HEADER    ELECTRON TRANSPORT                      16-MAY-01   1J7B              
TITLE     STRUCTURE OF THE ANABAENA FERREDOXIN MUTANT E94K                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERREDOXIN I;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NOSTOC SP. PCC;                                 
SOURCE   3 ORGANISM_TAXID: 103690;                                              
SOURCE   4 STRAIN: 7120;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: JM109;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PAN662                                    
KEYWDS    ELECTRON TRANSPORT, IRON SULFUR, FERREDOXIN                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.HURLEY,A.M.WEBER-MAIN,M.T.STANKOVICH,M.M.BENNING,J.B.THODEN,      
AUTHOR   2 J.L.VANHOOKE,H.M.HOLDEN,Y.K.CHAE,B.XIA,H.CHENG,J.L.MARKLEY,          
AUTHOR   3 M.MARTINEZ-JULVEZ,C.GOMEZ-MORENO,J.L.SCHMEITS,G.TOLLIN               
REVDAT   7   07-FEB-24 1J7B    1       REMARK                                   
REVDAT   6   27-OCT-21 1J7B    1       REMARK SEQADV LINK                       
REVDAT   5   04-OCT-17 1J7B    1       REMARK                                   
REVDAT   4   13-JUL-11 1J7B    1       VERSN                                    
REVDAT   3   24-FEB-09 1J7B    1       VERSN                                    
REVDAT   2   01-APR-03 1J7B    1       JRNL                                     
REVDAT   1   23-MAY-01 1J7B    0                                                
SPRSDE     23-MAY-01 1J7B      1QOD                                             
JRNL        AUTH   J.K.HURLEY,A.M.WEBER-MAIN,M.T.STANKOVICH,M.M.BENNING,        
JRNL        AUTH 2 J.B.THODEN,J.L.VANHOOKE,H.M.HOLDEN,Y.K.CHAE,B.XIA,H.CHENG,   
JRNL        AUTH 3 J.L.MARKLEY,M.MARTINEZ-JULVEZ,C.GOMEZ-MORENO,J.L.SCHMEITS,   
JRNL        AUTH 4 G.TOLLIN                                                     
JRNL        TITL   STRUCTURE-FUNCTION RELATIONSHIPS IN ANABAENA FERREDOXIN:     
JRNL        TITL 2 CORRELATIONS BETWEEN X-RAY CRYSTAL STRUCTURES, REDUCTION     
JRNL        TITL 3 POTENTIALS, AND RATE CONSTANTS OF ELECTRON TRANSFER TO       
JRNL        TITL 4 FERREDOXIN:NADP+ REDUCTASE FOR SITE-SPECIFIC FERREDOXIN      
JRNL        TITL 5 MUTANTS.                                                     
JRNL        REF    BIOCHEMISTRY                  V.  36 11100 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9287153                                                      
JRNL        DOI    10.1021/BI9709001                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 81.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 9797                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.183                  
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) : 9797                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 750                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 68                                      
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.012 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.275 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : ENGH & HUBER                                     
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1J7B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013449.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : SUPPER MIRRORS                     
REMARK 200  OPTICS                         : SUPPER MIRRORS                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : FRAMBO                             
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10375                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.03300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: TNT                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM SUCCINATE,   
REMARK 280  2-METHYL-2,4-PENTANEDIOL, PH 5.5, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.80000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       45.40000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       45.40000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       90.80000            
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 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    GLU A  17   CD    GLU A  17   OE2     0.088                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  22   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A  22   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP A  23   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TYR A  25   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A  36   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A  42   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP A  59   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A  62   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A  62   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP A  67   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ASP A  68   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A  69   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ASP A  86   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  86   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A  96   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  40      -80.01   -143.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES A 100  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  41   SG                                                     
REMARK 620 2 FES A 100   S1  121.7                                              
REMARK 620 3 FES A 100   S2   98.7 105.1                                        
REMARK 620 4 CYS A  46   SG  107.2 107.5 117.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES A 100  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  49   SG                                                     
REMARK 620 2 FES A 100   S1  110.6                                              
REMARK 620 3 FES A 100   S2  111.0 103.8                                        
REMARK 620 4 CYS A  79   SG  109.8 119.5 101.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 100                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1J7A   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE ANABAENA FERREDOXIN D68K MUTANT                     
REMARK 900 RELATED ID: 1J7C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE ANABAENA FERREDOXIN MUTANT E95K                     
DBREF  1J7B A    1    98  UNP    P0A3C7   FER1_ANASP       1     98             
SEQADV 1J7B LYS A   94  UNP  P0A3C7    GLU    94 ENGINEERED MUTATION            
SEQRES   1 A   98  ALA THR PHE LYS VAL THR LEU ILE ASN GLU ALA GLU GLY          
SEQRES   2 A   98  THR LYS HIS GLU ILE GLU VAL PRO ASP ASP GLU TYR ILE          
SEQRES   3 A   98  LEU ASP ALA ALA GLU GLU GLN GLY TYR ASP LEU PRO PHE          
SEQRES   4 A   98  SER CYS ARG ALA GLY ALA CYS SER THR CYS ALA GLY LYS          
SEQRES   5 A   98  LEU VAL SER GLY THR VAL ASP GLN SER ASP GLN SER PHE          
SEQRES   6 A   98  LEU ASP ASP ASP GLN ILE GLU ALA GLY TYR VAL LEU THR          
SEQRES   7 A   98  CYS VAL ALA TYR PRO THR SER ASP VAL VAL ILE GLN THR          
SEQRES   8 A   98  HIS LYS LYS GLU ASP LEU TYR                                  
HET    FES  A 100       4                                                       
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
FORMUL   2  FES    FE2 S2                                                       
FORMUL   3  HOH   *68(H2 O)                                                     
HELIX    1   1 TYR A   25  GLN A   33  1                                   9    
HELIX    2   2 ASP A   67  ALA A   73  1                                   7    
HELIX    3   3 CYS A   79  ALA A   81  5                                   3    
HELIX    4   4 LYS A   93  LEU A   97  5                                   5    
SHEET    1   A 5 THR A  14  PRO A  21  0                                        
