       C  
ATOM     18  CG  TYR A   2       8.817  20.343  68.914  1.00  5.95           C  
ANISOU   18  CG  TYR A   2      769    849    585    -79    -14     21       C  
ATOM     19  CD1 TYR A   2       9.872  21.185  68.706  1.00  6.32           C  
ANISOU   19  CD1 TYR A   2      854    793    695    -33   -120      2       C  
ATOM     20  CD2 TYR A   2       8.953  19.311  69.856  1.00  6.86           C  
ANISOU   20  CD2 TYR A   2      978    929    637   -139   -128     66       C  
ATOM     21  CE1 TYR A   2      11.087  21.049  69.416  1.00  6.88           C  
ANISOU   21  CE1 TYR A   2      852    956    740   -185    -89    -50       C  
ATOM     22  CE2 TYR A   2      10.152  19.162  70.542  1.00  7.62           C  
ANISOU   22  CE2 TYR A   2     1012   1007    806    -26   -132    106       C  
ATOM     23  CZ  TYR A   2      11.200  20.016  70.331  1.00  6.83           C  
ANISOU   23  CZ  TYR A   2      875   1024    632     62    -93     52       C  
ATOM     24  OH  TYR A   2      12.411  19.848  70.983  1.00  9.73           O  
ANISOU   24  OH  TYR A   2     1066   1596    944     92   -322    -63       O  
ATOM     25  H   TYR A   2       7.604  22.562  66.783  1.00  7.31           H  
ANISOU   25  H   TYR A   2      926    926    926      0      0      0       H  
ATOM     26  HA  TYR A   2       8.371  20.002  66.353  1.00  6.48           H  
ANISOU   26  HA  TYR A   2      821    821    821      0      0      0       H  
ATOM     27  HB2 TYR A   2       7.048  21.296  68.503  1.00  7.50           H  
ANISOU   27  HB2 TYR A   2      950    950    950      0      0      0       H  
ATOM     28  HB3 TYR A   2       6.921  19.737  68.419  1.00  7.50           H  
ANISOU   28  HB3 TYR A   2      950    950    950      0      0      0       H  
ATOM     29  HD1 TYR A   2       9.788  21.868  68.080  1.00  7.58           H  
ANISOU   29  HD1 TYR A   2      960    960    960      0      0      0       H  
ATOM     30  HD2 TYR A   2       8.244  18.732  70.020  1.00  8.24           H  
ANISOU   30  HD2 TYR A   2     1044   1044   1044      0      0      0       H  
ATOM     31  HE1 TYR A   2      11.793  21.638  69.272  1.00  8.25           H  
ANISOU   31  HE1 TYR A   2     1045   1045   1045      0      0      0       H  
ATOM     32  HE2 TYR A   2      10.244  18.469  71.155  1.00  9.15           H  
ANISOU   32  HE2 TYR A   2     1159   1159   1159      0      0      0       H  
ATOM     33  HH  TYR A   2      12.370  19.190  71.471  1.00 14.59           H  
ANISOU   33  HH  TYR A   2     1848   1848   1848      0      0      0       H  
ATOM     34  N   VAL A   3       6.191  18.755  65.886  1.00  5.72           N  
ANISOU   34  N   VAL A   3      812    690    619   -121     -6     48       N  
ATOM     35  CA  VAL A   3       4.953  18.156  65.421  1.00  5.29           C  
ANISOU   35  CA  VAL A   3      830    717    416    -20    -47     12       C  
ATOM     36  C   VAL A   3       4.620  17.028  66.417  1.00  5.56           C  
ANISOU   36  C   VAL A   3      777    802    484    -25    110    110       C  
ATOM     37  O   VAL A   3       5.528  16.340  66.899  1.00  6.03           O  
ANISOU   37  O   VAL A   3      785    811    639      7    -23    170       O  
ATOM     38  CB  VAL A   3       5.060  17.643  63.976  1.00  5.58           C  
ANISOU   38  CB  VAL A   3      830    756    481    -85    -28     60       C  
ATOM     39  CG1 VAL A   3       6.062  16.528  63.828  1.00  7.36           C  
ANISOU   39  CG1 VAL A   3     1056    991    681     99    -63   -289       C  
ATOM     40  CG2 VAL A   3       3.716  17.243  63.399  1.00  6.93           C  
ANISOU   40  CG2 VAL A   3      904   1184    481    -83    -55     -3       C  
ATOM     41  H   VAL A   3       6.851  18.245  66.100  1.00  6.87           H  
ANISOU   41  H   VAL A   3      870    870    870      0      0      0       H  
ATOM     42  HA  VAL A   3       4.243  18.831  65.463  1.00  6.35           H  
ANISOU   42  HA  VAL A   3      804    804    804      0      0      0       H  
ATOM     43  HB  VAL A   3       5.388  18.391  63.435  1.00  6.69           H  
ANISOU   43  HB  VAL A   3      847    847    847      0      0      0       H  
ATOM     44 HG11 VAL A   3       6.901  16.799  64.208  1.00 11.05           H  
ANISOU   44 HG11 VAL A   3     1399   1399   1399      0      0      0       H  
ATOM     45 HG12 VAL A   3       5.741  15.746  64.285  1.00 11.05           H  
ANISOU   45 HG12 VAL A   3     1399   1399   1399      0      0      0       H  
ATOM     46 HG13 VAL A   3       6.183  16.327  62.897  1.00 11.05           H  
ANISOU   46 HG13 VAL A   3     1399   1399   1399      0      0      0       H  
ATOM     47 HG21 VAL A   3       3.093  17.966  63.507  1.00 10.40           H  
ANISOU   47 HG21 VAL A   3     1317   1317   1317      0      0      0       H  
ATOM     48 HG22 VAL A   3       3.815  17.043  62.466  1.00 10.40           H  
ANISOU   48 HG22 VAL A   3     1317   1317   1317      0      0      0       H  
ATOM     49 HG23 VAL A   3       3.388  16.467  63.860  1.00 10.40           H  
ANISOU   49 HG23 VAL A   3     1317   1317   1317      0      0      0       H  
ATOM     50  N   ILE A   4       3.350  16.850  66.710  1.00  5.58           N  
ANISOU   50  N   ILE A   4      830    702    537    -88    -30     70       N  
ATOM     51  CA  ILE A   4       2.915  15.799  67.650  1.00  5.34           C  
ANISOU   51  CA  ILE A   4      757    747    474   -108    -41    120       C  
ATOM     52  C   ILE A   4       2.634  14.548  66.867  1.00  6.15           C  
ANISOU   52  C   ILE A   4      906    739    636    -73      5     32       C  
ATOM     53  O   ILE A   4       1.734  14.471  65.999  1.00  6.87           O  
ANISOU   53  O   ILE A   4     1171    814    559    -53   -118     -5       O  
ATOM     54  CB  ILE A   4       1.703  16.272  68.471  1.00  5.88           C  
ANISOU   54  CB  ILE A   4      797    818    565    -11    -51     82       C  
ATOM     55  CG1 ILE A   4       2.099  17.423  69.396  1.00  6.67           C  
ANISOU   55  CG1 ILE A   4      960    851    660     19     65     31       C  
ATOM     56  CG2 ILE A   4       1.131  15.093  69.267  1.00  6.83           C  
ANISOU   56  CG2 ILE A   4     1019    819    695     16    201    130       C  
ATOM     57  CD1 ILE A   4       0.999  18.112  70.168  1.00  7.28           C  
ANISOU   57  CD1 ILE A   4     1027   1010    662    131    139     55       C  
ATOM     58  H   ILE A   4       2.760  17.358  66.344  1.00  6.70           H  
ANISOU   58  H   ILE A   4      849    849    849      0      0      0       H  
ATOM     59  HA  ILE A   4       3.652  15.616  68.269  1.00  6.40           H  
ANISOU   59  HA  ILE A   4      811    811    811      0      0      0       H  
ATOM     60  HB  ILE A   4       1.014  16.593  67.852  1.00  7.06           H  
ANISOU   60  HB  ILE A   4      894    894    894      0      0      0       H  
ATOM     61 HG12 ILE A   4       2.744  17.083  70.036  1.00  8.00           H  
ANISOU   61 HG12 ILE A   4     1013   1013   1013      0      0      0       H  
ATOM     62 HG13 ILE A   4       2.552  18.094  68.861  1.00  8.00           H  
ANISOU   62 HG13 ILE A   4     1013   1013   1013      0      0      0       H  
ATOM     63 HG21 ILE A   4       0.889  14.387  68.664  1.00 10.25           H  
ANISOU   63 HG21 ILE A   4     1298   1298   1298      0      0      0       H  
ATOM     64 HG22 ILE A   4       1.792  14.774  69.886  1.00 10.25           H  
ANISOU   64 HG22 ILE A   4     1298   1298   1298      0      0      0       H  
ATOM     65 HG23 ILE A   4       0.353  15.381  69.750  1.00 10.25           H  
ANISOU   65 HG23 ILE A   4     1298   1298   1298      0      0      0       H  
ATOM     66 HD11 ILE A   4       0.556  17.473  70.732  1.00 10.93           H  
ANISOU   66 HD11 ILE A   4     1384   1384   1384      0      0      0       H  
ATOM     67 HD12 ILE A   4       1.376  18.809  70.709  1.00 10.93           H  
ANISOU   67 HD12 ILE A   4     1384   1384   1384      0      0      0       H  
ATOM     68 HD13 ILE A   4       0.365  18.490  69.554  1.00 10.93           H  
ANISOU   68 HD13 ILE A   4     1384   1384   1384      0      0      0       H  
ATOM     69  N  AASN A   5       3.371  13.521  67.230  0.74  5.18           N  
ANISOU   69  N  AASN A   5      705    716    500    -96    205     31       N  
ATOM     70  N  BASN A   5       3.616  13.422  66.888  0.26  5.66           N  
ANISOU   70  N  BASN A   5      886    901    310     -7    187    -21       N  
ATOM     71  CA AASN A   5       3.263  12.221  66.573  0.74  5.54           C  
ANISOU   71  CA AASN A   5      811    798    442    102    132    -54       C  
ATOM     72  CA BASN A   5       3.556  12.199  66.089  0.26  7.76           C  
ANISOU   72  CA BASN A   5     1126    942    807    -15    356   -253       C  
ATOM     73  C  AASN A   5       2.056  11.443  67.105  0.74  5.91           C  
ANISOU   73  C  AASN A   5      881    756    551    -46    125     33       C  
ATOM     74  C  BASN A   5       2.435  11.270  66.583  0.26  7.41           C  
ANISOU   74  C  BASN A   5     1116    846    784     21    173   -116       C  
ATOM     75  O  AASN A   5       1.502  11.750  68.194  0.74  6.03           O  
ANISOU   75  O  AASN A   5      761    903    572    -17    136   -123       O  
ATOM     76  O  BASN A   5       1.669  11.594  67.491  0.26  7.16           O  
ANISOU   76  O  BASN A   5      760    525   1369   -105    276   -201       O  
ATOM     77  CB AASN A   5       4.526  11.410  66.788  0.74  5.70           C  
ANISOU   77  CB AASN A   5      811    955    346    162     37    -43       C  
ATOM     78  CB BASN A   5       4.902  11.484  66.094  0.26  8.86           C  
ANISOU   78  CB BASN A   5     1188   1007   1089     14    294   -399       C  
ATOM     79  CG AASN A   5       5.748  11.875  66.000  0.74  5.72           C  
ANISOU   79  CG AASN A   5      774    843    502     31     89   -143       C  
ATOM     80  CG BASN A   5       5.365  10.887  67.402  0.26 10.16           C  
ANISOU   80  CG BASN A   5     1443   1008   1316    231    158   -264       C  
ATOM     81  OD1AASN A   5       5.620  12.537  64.978  0.74  7.05           O  
ANISOU   81  OD1AASN A   5      867   1062    685     49    131    174       O  
ATOM     82  OD1BASN A   5       4.539  10.622  68.284  0.26 10.07           O  
ANISOU   82  OD1BASN A   5     1762    854   1117    308    276   -330       O  
ATOM     83  ND2AASN A   5       6.927  11.436  66.443  0.74  6.57           N  
ANISOU   83  ND2AASN A   5      826    854    756    233    125   -133       N  
ATOM     84  ND2BASN A   5       6.689  10.730  67.537  0.26 13.07           N  
ANISOU   84  ND2BASN A   5     1431    993   2421     23    -68    218       N  
ATOM     85  N  AGLU A   6       1.690  10.405  66.377  0.74  6.37           N  
ANISOU   85  N  AGLU A   6      745    991    626    -22     -4   -131       N  
ATOM     86  N  BGLU A   6       2.298  10.117  65.940  0.26  8.93           N  
ANISOU   86  N  BGLU A   6     1493    925    889    -98    294   -172       N  
ATOM     87  CA AGLU A   6       0.527   9.550  66.692  0.74  7.35           C  
ANISOU   87  CA AGLU A   6     1043    862    819   -166     17   -129       C  
ATOM     88  CA BGLU A   6       1.226   9.148  66.146  0.26  9.95           C  
ANISOU   88  CA BGLU A   6     1561   1204    921   -303     14   -264       C  
ATOM     89  C  AGLU A   6       0.678   8.779  67.984  0.74  8.00           C  
ANISOU   89  C  AGLU A   6     1120    966    878   -178    181   -119       C  
ATOM     90  C  BGLU A   6       1.277   8.517  67.502  0.26  8.97           C  
ANISOU   90  C  BGLU A   6     1395    816   1114   -436    -47   -170       C  
ATOM     91  O  AGLU A   6      -0.337   8.331  68.503  0.74  8.94           O  
ANISOU   91  O  AGLU A   6     1259   1012   1043   -448    244    -59       O  
ATOM     92  O  BGLU A   6       0.467   7.697  67.916  0.26 10.02           O  
ANISOU   92  O  BGLU A   6     1447    848   1418   -416    518   -438       O  
ATOM     93  CB AGLU A   6       0.262   8.558  65.543  0.74  8.44           C  
ANISOU   93  CB AGLU A   6     1171   1045    913   -137   -158   -164       C  
ATOM     94  CB BGLU A   6       1.265   8.176  64.958  0.26 11.56           C  
ANISOU   94  CB BGLU A   6     1931   1067   1288    -30    173   -449       C  
ATOM     95  CG AGLU A   6       1.395   7.529  65.328  0.74 12.64           C  
ANISOU   95  CG AGLU A   6     1895   1047   1744     69    525   -337       C  
ATOM     96  CG BGLU A   6       0.657   6.796  65.120  0.26 15.43           C  
ANISOU   96  CG BGLU A   6     2271    999   2450    -73      8   -460       C  
ATOM     97  CD AGLU A   6       1.114   6.232  66.065  0.74 14.79           C  
ANISOU   97  CD AGLU A   6     2388   1224   1869    302    250     55       C  
ATOM     98  CD BGLU A   6      -0.013   6.380  63.825  0.26 17.09           C  
ANISOU   98  CD BGLU A   6     2608   1241   2485   -238    130   -867       C  
ATOM     99  OE1AGLU A   6       0.035   5.613  65.869  0.74 28.30           O  
ANISOU   99  OE1AGLU A   6     3218   1840   5428   -818    202    466       O  
ATOM    100  OE1BGLU A   6       0.506   6.859  62.800  0.26 17.06           O  
ANISOU  100  OE1BGLU A   6     2737    966   2620   -435   -774    122       O  
ATOM    101  OE2AGLU A   6       1.993   5.751  66.870  0.74 23.85           O  
ANISOU  101  OE2AGLU A   6     4096   3242   1502   2110     51    -76       O  
ATOM    102  OE2BGLU A   6      -1.020   5.632  63.836  0.26 24.09           O  
ANISOU  102  OE2BGLU A   6     3638   2979   2311  -1528   -220   -339       O  
ATOM    103  N   ALA A   7       1.928   8.721  68.571  1.00  8.58           N  
ANISOU  103  N   ALA A   7     1321    901    958    -60    -30    -90       N  
ATOM    104  CA  ALA A   7       1.995   8.187  69.921  1.00  8.79           C  
ANISOU  104  CA  ALA A   7     1390    849   1017      0    170    132       C  
ATOM    105  C   ALA A   7       1.166   8.934  70.905  1.00  7.78           C  
ANISOU  105  C   ALA A   7     1171    841    871   -114    -32    -38       C  
ATOM    106  O   ALA A   7       0.813   8.411  71.999  1.00  8.81           O  
ANISOU  106  O   ALA A   7     1528    938    800    -30     69     86       O  
ATOM    107  CB  ALA A   7       3.431   8.148  70.388  1.00 10.78           C  
ANISOU  107  CB  ALA A   7     1381   1575   1037    380    284    410       C  
ATOM    108  H   ALA A   7       2.633   8.987  68.157  1.00 10.30           H  
ANISOU  108  H   ALA A   7     1305   1305   1305      0      0      0       H  
ATOM    109  HA  ALA A   7       1.665   7.265  69.893  1.00 10.54           H  
ANISOU  109  HA  ALA A   7     1335   1335   1335      0      0      0       H  
ATOM    110  HB1 ALA A   7       3.960   7.660  69.754  1.00 16.16           H  
ANISOU  110  HB1 ALA A   7     2047   2047   2047      0      0      0       H  
ATOM    111  HB2 ALA A   7       3.767   9.044  70.464  1.00 16.16           H  
ANISOU  111  HB2 ALA A   7     2047   2047   2047      0      0      0       H  
ATOM    112  HB3 ALA A   7       3.477   7.716  71.244  1.00 16.16           H  
ANISOU  112  HB3 ALA A   7     2047   2047   2047      0      0      0       H  
ATOM    113  N   CYS A   8       0.827  10.188  70.627  1.00  7.12           N  
ANISOU  113  N   CYS A   8      923    905    810   -125    -24     67       N  
ATOM    114  CA  CYS A   8      -0.005  10.954  71.514  1.00  6.69           C  
ANISOU  114  CA  CYS A   8      932    909    637    -68     52     82       C  
ATOM    115  C   CYS A   8      -1.211  10.172  71.965  1.00  7.01           C  
ANISOU  115  C   CYS A   8      960    926    711    -72     21     66       C  
ATOM    116  O   CYS A   8      -1.966   9.597  71.160  1.00  8.01           O  
ANISOU  116  O   CYS A   8     1100   1155    712   -213     24     14       O  
ATOM    117  CB  CYS A   8      -0.447  12.219  70.740  1.00  6.46           C  
ANISOU  117  CB  CYS A   8      814    939    641   -168    -61     19       C  
ATOM    118  SG  CYS A   8      -1.541  13.335  71.688  1.00  6.39           S  
ANISOU  118  SG  CYS A   8      875    897    597   -142    -21     90       S  
ATOM    119  H   CYS A   8       1.111  10.549  69.900  1.00  8.54           H  
ANISOU  119  H   CYS A   8     1082   1082   1082      0      0      0       H  
ATOM    120  HA  CYS A   8       0.519  11.222  72.298  1.00  8.02           H  
ANISOU  120  HA  CYS A   8     1016   1016   1016      0      0      0       H  
ATOM    121  HB2 CYS A   8       0.344  12.712  70.473  1.00  7.76           H  
ANISOU  121  HB2 CYS A   8      983    983    983      0      0      0       H  