SHEET    2   A 5 THR A   2  ASN A   9 -1  N  PHE A   3   O  VAL A  20           
SHEET    3   A 5 VAL A  87  GLN A  90  1  O  VAL A  87   N  THR A   6           
SHEET    4   A 5 ALA A  50  SER A  55 -1  N  LYS A  52   O  GLN A  90           
SHEET    5   A 5 TYR A  75  LEU A  77 -1  N  VAL A  76   O  GLY A  51           
SHEET    1   B 2 VAL A  58  ASP A  59  0                                        
SHEET    2   B 2 TYR A  82  PRO A  83 -1  N  TYR A  82   O  ASP A  59           
LINK         SG  CYS A  41                FE1  FES A 100     1555   1555  2.29  
LINK         SG  CYS A  46                FE1  FES A 100     1555   1555  2.26  
LINK         SG  CYS A  49                FE2  FES A 100     1555   1555  2.25  
LINK         SG  CYS A  79                FE2  FES A 100     1555   1555  2.27  
SITE     1 AC1  8 SER A  40  CYS A  41  ARG A  42  GLY A  44                    
SITE     2 AC1  8 ALA A  45  CYS A  46  CYS A  49  CYS A  79                    
CRYST1   38.300   38.300  136.200  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.026110  0.015074  0.000000        0.00000                         
SCALE2      0.000000  0.030149  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007342        0.00000                         
ATOM      1  N   ALA A   1       2.377  -9.449  67.746  1.00 27.15           N  
ATOM      2  CA  ALA A   1       3.023 -10.377  66.824  1.00 34.81           C  
ATOM      3  C   ALA A   1       4.470 -10.011  66.743  1.00 29.25           C  
ATOM      4  O   ALA A   1       4.864  -8.934  67.155  1.00 30.77           O  
ATOM      5  CB  ALA A   1       2.463 -10.270  65.417  1.00 29.55           C  
ATOM      6  N   THR A   2       5.239 -10.906  66.179  1.00 23.88           N  
ATOM      7  CA  THR A   2       6.672 -10.726  65.993  1.00 42.14           C  
ATOM      8  C   THR A   2       6.990 -11.084  64.545  1.00 31.88           C  
ATOM      9  O   THR A   2       6.663 -12.202  64.103  1.00 39.74           O  
ATOM     10  CB  THR A   2       7.462 -11.633  66.961  1.00 37.23           C  
ATOM     11  OG1 THR A   2       7.044 -11.385  68.290  1.00 35.80           O  
ATOM     12  CG2 THR A   2       8.959 -11.388  66.830  1.00 24.81           C  
ATOM     13  N   PHE A   3       7.611 -10.150  63.795  1.00 26.02           N  
ATOM     14  CA  PHE A   3       7.914 -10.380  62.380  1.00 23.14           C  
ATOM     15  C   PHE A   3       9.351 -10.697  62.073  1.00 36.68           C  
ATOM     16  O   PHE A   3      10.284 -10.177  62.691  1.00 25.57           O  
ATOM     17  CB  PHE A   3       7.488  -9.161  61.538  1.00 23.13           C  
ATOM     18  CG  PHE A   3       6.029  -8.899  61.709  1.00 23.46           C  
ATOM     19  CD1 PHE A   3       5.082  -9.773  61.175  1.00 32.11           C  
ATOM     20  CD2 PHE A   3       5.580  -7.792  62.423  1.00 29.21           C  
ATOM     21  CE1 PHE A   3       3.716  -9.530  61.336  1.00 26.61           C  
ATOM     22  CE2 PHE A   3       4.217  -7.529  62.584  1.00 41.39           C  
ATOM     23  CZ  PHE A   3       3.280  -8.403  62.032  1.00 34.21           C  
ATOM     24  N   LYS A   4       9.539 -11.525  61.061  1.00 24.00           N  
ATOM     25  CA  LYS A   4      10.885 -11.805  60.653  1.00 20.29           C  
ATOM     26  C   LYS A   4      11.318 -10.663  59.750  1.00 36.37           C  
ATOM     27  O   LYS A   4      10.514 -10.230  58.907  1.00 28.87           O  
ATOM     28  CB  LYS A   4      10.905 -13.074  59.849  1.00 35.64           C  
ATOM     29  CG  LYS A   4      12.282 -13.502  59.365  1.00 42.82           C  
ATOM     30  CD  LYS A   4      12.150 -14.855  58.690  1.00 72.50           C  
ATOM     31  CE  LYS A   4      13.432 -15.445  58.144  1.00100.00           C  
ATOM     32  NZ  LYS A   4      13.313 -16.898  57.931  1.00100.00           N  
ATOM     33  N   VAL A   5      12.555 -10.190  59.944  1.00 25.68           N  
ATOM     34  CA  VAL A   5      13.120  -9.104  59.145  1.00 22.12           C  
ATOM     35  C   VAL A   5      14.466  -9.518  58.608  1.00 24.33           C  
ATOM     36  O   VAL A   5      15.423  -9.835  59.347  1.00 24.55           O  
ATOM     37  CB  VAL A   5      13.193  -7.764  59.886  1.00 29.92           C  
ATOM     38  CG1 VAL A   5      13.906  -6.722  59.014  1.00 21.92           C  
ATOM     39  CG2 VAL A   5      11.800  -7.289  60.242  1.00 20.49           C  
ATOM     40  N   THR A   6      14.540  -9.549  57.284  1.00 20.66           N  
ATOM     41  CA  THR A   6      15.771  -9.955  56.646  1.00 19.42           C  
ATOM     42  C   THR A   6      16.564  -8.746  56.185  1.00 26.55           C  
ATOM     43  O   THR A   6      16.051  -7.955  55.437  1.00 26.62           O  
ATOM     44  CB  THR A   6      15.477 -10.915  55.469  1.00 40.30           C  
ATOM     45  OG1 THR A   6      14.776 -12.064  55.930  1.00 29.90           O  
ATOM     46  CG2 THR A   6      16.757 -11.320  54.758  1.00 30.26           C  
ATOM     47  N   LEU A   7      17.798  -8.603  56.657  1.00 24.79           N  
ATOM     48  CA  LEU A   7      18.625  -7.478  56.311  1.00 28.71           C  
ATOM     49  C   LEU A   7      19.619  -7.889  55.265  1.00 26.77           C  
ATOM     50  O   LEU A   7      20.368  -8.856  55.450  1.00 26.17           O  
ATOM     51  CB  LEU A   7      19.408  -6.903  57.517  1.00 23.37           C  
ATOM     52  CG  LEU A   7      18.533  -6.674  58.748  1.00 27.18           C  
ATOM     53  CD1 LEU A   7      19.420  -6.473  59.950  1.00 25.58           C  
ATOM     54  CD2 LEU A   7      17.643  -5.463  58.567  1.00 22.08           C  
ATOM     55  N   ILE A   8      19.657  -7.107  54.199  1.00 24.03           N  
ATOM     56  CA  ILE A   8      20.592  -7.410  53.123  1.00 21.57           C  
ATOM     57  C   ILE A   8      21.493  -6.267  52.790  1.00 17.55           C  
ATOM     58  O   ILE A   8      21.044  -5.168  52.486  1.00 27.87           O  
ATOM     59  CB  ILE A   8      19.802  -7.734  51.870  1.00 38.73           C  
ATOM     60  CG1 ILE A   8      19.126  -9.076  52.048  1.00 29.15           C  
ATOM     61  CG2 ILE A   8      20.695  -7.758  50.635  1.00 37.58           C  
ATOM     62  CD1 ILE A   8      17.806  -9.100  51.316  1.00 49.60           C  
ATOM     63  N   ASN A   9      22.775  -6.534  52.854  1.00 21.16           N  
ATOM     64  CA  ASN A   9      23.740  -5.535  52.521  1.00 25.80           C  
ATOM     65  C   ASN A   9      24.334  -5.986  51.199  1.00 35.20           C  
ATOM     66  O   ASN A   9      25.167  -6.892  51.123  1.00 31.22           O  
ATOM     67  CB  ASN A   9      24.807  -5.512  53.590  1.00 22.18           C  
ATOM     68  CG  ASN A   9      25.757  -4.376  53.356  1.00 35.63           C  
ATOM     69  OD1 ASN A   9      25.975  -3.958  52.221  1.00 30.23           O  
ATOM     70  ND2 ASN A   9      26.336  -3.877  54.436  1.00 35.11           N  
ATOM     71  N   GLU A  10      23.838  -5.388  50.140  1.00 25.77           N  
ATOM     72  CA  GLU A  10      24.270  -5.776  48.809  1.00 24.04           C  
ATOM     73  C   GLU A  10      25.770  -5.668  48.546  1.00 34.64           C  
ATOM     74  O   GLU A  10      26.358  -6.567  47.941  1.00 36.22           O  
ATOM     75  CB  GLU A  10      23.505  -4.950  47.758  1.00 25.38           C  
ATOM     76  CG  GLU A  10      22.032  -5.312  47.600  1.00 27.78           C  
ATOM     77  CD  GLU A  10      21.521  -4.659  46.339  1.00 29.63           C  
ATOM     78  OE1 GLU A  10      21.760  -3.497  46.069  1.00 28.81           O  
ATOM     79  OE2 GLU A  10      20.866  -5.473  45.542  1.00 32.29           O  
ATOM     80  N   ALA A  11      26.381  -4.534  48.944  1.00 21.64           N  
ATOM     81  CA  ALA A  11      27.793  -4.318  48.700  1.00 26.74           C  
ATOM     82  C   ALA A  11      28.658  -5.315  49.433  1.00 47.27           C  
ATOM     83  O   ALA A  11      29.763  -5.620  48.985  1.00 29.52           O  
ATOM     84  CB  ALA A  11      28.216  -2.895  49.022  1.00 25.74           C  