ATOM    122  HB3 CYS A   8      -0.908  11.943  69.932  1.00  7.76           H  
ANISOU  122  HB3 CYS A   8      983    983    983      0      0      0       H  
ATOM    123  N   ILE A   9      -1.425  10.165  73.294  1.00  7.24           N  
ANISOU  123  N   ILE A   9     1038    967    677   -368    -51    162       N  
ATOM    124  CA  ILE A   9      -2.547   9.522  73.966  1.00  7.25           C  
ANISOU  124  CA  ILE A   9     1003    922    764   -351     44    149       C  
ATOM    125  C   ILE A   9      -3.635  10.480  74.373  1.00  7.15           C  
ANISOU  125  C   ILE A   9      984    915    751   -263    -54    150       C  
ATOM    126  O   ILE A   9      -4.593  10.110  74.993  1.00  8.44           O  
ANISOU  126  O   ILE A   9     1045   1178    905   -379    143    229       O  
ATOM    127  CB  ILE A   9      -2.081   8.645  75.137  1.00  7.72           C  
ANISOU  127  CB  ILE A   9     1150    867    843   -156     -6    232       C  
ATOM    128  CG1 ILE A   9      -1.486   9.532  76.246  1.00  8.56           C  
ANISOU  128  CG1 ILE A   9     1180   1134    857   -300     43    186       C  
ATOM    129  CG2 ILE A   9      -1.093   7.611  74.637  1.00  9.03           C  
ANISOU  129  CG2 ILE A   9     1209   1025   1112   -173     45    194       C  
ATOM    130  CD1 ILE A   9      -0.849   8.738  77.431  1.00  8.42           C  
ANISOU  130  CD1 ILE A   9     1053   1141    928    -78     -5    107       C  
ATOM    131  H   ILE A   9      -0.851  10.573  73.788  1.00  8.69           H  
ANISOU  131  H   ILE A   9     1101   1101   1101      0      0      0       H  
ATOM    132  HA  ILE A   9      -2.947   8.913  73.310  1.00  8.71           H  
ANISOU  132  HA  ILE A   9     1103   1103   1103      0      0      0       H  
ATOM    133  HB  ILE A   9      -2.861   8.177  75.502  1.00  9.26           H  
ANISOU  133  HB  ILE A   9     1173   1173   1173      0      0      0       H  
ATOM    134 HG12 ILE A   9      -0.807  10.105  75.855  1.00 10.27           H  
ANISOU  134 HG12 ILE A   9     1301   1301   1301      0      0      0       H  
ATOM    135 HG13 ILE A   9      -2.186  10.105  76.596  1.00 10.27           H  
ANISOU  135 HG13 ILE A   9     1301   1301   1301      0      0      0       H  
ATOM    136 HG21 ILE A   9      -0.338   8.053  74.243  1.00 13.54           H  
ANISOU  136 HG21 ILE A   9     1715   1715   1715      0      0      0       H  
ATOM    137 HG22 ILE A   9      -0.798   7.069  75.373  1.00 13.54           H  
ANISOU  137 HG22 ILE A   9     1715   1715   1715      0      0      0       H  
ATOM    138 HG23 ILE A   9      -1.518   7.054  73.980  1.00 13.54           H  
ANISOU  138 HG23 ILE A   9     1715   1715   1715      0      0      0       H  
ATOM    139 HD11 ILE A   9      -1.517   8.183  77.840  1.00 12.63           H  
ANISOU  139 HD11 ILE A   9     1600   1600   1600      0      0      0       H  
ATOM    140 HD12 ILE A   9      -0.135   8.188  77.101  1.00 12.63           H  
ANISOU  140 HD12 ILE A   9     1600   1600   1600      0      0      0       H  
ATOM    141 HD13 ILE A   9      -0.504   9.355  78.081  1.00 12.63           H  
ANISOU  141 HD13 ILE A   9     1600   1600   1600      0      0      0       H  
ATOM    142  N   SER A  10      -3.470  11.783  73.969  1.00  7.27           N  
ANISOU  142  N   SER A  10      897    998    800   -216      2     90       N  
ATOM    143  CA  SER A  10      -4.494  12.776  74.152  1.00  7.29           C  
ANISOU  143  CA  SER A  10      751   1088    862   -118    -40    161       C  
ATOM    144  C   SER A  10      -4.846  12.994  75.618  1.00  7.80           C  
ANISOU  144  C   SER A  10      977   1035    878   -225     65    137       C  
ATOM    145  O   SER A  10      -5.977  13.297  75.993  1.00  9.17           O  
ANISOU  145  O   SER A  10     1005   1342   1050    -57    206    236       O  
ATOM    146  CB ASER A  10      -5.758  12.479  73.324  0.87  8.59           C  
ANISOU  146  CB ASER A  10      874   1378    931   -468   -149    414       C  
ATOM    147  CB BSER A  10      -6.314  12.280  73.653  0.13 10.12           C  
ANISOU  147  CB BSER A  10      883   1864   1003   -396   -327    720       C  
ATOM    148  OG ASER A  10      -5.447  12.625  71.957  0.87 10.53           O  
ANISOU  148  OG ASER A  10     1140   1881    881   -308   -188    224       O  
ATOM    149  OG BSER A  10      -6.533  13.408  72.827  0.13  7.85           O  
ANISOU  149  OG BSER A  10      684    866   1360     82   -106    105       O  
ATOM    150  H   SER A  10      -2.731  12.012  73.595  1.00  8.73           H  
ANISOU  150  H   SER A  10     1106   1106   1106      0      0      0       H  
ATOM    151  N   CYS A  11      -3.777  13.038  76.438  1.00  8.01           N  
ANISOU  151  N   CYS A  11     1022   1109    839   -253    109    131       N  
ATOM    152  CA  CYS A  11      -3.888  13.275  77.864  1.00  8.12           C  
ANISOU  152  CA  CYS A  11     1087   1189    734   -213    199    190       C  
ATOM    153  C   CYS A  11      -4.135  14.793  78.195  1.00  8.68           C  
ANISOU  153  C   CYS A  11     1156   1165    897   -133    103    108       C  
ATOM    154  O   CYS A  11      -4.584  15.157  79.301  1.00  9.90           O  
ANISOU  154  O   CYS A  11     1313   1432    923     13    318    198       O  
ATOM    155  CB  CYS A  11      -2.648  12.804  78.576  1.00  8.44           C  
ANISOU  155  CB  CYS A  11     1249   1108    770   -138    186    229       C  
ATOM    156  SG  CYS A  11      -1.126  13.800  78.370  1.00  7.60           S  
ANISOU  156  SG  CYS A  11     1124   1072    618   -165     53    165       S  
ATOM    157  H   CYS A  11      -2.995  12.920  76.100  1.00  9.62           H  
ANISOU  157  H   CYS A  11     1218   1218   1218      0      0      0       H  
ATOM    158  HA  CYS A  11      -4.650  12.760  78.201  1.00  9.74           H  
ANISOU  158  HA  CYS A  11     1234   1234   1234      0      0      0       H  
ATOM    159  HB2 CYS A  11      -2.849  12.756  79.524  1.00 10.12           H  
ANISOU  159  HB2 CYS A  11     1282   1282   1282      0      0      0       H  
ATOM    160  HB3 CYS A  11      -2.457  11.901  78.277  1.00 10.12           H  
ANISOU  160  HB3 CYS A  11     1282   1282   1282      0      0      0       H  
ATOM    161  N   GLY A  12      -3.738  15.652  77.270  1.00  7.95           N  
ANISOU  161  N   GLY A  12     1038   1035    874   -111    221     88       N  
ATOM    162  CA  GLY A  12      -3.893  17.080  77.465  1.00  8.73           C  
ANISOU  162  CA  GLY A  12     1056   1107   1070   -119     41     48       C  
ATOM    163  C   GLY A  12      -2.834  17.791  78.224  1.00  8.09           C  
ANISOU  163  C   GLY A  12     1253    957    787    -77     94    188       C  
ATOM    164  O   GLY A  12      -2.881  18.996  78.347  1.00  9.08           O  
ANISOU  164  O   GLY A  12     1117   1049   1200    -82     37     -8       O  
ATOM    165  H   GLY A  12      -3.383  15.359  76.544  1.00  9.54           H  
ANISOU  165  H   GLY A  12     1208   1208   1208      0      0      0       H  
ATOM    166  HA2 GLY A  12      -3.963  17.494  76.591  1.00 10.47           H  
ANISOU  166  HA2 GLY A  12     1326   1326   1326      0      0      0       H  
ATOM    167  HA3 GLY A  12      -4.737  17.229  77.920  1.00 10.47           H  
ANISOU  167  HA3 GLY A  12     1326   1326   1326      0      0      0       H  
ATOM    168  N   ALA A  13      -1.828  17.117  78.775  1.00  7.71           N  
ANISOU  168  N   ALA A  13     1204    981    672   -148     29    108       N  
ATOM    169  CA  ALA A  13      -0.928  17.732  79.727  1.00  8.17           C  
ANISOU  169  CA  ALA A  13     1341    955    732    -77     -4     19       C  
ATOM    170  C   ALA A  13      -0.109  18.871  79.150  1.00  7.20           C  
ANISOU  170  C   ALA A  13     1071    959    637     59    -67     35       C  
ATOM    171  O   ALA A  13       0.287  19.812  79.846  1.00  8.49           O  
ANISOU  171  O   ALA A  13     1333   1053    759   -128   -120     36       O  
ATOM    172  CB  ALA A  13      -0.003  16.702  80.342  1.00  8.67           C  
ANISOU  172  CB  ALA A  13     1350   1056    808    -81    -51    162       C  
ATOM    173  H   ALA A  13      -1.709  16.292  78.560  1.00  9.25           H  
ANISOU  173  H   ALA A  13     1172   1172   1172      0      0      0       H  
ATOM    174  HA  ALA A  13      -1.475  18.103  80.450  1.00  9.81           H  
ANISOU  174  HA  ALA A  13     1242   1242   1242      0      0      0       H  
ATOM    175  HB1 ALA A  13      -0.523  15.982  80.705  1.00 13.01           H  
ANISOU  175  HB1 ALA A  13     1648   1648   1648      0      0      0       H  
ATOM    176  HB2 ALA A  13       0.589  16.361  79.668  1.00 13.01           H  
ANISOU  176  HB2 ALA A  13     1648   1648   1648      0      0      0       H  
ATOM    177  HB3 ALA A  13       0.511  17.111  81.042  1.00 13.01           H  
ANISOU  177  HB3 ALA A  13     1648   1648   1648      0      0      0       H  
ATOM    178  N   CYS A  14       0.237  18.760  77.837  1.00  6.89           N  
ANISOU  178  N   CYS A  14      955    851    746    -17    -39     79       N  
ATOM    179  CA  CYS A  14       1.110  19.738  77.201  1.00  6.86           C  
ANISOU  179  CA  CYS A  14      875    903    765     -9    -20      5       C  
ATOM    180  C   CYS A  14       0.405  21.023  76.908  1.00  7.24           C  
ANISOU  180  C   CYS A  14      977    876    829    -60    -34    -35       C  
ATOM    181  O   CYS A  14       1.102  22.090  76.773  1.00  8.24           O  
ANISOU  181  O   CYS A  14     1116    909   1027   -137     87    -23       O  
ATOM    182  CB  CYS A  14       1.670  19.175  75.881  1.00  7.03           C  
ANISOU  182  CB  CYS A  14      902    886    816    -45     80     70       C  
ATOM    183  SG  CYS A  14       0.347  18.607  74.751  1.00  7.02           S  
ANISOU  183  SG  CYS A  14     1045    887    670      1    -72     95       S  
ATOM    184  H   CYS A  14      -0.065  18.101  77.375  1.00  8.27           H  
ANISOU  184  H   CYS A  14     1047   1047   1047      0      0      0       H  
ATOM    185  HA  CYS A  14       1.860  19.925  77.803  1.00  8.23           H  
ANISOU  185  HA  CYS A  14     1042   1042   1042      0      0      0       H  
ATOM    186  HB2 CYS A  14       2.193  19.862  75.439  1.00  8.43           H  
ANISOU  186  HB2 CYS A  14     1068   1068   1068      0      0      0       H  
ATOM    187  HB3 CYS A  14       2.261  18.432  76.078  1.00  8.43           H  
ANISOU  187  HB3 CYS A  14     1068   1068   1068      0      0      0       H  
ATOM    188  N   GLU A  15      -0.888  21.066  76.740  1.00  7.07           N  
ANISOU  188  N   GLU A  15      968    923    728      1    -27     59       N  
ATOM    189  CA  GLU A  15      -1.558  22.252  76.239  1.00  7.37           C  
ANISOU  189  CA  GLU A  15     1098    960    673     22    114     54       C  
ATOM    190  C   GLU A  15      -1.323  23.460  77.087  1.00  7.58           C  
ANISOU  190  C   GLU A  15     1125    973    711     30    134      2       C  
ATOM    191  O   GLU A  15      -0.976  24.536  76.558  1.00  8.42           O  
ANISOU  191  O   GLU A  15     1458    990    672    153    166     82       O  
ATOM    192  CB  GLU A  15      -3.023  21.956  75.954  1.00  7.84           C  
ANISOU  192  CB  GLU A  15      945   1148    812     51     82     60       C  
ATOM    193  CG  GLU A  15      -3.795  23.121  75.415  1.00  9.12           C  
ANISOU  193  CG  GLU A  15     1180   1174   1026    129    199     74       C  
ATOM    194  CD  GLU A  15      -5.209  22.843  75.007  1.00 13.19           C  
ANISOU  194  CD  GLU A  15     1123   1917   1847    257    -28    545       C  
ATOM    195  OE1 GLU A  15      -5.690  21.747  75.202  1.00 23.75           O  
ANISOU  195  OE1 GLU A  15     1541   1776   5485   -194   -910   -113       O  
ATOM    196  OE2 GLU A  15      -5.972  23.740  74.616  1.00 18.97           O  
ANISOU  196  OE2 GLU A  15     1872   2766   2393    960   -253    641       O  
ATOM    197  H   GLU A  15      -1.357  20.371  76.931  1.00  8.48           H  
ANISOU  197  H   GLU A  15     1074   1074   1074      0      0      0       H  
ATOM    198  HA  GLU A  15      -1.148  22.448  75.370  1.00  8.85           H  
ANISOU  198  HA  GLU A  15     1121   1121   1121      0      0      0       H  
ATOM    199  HB2 GLU A  15      -3.074  21.227  75.316  1.00  9.41           H  
ANISOU  199  HB2 GLU A  15     1192   1192   1192      0      0      0       H  
ATOM    200  HB3 GLU A  15      -3.444  21.658  76.775  1.00  9.41           H  
ANISOU  200  HB3 GLU A  15     1192   1192   1192      0      0      0       H  
ATOM    201  HG2 GLU A  15      -3.805  23.817  76.089  1.00 10.94           H  
ANISOU  201  HG2 GLU A  15     1386   1386   1386      0      0      0       H  
ATOM    202  HG3 GLU A  15      -3.320  23.470  74.645  1.00 10.94           H  
ANISOU  202  HG3 GLU A  15     1386   1386   1386      0      0      0       H  
ATOM    203  N   PRO A  16      -1.482  23.384  78.416  1.00  7.77           N  
ANISOU  203  N   PRO A  16     1285    892    701     31    173     25       N  
ATOM    204  CA  PRO A  16      -1.251  24.562  79.270  1.00  8.89           C  
ANISOU  204  CA  PRO A  16     1385   1185    725    -31    148    -64       C  
ATOM    205  C   PRO A  16       0.196  24.958  79.411  1.00  8.50           C  
ANISOU  205  C   PRO A  16     1491   1038    621    -73    144    -42       C  
ATOM    206  O   PRO A  16       0.511  26.061  79.858  1.00 10.16           O  
ANISOU  206  O   PRO A  16     1634   1058   1073   -121     65   -153       O  
ATOM    207  CB  PRO A  16      -1.865  24.131  80.613  1.00  9.86           C  
ANISOU  207  CB  PRO A  16     1503   1375    774    -24    273   -103       C  
ATOM    208  CG  PRO A  16      -2.083  22.720  80.525  1.00 14.76           C  
ANISOU  208  CG  PRO A  16     3054   1595    820   -766    454     18       C  
ATOM    209  CD  PRO A  16      -2.076  22.261  79.164  1.00  9.08           C  
ANISOU  209  CD  PRO A  16     1327   1248    791   -222    168    164       C  
ATOM    210  HA  PRO A  16      -1.759  25.321  78.913  1.00 10.67           H  
ANISOU  210  HA  PRO A  16     1351   1351   1351      0      0      0       H  
ATOM    211  HB2 PRO A  16      -1.260  24.335  81.343  1.00 11.83           H  
ANISOU  211  HB2 PRO A  16     1498   1498   1498      0      0      0       H  
ATOM    212  HB3 PRO A  16      -2.704  24.594  80.767  1.00 11.83           H  
ANISOU  212  HB3 PRO A  16     1498   1498   1498      0      0      0       H  
ATOM    213  HG2 PRO A  16      -1.389  22.258  81.022  1.00 17.71           H  
ANISOU  213  HG2 PRO A  16     2243   2243   2243      0      0      0       H  
ATOM    214  HG3 PRO A  16      -2.936  22.503  80.931  1.00 17.71           H  
ANISOU  214  HG3 PRO A  16     2243   2243   2243      0      0      0       H  
ATOM    215  HD2 PRO A  16      -1.539  21.459  79.071  1.00 10.90           H  
ANISOU  215  HD2 PRO A  16     1381   1381   1381      0      0      0       H  
ATOM    216  HD3 PRO A  16      -2.977  22.075  78.855  1.00 10.90           H  
ANISOU  216  HD3 PRO A  16     1381   1381   1381      0      0      0       H  
ATOM    217  N   GLU A  17       1.097  24.020  79.044  1.00  8.10           N  
ANISOU  217  N   GLU A  17     1325   1050    626   -105    144     -6       N  
ATOM    218  CA  GLU A  17       2.527  24.237  79.284  1.00  8.60           C  
ANISOU  218  CA  GLU A  17     1351   1219    615   -123     80    137       C  
ATOM    219  C   GLU A  17       3.213  24.924  78.118  1.00  7.91           C  
ANISOU  219  C   GLU A  17     1425    939    566   -296     -3     68       C  
ATOM    220  O   GLU A  17       4.329  25.389  78.269  1.00 11.07           O  
ANISOU  220  O   GLU A  17     1484   1689    930   -598   -211    360       O  
ATOM    221  CB AGLU A  17       3.190  22.940  79.742  0.68  9.54           C  
ANISOU  221  CB AGLU A  17     1498   1310    730     35     39    294       C  
ATOM    222  CB BGLU A  17       3.343  22.830  79.381  0.32  9.50           C  
ANISOU  222  CB BGLU A  17     1484   1231    803    -90   -323    312       C  
ATOM    223  CG AGLU A  17       2.473  22.411  81.008  0.68  9.72           C  
ANISOU  223  CG AGLU A  17     1395   1257    950    -38    119    336       C  
ATOM    224  CG BGLU A  17       3.145  22.381  80.849  0.32 12.65           C  
ANISOU  224  CG BGLU A  17     2056   1740    892     53   -214    398       C  
ATOM    225  CD AGLU A  17       2.416  23.362  82.182  0.68 12.02           C  
ANISOU  225  CD AGLU A  17     1867   2055    534   -573   -274    176       C  