ATOM     85  N   GLU A  12      28.146  -5.828  50.562  1.00 34.78           N  
ATOM     86  CA  GLU A  12      28.921  -6.784  51.327  1.00 31.50           C  
ATOM     87  C   GLU A  12      28.469  -8.197  51.094  1.00 27.88           C  
ATOM     88  O   GLU A  12      29.133  -9.136  51.505  1.00 51.01           O  
ATOM     89  CB  GLU A  12      28.940  -6.498  52.827  1.00 29.25           C  
ATOM     90  CG  GLU A  12      30.069  -5.507  53.208  1.00 52.94           C  
ATOM     91  CD  GLU A  12      29.788  -4.784  54.512  1.00100.00           C  
ATOM     92  OE1 GLU A  12      29.427  -5.332  55.554  1.00100.00           O  
ATOM     93  OE2 GLU A  12      29.958  -3.488  54.389  1.00100.00           O  
ATOM     94  N   GLY A  13      27.318  -8.354  50.457  1.00 32.06           N  
ATOM     95  CA  GLY A  13      26.811  -9.680  50.208  1.00 45.30           C  
ATOM     96  C   GLY A  13      26.466 -10.427  51.490  1.00 60.62           C  
ATOM     97  O   GLY A  13      26.710 -11.617  51.633  1.00 58.40           O  
ATOM     98  N   THR A  14      25.890  -9.726  52.435  1.00 45.14           N  
ATOM     99  CA  THR A  14      25.527 -10.381  53.663  1.00 35.34           C  
ATOM    100  C   THR A  14      24.039 -10.405  53.785  1.00 27.67           C  
ATOM    101  O   THR A  14      23.362  -9.588  53.196  1.00 31.14           O  
ATOM    102  CB  THR A  14      26.162  -9.713  54.869  1.00 36.19           C  
ATOM    103  OG1 THR A  14      25.693  -8.395  54.975  1.00 31.70           O  
ATOM    104  CG2 THR A  14      27.659  -9.686  54.634  1.00 38.33           C  
ATOM    105  N   LYS A  15      23.558 -11.371  54.529  1.00 31.07           N  
ATOM    106  CA  LYS A  15      22.153 -11.593  54.772  1.00 36.65           C  
ATOM    107  C   LYS A  15      21.980 -12.004  56.226  1.00 50.45           C  
ATOM    108  O   LYS A  15      22.495 -13.028  56.653  1.00 40.75           O  
ATOM    109  CB  LYS A  15      21.647 -12.699  53.873  1.00 32.77           C  
ATOM    110  CG  LYS A  15      20.216 -13.078  54.192  1.00 47.91           C  
ATOM    111  CD  LYS A  15      20.067 -14.574  54.406  1.00100.00           C  
ATOM    112  CE  LYS A  15      19.153 -15.221  53.372  1.00 91.71           C  
ATOM    113  NZ  LYS A  15      19.190 -16.694  53.402  1.00100.00           N  
ATOM    114  N   HIS A  16      21.301 -11.184  57.001  1.00 30.85           N  
ATOM    115  CA  HIS A  16      21.091 -11.468  58.409  1.00 29.21           C  
ATOM    116  C   HIS A  16      19.631 -11.467  58.686  1.00 43.80           C  
ATOM    117  O   HIS A  16      18.885 -10.628  58.174  1.00 29.96           O  
ATOM    118  CB  HIS A  16      21.613 -10.345  59.272  1.00 25.09           C  
ATOM    119  CG  HIS A  16      23.047 -10.188  59.038  1.00 32.52           C  
ATOM    120  ND1 HIS A  16      23.620  -8.931  58.991  1.00 37.53           N  
ATOM    121  CD2 HIS A  16      24.011 -11.141  58.896  1.00 41.93           C  
ATOM    122  CE1 HIS A  16      24.926  -9.137  58.802  1.00 30.78           C  
ATOM    123  NE2 HIS A  16      25.187 -10.454  58.734  1.00 35.90           N  
ATOM    124  N   GLU A  17      19.221 -12.387  59.532  1.00 31.15           N  
ATOM    125  CA  GLU A  17      17.808 -12.425  59.871  1.00 33.13           C  
ATOM    126  C   GLU A  17      17.537 -12.010  61.328  1.00 47.58           C  
ATOM    127  O   GLU A  17      18.259 -12.397  62.244  1.00 34.31           O  
ATOM    128  CB  GLU A  17      17.287 -13.813  59.503  1.00 35.02           C  
ATOM    129  CG  GLU A  17      15.940 -14.191  60.125  1.00100.00           C  
ATOM    130  CD  GLU A  17      15.724 -15.686  60.017  1.00100.00           C  
ATOM    131  OE1 GLU A  17      16.024 -16.332  58.991  1.00100.00           O  
ATOM    132  OE2 GLU A  17      15.223 -16.207  61.145  1.00100.00           O  
ATOM    133  N   ILE A  18      16.529 -11.171  61.573  1.00 28.97           N  
ATOM    134  CA  ILE A  18      16.212 -10.756  62.956  1.00 34.20           C  
ATOM    135  C   ILE A  18      14.724 -10.888  63.208  1.00 31.79           C  
ATOM    136  O   ILE A  18      13.961 -11.016  62.250  1.00 26.49           O  
ATOM    137  CB  ILE A  18      16.709  -9.351  63.340  1.00 28.29           C  
ATOM    138  CG1 ILE A  18      16.041  -8.320  62.428  1.00 29.75           C  
ATOM    139  CG2 ILE A  18      18.235  -9.332  63.151  1.00 25.96           C  
ATOM    140  CD1 ILE A  18      16.288  -6.860  62.829  1.00 27.39           C  
ATOM    141  N   GLU A  19      14.324 -10.913  64.484  1.00 26.60           N  
ATOM    142  CA  GLU A  19      12.924 -11.006  64.851  1.00 21.02           C  
ATOM    143  C   GLU A  19      12.585  -9.691  65.486  1.00 22.67           C  
ATOM    144  O   GLU A  19      13.284  -9.237  66.383  1.00 22.78           O  
ATOM    145  CB  GLU A  19      12.649 -12.161  65.834  1.00 24.82           C  
ATOM    146  CG  GLU A  19      13.163 -13.497  65.282  1.00 25.51           C  
ATOM    147  CD  GLU A  19      12.283 -14.024  64.183  1.00 77.25           C  
ATOM    148  OE1 GLU A  19      11.137 -13.640  64.033  1.00 40.80           O  
ATOM    149  OE2 GLU A  19      12.870 -14.921  63.423  1.00 81.40           O  
ATOM    150  N   VAL A  20      11.536  -9.058  64.973  1.00 19.33           N  
ATOM    151  CA  VAL A  20      11.139  -7.759  65.420  1.00 22.82           C  
ATOM    152  C   VAL A  20       9.700  -7.705  65.875  1.00 33.07           C  
ATOM    153  O   VAL A  20       8.789  -8.088  65.140  1.00 27.62           O  
ATOM    154  CB  VAL A  20      11.346  -6.723  64.279  1.00 26.64           C  
ATOM    155  CG1 VAL A  20      11.044  -5.295  64.708  1.00 20.59           C  
ATOM    156  CG2 VAL A  20      12.732  -6.804  63.663  1.00 24.20           C  
ATOM    157  N   PRO A  21       9.511  -7.163  67.074  1.00 28.07           N  
ATOM    158  CA  PRO A  21       8.170  -6.959  67.618  1.00 38.47           C  
ATOM    159  C   PRO A  21       7.408  -5.869  66.842  1.00 52.01           C  
ATOM    160  O   PRO A  21       7.962  -4.867  66.389  1.00 27.64           O  
ATOM    161  CB  PRO A  21       8.329  -6.530  69.087  1.00 21.41           C  
ATOM    162  CG  PRO A  21       9.796  -6.762  69.427  1.00 22.45           C  
ATOM    163  CD  PRO A  21      10.565  -7.026  68.119  1.00 24.70           C  
ATOM    164  N   ASP A  22       6.105  -6.073  66.687  1.00 26.62           N  
ATOM    165  CA  ASP A  22       5.221  -5.164  65.996  1.00 22.57           C  
ATOM    166  C   ASP A  22       5.255  -3.771  66.553  1.00 32.10           C  
ATOM    167  O   ASP A  22       4.794  -2.824  65.922  1.00 28.28           O  
ATOM    168  CB  ASP A  22       3.764  -5.676  65.988  1.00 35.14           C  
ATOM    169  CG  ASP A  22       3.111  -5.831  67.352  1.00 42.97           C  
ATOM    170  OD1 ASP A  22       3.288  -5.076  68.289  1.00 64.78           O  
ATOM    171  OD2 ASP A  22       2.321  -6.871  67.399  1.00 79.38           O  
ATOM    172  N   ASP A  23       5.778  -3.634  67.757  1.00 22.76           N  
ATOM    173  CA  ASP A  23       5.786  -2.312  68.348  1.00 24.37           C  
ATOM    174  C   ASP A  23       7.183  -1.809  68.614  1.00 23.75           C  
ATOM    175  O   ASP A  23       7.361  -0.964  69.471  1.00 28.78           O  
ATOM    176  CB  ASP A  23       4.909  -2.237  69.626  1.00 30.56           C  
ATOM    177  CG  ASP A  23       5.353  -3.168  70.737  1.00 29.62           C  
ATOM    178  OD1 ASP A  23       6.195  -4.037  70.606  1.00 37.88           O  
ATOM    179  OD2 ASP A  23       4.784  -2.901  71.887  1.00 69.00           O  
ATOM    180  N   GLU A  24       8.173  -2.338  67.894  1.00 20.42           N  
ATOM    181  CA  GLU A  24       9.558  -1.887  68.062  1.00 23.13           C  
ATOM    182  C   GLU A  24      10.127  -1.422  66.713  1.00 35.64           C  
ATOM    183  O   GLU A  24       9.878  -2.092  65.736  1.00 24.19           O  
ATOM    184  CB  GLU A  24      10.476  -3.023  68.610  1.00 21.80           C  
ATOM    185  CG  GLU A  24      11.917  -2.553  68.947  1.00 18.77           C  
ATOM    186  CD  GLU A  24      12.787  -3.637  69.531  1.00 22.34           C  
ATOM    187  OE1 GLU A  24      12.513  -4.815  69.514  1.00 25.71           O  
ATOM    188  OE2 GLU A  24      13.920  -3.211  69.993  1.00 23.68           O  
ATOM    189  N   TYR A  25      10.904  -0.344  66.642  1.00 20.49           N  
ATOM    190  CA  TYR A  25      11.491   0.045  65.347  1.00 23.61           C  
ATOM    191  C   TYR A  25      12.527  -0.945  64.906  1.00 25.87           C  
ATOM    192  O   TYR A  25      13.276  -1.507  65.735  1.00 24.66           O  
ATOM    193  CB  TYR A  25      12.274   1.340  65.424  1.00 16.37           C  
ATOM    194  CG  TYR A  25      11.405   2.489  65.705  1.00 31.65           C  
ATOM    195  CD1 TYR A  25      10.179   2.669  65.068  1.00 27.80           C  
ATOM    196  CD2 TYR A  25      11.849   3.386  66.671  1.00 21.45           C  
ATOM    197  CE1 TYR A  25       9.404   3.779  65.398  1.00 21.61           C  
ATOM    198  CE2 TYR A  25      11.100   4.510  66.990  1.00 21.62           C  
ATOM    199  CZ  TYR A  25       9.879   4.684  66.348  1.00 28.70           C  
ATOM    200  OH  TYR A  25       9.176   5.777  66.706  1.00 34.11           O  
ATOM    201  N   ILE A  26      12.673  -1.090  63.592  1.00 19.43           N  
ATOM    202  CA  ILE A  26      13.643  -2.047  63.083  1.00 17.07           C  
ATOM    203  C   ILE A  26      15.075  -1.820  63.536  1.00 21.12           C  
ATOM    204  O   ILE A  26      15.843  -2.747  63.831  1.00 21.71           O  
ATOM    205  CB  ILE A  26      13.555  -2.065  61.544  1.00 26.95           C  
ATOM    206  CG1 ILE A  26      12.246  -2.762  61.161  1.00 24.30           C  
ATOM    207  CG2 ILE A  26      14.737  -2.784  60.913  1.00 21.38           C  
ATOM    208  CD1 ILE A  26      11.946  -2.733  59.662  1.00 28.64           C  
ATOM    209  N   LEU A  27      15.494  -0.580  63.528  1.00 17.91           N  
ATOM    210  CA  LEU A  27      16.887  -0.320  63.892  1.00 15.73           C  
ATOM    211  C   LEU A  27      17.214  -0.784  65.344  1.00 23.38           C  
ATOM    212  O   LEU A  27      18.296  -1.351  65.673  1.00 21.39           O  
ATOM    213  CB  LEU A  27      17.166   1.203  63.744  1.00 14.29           C  
ATOM    214  CG  LEU A  27      18.572   1.656  64.168  1.00 18.79           C  
ATOM    215  CD1 LEU A  27      19.678   1.008  63.331  1.00 21.39           C  
ATOM    216  CD2 LEU A  27      18.708   3.179  64.105  1.00 22.82           C  
ATOM    217  N   ASP A  28      16.236  -0.521  66.214  1.00 22.84           N  
ATOM    218  CA  ASP A  28      16.419  -0.879  67.605  1.00 22.56           C  
ATOM    219  C   ASP A  28      16.606  -2.380  67.781  1.00 21.71           C  
ATOM    220  O   ASP A  28      17.509  -2.854  68.469  1.00 21.41           O  
ATOM    221  CB  ASP A  28      15.252  -0.320  68.427  1.00 27.49           C  
ATOM    222  CG  ASP A  28      15.319   1.170  68.679  1.00 25.38           C  
ATOM    223  OD1 ASP A  28      16.361   1.745  68.856  1.00 58.03           O  
ATOM    224  OD2 ASP A  28      14.142   1.754  68.760  1.00 53.83           O  
ATOM    225  N   ALA A  29      15.761  -3.146  67.113  1.00 18.26           N  
ATOM    226  CA  ALA A  29      15.839  -4.593  67.199  1.00 20.91           C  
ATOM    227  C   ALA A  29      17.132  -5.123  66.617  1.00 23.60           C  
ATOM    228  O   ALA A  29      17.751  -6.078  67.136  1.00 22.65           O  
ATOM    229  CB  ALA A  29      14.633  -5.211  66.488  1.00 21.83           C  
ATOM    230  N   ALA A  30      17.561  -4.488  65.502  1.00 18.81           N  
ATOM    231  CA  ALA A  30      18.801  -4.914  64.869  1.00 15.57           C  
ATOM    232  C   ALA A  30      19.957  -4.742  65.826  1.00 14.91           C  
ATOM    233  O   ALA A  30      20.754  -5.657  66.044  1.00 20.98           O  
ATOM    234  CB  ALA A  30      19.071  -4.120  63.585  1.00 18.17           C  
ATOM    235  N   GLU A  31      20.022  -3.556  66.432  1.00 19.88           N  
ATOM    236  CA  GLU A  31      21.130  -3.371  67.360  1.00 21.83           C  
ATOM    237  C   GLU A  31      21.099  -4.387  68.519  1.00 18.67           C  
ATOM    238  O   GLU A  31      22.104  -5.013  68.835  1.00 21.73           O  
ATOM    239  CB  GLU A  31      21.173  -1.938  67.902  1.00 21.38           C  
ATOM    240  CG  GLU A  31      21.458  -0.886  66.806  1.00 28.36           C  
ATOM    241  CD  GLU A  31      20.982   0.506  67.196  1.00 30.61           C  
ATOM    242  OE1 GLU A  31      20.148   0.770  68.052  1.00 25.71           O  
ATOM    243  OE2 GLU A  31      21.535   1.436  66.490  1.00 24.49           O  
ATOM    244  N   GLU A  32      19.932  -4.540  69.152  1.00 21.08           N  
ATOM    245  CA  GLU A  32      19.820  -5.490  70.253  1.00 19.59           C  
ATOM    246  C   GLU A  32      20.254  -6.871  69.838  1.00 40.97           C  
ATOM    247  O   GLU A  32      20.812  -7.621  70.632  1.00 23.26           O  
ATOM    248  CB  GLU A  32      18.395  -5.574  70.779  1.00 22.87           C  
ATOM    249  CG  GLU A  32      17.994  -4.281  71.478  1.00 23.47           C  
ATOM    250  CD  GLU A  32      16.500  -4.181  71.519  1.00 41.80           C  
ATOM    251  OE1 GLU A  32      15.765  -5.033  71.057  1.00 31.69           O  
ATOM    252  OE2 GLU A  32      16.075  -3.059  72.023  1.00 37.66           O  
ATOM    253  N   GLN A  33      19.944  -7.225  68.605  1.00 20.71           N  
ATOM    254  CA  GLN A  33      20.314  -8.521  68.115  1.00 18.08           C  
ATOM    255  C   GLN A  33      21.741  -8.595  67.591  1.00 31.98           C  
ATOM    256  O   GLN A  33      22.148  -9.574  66.994  1.00 25.71           O  
ATOM    257  CB  GLN A  33      19.241  -9.104  67.183  1.00 17.77           C  
ATOM    258  CG  GLN A  33      17.958  -9.307  68.021  1.00 19.52           C  
ATOM    259  CD  GLN A  33      16.735  -9.625  67.193  1.00 18.37           C  
ATOM    260  OE1 GLN A  33      16.735 -10.566  66.402  1.00 22.50           O  
ATOM    261  NE2 GLN A  33      15.660  -8.894  67.432  1.00 19.05           N  
ATOM    262  N   GLY A  34      22.524  -7.552  67.822  1.00 23.71           N  
ATOM    263  CA  GLY A  34      23.926  -7.606  67.446  1.00 23.55           C  
ATOM    264  C   GLY A  34      24.364  -7.081  66.092  1.00 28.09           C  
ATOM    265  O   GLY A  34      25.512  -7.322  65.673  1.00 29.39           O  
ATOM    266  N   TYR A  35      23.474  -6.375  65.420  1.00 21.39           N  
ATOM    267  CA  TYR A  35      23.833  -5.856  64.123  1.00 25.63           C  
ATOM    268  C   TYR A  35      23.818  -4.361  64.147  1.00 32.02           C  
ATOM    269  O   TYR A  35      22.756  -3.774  64.213  1.00 31.14           O  
ATOM    270  CB  TYR A  35      22.845  -6.306  63.040  1.00 27.58           C  
ATOM    271  CG  TYR A  35      22.848  -7.787  62.944  1.00 24.53           C  
ATOM    272  CD1 TYR A  35      23.924  -8.448  62.356  1.00 23.43           C  
ATOM    273  CD2 TYR A  35      21.820  -8.532  63.515  1.00 30.31           C  
ATOM    274  CE1 TYR A  35      23.965  -9.840  62.330  1.00 33.21           C  
ATOM    275  CE2 TYR A  35      21.847  -9.923  63.497  1.00 29.42           C  
ATOM    276  CZ  TYR A  35      22.912 -10.571  62.879  1.00 36.64           C  
ATOM    277  OH  TYR A  35      22.905 -11.940  62.829  1.00 45.01           O  
ATOM    278  N   ASP A  36      24.983  -3.745  64.058  1.00 24.41           N  
ATOM    279  CA  ASP A  36      25.001  -2.288  64.040  1.00 22.97           C  
ATOM    280  C   ASP A  36      24.717  -1.820  62.622  1.00 35.26           C  
ATOM    281  O   ASP A  36      25.310  -2.338  61.686  1.00 40.09           O  
ATOM    282  CB  ASP A  36      26.368  -1.761  64.466  1.00 28.88           C  
ATOM    283  CG  ASP A  36      26.718  -2.149  65.898  1.00 36.71           C  