ATOM    226  CD BGLU A  17       3.815  23.258  81.894  0.32 13.69           C  
ANISOU  226  CD BGLU A  17     2310   2042    721     55   -659    611       C  
ATOM    227  OE1AGLU A  17       3.553  23.710  82.553  0.68 17.11           O  
ANISOU  227  OE1AGLU A  17     2480   2507   1354  -1266  -1138   1264       O  
ATOM    228  OE1BGLU A  17       5.047  23.246  81.723  0.32 16.92           O  
ANISOU  228  OE1BGLU A  17     2299   1642   2327    -94   -634    620       O  
ATOM    229  OE2AGLU A  17       1.265  23.686  82.675  0.68 14.58           O  
ANISOU  229  OE2AGLU A  17     2619   1645   1140   -697    879   -121       O  
ATOM    230  OE2BGLU A  17       3.194  24.373  82.211  0.32 13.21           O  
ANISOU  230  OE2BGLU A  17     2098   1675   1121   -409   -572    457       O  
ATOM    231  H   GLU A  17       0.831  23.293  78.668  1.00  9.72           H  
ANISOU  231  H   GLU A  17     1231   1231   1231      0      0      0       H  
ATOM    232  N   CYS A  18       2.574  25.004  76.986  1.00  6.94           N  
ANISOU  232  N   CYS A  18     1047    959    565   -142    120     14       N  
ATOM    233  CA  CYS A  18       3.204  25.683  75.784  1.00  6.83           C  
ANISOU  233  CA  CYS A  18     1028    961    540   -201     67     28       C  
ATOM    234  C   CYS A  18       3.268  27.162  76.102  1.00  6.71           C  
ANISOU  234  C   CYS A  18     1048    861    577   -126     -9     31       C  
ATOM    235  O   CYS A  18       2.237  27.811  76.351  1.00  7.88           O  
ANISOU  235  O   CYS A  18     1123    941    856   -115    121    -91       O  
ATOM    236  CB  CYS A  18       2.390  25.439  74.589  1.00  6.51           C  
ANISOU  236  CB  CYS A  18      981    842    589   -184    -22     83       C  
ATOM    237  SG  CYS A  18       3.083  26.353  73.161  1.00  6.44           S  
ANISOU  237  SG  CYS A  18      955    866    566    -24     19     24       S  
ATOM    238  H   CYS A  18       1.786  24.667  76.919  1.00  8.33           H  
ANISOU  238  H   CYS A  18     1055   1055   1055      0      0      0       H  
ATOM    239  HA  CYS A  18       4.110  25.335  75.644  1.00  8.19           H  
ANISOU  239  HA  CYS A  18     1037   1037   1037      0      0      0       H  
ATOM    240  HB2 CYS A  18       2.376  24.489  74.392  1.00  7.81           H  
ANISOU  240  HB2 CYS A  18      989    989    989      0      0      0       H  
ATOM    241  HB3 CYS A  18       1.479  25.728  74.750  1.00  7.81           H  
ANISOU  241  HB3 CYS A  18      989    989    989      0      0      0       H  
ATOM    242  N   PRO A  19       4.467  27.776  76.027  1.00  6.68           N  
ANISOU  242  N   PRO A  19     1042    842    592    -86   -104    -48       N  
ATOM    243  CA  PRO A  19       4.593  29.187  76.392  1.00  7.66           C  
ANISOU  243  CA  PRO A  19     1172   1038    629   -251   -114    -15       C  
ATOM    244  C   PRO A  19       3.900  30.146  75.440  1.00  7.50           C  
ANISOU  244  C   PRO A  19     1141    944    693    -10     11    -55       C  
ATOM    245  O   PRO A  19       3.716  31.310  75.776  1.00  9.11           O  
ANISOU  245  O   PRO A  19     1544   1051    780    -31   -106   -103       O  
ATOM    246  CB  PRO A  19       6.123  29.453  76.402  1.00  8.44           C  
ANISOU  246  CB  PRO A  19     1052   1127    947   -271   -198    -22       C  
ATOM    247  CG  PRO A  19       6.646  28.425  75.443  1.00  9.12           C  
ANISOU  247  CG  PRO A  19     1162   1142   1073   -244    -35     13       C  
ATOM    248  CD  PRO A  19       5.771  27.192  75.707  1.00  7.80           C  
ANISOU  248  CD  PRO A  19     1074    997    819   -166   -167    -37       C  
ATOM    249  HA  PRO A  19       4.237  29.318  77.296  1.00  9.19           H  
ANISOU  249  HA  PRO A  19     1164   1164   1164      0      0      0       H  
ATOM    250  HB2 PRO A  19       6.325  30.351  76.098  1.00 10.12           H  
ANISOU  250  HB2 PRO A  19     1282   1282   1282      0      0      0       H  
ATOM    251  HB3 PRO A  19       6.495  29.326  77.289  1.00 10.12           H  
ANISOU  251  HB3 PRO A  19     1282   1282   1282      0      0      0       H  
ATOM    252  HG2 PRO A  19       6.552  28.727  74.526  1.00 10.94           H  
ANISOU  252  HG2 PRO A  19     1386   1386   1386      0      0      0       H  
ATOM    253  HG3 PRO A  19       7.580  28.231  75.618  1.00 10.94           H  
ANISOU  253  HG3 PRO A  19     1386   1386   1386      0      0      0       H  
ATOM    254  HD2 PRO A  19       5.718  26.626  74.921  1.00  9.36           H  
ANISOU  254  HD2 PRO A  19     1185   1185   1185      0      0      0       H  
ATOM    255  HD3 PRO A  19       6.114  26.672  76.450  1.00  9.36           H  
ANISOU  255  HD3 PRO A  19     1185   1185   1185      0      0      0       H  
ATOM    256  N   VAL A  20       3.559  29.703  74.247  1.00  7.71           N  
ANISOU  256  N   VAL A  20     1319    832    707    -98    -77    -29       N  
ATOM    257  CA  VAL A  20       2.968  30.512  73.198  1.00  7.40           C  
ANISOU  257  CA  VAL A  20     1258    833    651   -123    -33   -105       C  
ATOM    258  C   VAL A  20       1.562  30.027  72.810  1.00  7.06           C  
ANISOU  258  C   VAL A  20     1070    862    687     11     99    -95       C  
ATOM    259  O   VAL A  20       1.010  30.455  71.829  1.00  7.51           O  
ANISOU  259  O   VAL A  20     1016    999    768     49     32     14       O  
ATOM    260  CB  VAL A  20       3.890  30.688  71.975  1.00  7.18           C  
ANISOU  260  CB  VAL A  20      982    924    755    -94    -21     31       C  
ATOM    261  CG1 VAL A  20       5.092  31.548  72.318  1.00  8.56           C  
ANISOU  261  CG1 VAL A  20     1151    937   1086   -155    -61    -55       C  
ATOM    262  CG2 VAL A  20       4.300  29.330  71.403  1.00  7.51           C  
ANISOU  262  CG2 VAL A  20     1127    870    786   -128    102    -29       C  
ATOM    263  H   VAL A  20       3.698  28.872  74.077  1.00  9.26           H  
ANISOU  263  H   VAL A  20     1173   1173   1173      0      0      0       H  
ATOM    264  HA  VAL A  20       2.851  31.407  73.579  1.00  8.88           H  
ANISOU  264  HA  VAL A  20     1125   1125   1125      0      0      0       H  
ATOM    265  HB  VAL A  20       3.378  31.157  71.283  1.00  8.62           H  
ANISOU  265  HB  VAL A  20     1092   1092   1092      0      0      0       H  
ATOM    266 HG11 VAL A  20       4.793  32.388  72.673  1.00 12.85           H  
ANISOU  266 HG11 VAL A  20     1627   1627   1627      0      0      0       H  
ATOM    267 HG12 VAL A  20       5.632  31.098  72.972  1.00 12.85           H  
ANISOU  267 HG12 VAL A  20     1627   1627   1627      0      0      0       H  
ATOM    268 HG13 VAL A  20       5.612  31.703  71.526  1.00 12.85           H  
ANISOU  268 HG13 VAL A  20     1627   1627   1627      0      0      0       H  
ATOM    269 HG21 VAL A  20       3.514  28.823  71.188  1.00 11.26           H  
ANISOU  269 HG21 VAL A  20     1426   1426   1426      0      0      0       H  
ATOM    270 HG22 VAL A  20       4.823  29.462  70.609  1.00 11.26           H  
ANISOU  270 HG22 VAL A  20     1426   1426   1426      0      0      0       H  
ATOM    271 HG23 VAL A  20       4.821  28.853  72.053  1.00 11.26           H  
ANISOU  271 HG23 VAL A  20     1426   1426   1426      0      0      0       H  
ATOM    272  N   ASN A  21       0.984  29.108  73.593  1.00  7.14           N  
ANISOU  272  N   ASN A  21     1010    938    698    -26    111    -53       N  
ATOM    273  CA  ASN A  21      -0.359  28.617  73.363  1.00  7.65           C  
ANISOU  273  CA  ASN A  21      966    963    906     97    168   -118       C  
ATOM    274  C   ASN A  21      -0.574  28.075  71.963  1.00  7.45           C  
ANISOU  274  C   ASN A  21      983    876    901     58     28    -34       C  
ATOM    275  O   ASN A  21      -1.609  28.279  71.335  1.00  8.90           O  
ANISOU  275  O   ASN A  21     1026   1340    931    189     38      1       O  
ATOM    276  CB AASN A  21      -1.398  29.716  73.673  0.59  8.98           C  
ANISOU  276  CB AASN A  21     1238   1132    959    381    128    -28       C  
ATOM    277  CB BASN A  21      -1.436  29.871  73.505  0.41 10.53           C  
ANISOU  277  CB BASN A  21     1098   1329   1474    292    476   -179       C  
ATOM    278  CG AASN A  21      -2.815  29.231  73.639  0.59 12.49           C  
ANISOU  278  CG AASN A  21     1220   1745   1664    387    452   -351       C  
ATOM    279  CG BASN A  21      -1.061  30.454  74.817  0.41 11.19           C  
ANISOU  279  CG BASN A  21     1113   1518   1515    246    618   -337       C  
ATOM    280  OD1AASN A  21      -3.134  28.103  74.094  0.59 18.49           O  
ANISOU  280  OD1AASN A  21     1672   1965   3215   -223    636   -271       O  
ATOM    281  OD1BASN A  21      -0.894  31.710  74.967  0.41 17.49           O  
ANISOU  281  OD1BASN A  21     2445   1620   2416    236    416   -700       O  
ATOM    282  ND2AASN A  21      -3.802  29.985  73.201  0.59 18.18           N  
ANISOU  282  ND2AASN A  21     1243   1922   3572    612   -120  -1087       N  
ATOM    283  ND2BASN A  21      -0.810  29.758  75.887  0.41 15.38           N  
ANISOU  283  ND2BASN A  21     1904   2401   1394    121    585   -100       N  
ATOM    284  H   ASN A  21       1.429  28.795  74.260  1.00  8.57           H  
ANISOU  284  H   ASN A  21     1085   1085   1085      0      0      0       H  
ATOM    285  N   ALA A  22       0.421  27.319  71.456  1.00  6.42           N  
ANISOU  285  N   ALA A  22      985    737    657     31    -49    -60       N  
ATOM    286  CA  ALA A  22       0.407  26.798  70.109  1.00  6.78           C  
ANISOU  286  CA  ALA A  22     1020    782    712     12    -17     56       C  
ATOM    287  C   ALA A  22      -0.219  25.400  69.984  1.00  6.31           C  
ANISOU  287  C   ALA A  22      891    802    647     -4     -1    -54       C  
ATOM    288  O   ALA A  22      -0.284  24.856  68.899  1.00  7.70           O  
ANISOU  288  O   ALA A  22     1301    988    563    -84    186    -36       O  
ATOM    289  CB  ALA A  22       1.810  26.773  69.491  1.00  7.57           C  
ANISOU  289  CB  ALA A  22     1014   1072    721    -78     59    -79       C  
ATOM    290  H   ALA A  22       1.096  27.139  71.958  1.00  7.70           H  
ANISOU  290  H   ALA A  22      975    975    975      0      0      0       H  
ATOM    291  HA  ALA A  22      -0.137  27.408  69.568  1.00  8.14           H  
ANISOU  291  HA  ALA A  22     1031   1031   1031      0      0      0       H  
ATOM    292  HB1 ALA A  22       2.206  27.644  69.561  1.00 11.36           H  
ANISOU  292  HB1 ALA A  22     1439   1439   1439      0      0      0       H  
ATOM    293  HB2 ALA A  22       2.354  26.135  69.958  1.00 11.36           H  
ANISOU  293  HB2 ALA A  22     1439   1439   1439      0      0      0       H  
ATOM    294  HB3 ALA A  22       1.748  26.523  68.566  1.00 11.36           H  
ANISOU  294  HB3 ALA A  22     1439   1439   1439      0      0      0       H  
ATOM    295  N   ILE A  23      -0.611  24.799  71.123  1.00  6.80           N  
ANISOU  295  N   ILE A  23     1104    868    547   -107     85    -17       N  
ATOM    296  CA  ILE A  23      -1.200  23.437  71.099  1.00  6.76           C  
ANISOU  296  CA  ILE A  23      825    957    724    -58    -10     76       C  
ATOM    297  C   ILE A  23      -2.690  23.524  71.314  1.00  6.99           C  
ANISOU  297  C   ILE A  23      869    956    766     34    126     82       C  
ATOM    298  O   ILE A  23      -3.208  24.239  72.181  1.00  8.58           O  
ANISOU  298  O   ILE A  23     1151   1099    930    183    126    -45       O  
ATOM    299  CB  ILE A  23      -0.518  22.552  72.186  1.00  6.35           C  
ANISOU  299  CB  ILE A  23      873    949    531    -42     57     56       C  
ATOM    300  CG1 ILE A  23       0.942  22.398  71.835  1.00  8.28           C  
ANISOU  300  CG1 ILE A  23      773   1358    939     31      6    365       C  
ATOM    301  CG2 ILE A  23      -1.249  21.273  72.395  1.00  7.64           C  
ANISOU  301  CG2 ILE A  23      936    955    940    -67     64    175       C  
ATOM    302  CD1 ILE A  23       1.785  21.682  72.858  1.00  8.76           C  
ANISOU  302  CD1 ILE A  23      967   1273   1009   -241   -216    404       C  
ATOM    303  H   ILE A  23      -0.519  25.209  71.873  1.00  8.15           H  
ANISOU  303  H   ILE A  23     1032   1032   1032      0      0      0       H  
ATOM    304  HA  ILE A  23      -1.032  23.039  70.220  1.00  8.12           H  
ANISOU  304  HA  ILE A  23     1028   1028   1028      0      0      0       H  
ATOM    305  HB  ILE A  23      -0.561  23.049  73.030  1.00  7.62           H  
ANISOU  305  HB  ILE A  23      965    965    965      0      0      0       H  
ATOM    306 HG12 ILE A  23       1.005  21.916  70.995  1.00  9.94           H  
ANISOU  306 HG12 ILE A  23     1259   1259   1259      0      0      0       H  
ATOM    307 HG13 ILE A  23       1.317  23.281  71.692  1.00  9.94           H  
ANISOU  307 HG13 ILE A  23     1259   1259   1259      0      0      0       H  
ATOM    308 HG21 ILE A  23      -2.163  21.460  72.620  1.00 11.46           H  
ANISOU  308 HG21 ILE A  23     1451   1451   1451      0      0      0       H  
ATOM    309 HG22 ILE A  23      -1.217  20.752  71.590  1.00 11.46           H  
ANISOU  309 HG22 ILE A  23     1451   1451   1451      0      0      0       H  
ATOM    310 HG23 ILE A  23      -0.837  20.783  73.111  1.00 11.46           H  
ANISOU  310 HG23 ILE A  23     1451   1451   1451      0      0      0       H  
ATOM    311 HD11 ILE A  23       1.443  20.795  72.991  1.00 13.15           H  
ANISOU  311 HD11 ILE A  23     1665   1665   1665      0      0      0       H  
ATOM    312 HD12 ILE A  23       2.692  21.632  72.548  1.00 13.15           H  
ANISOU  312 HD12 ILE A  23     1665   1665   1665      0      0      0       H  
ATOM    313 HD13 ILE A  23       1.757  22.163  73.689  1.00 13.15           H  
ANISOU  313 HD13 ILE A  23     1665   1665   1665      0      0      0       H  
ATOM    314  N   SER A  24      -3.396  22.674  70.558  1.00  7.98           N  
ANISOU  314  N   SER A  24      843   1259    856      2     -5     20       N  
ATOM    315  CA  SER A  24      -4.849  22.489  70.757  1.00  8.97           C  
ANISOU  315  CA  SER A  24      857   1372   1096     -8      1     82       C  
ATOM    316  C   SER A  24      -5.152  21.006  70.553  1.00  8.28           C  
ANISOU  316  C   SER A  24      893   1359    817   -156    -20    164       C  
ATOM    317  O   SER A  24      -4.366  20.208  70.057  1.00  8.48           O  
ANISOU  317  O   SER A  24      864   1317    960   -223     86    134       O  
ATOM    318  CB ASER A  24      -5.654  23.351  69.802  0.69 10.78           C  
ANISOU  318  CB ASER A  24      954   1560   1482    451    299    244       C  
ATOM    319  CB BSER A  24      -5.456  23.067  69.307  0.31  9.23           C  
ANISOU  319  CB BSER A  24      797   1303   1320    675     81     99       C  
ATOM    320  OG ASER A  24      -5.344  23.047  68.451  0.69 10.52           O  
ANISOU  320  OG ASER A  24      953   1784   1161   -184    -71    413       O  
ATOM    321  OG BSER A  24      -5.290  24.477  69.321  0.31 12.74           O  
ANISOU  321  OG BSER A  24      902   1341   2479    437    -38    341       O  
ATOM    322  H   SER A  24      -2.996  22.226  69.943  1.00  9.58           H  
ANISOU  322  H   SER A  24     1213   1213   1213      0      0      0       H  
ATOM    323  N  ASER A  25      -6.362  20.643  70.990  0.48  9.97           N  
ANISOU  323  N  ASER A  25      991   1766    937   -324    196     79       N  
ATOM    324  N  BSER A  25      -6.375  20.692  71.187  0.52  9.62           N  
ANISOU  324  N  BSER A  25      889   1817    858   -312     33     50       N  
ATOM    325  CA ASER A  25      -6.816  19.252  70.920  0.48 11.26           C  
ANISOU  325  CA ASER A  25     1233   1834   1107   -564    160    120       C  
ATOM    326  CA BSER A  25      -6.802  19.336  70.829  0.52 10.78           C  
ANISOU  326  CA BSER A  25     1023   1910   1060   -523    167   -110       C  
ATOM    327  C  ASER A  25      -7.110  18.831  69.482  0.48 10.93           C  
ANISOU  327  C  ASER A  25     1251   1647   1151   -497      3    241       C  
ATOM    328  C  BSER A  25      -7.300  19.312  69.381  0.52 11.12           C  
ANISOU  328  C  BSER A  25     1099   1869   1153   -402     38    -73       C  
ATOM    329  O  ASER A  25      -7.320  19.742  68.653  0.48 11.94           O  
ANISOU  329  O  ASER A  25     1150   1838   1437   -128   -102    401       O  
ATOM    330  O  BSER A  25      -8.254  20.042  69.078  0.52 15.71           O  
ANISOU  330  O  BSER A  25     1614   1924   2285   -181   -680   -213       O  
ATOM    331  CB ASER A  25      -7.974  19.040  71.887  0.48 11.59           C  
ANISOU  331  CB ASER A  25     1290   1602   1402   -276    346    294       C  
ATOM    332  CB BSER A  25      -7.864  18.845  71.804  0.52 11.14           C  
ANISOU  332  CB BSER A  25     1056   1635   1436    -95    298    405       C  
ATOM    333  OG ASER A  25      -8.516  17.778  71.571  0.48 12.33           O  
ANISOU  333  OG ASER A  25     1297   1955   1319   -605    310     91       O  
ATOM    334  OG BSER A  25      -9.051  19.543  71.463  0.52 13.69           O  
ANISOU  334  OG BSER A  25      922   2292   1858    -27    171    519       O  
ATOM    335  N  AGLY A  26      -7.110  17.541  69.140  0.48 10.91           N  
ANISOU  335  N  AGLY A  26     1208   1683   1152   -156     56    122       N  
ATOM    336  N  BGLY A  26      -6.650  18.494  68.535  0.52 12.09           N  
ANISOU  336  N  BGLY A  26     1751   1753    976   -484    236    -37       N  
ATOM    337  CA AGLY A  26      -7.409  17.110  67.757  0.48 13.01           C  
ANISOU  337  CA AGLY A  26     1646   1839   1337   -220   -187     69       C  
ATOM    338  CA BGLY A  26      -7.084  18.348  67.152  0.52 13.62           C  
ANISOU  338  CA BGLY A  26     1887   2092   1067   -507    123     -3       C  
ATOM    339  C  AGLY A  26      -8.115  15.755  67.868  0.48 17.17           C  
ANISOU  339  C  AGLY A  26     2453   1944   1965   -584   -314    -13       C  
ATOM    340  C  BGLY A  26      -8.151  17.272  67.020  0.52 12.45           C  
ANISOU  340  C  BGLY A  26     1714   1960    939   -394    -31    172       C  
ATOM    341  O  AGLY A  26      -8.414  15.262  68.976  0.48 21.83           O  
ANISOU  341  O  AGLY A  26     4002   1896   2192   -967   -246    272       O  
ATOM    342  O  BGLY A  26      -8.732  16.733  67.974  0.52 13.10           O  
ANISOU  342  O  BGLY A  26     1673   2063   1119   -381   -394    510       O  
ATOM    343  N  AASP A  27      -8.380  15.153  66.730  0.48 17.88           N  
ANISOU  343  N  AASP A  27     2285   2150   2189   -342   -279   -350       N  
ATOM    344  N  BASP A  27      -8.493  16.922  65.775  0.52 13.06           N  
ANISOU  344  N  BASP A  27     1696   1982   1161   -344    258   -270       N  
ATOM    345  CA AASP A  27      -9.158  13.917  66.624  0.48 18.16           C  
ANISOU  345  CA AASP A  27     2749   1984   1997   -318   -451   -289       C  
ATOM    346  CA BASP A  27      -9.570  15.956  65.586  0.52 14.48           C  
ANISOU  346  CA BASP A  27     1928   2038   1400   -481   -174    -40       C  
ATOM    347  C  AASP A  27      -8.570  12.776  67.417  0.48 19.91           C  
ANISOU  347  C  AASP A  27     2675   2528   2176   -116     61    297       C  
ATOM    348  C  BASP A  27      -9.181  14.510  65.894  0.52 16.19           C  
ANISOU  348  C  BASP A  27     2181   1970   1849   -493   -235   -170       C  
ATOM    349  O  AASP A  27      -9.096  12.305  68.451  0.48 32.39           O  
ANISOU  349  O  AASP A  27     4425   5079   2500   1196   1094   1343       O  
ATOM    350  O  BASP A  27     -10.050  13.703  66.301  0.52 17.92           O  
ANISOU  350  O  BASP A  27     2321   2090   2229   -500   -181    286       O  
ATOM    351  CB AASP A  27      -9.453  13.530  65.161  0.48 21.04           C  
ANISOU  351  CB AASP A  27     2935   2813   2047   -447   -606   -438       C  
ATOM    352  CB BASP A  27     -10.097  15.998  64.160  0.52 18.15           C  
ANISOU  352  CB BASP A  27     2209   2974   1542     46   -511   -310       C  
ATOM    353  CG AASP A  27     -10.675  14.291  64.695  0.48 25.40           C  
ANISOU  353  CG AASP A  27     3135   4152   2125     68   -610   -275       C  
ATOM    354  CG BASP A  27     -11.046  17.178  63.952  0.52 22.89           C  
ANISOU  354  CG BASP A  27     3431   3371   1680    853   -848   -714       C  
ATOM    355  OD1AASP A  27     -11.566  14.689  65.476  0.48 29.78           O  
ANISOU  355  OD1AASP A  27     2875   4938   3222    -56     64     79       O  
ATOM    356  OD1BASP A  27     -10.812  18.128  64.750  0.52 35.57           O  
ANISOU  356  OD1BASP A  27     6911   3620   2649   1200  -1274  -1398       O  
ATOM    357  OD2AASP A  27     -10.782  14.542  63.471  0.48 30.40           O  
ANISOU  357  OD2AASP A  27     3572   5137   2556    -76   -531    835       O  
ATOM    358  OD2BASP A  27     -11.808  17.091  62.947  0.52 29.34           O  
ANISOU  358  OD2BASP A  27     4306   4670   1895   1363  -1423   -279       O  
ATOM    359  N  AASP A  28      -7.418  12.284  66.923  0.48 16.72           N  
ANISOU  359  N  AASP A  28     1651   2329   2215   -855   -464    247       N  
ATOM    360  N  BASP A  28      -7.893  14.242  65.708  0.52 15.57           N  
ANISOU  360  N  BASP A  28     2120   1916   1735   -423   -549   -151       N  
ATOM    361  CA AASP A  28      -6.835  11.289  67.806  0.48 19.62           C  
ANISOU  361  CA AASP A  28     2091   1767   3413   -955   -787    384       C  
ATOM    362  CA BASP A  28      -7.395  12.909  65.992  0.52 13.85           C  
ANISOU  362  CA BASP A  28     1798   1839   1495   -757   -315     87       C  
ATOM    363  C  AASP A  28      -5.436  11.662  68.302  0.48 15.27           C  
ANISOU  363  C  AASP A  28     1544   1563   2553   -534   -215    536       C  
ATOM    364  C  BASP A  28      -6.492  12.923  67.210  0.52 13.11           C  
ANISOU  364  C  BASP A  28     1805   1693   1360   -882   -228    227       C  
ATOM    365  O  AASP A  28      -4.763  10.785  68.799  0.48 18.25           O  
ANISOU  365  O  AASP A  28     2524   1701   2537   -760   -877    951       O  
ATOM    366  O  BASP A  28      -6.385  11.880  67.874  0.52 14.63           O  
ANISOU  366  O  BASP A  28     2136   1675   1609   -798    -55    405       O  
ATOM    367  CB AASP A  28      -6.832   9.870  67.259  0.48 27.74           C  
ANISOU  367  CB AASP A  28     3338   2236   4705   -487  -1437   -550       C  
ATOM    368  CB BASP A  28      -6.676  12.316  64.775  0.52 17.84           C  
ANISOU  368  CB BASP A  28     3090   2243   1278    329   -409    296       C  
ATOM    369  CG AASP A  28      -6.811   9.873  65.740  0.48 30.45           C  
ANISOU  369  CG AASP A  28     3643   2927   4714    -51  -1387   -943       C  
ATOM    370  CG BASP A  28      -7.692  12.000  63.685  0.52 20.42           C  
ANISOU  370  CG BASP A  28     3504   2241   1822     31   -601   -434       C  
ATOM    371  OD1AASP A  28      -6.057  10.707  65.186  0.48 28.36           O  
ANISOU  371  OD1AASP A  28     2877   3275   4359    403   -925  -1050       O  
ATOM    372  OD1BASP A  28      -8.916  12.308  63.795  0.52 23.62           O  
ANISOU  372  OD1BASP A  28     3486   2534   2734    280  -1087    -34       O  
ATOM    373  OD2AASP A  28      -7.614   9.035  65.304  0.48 33.54           O  
ANISOU  373  OD2AASP A  28     3874   3429   5127   -221  -1648  -1249       O  
ATOM    374  OD2BASP A  28      -7.240  11.448  62.644  0.52 24.13           O  
ANISOU  374  OD2BASP A  28     5501   1974   1467    857   -560     -6       O  
ATOM    375  N  AARG A  29      -5.096  12.918  68.152  0.48 12.29           N  
ANISOU  375  N  AARG A  29     1389   1449   1719   -497   -369    177       N  
ATOM    376  N  BARG A  29      -5.781  14.001  67.518  0.52 11.32           N  
ANISOU  376  N  BARG A  29     1547   1357   1292   -390   -271      4       N  
ATOM    377  CA AARG A  29      -3.811  13.455  68.570  0.48  8.88           C  
ANISOU  377  CA AARG A  29     1027   1241   1024    -79    -49    -54       C  
ATOM    378  CA BARG A  29      -4.820  14.064  68.623  0.52 10.63           C  
ANISOU  378  CA BARG A  29     1221   1412   1307   -411   -142     25       C  
ATOM    379  C  AARG A  29      -3.962  14.975  68.666  0.48  8.36           C  
ANISOU  379  C  AARG A  29      901   1212    983   -183   -203     92       C  
ATOM    380  C  BARG A  29      -4.467  15.541  68.805  0.52 10.43           C  
ANISOU  380  C  BARG A  29     1529   1276   1059   -369   -469    322       C  
ATOM    381  O  AARG A  29      -4.645  15.607  67.876  0.48  8.94           O  
ANISOU  381  O  AARG A  29      984   1362    966   -202   -151    210       O  
ATOM    382  O  BARG A  29      -5.006  16.430  68.130  0.52 13.68           O  
ANISOU  382  O  BARG A  29     2174   1633   1264   -325   -714    544       O  
ATOM    383  CB AARG A  29      -2.596  13.027  67.761  0.48 11.22           C  
ANISOU  383  CB AARG A  29     1430   1737    989    111     52   -104       C  
ATOM    384  CB BARG A  29      -3.580  13.262  68.295  0.52  9.77           C  
ANISOU  384  CB BARG A  29     1406   1455    761   -373    -67    -39       C  
ATOM    385  CG AARG A  29      -2.443  13.413  66.313  0.48 11.60           C  
ANISOU  385  CG AARG A  29     1614   1595   1089    111    166    103       C  
ATOM    386  CG BARG A  29      -2.828  13.673  67.008  0.52 10.84           C  
ANISOU  386  CG BARG A  29     1770   1577    669     49      1     25       C  
ATOM    387  CD AARG A  29      -1.053  13.184  65.720  0.48 14.61           C  
ANISOU  387  CD AARG A  29     2077   1789   1546    435    603   -308       C  
ATOM    388  CD BARG A  29      -1.659  12.757  66.714  0.52 13.76           C  
ANISOU  388  CD BARG A  29     2040   1778   1281    159    268   -273       C  
ATOM    389  NE AARG A  29      -1.018  12.803  64.318  0.48 17.66           N  
ANISOU  389  NE AARG A  29     2486   2540   1520    586    548   -134       N  
ATOM    390  NE BARG A  29      -0.986  12.840  65.438  0.52 13.79           N  
ANISOU  390  NE BARG A  29     2161   1794   1154    280     93   -768       N  
ATOM    391  CZ AARG A  29      -0.077  12.831  63.396  0.48 14.32           C  
ANISOU  391  CZ AARG A  29     1781   2394   1134    673     76   -200       C  
ATOM    392  CZ BARG A  29      -1.376  12.504  64.187  0.52 14.75           C  
ANISOU  392  CZ BARG A  29     1975   2278   1214    -17     -5   -502       C  
ATOM    393  NH1AARG A  29       1.106  13.411  63.486  0.48 12.08           N  
ANISOU  393  NH1AARG A  29     1437   2553    485   1075   -514   -943       N  
ATOM    394  NH1BARG A  29      -2.588  12.045  63.915  0.52 25.34           N  
ANISOU  394  NH1BARG A  29     2693   2992   3705   -549   -579  -2020       N  
ATOM    395  NH2AARG A  29      -0.455  12.273  62.219  0.48 12.01           N  
ANISOU  395  NH2AARG A  29      952   2184   1316   -212     64    -42       N  
ATOM    396  NH2BARG A  29      -0.470  12.632  63.218  0.52 19.65           N  
ANISOU  396  NH2BARG A  29     3272   2689   1321   1273    798    267       N  
ATOM    397  N   TYR A  30      -3.415  15.612  69.688  1.00  9.02           N  
ANISOU  397  N   TYR A  30     1410   1205    729   -481   -149    240       N  
ATOM    398  CA  TYR A  30      -3.204  17.036  69.861  1.00  8.21           C  
ANISOU  398  CA  TYR A  30      955   1188    899   -444    -11    247       C  
ATOM    399  C   TYR A  30      -2.365  17.538  68.669  1.00  7.83           C  
ANISOU  399  C   TYR A  30     1030   1149    723   -124     93    256       C  
ATOM    400  O   TYR A  30      -1.679  16.763  68.006  1.00  8.24           O  
ANISOU  400  O   TYR A  30     1068   1047    940    -76     18    186       O  
ATOM    401  CB  TYR A  30      -2.591  17.271  71.230  1.00  7.50           C  
ANISOU  401  CB  TYR A  30     1168    912    699    -64     28    112       C  
ATOM    402  CG  TYR A  30      -3.635  17.359  72.317  1.00  7.49           C  
ANISOU  402  CG  TYR A  30      862   1047    865   -129     58    -41       C  
ATOM    403  CD1 TYR A  30      -4.486  16.312  72.611  1.00  7.74           C  
ANISOU  403  CD1 TYR A  30     1031    995    842    -67    -58     27       C  
ATOM    404  CD2 TYR A  30      -3.758  18.493  73.083  1.00  8.37           C  
ANISOU  404  CD2 TYR A  30     1164   1125    813   -266     98    -46       C  
ATOM    405  CE1 TYR A  30      -5.443  16.398  73.618  1.00  8.73           C  
ANISOU  405  CE1 TYR A  30     1089   1179    966   -283     61      4       C  
ATOM    406  CE2 TYR A  30      -4.726  18.596  74.076  1.00  9.58           C  
ANISOU  406  CE2 TYR A  30     1319   1248    983   -319    205   -204       C  
ATOM    407  CZ  TYR A  30      -5.584  17.550  74.313  1.00  8.97           C  
ANISOU  407  CZ  TYR A  30     1186   1304    834   -121    179     91       C  
ATOM    408  OH  TYR A  30      -6.538  17.714  75.305  1.00 10.55           O  
ANISOU  408  OH  TYR A  30     1333   1472   1104   -152    303     -2       O  
ATOM    409  H   TYR A  30      -3.148  15.115  70.337  1.00 10.83           H  
ANISOU  409  H   TYR A  30     1372   1372   1372      0      0      0       H  
ATOM    410  HA  TYR A  30      -4.076  17.482  69.833  1.00  9.85           H  
ANISOU  410  HA  TYR A  30     1248   1248   1248      0      0      0       H  
ATOM    411  HB2 TYR A  30      -1.979  16.546  71.434  1.00  9.00           H  
ANISOU  411  HB2 TYR A  30     1140   1140   1140      0      0      0       H  
ATOM    412  HB3 TYR A  30      -2.080  18.096  71.213  1.00  9.00           H  
ANISOU  412  HB3 TYR A  30     1140   1140   1140      0      0      0       H  
ATOM    413  HD1 TYR A  30      -4.418  15.525  72.120  1.00  9.29           H  
ANISOU  413  HD1 TYR A  30     1177   1177   1177      0      0      0       H  
ATOM    414  HD2 TYR A  30      -3.180  19.207  72.935  1.00 10.05           H  
ANISOU  414  HD2 TYR A  30     1273   1273   1273      0      0      0       H  
ATOM    415  HE1 TYR A  30      -5.983  15.666  73.813  1.00 10.47           H  
ANISOU  415  HE1 TYR A  30     1326   1326   1326      0      0      0       H  
ATOM    416  HE2 TYR A  30      -4.792  19.375  74.581  1.00 11.49           H  
ANISOU  416  HE2 TYR A  30     1455   1455   1455      0      0      0       H  
ATOM    417  HH  TYR A  30      -6.968  17.021  75.389  1.00 15.83           H  
ANISOU  417  HH  TYR A  30     2005   2005   2005      0      0      0       H  
ATOM    418  N   VAL A  31      -2.398  18.864  68.439  1.00  6.97           N  
ANISOU  418  N   VAL A  31      942    977    665   -213     47    128       N  
ATOM    419  CA  VAL A  31      -1.774  19.426  67.234  1.00  7.44           C  
ANISOU  419  CA  VAL A  31     1102   1005    650   -367   -166    186       C  
ATOM    420  C   VAL A  31      -1.146  20.789  67.573  1.00  5.83           C  
ANISOU  420  C   VAL A  31      745    873    542    -11    -29    125       C  
ATOM    421  O   VAL A  31      -1.652  21.590  68.335  1.00  7.12           O  
ANISOU  421  O   VAL A  31      828   1034    775   -121    107      7       O  
ATOM    422  CB AVAL A  31      -2.791  19.503  66.077  0.85  7.47           C  
ANISOU  422  CB AVAL A  31      936   1148    683   -177   -139    239       C  
ATOM    423  CB BVAL A  31      -3.192  20.012  66.478  0.15  7.16           C  
ANISOU  423  CB BVAL A  31     1033    784    835   -418    -89    270       C  
ATOM    424  CG1AVAL A  31      -3.904  20.516  66.360  0.85  8.96           C  
ANISOU  424  CG1AVAL A  31      900   1593    827    -97    -26    161       C  
ATOM    425  CG1BVAL A  31      -2.793  20.880  65.295  0.15  5.58           C  
ANISOU  425  CG1BVAL A  31      858    603    608   -142    128     50       C  
ATOM    426  CG2AVAL A  31      -2.108  19.769  64.750  0.85  7.73           C  
ANISOU  426  CG2AVAL A  31     1053   1203    610   -250    -68    220       C  
ATOM    427  CG2BVAL A  31      -3.821  18.711  65.970  0.15  7.48           C  
ANISOU  427  CG2BVAL A  31     1429    459    884   -178   -626    392       C  
ATOM    428  H   VAL A  31      -2.787  19.385  69.001  1.00  8.37           H  
ANISOU  428  H   VAL A  31     1060   1060   1060      0      0      0       H  
ATOM    429  N   ILE A  32       0.001  20.979  66.918  1.00  5.63           N  
ANISOU  429  N   ILE A  32      781    794    510    -56    -10     41       N  
ATOM    430  CA  ILE A  32       0.816  22.181  67.053  1.00  5.64           C  
ANISOU  430  CA  ILE A  32      725    784    580      4    -26     89       C  
ATOM    431  C   ILE A  32       0.584  23.125  65.886  1.00  5.65           C  
ANISOU  431  C   ILE A  32      793    788    512    -71    -18     84       C  
ATOM    432  O   ILE A  32       0.567  22.735  64.704  1.00  6.20           O  
ANISOU  432  O   ILE A  32      970    834    493      0    -55    -25       O  
ATOM    433  CB  ILE A  32       2.320  21.819  67.150  1.00  5.53           C  
ANISOU  433  CB  ILE A  32      778    772    499     21     63     26       C  