ATOM    284  OD1 ASP A  36      25.889  -2.356  66.781  1.00 36.47           O  
ATOM    285  OD2 ASP A  36      28.000  -2.259  66.076  1.00 40.81           O  
ATOM    286  N   LEU A  37      23.796  -0.886  62.501  1.00 27.09           N  
ATOM    287  CA  LEU A  37      23.345  -0.273  61.251  1.00 19.36           C  
ATOM    288  C   LEU A  37      23.577   1.224  61.305  1.00 36.98           C  
ATOM    289  O   LEU A  37      23.583   1.864  62.365  1.00 23.31           O  
ATOM    290  CB  LEU A  37      21.851  -0.519  60.966  1.00 16.52           C  
ATOM    291  CG  LEU A  37      21.495  -1.988  60.702  1.00 23.53           C  
ATOM    292  CD1 LEU A  37      19.978  -2.127  60.608  1.00 21.88           C  
ATOM    293  CD2 LEU A  37      22.061  -2.439  59.362  1.00 34.28           C  
ATOM    294  N   PRO A  38      23.764   1.821  60.149  1.00 31.93           N  
ATOM    295  CA  PRO A  38      24.023   3.256  60.095  1.00 26.52           C  
ATOM    296  C   PRO A  38      22.877   4.086  60.582  1.00 23.66           C  
ATOM    297  O   PRO A  38      21.707   3.766  60.346  1.00 23.40           O  
ATOM    298  CB  PRO A  38      24.129   3.578  58.594  1.00 31.33           C  
ATOM    299  CG  PRO A  38      23.526   2.396  57.859  1.00 40.53           C  
ATOM    300  CD  PRO A  38      23.713   1.207  58.794  1.00 28.21           C  
ATOM    301  N   PHE A  39      23.216   5.206  61.212  1.00 18.93           N  
ATOM    302  CA  PHE A  39      22.222   6.161  61.704  1.00 22.04           C  
ATOM    303  C   PHE A  39      22.848   7.500  62.079  1.00 24.38           C  
ATOM    304  O   PHE A  39      24.061   7.610  62.232  1.00 22.45           O  
ATOM    305  CB  PHE A  39      21.403   5.622  62.899  1.00 23.36           C  
ATOM    306  CG  PHE A  39      22.175   5.515  64.197  1.00 19.01           C  
ATOM    307  CD1 PHE A  39      22.196   6.576  65.104  1.00 28.19           C  
ATOM    308  CD2 PHE A  39      22.851   4.339  64.526  1.00 22.05           C  
ATOM    309  CE1 PHE A  39      22.905   6.475  66.301  1.00 27.43           C  
ATOM    310  CE2 PHE A  39      23.567   4.208  65.720  1.00 19.31           C  
ATOM    311  CZ  PHE A  39      23.600   5.299  66.588  1.00 20.56           C  
ATOM    312  N   SER A  40      22.028   8.519  62.265  1.00 21.63           N  
ATOM    313  CA  SER A  40      22.564   9.796  62.674  1.00 18.20           C  
ATOM    314  C   SER A  40      21.599  10.467  63.650  1.00 30.96           C  
ATOM    315  O   SER A  40      21.757  10.396  64.848  1.00 27.21           O  
ATOM    316  CB  SER A  40      22.808  10.639  61.431  1.00 25.93           C  
ATOM    317  OG  SER A  40      23.428  11.829  61.855  1.00 32.71           O  
ATOM    318  N   CYS A  41      20.556  11.078  63.104  1.00 28.30           N  
ATOM    319  CA  CYS A  41      19.520  11.796  63.822  1.00 18.11           C  
ATOM    320  C   CYS A  41      18.618  10.916  64.711  1.00 37.07           C  
ATOM    321  O   CYS A  41      18.164  11.343  65.771  1.00 23.76           O  
ATOM    322  CB  CYS A  41      18.666  12.579  62.765  1.00 31.99           C  
ATOM    323  SG  CYS A  41      17.257  11.691  62.003  1.00 24.45           S  
ATOM    324  N   ARG A  42      18.320   9.693  64.252  1.00 30.10           N  
ATOM    325  CA  ARG A  42      17.459   8.761  64.960  1.00 22.58           C  
ATOM    326  C   ARG A  42      16.132   9.340  65.096  1.00 24.65           C  
ATOM    327  O   ARG A  42      15.339   8.908  65.899  1.00 26.80           O  
ATOM    328  CB  ARG A  42      17.927   8.278  66.345  1.00 21.61           C  
ATOM    329  CG  ARG A  42      18.882   7.125  66.238  1.00 29.14           C  
ATOM    330  CD  ARG A  42      19.279   6.508  67.579  1.00 45.87           C  
ATOM    331  NE  ARG A  42      18.640   5.219  67.804  1.00 27.06           N  
ATOM    332  CZ  ARG A  42      19.241   4.048  67.603  1.00 20.28           C  
ATOM    333  NH1 ARG A  42      20.505   3.906  67.188  1.00 19.51           N  
ATOM    334  NH2 ARG A  42      18.570   2.941  67.854  1.00 24.55           N  
ATOM    335  N   ALA A  43      15.861  10.332  64.310  1.00 22.81           N  
ATOM    336  CA  ALA A  43      14.534  10.836  64.493  1.00 18.68           C  
ATOM    337  C   ALA A  43      13.708  10.904  63.203  1.00 39.69           C  
ATOM    338  O   ALA A  43      12.772  11.674  63.150  1.00 26.98           O  
ATOM    339  CB  ALA A  43      14.623  12.203  65.123  1.00 22.36           C  
ATOM    340  N   GLY A  44      13.978  10.123  62.166  1.00 22.25           N  
ATOM    341  CA  GLY A  44      13.098  10.242  61.011  1.00 20.69           C  
ATOM    342  C   GLY A  44      13.346  11.504  60.166  1.00 38.16           C  
ATOM    343  O   GLY A  44      12.570  11.826  59.256  1.00 29.36           O  
ATOM    344  N   ALA A  45      14.437  12.218  60.428  1.00 27.38           N  
ATOM    345  CA  ALA A  45      14.636  13.458  59.669  1.00 28.25           C  
ATOM    346  C   ALA A  45      15.920  13.564  58.868  1.00 30.91           C  
ATOM    347  O   ALA A  45      16.410  14.648  58.582  1.00 30.04           O  
ATOM    348  CB  ALA A  45      14.559  14.652  60.609  1.00 28.33           C  
ATOM    349  N   CYS A  46      16.481  12.445  58.482  1.00 31.40           N  
ATOM    350  CA  CYS A  46      17.694  12.478  57.695  1.00 21.71           C  
ATOM    351  C   CYS A  46      17.689  11.261  56.812  1.00 26.27           C  
ATOM    352  O   CYS A  46      16.717  10.514  56.793  1.00 23.38           O  
ATOM    353  CB  CYS A  46      18.949  12.596  58.569  1.00 23.76           C  
ATOM    354  SG  CYS A  46      19.554  11.041  59.230  1.00 25.58           S  
ATOM    355  N   SER A  47      18.764  11.024  56.113  1.00 19.32           N  
ATOM    356  CA  SER A  47      18.722   9.849  55.276  1.00 23.84           C  
ATOM    357  C   SER A  47      19.731   8.782  55.642  1.00 30.77           C  
ATOM    358  O   SER A  47      19.869   7.787  54.950  1.00 24.00           O  
ATOM    359  CB  SER A  47      19.037  10.276  53.858  1.00 36.18           C  
ATOM    360  OG  SER A  47      20.380  10.752  53.796  1.00 28.60           O  
ATOM    361  N   THR A  48      20.483   8.964  56.696  1.00 19.34           N  
ATOM    362  CA  THR A  48      21.520   8.002  56.990  1.00 19.69           C  
ATOM    363  C   THR A  48      21.104   6.562  57.170  1.00 15.12           C  
ATOM    364  O   THR A  48      21.859   5.638  56.871  1.00 22.70           O  
ATOM    365  CB  THR A  48      22.269   8.497  58.252  1.00 25.57           C  
ATOM    366  OG1 THR A  48      22.762   9.775  57.970  1.00 30.65           O  
ATOM    367  CG2 THR A  48      23.465   7.632  58.595  1.00 21.11           C  
ATOM    368  N   CYS A  49      19.952   6.375  57.792  1.00 20.79           N  
ATOM    369  CA  CYS A  49      19.477   5.051  58.106  1.00 22.47           C  
ATOM    370  C   CYS A  49      18.651   4.463  56.992  1.00 34.88           C  
ATOM    371  O   CYS A  49      17.993   3.468  57.212  1.00 24.67           O  
ATOM    372  CB  CYS A  49      18.654   5.067  59.417  1.00 14.71           C  
ATOM    373  SG  CYS A  49      17.150   5.949  59.146  1.00 20.32           S  
ATOM    374  N   ALA A  50      18.675   5.074  55.807  1.00 25.53           N  
ATOM    375  CA  ALA A  50      17.843   4.595  54.711  1.00 20.47           C  
ATOM    376  C   ALA A  50      18.074   3.150  54.268  1.00 15.89           C  
ATOM    377  O   ALA A  50      19.207   2.652  54.195  1.00 18.89           O  
ATOM    378  CB  ALA A  50      17.948   5.556  53.524  1.00 23.53           C  
ATOM    379  N   GLY A  51      16.957   2.477  53.979  1.00 21.88           N  
ATOM    380  CA  GLY A  51      16.921   1.103  53.510  1.00 23.03           C  
ATOM    381  C   GLY A  51      15.938   1.020  52.338  1.00 23.78           C  
ATOM    382  O   GLY A  51      15.182   1.979  52.100  1.00 20.92           O  