ATOM    434  CG1 ILE A  32       2.549  21.116  68.495  1.00  5.61           C  
ANISOU  434  CG1 ILE A  32      780    740    560     60     -3    -21       C  
ATOM    435  CG2 ILE A  32       3.218  23.051  66.969  1.00  6.30           C  
ANISOU  435  CG2 ILE A  32      792    903    639    -80     -5     61       C  
ATOM    436  CD1 ILE A  32       3.942  20.520  68.648  1.00  6.14           C  
ANISOU  436  CD1 ILE A  32      778    790    706     53      7      7       C  
ATOM    437  H   ILE A  32       0.275  20.359  66.388  1.00  6.75           H  
ANISOU  437  H   ILE A  32      855    855    855      0      0      0       H  
ATOM    438  HA  ILE A  32       0.555  22.641  67.878  1.00  6.76           H  
ANISOU  438  HA  ILE A  32      856    856    856      0      0      0       H  
ATOM    439  HB  ILE A  32       2.528  21.182  66.434  1.00  6.64           H  
ANISOU  439  HB  ILE A  32      841    841    841      0      0      0       H  
ATOM    440 HG12 ILE A  32       2.402  21.754  69.211  1.00  6.73           H  
ANISOU  440 HG12 ILE A  32      852    852    852      0      0      0       H  
ATOM    441 HG13 ILE A  32       1.893  20.408  68.593  1.00  6.73           H  
ANISOU  441 HG13 ILE A  32      852    852    852      0      0      0       H  
ATOM    442 HG21 ILE A  32       3.036  23.457  66.119  1.00  9.45           H  
ANISOU  442 HG21 ILE A  32     1197   1197   1197      0      0      0       H  
ATOM    443 HG22 ILE A  32       3.040  23.682  67.670  1.00  9.45           H  
ANISOU  443 HG22 ILE A  32     1197   1197   1197      0      0      0       H  
ATOM    444 HG23 ILE A  32       4.139  22.784  67.006  1.00  9.45           H  
ANISOU  444 HG23 ILE A  32     1197   1197   1197      0      0      0       H  
ATOM    445 HD11 ILE A  32       4.598  21.216  68.573  1.00  9.21           H  
ANISOU  445 HD11 ILE A  32     1166   1166   1166      0      0      0       H  
ATOM    446 HD12 ILE A  32       4.018  20.100  69.508  1.00  9.21           H  
ANISOU  446 HD12 ILE A  32     1166   1166   1166      0      0      0       H  
ATOM    447 HD13 ILE A  32       4.088  19.867  67.959  1.00  9.21           H  
ANISOU  447 HD13 ILE A  32     1166   1166   1166      0      0      0       H  
ATOM    448  N   ASP A  33       0.392  24.404  66.245  1.00  5.63           N  
ANISOU  448  N   ASP A  33      819    805    464    -64    -38     71       N  
ATOM    449  CA  ASP A  33       0.380  25.534  65.256  1.00  5.87           C  
ANISOU  449  CA  ASP A  33      896    734    546    -43    -16     92       C  
ATOM    450  C   ASP A  33       1.826  25.866  64.893  1.00  5.46           C  
ANISOU  450  C   ASP A  33      799    680    546    -86    -22     62       C  
ATOM    451  O   ASP A  33       2.588  26.457  65.636  1.00  5.90           O  
ANISOU  451  O   ASP A  33      912    755    518     -4    -31    -39       O  
ATOM    452  CB  ASP A  33      -0.287  26.712  65.901  1.00  6.31           C  
ANISOU  452  CB  ASP A  33      825    821    692     27    -45     68       C  
ATOM    453  CG  ASP A  33      -0.211  27.957  65.012  1.00  7.22           C  
ANISOU  453  CG  ASP A  33      960    906    812    141     55     96       C  
ATOM    454  OD1 ASP A  33       0.199  27.891  63.875  1.00  7.58           O  
ANISOU  454  OD1 ASP A  33     1095   1027    688    120    132    118       O  
ATOM    455  OD2 ASP A  33      -0.612  29.040  65.547  1.00 10.28           O  
ANISOU  455  OD2 ASP A  33     1783    992   1035    528     70     19       O  
ATOM    456  H   ASP A  33       0.270  24.583  67.077  1.00  6.76           H  
ANISOU  456  H   ASP A  33      856    856    856      0      0      0       H  
ATOM    457  HA  ASP A  33      -0.114  25.270  64.452  1.00  7.04           H  
ANISOU  457  HA  ASP A  33      892    892    892      0      0      0       H  
ATOM    458  HB2 ASP A  33      -1.217  26.499  66.076  1.00  7.57           H  
ANISOU  458  HB2 ASP A  33      959    959    959      0      0      0       H  
ATOM    459  HB3 ASP A  33       0.142  26.899  66.751  1.00  7.57           H  
ANISOU  459  HB3 ASP A  33      959    959    959      0      0      0       H  
ATOM    460  N   ALA A  34       2.226  25.356  63.697  1.00  5.75           N  
ANISOU  460  N   ALA A  34      863    724    543    -50     -7     29       N  
ATOM    461  CA  ALA A  34       3.546  25.547  63.195  1.00  5.92           C  
ANISOU  461  CA  ALA A  34      898    815    479    -96    -29     24       C  
ATOM    462  C   ALA A  34       3.894  26.987  62.873  1.00  5.97           C  
ANISOU  462  C   ALA A  34      907    822    482    -88      0     51       C  
ATOM    463  O   ALA A  34       5.068  27.346  62.706  1.00  6.75           O  
ANISOU  463  O   ALA A  34      879    806    817    -50     -7    123       O  
ATOM    464  CB  ALA A  34       3.746  24.696  61.929  1.00  6.95           C  
ANISOU  464  CB  ALA A  34      966    905    704     43    106   -112       C  
ATOM    465  H   ALA A  34       1.664  24.904  63.229  1.00  6.90           H  
ANISOU  465  H   ALA A  34      874    874    874      0      0      0       H  
ATOM    466  HA  ALA A  34       4.177  25.229  63.875  1.00  7.10           H  
ANISOU  466  HA  ALA A  34      899    899    899      0      0      0       H  
ATOM    467  HB1 ALA A  34       3.525  23.782  62.120  1.00 10.42           H  
ANISOU  467  HB1 ALA A  34     1320   1320   1320      0      0      0       H  
ATOM    468  HB2 ALA A  34       3.175  25.024  61.230  1.00 10.42           H  
ANISOU  468  HB2 ALA A  34     1320   1320   1320      0      0      0       H  
ATOM    469  HB3 ALA A  34       4.662  24.752  61.647  1.00 10.42           H  
ANISOU  469  HB3 ALA A  34     1320   1320   1320      0      0      0       H  
ATOM    470  N   ASP A  35       2.899  27.879  62.811  1.00  5.84           N  
ANISOU  470  N   ASP A  35      805    754    606   -134     -3    119       N  
ATOM    471  CA  ASP A  35       3.142  29.289  62.604  1.00  6.20           C  
ANISOU  471  CA  ASP A  35      941    824    534    -48     87     69       C  
ATOM    472  C   ASP A  35       3.440  30.032  63.899  1.00  6.16           C  
ANISOU  472  C   ASP A  35      870    787    627   -103    -29     43       C  
ATOM    473  O   ASP A  35       3.785  31.218  63.842  1.00  7.63           O  
ANISOU  473  O   ASP A  35     1246    897    684   -112    -83      9       O  
ATOM    474  CB  ASP A  35       1.983  29.905  61.848  1.00  6.47           C  
ANISOU  474  CB  ASP A  35     1011    752    635     31    -71      4       C  
ATOM    475  CG  ASP A  35       1.854  29.354  60.428  1.00  7.84           C  
ANISOU  475  CG  ASP A  35     1143   1131    634    -44    -57     74       C  
ATOM    476  OD1 ASP A  35       2.852  28.867  59.854  1.00  8.74           O  
ANISOU  476  OD1 ASP A  35     1486   1109    646      6     86    -33       O  
ATOM    477  OD2 ASP A  35       0.745  29.494  59.881  1.00 10.75           O  
ANISOU  477  OD2 ASP A  35     1357   1575   1052     27   -468   -147       O  
ATOM    478  H   ASP A  35       2.088  27.605  62.898  1.00  7.01           H  
ANISOU  478  H   ASP A  35      888    888    888      0      0      0       H  
ATOM    479  HA  ASP A  35       3.936  29.366  62.034  1.00  7.44           H  
ANISOU  479  HA  ASP A  35      942    942    942      0      0      0       H  
ATOM    480  HB2 ASP A  35       1.160  29.731  62.332  1.00  7.77           H  
ANISOU  480  HB2 ASP A  35      984    984    984      0      0      0       H  
ATOM    481  HB3 ASP A  35       2.106  30.866  61.807  1.00  7.77           H  
ANISOU  481  HB3 ASP A  35      984    984    984      0      0      0       H  
ATOM    482  N   THR A  36       3.335  29.365  65.025  1.00  6.47           N  
ANISOU  482  N   THR A  36     1046    853    500    -31    -28     -2       N  
ATOM    483  CA  THR A  36       3.564  29.962  66.364  1.00  7.21           C  
ANISOU  483  CA  THR A  36     1305    833    532    114   -214   -139       C  
ATOM    484  C   THR A  36       4.644  29.254  67.134  1.00  6.13           C  
ANISOU  484  C   THR A  36     1020    788    462    -32    -10     33       C  
ATOM    485  O   THR A  36       5.347  29.847  67.957  1.00  6.71           O  
ANISOU  485  O   THR A  36     1122    778    588    -69    -66     89       O  
ATOM    486  CB  THR A  36       2.179  29.966  67.146  1.00  9.71           C  
ANISOU  486  CB  THR A  36     1395   1670    532    915   -287   -332       C  
ATOM    487  OG1 THR A  36       1.302  30.825  66.393  1.00 10.72           O  
ANISOU  487  OG1 THR A  36     1563   1558    852    569   -154    -56       O  
ATOM    488  CG2 THR A  36       2.306  30.574  68.510  1.00 11.23           C  
ANISOU  488  CG2 THR A  36     1616   1771    776    400    -42   -397       C  
ATOM    489  H   THR A  36       3.121  28.533  64.985  1.00  7.77           H  
ANISOU  489  H   THR A  36      984    984    984      0      0      0       H  
ATOM    490  HA  THR A  36       3.843  30.893  66.237  1.00  8.65           H  
ANISOU  490  HA  THR A  36     1096   1096   1096      0      0      0       H  
ATOM    491  HB  THR A  36       1.811  29.060  67.204  1.00 11.65           H  
ANISOU  491  HB  THR A  36     1475   1475   1475      0      0      0       H  
ATOM    492  HG1 THR A  36       1.205  30.521  65.637  1.00 16.08           H  
ANISOU  492  HG1 THR A  36     2037   2037   2037      0      0      0       H  
ATOM    493 HG21 THR A  36       2.941  30.072  69.026  1.00 16.85           H  
ANISOU  493 HG21 THR A  36     2134   2134   2134      0      0      0       H  
ATOM    494 HG22 THR A  36       2.607  31.482  68.428  1.00 16.85           H  
ANISOU  494 HG22 THR A  36     2134   2134   2134      0      0      0       H  
ATOM    495 HG23 THR A  36       1.452  30.558  68.948  1.00 16.85           H  
ANISOU  495 HG23 THR A  36     2134   2134   2134      0      0      0       H  
ATOM    496  N   CYS A  37       4.803  27.935  66.939  1.00  6.04           N  
ANISOU  496  N   CYS A  37      902    834    503      2    -91    -10       N  
ATOM    497  CA  CYS A  37       5.787  27.165  67.675  1.00  5.72           C  
ANISOU  497  CA  CYS A  37      772    791    556   -105    -15     79       C  
ATOM    498  C   CYS A  37       7.216  27.727  67.474  1.00  5.97           C  
ANISOU  498  C   CYS A  37      893    728    592   -140    -55     13       C  
ATOM    499  O   CYS A  37       7.633  28.045  66.363  1.00  6.32           O  
ANISOU  499  O   CYS A  37      947    850    544   -123     -9    126       O  
ATOM    500  CB  CYS A  37       5.730  25.726  67.226  1.00  5.98           C  
ANISOU  500  CB  CYS A  37      827    781    608   -175    -74    -86       C  
ATOM    501  SG  CYS A  37       6.944  24.621  68.008  1.00  5.92           S  
ANISOU  501  SG  CYS A  37      873    768    553    -89     -8     38       S  
ATOM    502  H   CYS A  37       4.307  27.535  66.361  1.00  7.25           H  
ANISOU  502  H   CYS A  37      918    918    918      0      0      0       H  
ATOM    503  HA  CYS A  37       5.567  27.204  68.629  1.00  6.86           H  
ANISOU  503  HA  CYS A  37      869    869    869      0      0      0       H  
ATOM    504  HB2 CYS A  37       4.841  25.383  67.406  1.00  7.18           H  
ANISOU  504  HB2 CYS A  37      909    909    909      0      0      0       H  
ATOM    505  HB3 CYS A  37       5.863  25.698  66.265  1.00  7.18           H  
ANISOU  505  HB3 CYS A  37      909    909    909      0      0      0       H  
ATOM    506  N   ILE A  38       7.968  27.829  68.574  1.00  6.43           N  
ANISOU  506  N   ILE A  38      913    911    557   -283    -59     46       N  
ATOM    507  CA  ILE A  38       9.321  28.327  68.628  1.00  6.19           C  
ANISOU  507  CA  ILE A  38      895    781    619   -363      3     65       C  
ATOM    508  C   ILE A  38      10.313  27.292  69.137  1.00  6.24           C  
ANISOU  508  C   ILE A  38      864    829    618   -327     31    -12       C  
ATOM    509  O   ILE A  38      11.449  27.609  69.512  1.00  6.98           O  
ANISOU  509  O   ILE A  38      976    902    707   -250    -86     39       O  
ATOM    510  CB  ILE A  38       9.417  29.678  69.372  1.00  6.59           C  
ANISOU  510  CB  ILE A  38     1013    795    633   -192    -60    -52       C  
ATOM    511  CG1 ILE A  38       8.729  29.657  70.711  1.00  6.99           C  
ANISOU  511  CG1 ILE A  38     1044    820    728   -251    -35    -90       C  
ATOM    512  CG2 ILE A  38       8.833  30.805  68.485  1.00  7.71           C  
ANISOU  512  CG2 ILE A  38     1034    860    961    -89     71     98       C  
ATOM    513  CD1 ILE A  38       9.231  28.631  71.711  1.00  8.27           C  
ANISOU  513  CD1 ILE A  38     1208   1097    761   -367    -46    172       C  
ATOM    514  H   ILE A  38       7.613  27.577  69.316  1.00  7.71           H  
ANISOU  514  H   ILE A  38      976    976    976      0      0      0       H  
ATOM    515  HA  ILE A  38       9.577  28.511  67.700  1.00  7.43           H  
ANISOU  515  HA  ILE A  38      941    941    941      0      0      0       H  
ATOM    516  HB  ILE A  38      10.366  29.873  69.522  1.00  7.90           H  
ANISOU  516  HB  ILE A  38     1001   1001   1001      0      0      0       H  
ATOM    517 HG12 ILE A  38       8.817  30.537  71.110  1.00  8.39           H  
ANISOU  517 HG12 ILE A  38     1063   1063   1063      0      0      0       H  
ATOM    518 HG13 ILE A  38       7.784  29.499  70.563  1.00  8.39           H  
ANISOU  518 HG13 ILE A  38     1063   1063   1063      0      0      0       H  
ATOM    519 HG21 ILE A  38       9.278  30.807  67.635  1.00 11.56           H  
ANISOU  519 HG21 ILE A  38     1464   1464   1464      0      0      0       H  
ATOM    520 HG22 ILE A  38       7.894  30.655  68.354  1.00 11.56           H  
ANISOU  520 HG22 ILE A  38     1464   1464   1464      0      0      0       H  
ATOM    521 HG23 ILE A  38       8.964  31.652  68.917  1.00 11.56           H  
ANISOU  521 HG23 ILE A  38     1464   1464   1464      0      0      0       H  
ATOM    522 HD11 ILE A  38      10.160  28.790  71.894  1.00 12.41           H  
ANISOU  522 HD11 ILE A  38     1572   1572   1572      0      0      0       H  
ATOM    523 HD12 ILE A  38       8.727  28.705  72.525  1.00 12.41           H  
ANISOU  523 HD12 ILE A  38     1572   1572   1572      0      0      0       H  
ATOM    524 HD13 ILE A  38       9.123  27.750  71.347  1.00 12.41           H  
ANISOU  524 HD13 ILE A  38     1572   1572   1572      0      0      0       H  
ATOM    525  N   ASP A  39       9.946  25.998  69.113  1.00  6.50           N  
ANISOU  525  N   ASP A  39      783    865    761   -164    -93     51       N  
ATOM    526  CA  ASP A  39      10.848  24.873  69.281  1.00  6.91           C  
ANISOU  526  CA  ASP A  39      904    816    842   -117    -84     52       C  
ATOM    527  C   ASP A  39      11.409  24.759  70.663  1.00  7.64           C  
ANISOU  527  C   ASP A  39     1020    881    932      1    -92    130       C  
ATOM    528  O   ASP A  39      12.509  24.217  70.881  1.00  9.68           O  
ANISOU  528  O   ASP A  39     1165   1300   1121    121   -242    120       O  
ATOM    529  CB  ASP A  39      11.958  24.905  68.276  1.00  7.66           C  
ANISOU  529  CB  ASP A  39     1021    923    894    -64    -62      9       C  
ATOM    530  CG  ASP A  39      11.538  24.956  66.846  1.00  7.37           C  
ANISOU  530  CG  ASP A  39      874    849   1009    -97     73     99       C  
ATOM    531  OD1 ASP A  39      10.604  24.207  66.459  1.00  8.08           O  
ANISOU  531  OD1 ASP A  39     1075   1041    878   -227    -63    129       O  
ATOM    532  OD2 ASP A  39      12.208  25.676  66.080  1.00  9.30           O  
ANISOU  532  OD2 ASP A  39     1110   1230   1105   -357   -111    339       O  
ATOM    533  H   ASP A  39       9.113  25.824  68.989  1.00  7.80           H  
ANISOU  533  H   ASP A  39      988    988    988      0      0      0       H  
ATOM    534  HA  ASP A  39      10.329  24.059  69.112  1.00  8.30           H  
ANISOU  534  HA  ASP A  39     1051   1051   1051      0      0      0       H  
ATOM    535  HB2 ASP A  39      12.512  25.680  68.459  1.00  9.19           H  
ANISOU  535  HB2 ASP A  39     1164   1164   1164      0      0      0       H  
ATOM    536  HB3 ASP A  39      12.509  24.118  68.405  1.00  9.19           H  
ANISOU  536  HB3 ASP A  39     1164   1164   1164      0      0      0       H  
ATOM    537  N   CYS A  40      10.733  25.224  71.696  1.00  7.31           N  
ANISOU  537  N   CYS A  40      949    894    865   -331   -218     32       N  
ATOM    538  CA  CYS A  40      11.258  25.185  73.028  1.00  7.58           C  
ANISOU  538  CA  CYS A  40     1016   1045    748   -363   -217    216       C  
ATOM    539  C   CYS A  40      11.366  23.804  73.600  1.00  7.74           C  
ANISOU  539  C   CYS A  40      962    987    919   -199   -167    116       C  
ATOM    540  O   CYS A  40      12.132  23.609  74.596  1.00  9.47           O  
ANISOU  540  O   CYS A  40     1322   1203    984   -257   -505    202       O  
ATOM    541  CB  CYS A  40      10.386  26.065  73.984  1.00  7.88           C  
ANISOU  541  CB  CYS A  40     1202    874    843   -273   -330     72       C  
ATOM    542  SG  CYS A  40       8.755  25.434  74.404  1.00  7.37           S  
ANISOU  542  SG  CYS A  40     1135    861    735   -151   -218    -19       S  
ATOM    543  H   CYS A  40       9.953  25.561  71.565  1.00  8.77           H  
ANISOU  543  H   CYS A  40     1111   1111   1111      0      0      0       H  
ATOM    544  HA  CYS A  40      12.159  25.570  73.006  1.00  9.10           H  
ANISOU  544  HA  CYS A  40     1153   1153   1153      0      0      0       H  
ATOM    545  HB2 CYS A  40      10.880  26.196  74.808  1.00  9.45           H  
ANISOU  545  HB2 CYS A  40     1197   1197   1197      0      0      0       H  
ATOM    546  HB3 CYS A  40      10.275  26.937  73.573  1.00  9.45           H  
ANISOU  546  HB3 CYS A  40     1197   1197   1197      0      0      0       H  
ATOM    547  N   GLY A  41      10.575  22.853  73.139  1.00  6.96           N  
ANISOU  547  N   GLY A  41      834    872    872   -130   -131    171       N  
ATOM    548  CA  GLY A  41      10.552  21.485  73.615  1.00  6.95           C  
ANISOU  548  CA  GLY A  41      759    903    913     79    -49    190       C  
ATOM    549  C   GLY A  41       9.759  21.264  74.884  1.00  6.46           C  
ANISOU  549  C   GLY A  41      847    916    632   -120   -182    -18       C  
ATOM    550  O   GLY A  41       9.759  20.129  75.388  1.00  7.32           O  
ANISOU  550  O   GLY A  41     1064    872    778   -111    -67    176       O  
ATOM    551  H   GLY A  41      10.031  23.062  72.506  1.00  8.35           H  
ANISOU  551  H   GLY A  41     1058   1058   1058      0      0      0       H  
ATOM    552  HA2 GLY A  41      10.181  20.922  72.917  1.00  8.34           H  
ANISOU  552  HA2 GLY A  41     1056   1056   1056      0      0      0       H  
ATOM    553  HA3 GLY A  41      11.465  21.197  73.768  1.00  8.34           H  
ANISOU  553  HA3 GLY A  41     1056   1056   1056      0      0      0       H  
ATOM    554  N   ALA A  42       9.046  22.270  75.388  1.00  6.54           N  
ANISOU  554  N   ALA A  42      907    888    627   -110   -129     11       N  
ATOM    555  CA  ALA A  42       8.383  22.064  76.688  1.00  6.81           C  
ANISOU  555  CA  ALA A  42     1043    988    493    -47   -132     70       C  
ATOM    556  C   ALA A  42       7.286  21.016  76.625  1.00  6.42           C  
ANISOU  556  C   ALA A  42     1014    803    563      0    -31    128       C  
ATOM    557  O   ALA A  42       7.074  20.305  77.604  1.00  7.16           O  
ANISOU  557  O   ALA A  42     1107    915    631    -22   -105    168       O  
ATOM    558  CB  ALA A  42       7.798  23.371  77.213  1.00  7.66           C  
ANISOU  558  CB  ALA A  42     1244    914    679   -134    -31    -66       C  
ATOM    559  H   ALA A  42       8.974  23.017  74.967  1.00  7.84           H  
ANISOU  559  H   ALA A  42      993    993    993      0      0      0       H  
ATOM    560  HA  ALA A  42       9.059  21.756  77.327  1.00  8.17           H  
ANISOU  560  HA  ALA A  42     1035   1035   1035      0      0      0       H  
ATOM    561  HB1 ALA A  42       8.489  24.036  77.256  1.00 11.48           H  
ANISOU  561  HB1 ALA A  42     1454   1454   1454      0      0      0       H  
ATOM    562  HB2 ALA A  42       7.103  23.670  76.622  1.00 11.48           H  
ANISOU  562  HB2 ALA A  42     1454   1454   1454      0      0      0       H  
ATOM    563  HB3 ALA A  42       7.435  23.229  78.090  1.00 11.48           H  
ANISOU  563  HB3 ALA A  42     1454   1454   1454      0      0      0       H  
ATOM    564  N   CYS A  43       6.585  20.927  75.502  1.00  6.15           N  
ANISOU  564  N   CYS A  43      981    717    580      1    -43    155       N  
ATOM    565  CA  CYS A  43       5.545  19.947  75.322  1.00  5.87           C  
ANISOU  565  CA  CYS A  43      843    808    525    -16     42     55       C  
ATOM    566  C   CYS A  43       6.087  18.517  75.418  1.00  5.99           C  
ANISOU  566  C   CYS A  43      939    765    514    -30    -27      4       C  
ATOM    567  O   CYS A  43       5.507  17.688  76.089  1.00  6.72           O  
ANISOU  567  O   CYS A  43      929    833    729    -82    119    104       O  
ATOM    568  CB  CYS A  43       4.782  20.215  74.017  1.00  6.01           C  
ANISOU  568  CB  CYS A  43      884    776    567    -61    -31    111       C  
ATOM    569  SG  CYS A  43       5.872  20.376  72.539  1.00  6.04           S  
ANISOU  569  SG  CYS A  43      943    789    508    -26    -39     12       S  
ATOM    570  H   CYS A  43       6.758  21.473  74.860  1.00  7.38           H  
ANISOU  570  H   CYS A  43      935    935    935      0      0      0       H  
ATOM    571  HA  CYS A  43       4.908  20.064  76.058  1.00  7.05           H  
ANISOU  571  HA  CYS A  43      893    893    893      0      0      0       H  
ATOM    572  HB2 CYS A  43       4.156  19.489  73.867  1.00  7.21           H  
ANISOU  572  HB2 CYS A  43      913    913    913      0      0      0       H  
ATOM    573  HB3 CYS A  43       4.268  21.031  74.117  1.00  7.21           H  
ANISOU  573  HB3 CYS A  43      913    913    913      0      0      0       H  
ATOM    574  N   ALA A  44       7.199  18.262  74.732  1.00  6.04           N  
ANISOU  574  N   ALA A  44      925    763    550     16     -9    108       N  
ATOM    575  CA  ALA A  44       7.821  16.960  74.836  1.00  5.96           C  
ANISOU  575  CA  ALA A  44      864    808    537     63    -58      8       C  
ATOM    576  C   ALA A  44       8.255  16.708  76.293  1.00  6.04           C  
ANISOU  576  C   ALA A  44      905    867    467    -96    -33    111       C  
ATOM    577  O   ALA A  44       8.134  15.587  76.797  1.00  6.62           O  
ANISOU  577  O   ALA A  44      932    874    646   -102    -83    112       O  
ATOM    578  CB  ALA A  44       8.992  16.820  73.874  1.00  7.01           C  
ANISOU  578  CB  ALA A  44      948   1037    613     12     33      9       C  
ATOM    579  H   ALA A  44       7.546  18.868  74.231  1.00  7.25           H  
ANISOU  579  H   ALA A  44      918    918    918      0      0      0       H  
ATOM    580  HA  ALA A  44       7.152  16.285  74.599  1.00  7.15           H  
ANISOU  580  HA  ALA A  44      906    906    906      0      0      0       H  
ATOM    581  HB1 ALA A  44       8.692  16.990  72.978  1.00 10.52           H  
ANISOU  581  HB1 ALA A  44     1332   1332   1332      0      0      0       H  
ATOM    582  HB2 ALA A  44       9.676  17.453  74.108  1.00 10.52           H  
ANISOU  582  HB2 ALA A  44     1332   1332   1332      0      0      0       H  
ATOM    583  HB3 ALA A  44       9.347  15.930  73.930  1.00 10.52           H  
ANISOU  583  HB3 ALA A  44     1332   1332   1332      0      0      0       H  
ATOM    584  N   GLY A  45       8.721  17.750  76.969  1.00  6.03           N  
ANISOU  584  N   GLY A  45      980    788    468    -45    -29     99       N  
ATOM    585  CA  GLY A  45       9.202  17.612  78.327  1.00  7.05           C  
ANISOU  585  CA  GLY A  45      957   1059    596   -161   -116    147       C  
ATOM    586  C   GLY A  45       8.104  17.217  79.319  1.00  6.17           C  
ANISOU  586  C   GLY A  45      849    932    504   -140    -41     95       C  
ATOM    587  O   GLY A  45       8.467  16.710  80.422  1.00  8.29           O  
ANISOU  587  O   GLY A  45      935   1459    677   -220   -115    371       O  
ATOM    588  H   GLY A  45       8.738  18.523  76.592  1.00  7.24           H  
ANISOU  588  H   GLY A  45      917    917    917      0      0      0       H  
ATOM    589  HA2 GLY A  45       9.901  16.939  78.346  1.00  8.46           H  
ANISOU  589  HA2 GLY A  45     1071   1071   1071      0      0      0       H  
ATOM    590  HA3 GLY A  45       9.594  18.453  78.609  1.00  8.46           H  
ANISOU  590  HA3 GLY A  45     1071   1071   1071      0      0      0       H  
ATOM    591  N   VAL A  46       6.842  17.466  79.034  1.00  5.93           N  
ANISOU  591  N   VAL A  46      903    819    475     31    -38     43       N  
ATOM    592  CA  VAL A  46       5.730  17.066  79.884  1.00  6.19           C  
ANISOU  592  CA  VAL A  46      913    851    528    -18     16     42       C  
ATOM    593  C   VAL A  46       4.928  15.950  79.255  1.00  5.79           C  
ANISOU  593  C   VAL A  46      782    864    500    -20   -137    162       C  
ATOM    594  O   VAL A  46       3.825  15.613  79.724  1.00  6.86           O  
ANISOU  594  O   VAL A  46      951   1027    565   -146     23     16       O  
ATOM    595  CB  VAL A  46       4.851  18.223  80.320  1.00  6.76           C  
ANISOU  595  CB  VAL A  46      906   1004    596     38    119     -3       C  
ATOM    596  CG1 VAL A  46       5.690  19.231  81.102  1.00  7.17           C  
ANISOU  596  CG1 VAL A  46     1004    894    760    -84     91    -57       C  
ATOM    597  CG2 VAL A  46       4.119  18.876  79.163  1.00  7.65           C  
ANISOU  597  CG2 VAL A  46     1067   1063    703    118     -6     82       C  
ATOM    598  H   VAL A  46       6.665  17.887  78.305  1.00  7.11           H  
ANISOU  598  H   VAL A  46      900    900    900      0      0      0       H  
ATOM    599  HA  VAL A  46       6.126  16.695  80.701  1.00  7.42           H  
ANISOU  599  HA  VAL A  46      940    940    940      0      0      0       H  
ATOM    600  HB  VAL A  46       4.174  17.865  80.932  1.00  8.11           H  
ANISOU  600  HB  VAL A  46     1027   1027   1027      0      0      0       H  
ATOM    601 HG11 VAL A  46       6.139  18.783  81.822  1.00 10.75           H  
ANISOU  601 HG11 VAL A  46     1362   1362   1362      0      0      0       H  
ATOM    602 HG12 VAL A  46       6.339  19.629  80.517  1.00 10.75           H  
ANISOU  602 HG12 VAL A  46     1362   1362   1362      0      0      0       H  
ATOM    603 HG13 VAL A  46       5.118  19.916  81.458  1.00 10.75           H  
ANISOU  603 HG13 VAL A  46     1362   1362   1362      0      0      0       H  
ATOM    604 HG21 VAL A  46       4.757  19.213  78.530  1.00 11.47           H  
ANISOU  604 HG21 VAL A  46     1453   1453   1453      0      0      0       H  
ATOM    605 HG22 VAL A  46       3.554  18.229  78.735  1.00 11.47           H  
ANISOU  605 HG22 VAL A  46     1453   1453   1453      0      0      0       H  
ATOM    606 HG23 VAL A  46       3.582  19.601  79.492  1.00 11.47           H  
ANISOU  606 HG23 VAL A  46     1453   1453   1453      0      0      0       H  
ATOM    607  N   CYS A  47       5.442  15.293  78.191  1.00  5.67           N  
ANISOU  607  N   CYS A  47      732    809    559    -59    -33     94       N  
ATOM    608  CA  CYS A  47       4.707  14.295  77.474  1.00  5.69           C  
ANISOU  608  CA  CYS A  47      803    873    431    -26    -43      1       C  
ATOM    609  C   CYS A  47       5.124  12.920  77.931  1.00  6.12           C  
ANISOU  609  C   CYS A  47      880    884    504    148    -29     49       C  
ATOM    610  O   CYS A  47       6.289  12.523  77.674  1.00  6.52           O  
ANISOU  610  O   CYS A  47      944    894    577     72    -41     41       O  
ATOM    611  CB  CYS A  47       4.908  14.434  75.955  1.00  5.60           C  
ANISOU  611  CB  CYS A  47      793    764    517    -69     51     82       C  
ATOM    612  SG  CYS A  47       3.897  13.134  75.135  1.00  6.03           S  
ANISOU  612  SG  CYS A  47      884    852    496    -25    -21     41       S  
ATOM    613  H   CYS A  47       6.242  15.481  77.936  1.00  6.80           H  
ANISOU  613  H   CYS A  47      861    861    861      0      0      0       H  
ATOM    614  HA  CYS A  47       3.754  14.411  77.672  1.00  6.82           H  
ANISOU  614  HA  CYS A  47      864    864    864      0      0      0       H  
ATOM    615  HB2 CYS A  47       4.624  15.314  75.660  1.00  6.72           H  
ANISOU  615  HB2 CYS A  47      851    851    851      0      0      0       H  
ATOM    616  HB3 CYS A  47       5.844  14.322  75.730  1.00  6.72           H  
ANISOU  616  HB3 CYS A  47      851    851    851      0      0      0       H  
ATOM    617  N   PRO A  48       4.251  12.090  78.516  1.00  6.52           N  
ANISOU  617  N   PRO A  48      944    901    572     15    -51    108       N  
ATOM    618  CA  PRO A  48       4.704  10.789  79.026  1.00  7.22           C  
ANISOU  618  CA  PRO A  48     1116    878    683     32    -70    135       C  
ATOM    619  C   PRO A  48       5.163   9.853  77.962  1.00  7.44           C  
ANISOU  619  C   PRO A  48     1088    958    712    -19   -122     98       C  
ATOM    620  O   PRO A  48       5.908   8.904  78.236  1.00  9.46           O  
ANISOU  620  O   PRO A  48     1544   1167    794    376   -276     77       O  
ATOM    621  CB  PRO A  48       3.464  10.245  79.763  1.00  7.68           C  
ANISOU  621  CB  PRO A  48     1174    866    806   -119     -6     -7       C  
ATOM    622  CG  PRO A  48       2.287  10.945  79.125  1.00  7.05           C  
ANISOU  622  CG  PRO A  48     1051    862    700   -140     75    139       C  
ATOM    623  CD  PRO A  48       2.810  12.353  78.818  1.00  6.75           C  
ANISOU  623  CD  PRO A  48      862   1029    610   -122     -1     -8       C  
ATOM    624  HA  PRO A  48       5.430  10.928  79.670  1.00  8.67           H  
ANISOU  624  HA  PRO A  48     1098   1098   1098      0      0      0       H  
ATOM    625  HB2 PRO A  48       3.392   9.284  79.653  1.00  9.21           H  
ANISOU  625  HB2 PRO A  48     1166   1166   1166      0      0      0       H  
ATOM    626  HB3 PRO A  48       3.511  10.449  80.711  1.00  9.21           H  
ANISOU  626  HB3 PRO A  48     1166   1166   1166      0      0      0       H  
ATOM    627  HG2 PRO A  48       2.014  10.492  78.312  1.00  8.46           H  
ANISOU  627  HG2 PRO A  48     1071   1071   1071      0      0      0       H  
ATOM    628  HG3 PRO A  48       1.533  10.981  79.734  1.00  8.46           H  
ANISOU  628  HG3 PRO A  48     1071   1071   1071      0      0      0       H  
ATOM    629  HD2 PRO A  48       2.354  12.741  78.054  1.00  8.10           H  
ANISOU  629  HD2 PRO A  48     1026   1026   1026      0      0      0       H  
ATOM    630  HD3 PRO A  48       2.710  12.942  79.582  1.00  8.10           H  
ANISOU  630  HD3 PRO A  48     1026   1026   1026      0      0      0       H  
ATOM    631  N   VAL A  49       4.694  10.039  76.720  1.00  7.28           N  
ANISOU  631  N   VAL A  49     1217    859    622    124   -188     91       N  
ATOM    632  CA  VAL A  49       5.005   9.157  75.603  1.00  7.98           C  
ANISOU  632  CA  VAL A  49     1258    967    732    145    -76     63       C  
ATOM    633  C   VAL A  49       5.939   9.824  74.610  1.00  7.61           C  
ANISOU  633  C   VAL A  49     1102   1012    705    150   -161    -51       C  
ATOM    634  O   VAL A  49       6.182   9.245  73.532  1.00  9.45           O  
ANISOU  634  O   VAL A  49     1712   1095    694    318     25    -66       O  
ATOM    635  CB  VAL A  49       3.725   8.661  74.934  1.00  8.32           C  
ANISOU  635  CB  VAL A  49     1323    899    861    -21    -95     -9       C  
ATOM    636  CG1 VAL A  49       2.968   7.763  75.907  1.00 10.34           C  
ANISOU  636  CG1 VAL A  49     1834   1083    913   -262   -132    221       C  
ATOM    637  CG2 VAL A  49       2.881   9.795  74.349  1.00 10.38           C  
ANISOU  637  CG2 VAL A  49     1728   1052   1068   -105   -588    242       C  
ATOM    638  H   VAL A  49       4.182  10.715  76.575  1.00  8.74           H  
ANISOU  638  H   VAL A  49     1107   1107   1107      0      0      0       H  
ATOM    639  HA  VAL A  49       5.470   8.374  75.966  1.00  9.57           H  
ANISOU  639  HA  VAL A  49     1212   1212   1212      0      0      0       H  
ATOM    640  HB  VAL A  49       4.000   8.095  74.182  1.00  9.98           H  
ANISOU  640  HB  VAL A  49     1264   1264   1264      0      0      0       H  
ATOM    641 HG11 VAL A  49       2.750   8.261  76.698  1.00 15.51           H  
ANISOU  641 HG11 VAL A  49     1964   1964   1964      0      0      0       H  