ATOM    383  N   LYS A  52      15.934  -0.095  51.617  1.00 18.16           N  
ATOM    384  CA  LYS A  52      14.993  -0.199  50.516  1.00 25.12           C  
ATOM    385  C   LYS A  52      14.270  -1.535  50.597  1.00 22.35           C  
ATOM    386  O   LYS A  52      14.890  -2.591  50.655  1.00 23.72           O  
ATOM    387  CB  LYS A  52      15.706   0.004  49.180  1.00 28.57           C  
ATOM    388  CG  LYS A  52      14.704   0.087  48.036  1.00 33.34           C  
ATOM    389  CD  LYS A  52      15.328   0.157  46.646  1.00 40.30           C  
ATOM    390  CE  LYS A  52      15.986  -1.152  46.234  1.00100.00           C  
ATOM    391  NZ  LYS A  52      15.049  -2.288  46.193  1.00 77.03           N  
ATOM    392  N   LEU A  53      12.958  -1.478  50.595  1.00 19.16           N  
ATOM    393  CA  LEU A  53      12.142  -2.674  50.709  1.00 20.23           C  
ATOM    394  C   LEU A  53      12.278  -3.568  49.535  1.00 30.51           C  
ATOM    395  O   LEU A  53      12.284  -3.126  48.412  1.00 32.70           O  
ATOM    396  CB  LEU A  53      10.648  -2.368  50.697  1.00 21.89           C  
ATOM    397  CG  LEU A  53      10.162  -1.918  52.045  1.00 38.86           C  
ATOM    398  CD1 LEU A  53      10.205  -3.101  53.021  1.00 39.62           C  
ATOM    399  CD2 LEU A  53      11.200  -0.941  52.513  1.00 96.21           C  
ATOM    400  N   VAL A  54      12.322  -4.832  49.800  1.00 28.25           N  
ATOM    401  CA  VAL A  54      12.371  -5.827  48.761  1.00 31.54           C  
ATOM    402  C   VAL A  54      10.994  -6.457  48.806  1.00 41.28           C  
ATOM    403  O   VAL A  54      10.323  -6.625  47.819  1.00 28.98           O  
ATOM    404  CB  VAL A  54      13.500  -6.824  48.950  1.00 34.17           C  
ATOM    405  CG1 VAL A  54      13.281  -8.048  48.055  1.00 29.80           C  
ATOM    406  CG2 VAL A  54      14.821  -6.130  48.640  1.00 36.06           C  
ATOM    407  N   SER A  55      10.528  -6.758  49.990  1.00 28.24           N  
ATOM    408  CA  SER A  55       9.199  -7.270  50.127  1.00 28.34           C  
ATOM    409  C   SER A  55       8.768  -7.024  51.516  1.00 39.64           C  
ATOM    410  O   SER A  55       9.612  -6.923  52.416  1.00 28.96           O  
ATOM    411  CB  SER A  55       9.008  -8.745  49.862  1.00 42.59           C  
ATOM    412  OG  SER A  55       9.878  -9.488  50.665  1.00 40.96           O  
ATOM    413  N   GLY A  56       7.449  -6.966  51.649  1.00 28.75           N  
ATOM    414  CA  GLY A  56       6.820  -6.743  52.936  1.00 27.61           C  
ATOM    415  C   GLY A  56       6.402  -5.308  53.146  1.00 32.33           C  
ATOM    416  O   GLY A  56       6.648  -4.487  52.272  1.00 35.22           O  
ATOM    417  N   THR A  57       5.758  -5.021  54.306  1.00 21.49           N  
ATOM    418  CA  THR A  57       5.259  -3.679  54.619  1.00 21.64           C  
ATOM    419  C   THR A  57       5.754  -3.121  55.948  1.00 36.35           C  
ATOM    420  O   THR A  57       6.052  -3.879  56.850  1.00 26.49           O  
ATOM    421  CB  THR A  57       3.733  -3.686  54.705  1.00 38.12           C  
ATOM    422  OG1 THR A  57       3.344  -4.786  55.503  1.00 36.26           O  
ATOM    423  CG2 THR A  57       3.114  -3.806  53.307  1.00 35.56           C  
ATOM    424  N   VAL A  58       5.798  -1.795  56.058  1.00 27.23           N  
ATOM    425  CA  VAL A  58       6.219  -1.117  57.273  1.00 27.88           C  
ATOM    426  C   VAL A  58       5.295   0.047  57.527  1.00 27.74           C  
ATOM    427  O   VAL A  58       4.597   0.498  56.640  1.00 31.95           O  
ATOM    428  CB  VAL A  58       7.672  -0.593  57.278  1.00 20.41           C  
ATOM    429  CG1 VAL A  58       8.732  -1.682  57.033  1.00 21.50           C  
ATOM    430  CG2 VAL A  58       7.837   0.550  56.298  1.00 26.93           C  
ATOM    431  N   ASP A  59       5.282   0.507  58.767  1.00 26.19           N  
ATOM    432  CA  ASP A  59       4.572   1.686  59.177  1.00 22.22           C  
ATOM    433  C   ASP A  59       5.668   2.646  59.602  1.00 29.28           C  
ATOM    434  O   ASP A  59       6.365   2.406  60.587  1.00 27.98           O  
ATOM    435  CB  ASP A  59       3.531   1.475  60.300  1.00 25.77           C  
ATOM    436  CG  ASP A  59       3.099   2.766  60.975  1.00 36.35           C  
ATOM    437  OD1 ASP A  59       3.286   3.871  60.512  1.00 39.02           O  
ATOM    438  OD2 ASP A  59       2.533   2.587  62.150  1.00 69.47           O  
ATOM    439  N   GLN A  60       5.867   3.686  58.813  1.00 21.94           N  
ATOM    440  CA  GLN A  60       6.896   4.639  59.116  1.00 22.94           C  
ATOM    441  C   GLN A  60       6.294   6.034  59.216  1.00 38.07           C  
ATOM    442  O   GLN A  60       6.899   7.065  58.939  1.00 27.93           O  
ATOM    443  CB  GLN A  60       8.100   4.476  58.159  1.00 23.61           C  
ATOM    444  CG  GLN A  60       7.827   4.823  56.681  1.00 19.77           C  
ATOM    445  CD  GLN A  60       9.083   4.776  55.771  1.00 24.11           C  
ATOM    446  OE1 GLN A  60      10.228   5.163  56.104  1.00 23.16           O  
ATOM    447  NE2 GLN A  60       8.860   4.292  54.561  1.00 28.94           N  
ATOM    448  N   SER A  61       5.044   6.024  59.629  1.00 24.70           N  
ATOM    449  CA  SER A  61       4.269   7.226  59.811  1.00 25.36           C  
ATOM    450  C   SER A  61       5.011   8.326  60.566  1.00 37.43           C  
ATOM    451  O   SER A  61       4.695   9.513  60.461  1.00 38.07           O  
ATOM    452  CB  SER A  61       2.921   6.891  60.466  1.00 27.41           C  
ATOM    453  OG  SER A  61       3.137   6.408  61.776  1.00 65.74           O  
ATOM    454  N   ASP A  62       6.027   7.978  61.350  1.00 34.24           N  
ATOM    455  CA  ASP A  62       6.713   9.048  62.069  1.00 28.01           C  
ATOM    456  C   ASP A  62       7.844   9.701  61.284  1.00 39.67           C  
ATOM    457  O   ASP A  62       8.507  10.643  61.726  1.00 33.71           O  
ATOM    458  CB  ASP A  62       7.248   8.550  63.422  1.00 48.03           C  
ATOM    459  CG  ASP A  62       6.170   8.060  64.350  1.00100.00           C  
ATOM    460  OD1 ASP A  62       5.122   8.647  64.558  1.00 50.97           O  
ATOM    461  OD2 ASP A  62       6.493   6.931  64.919  1.00 46.05           O  
ATOM    462  N   GLN A  63       8.114   9.190  60.102  1.00 32.54           N  
ATOM    463  CA  GLN A  63       9.208   9.769  59.328  1.00 28.65           C  
ATOM    464  C   GLN A  63       8.816  11.086  58.750  1.00 26.71           C  
ATOM    465  O   GLN A  63       7.622  11.352  58.614  1.00 28.66           O  
ATOM    466  CB  GLN A  63       9.692   8.858  58.191  1.00 28.54           C  
ATOM    467  CG  GLN A  63       8.798   8.865  56.943  1.00 24.58           C  
ATOM    468  CD  GLN A  63       9.318   9.883  55.934  1.00 25.05           C  
ATOM    469  OE1 GLN A  63      10.546  10.140  55.827  1.00 27.76           O  
ATOM    470  NE2 GLN A  63       8.365  10.504  55.232  1.00 27.62           N  
ATOM    471  N   SER A  64       9.802  11.895  58.386  1.00 25.89           N  
ATOM    472  CA  SER A  64       9.445  13.159  57.779  1.00 32.88           C  
ATOM    473  C   SER A  64      10.332  13.554  56.618  1.00 31.93           C  
ATOM    474  O   SER A  64      10.026  14.464  55.881  1.00 44.47           O  
ATOM    475  CB  SER A  64       9.378  14.288  58.791  1.00 30.67           C  
ATOM    476  OG  SER A  64      10.660  14.512  59.351  1.00 47.20           O  
ATOM    477  N   PHE A  65      11.436  12.892  56.464  1.00 25.73           N  
ATOM    478  CA  PHE A  65      12.369  13.243  55.439  1.00 24.10           C  
ATOM    479  C   PHE A  65      12.013  12.837  54.011  1.00 33.16           C  
ATOM    480  O   PHE A  65      12.211  13.613  53.081  1.00 28.61           O  
ATOM    481  CB  PHE A  65      13.698  12.632  55.821  1.00 31.10           C  
ATOM    482  CG  PHE A  65      14.822  12.971  54.879  1.00 32.82           C  