ATOM    642 HG12 VAL A  49       2.160   7.452  75.493  1.00 15.51           H  
ANISOU  642 HG12 VAL A  49     1964   1964   1964      0      0      0       H  
ATOM    643 HG13 VAL A  49       3.517   7.012  76.143  1.00 15.51           H  
ANISOU  643 HG13 VAL A  49     1964   1964   1964      0      0      0       H  
ATOM    644 HG21 VAL A  49       3.422  10.326  73.759  1.00 15.57           H  
ANISOU  644 HG21 VAL A  49     1972   1972   1972      0      0      0       H  
ATOM    645 HG22 VAL A  49       2.142   9.425  73.859  1.00 15.57           H  
ANISOU  645 HG22 VAL A  49     1972   1972   1972      0      0      0       H  
ATOM    646 HG23 VAL A  49       2.548  10.347  75.061  1.00 15.57           H  
ANISOU  646 HG23 VAL A  49     1972   1972   1972      0      0      0       H  
ATOM    647  N   ASP A  50       6.464  11.030  74.905  1.00  7.17           N  
ANISOU  647  N   ASP A  50     1044    992    619    120    -80     54       N  
ATOM    648  CA  ASP A  50       7.414  11.714  74.061  1.00  6.93           C  
ANISOU  648  CA  ASP A  50      791   1078    698    148    -30   -161       C  
ATOM    649  C   ASP A  50       6.931  11.863  72.597  1.00  7.22           C  
ANISOU  649  C   ASP A  50      961    990    725    371     50    103       C  
ATOM    650  O   ASP A  50       7.712  11.718  71.648  1.00  8.51           O  
ANISOU  650  O   ASP A  50     1076   1321    755    361     87    -99       O  
ATOM    651  CB  ASP A  50       8.754  10.991  74.108  1.00  8.41           C  
ANISOU  651  CB  ASP A  50      980   1293    843    303    -91    -91       C  
ATOM    652  CG  ASP A  50       9.945  11.874  73.783  1.00  8.51           C  
ANISOU  652  CG  ASP A  50      896   1459    797    356    104     -4       C  
ATOM    653  OD1 ASP A  50       9.938  13.085  74.186  1.00 10.01           O  
ANISOU  653  OD1 ASP A  50     1005   1395   1310     81    158    281       O  
ATOM    654  OD2 ASP A  50      10.834  11.377  73.078  1.00 14.13           O  
ANISOU  654  OD2 ASP A  50     1345   2290   1600    458    470     -9       O  
ATOM    655  H   ASP A  50       6.220  11.412  75.635  1.00  8.60           H  
ANISOU  655  H   ASP A  50     1089   1089   1089      0      0      0       H  
ATOM    656  HA  ASP A  50       7.546  12.613  74.427  1.00  8.31           H  
ANISOU  656  HA  ASP A  50     1052   1052   1052      0      0      0       H  
ATOM    657  HB2 ASP A  50       8.876  10.618  74.996  1.00 10.09           H  
ANISOU  657  HB2 ASP A  50     1278   1278   1278      0      0      0       H  
ATOM    658  HB3 ASP A  50       8.733  10.253  73.480  1.00 10.09           H  
ANISOU  658  HB3 ASP A  50     1278   1278   1278      0      0      0       H  
ATOM    659  N   ALA A  51       5.673  12.259  72.454  1.00  6.02           N  
ANISOU  659  N   ALA A  51      888    843    499    182    -16     93       N  
ATOM    660  CA  ALA A  51       5.094  12.374  71.101  1.00  6.09           C  
ANISOU  660  CA  ALA A  51      960    707    589     53    -61    106       C  
ATOM    661  C   ALA A  51       5.526  13.621  70.323  1.00  6.14           C  
ANISOU  661  C   ALA A  51      892    949    436    -20      8     55       C  
ATOM    662  O   ALA A  51       5.636  13.516  69.084  1.00  6.48           O  
ANISOU  662  O   ALA A  51      976    823    604     -5     16     -7       O  
ATOM    663  CB  ALA A  51       3.556  12.351  71.208  1.00  6.46           C  
ANISOU  663  CB  ALA A  51      918    810    666   -145   -101     58       C  
ATOM    664  H   ALA A  51       5.198  12.446  73.146  1.00  7.22           H  
ANISOU  664  H   ALA A  51      914    914    914      0      0      0       H  
ATOM    665  HA  ALA A  51       5.372  11.588  70.587  1.00  7.31           H  
ANISOU  665  HA  ALA A  51      926    926    926      0      0      0       H  
ATOM    666  HB1 ALA A  51       3.281  11.571  71.696  1.00  9.69           H  
ANISOU  666  HB1 ALA A  51     1227   1227   1227      0      0      0       H  
ATOM    667  HB2 ALA A  51       3.255  13.138  71.667  1.00  9.69           H  
ANISOU  667  HB2 ALA A  51     1227   1227   1227      0      0      0       H  
ATOM    668  HB3 ALA A  51       3.175  12.328  70.327  1.00  9.69           H  
ANISOU  668  HB3 ALA A  51     1227   1227   1227      0      0      0       H  
ATOM    669  N   PRO A  52       5.737  14.798  70.926  1.00  5.64           N  
ANISOU  669  N   PRO A  52      711    906    471    -30      6      5       N  
ATOM    670  CA  PRO A  52       6.159  15.949  70.149  1.00  5.74           C  
ANISOU  670  CA  PRO A  52      690    873    564     87    -13    -10       C  
ATOM    671  C   PRO A  52       7.631  15.827  69.794  1.00  5.92           C  
ANISOU  671  C   PRO A  52      857    832    506    -90     11    -63       C  
ATOM    672  O   PRO A  52       8.462  15.634  70.679  1.00  6.75           O  
ANISOU  672  O   PRO A  52      815   1122    565     16    -41    -70       O  
ATOM    673  CB  PRO A  52       5.907  17.135  71.083  1.00  6.05           C  
ANISOU  673  CB  PRO A  52      771    866    605    -50    -58    -84       C  
ATOM    674  CG  PRO A  52       5.023  16.602  72.192  1.00  6.66           C  
ANISOU  674  CG  PRO A  52      956    824    689     83     59    -34       C  
ATOM    675  CD  PRO A  52       5.434  15.155  72.304  1.00  5.66           C  
ANISOU  675  CD  PRO A  52      830    760    508     69    -13      0       C  
ATOM    676  HA  PRO A  52       5.617  16.032  69.337  1.00  6.89           H  
ANISOU  676  HA  PRO A  52      873    873    873      0      0      0       H  
ATOM    677  HB2 PRO A  52       6.743  17.469  71.444  1.00  7.26           H  
ANISOU  677  HB2 PRO A  52      919    919    919      0      0      0       H  
ATOM    678  HB3 PRO A  52       5.463  17.855  70.609  1.00  7.26           H  
ANISOU  678  HB3 PRO A  52      919    919    919      0      0      0       H  
ATOM    679  HG2 PRO A  52       5.183  17.075  73.024  1.00  8.00           H  
ANISOU  679  HG2 PRO A  52     1013   1013   1013      0      0      0       H  
ATOM    680  HG3 PRO A  52       4.085  16.682  71.959  1.00  8.00           H  
ANISOU  680  HG3 PRO A  52     1013   1013   1013      0      0      0       H  
ATOM    681  HD2 PRO A  52       6.213  15.054  72.872  1.00  6.79           H  
ANISOU  681  HD2 PRO A  52      860    860    860      0      0      0       H  
ATOM    682  HD3 PRO A  52       4.711  14.611  72.656  1.00  6.79           H  
ANISOU  682  HD3 PRO A  52      860    860    860      0      0      0       H  
ATOM    683  N   VAL A  53       7.928  15.987  68.504  1.00  5.54           N  
ANISOU  683  N   VAL A  53      683    799    572    -52    -67    -21       N  
ATOM    684  CA  VAL A  53       9.337  15.938  68.023  1.00  6.02           C  
ANISOU  684  CA  VAL A  53      797    831    603    -22    -18     68       C  
ATOM    685  C   VAL A  53       9.621  17.192  67.210  1.00  6.34           C  
ANISOU  685  C   VAL A  53      846    785    720    -85     35     31       C  
ATOM    686  O   VAL A  53       8.764  17.708  66.488  1.00  6.69           O  
ANISOU  686  O   VAL A  53      823    862    792     66    -22    180       O  
ATOM    687  CB  VAL A  53       9.657  14.665  67.253  1.00  6.75           C  
ANISOU  687  CB  VAL A  53      901    906    693     95    165     34       C  
ATOM    688  CG1 VAL A  53       9.494  13.423  68.135  1.00  8.21           C  
ANISOU  688  CG1 VAL A  53     1272    836    935    138     52    145       C  
ATOM    689  CG2 VAL A  53       8.846  14.537  65.999  1.00  7.75           C  
ANISOU  689  CG2 VAL A  53     1197    916    760     40     29    -72       C  
ATOM    690  H   VAL A  53       7.294  16.121  67.938  1.00  6.65           H  
ANISOU  690  H   VAL A  53      842    842    842      0      0      0       H  
ATOM    691  HA  VAL A  53       9.918  15.959  68.811  1.00  7.22           H  
ANISOU  691  HA  VAL A  53      914    914    914      0      0      0       H  
ATOM    692  HB  VAL A  53      10.599  14.714  66.987  1.00  8.09           H  
ANISOU  692  HB  VAL A  53     1025   1025   1025      0      0      0       H  
ATOM    693 HG11 VAL A  53      10.027  13.521  68.928  1.00 12.31           H  
ANISOU  693 HG11 VAL A  53     1559   1559   1559      0      0      0       H  
ATOM    694 HG12 VAL A  53       8.572  13.322  68.379  1.00 12.31           H  
ANISOU  694 HG12 VAL A  53     1559   1559   1559      0      0      0       H  
ATOM    695 HG13 VAL A  53       9.783  12.646  67.650  1.00 12.31           H  
ANISOU  695 HG13 VAL A  53     1559   1559   1559      0      0      0       H  
ATOM    696 HG21 VAL A  53       9.021  15.288  65.426  1.00 11.62           H  
ANISOU  696 HG21 VAL A  53     1472   1472   1472      0      0      0       H  
ATOM    697 HG22 VAL A  53       9.084  13.726  65.545  1.00 11.62           H  
ANISOU  697 HG22 VAL A  53     1472   1472   1472      0      0      0       H  
ATOM    698 HG23 VAL A  53       7.912  14.516  66.222  1.00 11.62           H  
ANISOU  698 HG23 VAL A  53     1472   1472   1472      0      0      0       H  
ATOM    699  N   GLN A  54      10.863  17.581  67.238  1.00  6.83           N  
ANISOU  699  N   GLN A  54      782    931    819   -126    103     73       N  
ATOM    700  CA  GLN A  54      11.351  18.670  66.360  1.00  6.28           C  
ANISOU  700  CA  GLN A  54      726    865    738    -87    -21     73       C  
ATOM    701  C   GLN A  54      11.305  18.204  64.907  1.00  6.39           C  
ANISOU  701  C   GLN A  54      751    867    751     37     -8     98       C  
ATOM    702  O   GLN A  54      11.876  17.151  64.562  1.00  7.66           O  
ANISOU  702  O   GLN A  54     1046   1061    730    288   -119    -91       O  
ATOM    703  CB  GLN A  54      12.827  18.989  66.726  1.00  7.51           C  
ANISOU  703  CB  GLN A  54      796   1024    963   -168    -51    155       C  
ATOM    704  CG AGLN A  54      13.506  20.034  65.841  0.86  8.26           C  
ANISOU  704  CG AGLN A  54      858   1070   1132    -69    227    174       C  
ATOM    705  CG BGLN A  54      13.340  20.182  66.063  0.14  7.27           C  
ANISOU  705  CG BGLN A  54      767   1129    799   -197     -3    151       C  
ATOM    706  CD AGLN A  54      12.916  21.378  66.162  0.86  7.37           C  
ANISOU  706  CD AGLN A  54      960   1106    666    -31     -5     39       C  
ATOM    707  CD BGLN A  54      14.287  20.990  66.905  0.14  6.57           C  
ANISOU  707  CD BGLN A  54      623    999    813   -101    -98    298       C  
ATOM    708  OE1AGLN A  54      13.292  22.026  67.182  0.86  9.13           O  
ANISOU  708  OE1AGLN A  54     1121   1355    906   -205    -42    -56       O  
ATOM    709  OE1BGLN A  54      14.556  20.616  68.095  0.14  8.66           O  
ANISOU  709  OE1BGLN A  54     1217   1412    580   -601     47    340       O  
ATOM    710  NE2AGLN A  54      11.998  21.861  65.375  0.86  8.04           N  
ANISOU  710  NE2AGLN A  54     1031   1072    875   -144   -121     99       N  
ATOM    711  NE2BGLN A  54      14.726  22.101  66.392  0.14  7.24           N  
ANISOU  711  NE2BGLN A  54      778   1294    613   -357   -181    399       N  
ATOM    712  H   GLN A  54      11.412  17.197  67.777  1.00  8.20           H  
ANISOU  712  H   GLN A  54     1039   1039   1039      0      0      0       H  
ATOM    713  HA  GLN A  54      10.796  19.469  66.475  1.00  7.54           H  
ANISOU  713  HA  GLN A  54      955    955    955      0      0      0       H  
ATOM    714  HB2 GLN A  54      12.856  19.299  67.645  1.00  9.01           H  
ANISOU  714  HB2 GLN A  54     1141   1141   1141      0      0      0       H  
ATOM    715  HB3 GLN A  54      13.340  18.167  66.679  1.00  9.01           H  
ANISOU  715  HB3 GLN A  54     1141   1141   1141      0      0      0       H  
ATOM    716  N   ALA A  55      10.650  19.012  64.083  1.00  7.02           N  
ANISOU  716  N   ALA A  55      973    890    740    135    -58    -23       N  
ATOM    717  CA  ALA A  55      10.589  18.786  62.625  1.00  7.97           C  
ANISOU  717  CA  ALA A  55     1171   1055    726    161   -146     14       C  
ATOM    718  C   ALA A  55      10.888  20.082  61.891  1.00  8.29           C  
ANISOU  718  C   ALA A  55     1143   1196    734      3   -118    -65       C  
ATOM    719  O   ALA A  55      11.481  21.028  62.513  1.00  8.14           O  
ANISOU  719  O   ALA A  55     1114   1075    828     70     42     54       O  
ATOM    720  CB  ALA A  55       9.252  18.139  62.226  1.00 10.00           C  
ANISOU  720  CB  ALA A  55     1353   1240   1115     13   -503    165       C  
ATOM    721  OXT ALA A  55      10.550  20.122  60.688  1.00  9.93           O  
ANISOU  721  OXT ALA A  55     1604   1182    893      4   -241    177       O  
ATOM    722  H   ALA A  55      10.245  19.696  64.411  1.00  8.43           H  
ANISOU  722  H   ALA A  55     1068   1068   1068      0      0      0       H  
ATOM    723  HA  ALA A  55      11.300  18.151  62.398  1.00  9.56           H  
ANISOU  723  HA  ALA A  55     1211   1211   1211      0      0      0       H  
ATOM    724  HB1 ALA A  55       9.130  17.325  62.719  1.00 15.01           H  
ANISOU  724  HB1 ALA A  55     1901   1901   1901      0      0      0       H  
ATOM    725  HB2 ALA A  55       8.533  18.744  62.423  1.00 15.01           H  
ANISOU  725  HB2 ALA A  55     1901   1901   1901      0      0      0       H  
ATOM    726  HB3 ALA A  55       9.259  17.946  61.285  1.00 15.01           H  
ANISOU  726  HB3 ALA A  55     1901   1901   1901      0      0      0       H  
TER     727      ALA A  55                                                      
HETATM  728 FE1  SF4 A  61      -0.383  14.097  73.478  1.00  6.17          FE  
ANISOU  728 FE1  SF4 A  61      829    877    579   -162    -85     93      FE  
HETATM  729 FE2  SF4 A  61      -0.472  14.212  76.235  1.00  6.22          FE  
ANISOU  729 FE2  SF4 A  61      820    907    578   -109      8    126      FE  
HETATM  730 FE3  SF4 A  61       0.411  16.375  74.732  1.00  5.87          FE  
ANISOU  730 FE3  SF4 A  61      794    816    567    -77     -6     87      FE  
HETATM  731 FE4  SF4 A  61       1.898  14.148  74.918  1.00  5.87          FE  
ANISOU  731 FE4  SF4 A  61      804    823    546    -67    -55     63      FE  
HETATM  732  S1  SF4 A  61       1.375  15.546  76.617  1.00  6.02           S  
ANISOU  732  S1  SF4 A  61      869    829    533    -39    -10     28       S  
HETATM  733  S2  SF4 A  61       1.497  15.333  73.029  1.00  6.00           S  
ANISOU  733  S2  SF4 A  61      827    841    555   -110    -13     88       S  
HETATM  734  S3  SF4 A  61       0.312  12.505  74.972  1.00  6.65           S  
ANISOU  734  S3  SF4 A  61      962    862    640   -153    -98    136       S  
HETATM  735  S4  SF4 A  61      -1.696  15.449  74.720  1.00  6.53           S  
ANISOU  735  S4  SF4 A  61      816    970    633    -97     -2    127       S  
HETATM  736 FE1  SF4 A  62       6.331  24.490  70.195  1.00  5.76          FE  
ANISOU  736 FE1  SF4 A  62      860    749    526    -85    -27     58      FE  
HETATM  737 FE2  SF4 A  62       7.400  24.788  72.689  1.00  6.10          FE  
ANISOU  737 FE2  SF4 A  62      911    786    563   -111    -77      5      FE  
HETATM  738 FE3  SF4 A  62       5.861  22.588  72.085  1.00  5.74          FE  
ANISOU  738 FE3  SF4 A  62      876    739    510    -75    -59     52      FE  
HETATM  739 FE4  SF4 A  62       4.733  25.052  72.285  1.00  5.93          FE  
ANISOU  739 FE4  SF4 A  62      896    781    521    -66     -6     23      FE  
HETATM  740  S1  SF4 A  62       5.700  23.824  73.948  1.00  6.20           S  
ANISOU  740  S1  SF4 A  62      987    788    521    -65    -63     30       S  
HETATM  741  S2  SF4 A  62       4.296  23.550  70.681  1.00  5.90           S  
ANISOU  741  S2  SF4 A  62      877    815    494    -62    -58     69       S  
HETATM  742  S3  SF4 A  62       6.383  26.386  71.399  1.00  6.04           S  
ANISOU  742  S3  SF4 A  62      907    750    582    -97     -6     37       S  
HETATM  743  S4  SF4 A  62       7.909  23.150  71.190  1.00  6.05           S  
ANISOU  743  S4  SF4 A  62      863    792    589    -73    -83     18       S  
HETATM  744  O   HOH A 101       1.235  18.553  65.615  1.00  6.40           O  
ANISOU  744  O   HOH A 101      869    912    589     30    -62     77       O  
HETATM  745  O   HOH A 102       3.440  15.437  82.376  1.00  6.50           O  
ANISOU  745  O   HOH A 102      830   1000    580     16     10    -56       O  
HETATM  746  O   HOH A 103       4.259  33.094  61.920  1.00  7.08           O  
ANISOU  746  O   HOH A 103      901    856    867   -109   -172     32       O  