ATOM    483  CD1 PHE A  65      15.511  14.175  54.999  1.00 34.16           C  
ATOM    484  CD2 PHE A  65      15.190  12.080  53.871  1.00 38.14           C  
ATOM    485  CE1 PHE A  65      16.561  14.494  54.139  1.00 38.93           C  
ATOM    486  CE2 PHE A  65      16.234  12.381  52.998  1.00 40.07           C  
ATOM    487  CZ  PHE A  65      16.914  13.593  53.133  1.00 35.99           C  
ATOM    488  N   LEU A  66      11.572  11.606  53.812  1.00 30.02           N  
ATOM    489  CA  LEU A  66      11.240  11.108  52.472  1.00 24.59           C  
ATOM    490  C   LEU A  66      10.005  11.785  51.854  1.00 35.85           C  
ATOM    491  O   LEU A  66       8.998  12.050  52.517  1.00 29.10           O  
ATOM    492  CB  LEU A  66      10.978   9.564  52.458  1.00 23.80           C  
ATOM    493  CG  LEU A  66      12.071   8.669  53.063  1.00 26.23           C  
ATOM    494  CD1 LEU A  66      11.669   7.182  53.112  1.00 20.56           C  
ATOM    495  CD2 LEU A  66      13.341   8.761  52.242  1.00 30.48           C  
ATOM    496  N   ASP A  67      10.033  12.021  50.551  1.00 25.23           N  
ATOM    497  CA  ASP A  67       8.863  12.570  49.916  1.00 23.20           C  
ATOM    498  C   ASP A  67       8.037  11.389  49.475  1.00 24.29           C  
ATOM    499  O   ASP A  67       8.525  10.251  49.489  1.00 25.86           O  
ATOM    500  CB  ASP A  67       9.163  13.501  48.732  1.00 38.90           C  
ATOM    501  CG  ASP A  67       9.874  12.839  47.580  1.00 30.91           C  
ATOM    502  OD1 ASP A  67       9.685  11.677  47.253  1.00 27.53           O  
ATOM    503  OD2 ASP A  67      10.712  13.666  46.969  1.00 29.44           O  
ATOM    504  N   ASP A  68       6.811  11.651  49.045  1.00 25.25           N  
ATOM    505  CA  ASP A  68       5.927  10.572  48.598  1.00 25.06           C  
ATOM    506  C   ASP A  68       6.448   9.652  47.518  1.00 30.85           C  
ATOM    507  O   ASP A  68       6.164   8.443  47.522  1.00 28.11           O  
ATOM    508  CB  ASP A  68       4.567  11.101  48.167  1.00 40.76           C  
ATOM    509  CG  ASP A  68       3.834  11.639  49.352  1.00 73.90           C  
ATOM    510  OD1 ASP A  68       4.130  11.368  50.499  1.00 83.80           O  
ATOM    511  OD2 ASP A  68       2.846  12.414  49.024  1.00100.00           O  
ATOM    512  N   ASP A  69       7.173  10.233  46.576  1.00 26.92           N  
ATOM    513  CA  ASP A  69       7.726   9.444  45.462  1.00 29.34           C  
ATOM    514  C   ASP A  69       8.755   8.421  45.929  1.00 24.42           C  
ATOM    515  O   ASP A  69       8.811   7.264  45.467  1.00 24.60           O  
ATOM    516  CB  ASP A  69       8.359  10.373  44.410  1.00 34.03           C  
ATOM    517  CG  ASP A  69       7.285  11.145  43.712  1.00 43.37           C  
ATOM    518  OD1 ASP A  69       6.181  10.689  43.494  1.00 32.34           O  
ATOM    519  OD2 ASP A  69       7.637  12.370  43.443  1.00 42.74           O  
ATOM    520  N   GLN A  70       9.595   8.892  46.864  1.00 29.97           N  
ATOM    521  CA  GLN A  70      10.653   8.070  47.450  1.00 26.65           C  
ATOM    522  C   GLN A  70      10.047   6.898  48.243  1.00 25.48           C  
ATOM    523  O   GLN A  70      10.517   5.734  48.252  1.00 27.32           O  
ATOM    524  CB  GLN A  70      11.515   8.943  48.359  1.00 30.17           C  
ATOM    525  CG  GLN A  70      12.420   9.868  47.559  1.00 22.70           C  
ATOM    526  CD  GLN A  70      13.107  10.881  48.429  1.00 25.48           C  
ATOM    527  OE1 GLN A  70      12.459  11.477  49.300  1.00 30.94           O  
ATOM    528  NE2 GLN A  70      14.407  11.088  48.174  1.00 22.19           N  
ATOM    529  N   ILE A  71       8.945   7.216  48.903  1.00 25.71           N  
ATOM    530  CA  ILE A  71       8.256   6.183  49.647  1.00 25.16           C  
ATOM    531  C   ILE A  71       7.729   5.160  48.644  1.00 43.55           C  
ATOM    532  O   ILE A  71       7.873   3.935  48.787  1.00 25.00           O  
ATOM    533  CB  ILE A  71       7.147   6.830  50.489  1.00 36.69           C  
ATOM    534  CG1 ILE A  71       7.766   7.463  51.736  1.00 32.78           C  
ATOM    535  CG2 ILE A  71       6.085   5.814  50.917  1.00 24.50           C  
ATOM    536  CD1 ILE A  71       6.764   8.279  52.525  1.00 35.97           C  
ATOM    537  N   GLU A  72       7.132   5.701  47.579  1.00 26.45           N  
ATOM    538  CA  GLU A  72       6.607   4.880  46.501  1.00 28.54           C  
ATOM    539  C   GLU A  72       7.674   3.939  45.955  1.00 23.12           C  
ATOM    540  O   GLU A  72       7.476   2.758  45.679  1.00 30.02           O  
ATOM    541  CB  GLU A  72       6.172   5.824  45.387  1.00 36.06           C  
ATOM    542  CG  GLU A  72       4.694   5.670  45.127  1.00 67.51           C  
ATOM    543  CD  GLU A  72       4.527   4.845  43.904  1.00100.00           C  
ATOM    544  OE1 GLU A  72       4.885   3.666  43.835  1.00100.00           O  
ATOM    545  OE2 GLU A  72       4.005   5.547  42.923  1.00100.00           O  
ATOM    546  N   ALA A  73       8.857   4.466  45.813  1.00 23.98           N  
ATOM    547  CA  ALA A  73       9.941   3.670  45.338  1.00 26.86           C  
ATOM    548  C   ALA A  73      10.352   2.583  46.325  1.00 28.27           C  
ATOM    549  O   ALA A  73      11.125   1.714  45.974  1.00 33.58           O  
ATOM    550  CB  ALA A  73      11.099   4.586  44.981  1.00 25.19           C  
ATOM    551  N   GLY A  74       9.849   2.602  47.548  1.00 26.30           N  
ATOM    552  CA  GLY A  74      10.223   1.556  48.515  1.00 31.60           C  
ATOM    553  C   GLY A  74      11.290   1.929  49.587  1.00 23.86           C  
ATOM    554  O   GLY A  74      11.818   1.075  50.324  1.00 23.20           O  
ATOM    555  N   TYR A  75      11.611   3.201  49.675  1.00 22.99           N  
ATOM    556  CA  TYR A  75      12.620   3.610  50.640  1.00 21.36           C  
ATOM    557  C   TYR A  75      12.040   3.673  52.049  1.00 25.57           C  
ATOM    558  O   TYR A  75      10.867   4.023  52.217  1.00 20.22           O  
ATOM    559  CB  TYR A  75      13.299   4.922  50.230  1.00 24.36           C  
ATOM    560  CG  TYR A  75      14.252   4.645  49.095  1.00 26.57           C  
ATOM    561  CD1 TYR A  75      15.534   4.135  49.306  1.00 21.67           C  
ATOM    562  CD2 TYR A  75      13.848   4.874  47.786  1.00 25.10           C  
ATOM    563  CE1 TYR A  75      16.430   3.853  48.272  1.00 29.25           C  
ATOM    564  CE2 TYR A  75      14.727   4.595  46.740  1.00 27.42           C  
ATOM    565  CZ  TYR A  75      16.001   4.079  46.968  1.00 34.62           C  
ATOM    566  OH  TYR A  75      16.821   3.796  45.914  1.00 33.77           O  
ATOM    567  N   VAL A  76      12.868   3.346  53.040  1.00 22.97           N  
ATOM    568  CA  VAL A  76      12.383   3.332  54.418  1.00 22.95           C  
ATOM    569  C   VAL A  76      13.424   3.886  55.348  1.00 23.17           C  
ATOM    570  O   VAL A  76      14.599   3.594  55.178  1.00 23.56           O  
ATOM    571  CB AVAL A  76      12.108   1.893  54.836  0.50 24.01           C  
ATOM    572  CB BVAL A  76      12.107   1.891  54.820  0.50 23.45           C  
ATOM    573  CG1AVAL A  76      10.830   1.446  54.180  0.50 27.90           C  
ATOM    574  CG1BVAL A  76      11.855   1.775  56.321  0.50  3.74           C  
ATOM    575  CG2AVAL A  76      13.230   0.992  54.363  0.50 28.31           C  
ATOM    576  CG2BVAL A  76      10.857   1.443  54.115  0.50 25.41           C  
ATOM    577  N   LEU A  77      12.999   4.648  56.348  1.00 21.25           N  
ATOM    578  CA  LEU A  77      13.971   5.140  57.332  1.00 18.65           C  
ATOM    579  C   LEU A  77      13.884   4.129  58.506  1.00 16.03           C  
ATOM    580  O   LEU A  77      12.925   4.110  59.274  1.00 21.56           O  
ATOM    581  CB  LEU A  77      13.641   6.581  57.730  1.00 21.23           C  