HETATM  747  O   HOH A 104       7.423  26.769  63.943  1.00  7.36           O  
ANISOU  747  O   HOH A 104     1059    892    777    -58    -77    -50       O  
HETATM  748  O   HOH A 105       4.233  21.440  63.148  1.00  7.48           O  
ANISOU  748  O   HOH A 105      966   1132    673      6    -12     57       O  
HETATM  749  O   HOH A 106      11.677  15.543  62.316  1.00  8.51           O  
ANISOU  749  O   HOH A 106     1373   1028    752    244     40    -47       O  
HETATM  750  O   HOH A 107      -0.493  16.372  65.476  0.88  7.69           O  
ANISOU  750  O   HOH A 107     1152    909    788   -202   -189      2       O  
HETATM  751  O   HOH A 108      -1.281  25.579  73.930  1.00  8.58           O  
ANISOU  751  O   HOH A 108     1434   1012    735    -96    220    104       O  
HETATM  752  O   HOH A 109      11.160  15.392  71.228  1.00  9.98           O  
ANISOU  752  O   HOH A 109      976   1735    986    169     36     87       O  
HETATM  753  O   HOH A 110       3.931  12.479  62.885  0.89  9.62           O  
ANISOU  753  O   HOH A 110     1444   1368    754    382   -117     11       O  
HETATM  754  O   HOH A 111      14.223  27.124  67.154  0.63  6.47           O  
ANISOU  754  O   HOH A 111      876    957    565   -253     68    207       O  
HETATM  755  O   HOH A 112       3.661  33.876  70.213  1.00  9.99           O  
ANISOU  755  O   HOH A 112     1581   1237    885     22    168     -5       O  
HETATM  756  O   HOH A 113      -2.975  24.247  67.649  1.00 10.71           O  
ANISOU  756  O   HOH A 113     1162   1870    937    -70      6    211       O  
HETATM  757  O   HOH A 114      12.553  17.633  72.492  1.00 10.77           O  
ANISOU  757  O   HOH A 114     1320   1565   1107     82   -253    247       O  
HETATM  758  O   HOH A 115      -0.893  19.853  82.506  1.00 10.80           O  
ANISOU  758  O   HOH A 115     1859   1325    818     15    -19    151       O  
HETATM  759  O   HOH A 116      12.061  18.564  75.142  1.00 11.73           O  
ANISOU  759  O   HOH A 116     1425   1479   1443     68    -64     24       O  
HETATM  760  O   HOH A 117       1.530   4.588  75.090  1.00 12.64           O  
ANISOU  760  O   HOH A 117     2391   1309    985     50    103     51       O  
HETATM  761  O   HOH A 118       8.569  10.840  78.016  0.79  9.66           O  
ANISOU  761  O   HOH A 118     1043   1365   1171    251      7   -194       O  
HETATM  762  O   HOH A 119       8.645  20.947  79.828  1.00 12.51           O  
ANISOU  762  O   HOH A 119     2051   1714    872   -521   -418    247       O  
HETATM  763  O   HOH A 120       1.093   5.759  72.636  1.00 13.74           O  
ANISOU  763  O   HOH A 120     3035   1032   1025    179    253     68       O  
HETATM  764  O   HOH A 121      11.487  18.093  58.998  1.00 12.78           O  
ANISOU  764  O   HOH A 121     2167   1514   1054    335      5    126       O  
HETATM  765  O   HOH A 122       9.684  13.260  77.003  1.00 12.55           O  
ANISOU  765  O   HOH A 122     1681   1608   1360    516   -331   -331       O  
HETATM  766  O   HOH A 123       0.878  28.541  57.323  1.00 13.95           O  
ANISOU  766  O   HOH A 123     2405   1804    960    -60   -539   -115       O  
HETATM  767  O   HOH A 124      12.578  25.010  63.565  0.86 13.84           O  
ANISOU  767  O   HOH A 124     2209   1327   1593   -703   1120   -337       O  
HETATM  768  O   HOH A 125      14.536  16.448  65.017  0.79 12.18           O  
ANISOU  768  O   HOH A 125     1448   1247   1818     84     45   -414       O  
HETATM  769  O   HOH A 126       6.773   9.589  68.842  0.74 11.81           O  
ANISOU  769  O   HOH A 126     2125   1428    823    720    340    -26       O  
HETATM  770  O   HOH A 127       9.621  10.542  70.013  0.77 12.46           O  
ANISOU  770  O   HOH A 127     1462   2005   1150    179    374     -1       O  
HETATM  771  O   HOH A 128       4.829  32.577  77.949  0.65 10.97           O  
ANISOU  771  O   HOH A 128     1301   1630   1134    -20   -295   -248       O  
HETATM  772  O   HOH A 129      -2.381  26.489  63.108  1.00 16.37           O  
ANISOU  772  O   HOH A 129     1726   2814   1526    287   -261   -803       O  
HETATM  773  O   HOH A 130      11.933  21.953  59.222  1.00 17.06           O  
ANISOU  773  O   HOH A 130     2372   2310   1639   -873   -583    633       O  
HETATM  774  O   HOH A 131       6.100   6.488  73.460  1.00 17.24           O  
ANISOU  774  O   HOH A 131     1620   2209   2559    532   -573  -1084       O  
HETATM  775  O   HOH A 132      -5.422  16.047  64.993  1.00 16.61           O  
ANISOU  775  O   HOH A 132     2510   2580   1067    571    498     77       O  
HETATM  776  O   HOH A 133      -1.857  29.032  67.993  0.72 15.63           O  
ANISOU  776  O   HOH A 133     2390   2165   1239     45    643    469       O  
HETATM  777  O   HOH A 134      -2.382   6.932  70.265  1.00 18.60           O  
ANISOU  777  O   HOH A 134     2625   2501   1765   -917    347   -146       O  
HETATM  778  O   HOH A 135      -7.738  22.528  72.743  1.00 20.40           O  
ANISOU  778  O   HOH A 135     1683   3587   2289     89    250  -1172       O  
HETATM  779  O   HOH A 136      -1.496  30.871  63.685  0.73 19.41           O  
ANISOU  779  O   HOH A 136     2875   2416   1902   1723    429   1052       O  
HETATM  780  O   HOH A 137      -0.563  27.316  76.789  1.00 17.63           O  
ANISOU  780  O   HOH A 137     3014   1842   1677     83   -448   -334       O  
HETATM  781  O   HOH A 138      -4.700   9.915  71.205  1.00 18.64           O  
ANISOU  781  O   HOH A 138     1610   3364   1935   -180   -187   -155       O  
HETATM  782  O   HOH A 139       7.657  20.460  83.783  0.75 16.49           O  
ANISOU  782  O   HOH A 139     2243   3010    859   -305    -54     24       O  
HETATM  783  O   HOH A 140      15.030  17.552  69.479  1.00 21.91           O  
ANISOU  783  O   HOH A 140     1875   3640   2602   -982    385  -1375       O  
HETATM  784  O   HOH A 141      -5.344  20.379  78.415  0.77 17.77           O  
ANISOU  784  O   HOH A 141     1270   1700   3614    195    702   -314       O  
HETATM  785  O   HOH A 142      -3.254  26.650  68.686  0.68 15.01           O  
ANISOU  785  O   HOH A 142     1783   1604   2174    277    785    416       O  
HETATM  786  O   HOH A 143      14.150  24.938  75.754  0.81 19.17           O  
ANISOU  786  O   HOH A 143     1607   2025   3471   -294   -684   -216       O  
HETATM  787  O   HOH A 144      14.261  21.309  59.798  0.89 21.13           O  
ANISOU  787  O   HOH A 144     2569   2538   2722   -391   1056   1249       O  
HETATM  788  O   HOH A 145      -1.520  29.595  61.260  1.00 28.43           O  
ANISOU  788  O   HOH A 145     1574   4801   4162    476   -128  -2219       O  
HETATM  789  O   HOH A 146      14.978  18.252  62.645  0.88 21.87           O  
ANISOU  789  O   HOH A 146     2891   2576   2637     40   -128   -636       O  
HETATM  790  O   HOH A 147       7.763   8.509  71.345  1.00 21.27           O  
ANISOU  790  O   HOH A 147     3251   2265   2367   1521   1167   -216       O  
HETATM  791  O   HOH A 148      13.967  21.950  71.537  0.63 15.41           O  
ANISOU  791  O   HOH A 148     1748   1329   2634    437   -769   -206       O  
HETATM  792  O   HOH A 149       4.110   4.110  74.820  0.42 23.90           O  
ANISOU  792  O   HOH A 149     3054   3054   2749   1562   -503    504       O  
HETATM  793  O   HOH A 150      15.185  21.277  68.920  0.62 21.91           O  
ANISOU  793  O   HOH A 150     1970   4380   1771    278   -985   -239       O  
HETATM  794  O   HOH A 151      -1.132  31.087  69.899  0.47 15.81           O  
ANISOU  794  O   HOH A 151     2610   2123   1127    -24    715     23       O  
HETATM  795  O   HOH A 152      -2.695   9.732  67.940  0.83 25.98           O  
ANISOU  795  O   HOH A 152     2013   4463   3152    594    484   1864       O  
HETATM  796  O   HOH A 153      11.342  20.907  78.854  0.78 26.02           O  
ANISOU  796  O   HOH A 153     3173   3701   2769    -29   -833   -350       O  
HETATM  797  O   HOH A 154       6.035  22.822  82.755  0.56 16.26           O  
ANISOU  797  O   HOH A 154     2213   1747   2064   -544   -333    121       O  
HETATM  798  O   HOH A 155       7.932  23.197  80.881  0.67 26.12           O  
ANISOU  798  O   HOH A 155     5364   2578   1735    939  -1486   -338       O  
HETATM  799  O   HOH A 156       6.538  25.980  79.612  0.69 26.27           O  
ANISOU  799  O   HOH A 156     2441   4993   2299   -131  -1327   -847       O  
HETATM  800  O   HOH A 157      13.445  26.034  78.572  0.66 21.54           O  
ANISOU  800  O   HOH A 157     3042   2434   2508   -544   -926    620       O  
HETATM  801  O   HOH A 158      11.818  22.559  77.315  0.55 24.52           O  
ANISOU  801  O   HOH A 158     2271   3561   3254  -1532   -806   1107       O  
HETATM  802  O   HOH A 159      -6.642  29.846  69.150  0.64 26.86           O  
ANISOU  802  O   HOH A 159     2788   3847   3320    736    343    308       O  
HETATM  803  O   HOH A 160      11.186  24.688  78.687  1.00 36.41           O  
ANISOU  803  O   HOH A 160     3167   3445   6882   -901   -272    389       O  
HETATM  804  O   HOH A 161      -7.222  15.301  70.595  0.86 28.96           O  
ANISOU  804  O   HOH A 161     2509   4760   3462     41   -275  -1911       O  
HETATM  805  O   HOH A 162      10.090  23.250  61.602  0.69  8.68           O  
ANISOU  805  O   HOH A 162     1341    836   1038     85    222    172       O  
HETATM  806  O   HOH A 163      11.549  12.598  71.034  0.53  8.14           O  
ANISOU  806  O   HOH A 163      941   1453    621    271      5    171       O  
HETATM  807  O   HOH A 164      -4.003  28.463  63.841  0.68 29.39           O  
ANISOU  807  O   HOH A 164     2323   2590   5978    821     42   -953       O  
HETATM  808  O   HOH A 165      14.220  20.954  62.357  0.39  9.80           O  
ANISOU  808  O   HOH A 165     1165   1446   1019    -37    -44   -197       O  
HETATM  809  O   HOH A 166      -4.283  27.147  71.347  0.63 17.93           O  
ANISOU  809  O   HOH A 166     1570   2443   2633     63   -459      8       O  
HETATM  810  O   HOH A 167      13.228  13.704  74.271  0.35 11.24           O  
ANISOU  810  O   HOH A 167      824   1997   1344   -253    -52    400       O  
HETATM  811  O   HOH A 168      12.167  14.464  74.150  0.47  9.25           O  
ANISOU  811  O   HOH A 168      873    900   1653    -88    404   -295       O  
HETATM  812  O   HOH A 169       9.054  26.728  77.586  0.53 13.62           O  
ANISOU  812  O   HOH A 169     2100   1198   1750    -69   -388     87       O  
HETATM  813  O   HOH A 170       2.474  33.810  74.917  0.55 15.22           O  
ANISOU  813  O   HOH A 170     2207   1150   2282   -135    842   -646       O  
HETATM  814  O   HOH A 171      -8.061  15.667  76.121  0.80 26.71           O  
ANISOU  814  O   HOH A 171     3214   2036   4649  -1087   1567  -1616       O  
HETATM  815  O   HOH A 172       1.075   8.998  61.839  0.59 15.63           O  
ANISOU  815  O   HOH A 172     1687   2465   1642    102   -425   -542       O  
HETATM  816  O   HOH A 173       1.334  33.179  71.410  0.46 19.05           O  
ANISOU  816  O   HOH A 173     1857   1122   4079    665   1932   1132       O  
HETATM  817  O   HOH A 174       1.874   8.895  60.695  0.44 17.37           O  
ANISOU  817  O   HOH A 174     1545   2862   2029    307   -440   -345       O  
HETATM  818  O   HOH A 175      -7.516  20.169  75.780  0.75 28.81           O  
ANISOU  818  O   HOH A 175     4408   2590   3677      1   2161   -890       O  
HETATM  819  O   HOH A 177      13.501  22.663  62.548  0.61 16.37           O  
ANISOU  819  O   HOH A 177     1829   1677   2559   -233    598   -196       O  
HETATM  820  O   HOH A 179     -10.711  17.809  69.778  0.81 31.04           O  
ANISOU  820  O   HOH A 179     2102   5398   4003  -1480    718  -1996       O  
HETATM  821  O   HOH A 180     -11.438  15.450  60.975  0.55 22.19           O  
ANISOU  821  O   HOH A 180     1602   4359   2261   -398    251    683       O  
HETATM  822  O   HOH A 181      -9.515  20.370  64.662  0.66 32.11           O  
ANISOU  822  O   HOH A 181     2126   5428   4346    482   1227   -844       O  
HETATM  823  O   HOH A 182      -9.982  25.496  73.835  0.48 22.48           O  
ANISOU  823  O   HOH A 182     3249   2114   2967   1535    512   -953       O  
HETATM  824  O   HOH A 183      -4.732  25.366  78.441  0.57 34.06           O  
ANISOU  824  O   HOH A 183     2862   6049   3711   1438  -1661  -1014       O  
HETATM  825  O   HOH A 184      16.431  16.462  67.382  0.53 24.79           O  
ANISOU  825  O   HOH A 184     2807   2872   3508   -204   -250   -222       O  
HETATM  826  O   HOH A 185      -9.969  21.221  73.915  0.45 28.07           O  
ANISOU  826  O   HOH A 185     2568   4302   3530    912   -130  -1639       O  
HETATM  827  O   HOH A 186       2.671  28.369  79.727  1.00 43.55           O  
ANISOU  827  O   HOH A 186     7687   5236   3217    354   1642    655       O  
HETATM  828  O   HOH A 187      -3.250  31.680  71.219  0.42 21.55           O  
ANISOU  828  O   HOH A 187     2732   3204   2050   1255   -474    146       O  
HETATM  829  O   HOH A 188      -7.390  21.960  66.609  0.51 31.47           O  
ANISOU  829  O   HOH A 188     1788   7413   2462     91    277   1605       O  
HETATM  830  O   HOH A 189      -5.399  25.954  73.214  0.58 29.85           O  
ANISOU  830  O   HOH A 189     4431   2339   4292   1715    724   -252       O  
HETATM  831  O   HOH A 190      15.302  21.554  73.767  0.55 30.50           O  
ANISOU  831  O   HOH A 190     2788   4931   3584   1278   -596  -1313       O  
HETATM  832  O   HOH A 191       0.187   8.176  59.534  0.41 27.74           O  
ANISOU  832  O   HOH A 191     3915   5461    902     38   -449    822       O  
HETATM  833  O   HOH A 192      -4.647   6.507  69.431  0.38 27.11           O  
ANISOU  833  O   HOH A 192     4366   3356   2325  -2078     42   -554       O  
HETATM  834  O   HOH A 193      -1.382   5.533  68.133  0.45 26.10           O  
ANISOU  834  O   HOH A 193     4886   2166   2618   -618   2136   -339       O  
HETATM  835  O   HOH A 194      13.673  20.398  75.853  0.44 32.45           O  
ANISOU  835  O   HOH A 194     4015   4438   3570     22   -737   1486       O  
HETATM  836  O   HOH A 195      -9.479  21.919  69.581  0.41 21.60           O  
ANISOU  836  O   HOH A 195     2998   1978   3030    897   -953    401       O  
HETATM  837  O   HOH A 196      16.398  18.001  66.329  0.47 23.92           O  
ANISOU  837  O   HOH A 196     1710   2587   4568    800  -1074   -162       O  
CONECT  118  728                                                                
CONECT  156  729                                                                
CONECT  183  730                                                                
CONECT  237  739                                                                
CONECT  501  736                                                                
CONECT  542  737                                                                
CONECT  569  738                                                                
CONECT  612  731                                                                
CONECT  728  118  733  734  735                                                 
CONECT  729  156  732  734  735                                                 
CONECT  730  183  732  733  735                                                 
CONECT  731  612  732  733  734                                                 
CONECT  732  729  730  731                                                      
CONECT  733  728  730  731                                                      
CONECT  734  728  729  731                                                      
CONECT  735  728  729  730                                                      
CONECT  736  501  741  742  743                                                 
CONECT  737  542  740  742  743                                                 
CONECT  738  569  740  741  743                                                 
CONECT  739  237  740  741  742                                                 
CONECT  740  737  738  739                                                      
CONECT  741  736  738  739                                                      
CONECT  742  736  737  739                                                      
CONECT  743  736  737  738                                                      
MASTER      291    0    2    2    2    0    4    6  836    1   24    5          
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.