ATOM    582  CG  LEU A  77      13.691   7.562  56.554  1.00 25.66           C  
ATOM    583  CD1 LEU A  77      13.402   8.983  57.080  1.00 23.98           C  
ATOM    584  CD2 LEU A  77      15.087   7.460  55.918  1.00 18.92           C  
ATOM    585  N   THR A  78      14.867   3.255  58.579  1.00 17.79           N  
ATOM    586  CA  THR A  78      14.841   2.195  59.546  1.00 21.33           C  
ATOM    587  C   THR A  78      14.710   2.632  60.962  1.00 25.36           C  
ATOM    588  O   THR A  78      14.222   1.857  61.774  1.00 24.20           O  
ATOM    589  CB  THR A  78      16.007   1.243  59.382  1.00 19.62           C  
ATOM    590  OG1 THR A  78      17.204   1.972  59.468  1.00 23.21           O  
ATOM    591  CG2 THR A  78      15.917   0.615  57.976  1.00 18.71           C  
ATOM    592  N   CYS A  79      15.141   3.839  61.217  1.00 21.99           N  
ATOM    593  CA  CYS A  79      15.096   4.335  62.579  1.00 22.04           C  
ATOM    594  C   CYS A  79      13.707   4.564  63.114  1.00 28.45           C  
ATOM    595  O   CYS A  79      13.499   4.595  64.311  1.00 27.38           O  
ATOM    596  CB  CYS A  79      15.991   5.556  62.826  1.00 17.06           C  
ATOM    597  SG  CYS A  79      15.336   7.099  62.150  1.00 22.97           S  
ATOM    598  N   VAL A  80      12.737   4.744  62.261  1.00 17.30           N  
ATOM    599  CA  VAL A  80      11.400   5.005  62.762  1.00 16.64           C  
ATOM    600  C   VAL A  80      10.405   4.086  62.123  1.00 19.62           C  
ATOM    601  O   VAL A  80       9.230   4.386  62.028  1.00 24.81           O  
ATOM    602  CB  VAL A  80      10.975   6.437  62.521  1.00 23.42           C  
ATOM    603  CG1 VAL A  80      11.751   7.379  63.419  1.00 21.41           C  
ATOM    604  CG2 VAL A  80      11.220   6.824  61.064  1.00 28.38           C  
ATOM    605  N   ALA A  81      10.881   2.942  61.663  1.00 24.32           N  
ATOM    606  CA  ALA A  81       9.975   2.023  60.989  1.00 25.54           C  
ATOM    607  C   ALA A  81       9.608   0.814  61.805  1.00 16.93           C  
ATOM    608  O   ALA A  81      10.486   0.082  62.312  1.00 23.44           O  
ATOM    609  CB  ALA A  81      10.626   1.524  59.667  1.00 18.90           C  
ATOM    610  N   TYR A  82       8.315   0.553  61.866  1.00 23.55           N  
ATOM    611  CA  TYR A  82       7.815  -0.668  62.525  1.00 25.34           C  
ATOM    612  C   TYR A  82       7.475  -1.653  61.417  1.00 38.22           C  
ATOM    613  O   TYR A  82       6.909  -1.246  60.405  1.00 28.70           O  
ATOM    614  CB  TYR A  82       6.482  -0.466  63.263  1.00 24.01           C  
ATOM    615  CG  TYR A  82       6.586   0.490  64.403  1.00 35.84           C  
ATOM    616  CD1 TYR A  82       7.276   0.117  65.555  1.00 27.88           C  
ATOM    617  CD2 TYR A  82       6.030   1.766  64.311  1.00 28.35           C  
ATOM    618  CE1 TYR A  82       7.402   0.999  66.628  1.00 31.06           C  
ATOM    619  CE2 TYR A  82       6.136   2.649  65.387  1.00 39.61           C  
ATOM    620  CZ  TYR A  82       6.814   2.257  66.541  1.00 35.02           C  
ATOM    621  OH  TYR A  82       6.947   3.125  67.578  1.00 42.20           O  
ATOM    622  N   PRO A  83       7.763  -2.936  61.559  1.00 27.47           N  
ATOM    623  CA  PRO A  83       7.379  -3.865  60.485  1.00 28.34           C  
ATOM    624  C   PRO A  83       5.874  -4.157  60.603  1.00 37.42           C  
ATOM    625  O   PRO A  83       5.332  -4.153  61.699  1.00 25.60           O  
ATOM    626  CB  PRO A  83       8.176  -5.151  60.734  1.00 24.95           C  
ATOM    627  CG  PRO A  83       8.660  -5.053  62.191  1.00 39.67           C  
ATOM    628  CD  PRO A  83       8.475  -3.613  62.679  1.00 24.48           C  
ATOM    629  N   THR A  84       5.155  -4.365  59.507  1.00 26.37           N  
ATOM    630  CA  THR A  84       3.730  -4.668  59.643  1.00 24.33           C  
ATOM    631  C   THR A  84       3.407  -6.031  59.057  1.00 28.91           C  
ATOM    632  O   THR A  84       2.235  -6.404  58.953  1.00 30.08           O  
ATOM    633  CB  THR A  84       2.760  -3.622  59.118  1.00 25.54           C  
ATOM    634  OG1 THR A  84       3.129  -3.334  57.799  1.00 30.59           O  
ATOM    635  CG2 THR A  84       2.839  -2.358  59.953  1.00 28.74           C  
ATOM    636  N   SER A  85       4.496  -6.727  58.697  1.00 22.43           N  
ATOM    637  CA  SER A  85       4.524  -8.068  58.147  1.00 23.48           C  
ATOM    638  C   SER A  85       5.991  -8.499  58.144  1.00 24.47           C  
ATOM    639  O   SER A  85       6.857  -7.711  58.545  1.00 31.58           O  
ATOM    640  CB  SER A  85       3.974  -8.018  56.714  1.00 32.12           C  
ATOM    641  OG  SER A  85       5.003  -7.611  55.819  1.00 32.93           O  
ATOM    642  N   ASP A  86       6.297  -9.722  57.689  1.00 25.18           N  
ATOM    643  CA  ASP A  86       7.692 -10.123  57.576  1.00 21.51           C  
ATOM    644  C   ASP A  86       8.254  -9.216  56.489  1.00 36.44           C  
ATOM    645  O   ASP A  86       7.495  -8.802  55.602  1.00 30.43           O  
ATOM    646  CB  ASP A  86       7.863 -11.575  57.178  1.00 23.70           C  
ATOM    647  CG  ASP A  86       7.359 -12.428  58.294  1.00 35.97           C  
ATOM    648  OD1 ASP A  86       7.214 -12.038  59.427  1.00 30.38           O  
ATOM    649  OD2 ASP A  86       7.072 -13.617  57.907  1.00 36.51           O  
ATOM    650  N   VAL A  87       9.536  -8.890  56.561  1.00 30.25           N  
ATOM    651  CA  VAL A  87      10.103  -7.957  55.598  1.00 26.43           C  
ATOM    652  C   VAL A  87      11.476  -8.335  55.097  1.00 38.22           C  
ATOM    653  O   VAL A  87      12.289  -8.899  55.817  1.00 32.11           O  
ATOM    654  CB  VAL A  87      10.211  -6.585  56.319  1.00 28.34           C  
ATOM    655  CG1 VAL A  87      11.173  -5.574  55.666  1.00 26.23           C  
ATOM    656  CG2 VAL A  87       8.835  -5.963  56.459  1.00 26.14           C  
ATOM    657  N   VAL A  88      11.748  -7.951  53.860  1.00 23.82           N  
ATOM    658  CA  VAL A  88      13.056  -8.149  53.301  1.00 25.40           C  
ATOM    659  C   VAL A  88      13.496  -6.764  52.867  1.00 25.02           C  
ATOM    660  O   VAL A  88      12.795  -6.115  52.088  1.00 25.56           O  
ATOM    661  CB  VAL A  88      13.066  -9.095  52.134  1.00 36.09           C  
ATOM    662  CG1 VAL A  88      14.518  -9.304  51.742  1.00 21.74           C  
ATOM    663  CG2 VAL A  88      12.506 -10.392  52.648  1.00 29.67           C  
ATOM    664  N   ILE A  89      14.607  -6.321  53.432  1.00 21.12           N  
ATOM    665  CA  ILE A  89      15.047  -4.997  53.150  1.00 24.88           C  
ATOM    666  C   ILE A  89      16.531  -4.875  52.973  1.00 26.90           C  
ATOM    667  O   ILE A  89      17.331  -5.521  53.648  1.00 24.26           O  
ATOM    668  CB  ILE A  89      14.595  -4.123  54.307  1.00 39.14           C  
ATOM    669  CG1 ILE A  89      15.021  -2.696  54.083  1.00 25.77           C  
ATOM    670  CG2 ILE A  89      15.226  -4.634  55.599  1.00 34.04           C  
ATOM    671  CD1 ILE A  89      14.236  -1.793  55.033  1.00 34.90           C  
ATOM    672  N   GLN A  90      16.876  -4.021  52.015  1.00 26.58           N  
ATOM    673  CA  GLN A  90      18.266  -3.725  51.715  1.00 33.13           C  
ATOM    674  C   GLN A  90      18.662  -2.506  52.544  1.00 22.60           C  
ATOM    675  O   GLN A  90      17.947  -1.494  52.533  1.00 23.58           O  
ATOM    676  CB  GLN A  90      18.437  -3.441  50.212  1.00 32.10           C  
ATOM    677  CG  GLN A  90      17.880  -4.617  49.401  1.00 25.75           C  
ATOM    678  CD  GLN A  90      17.933  -4.325  47.930  1.00 68.96           C  
ATOM    679  OE1 GLN A  90      17.829  -3.177  47.526  1.00 30.70           O  
ATOM    680  NE2 GLN A  90      18.133  -5.348  47.130  1.00 37.45           N  
ATOM    681  N   THR A  91      19.783  -2.662  53.255  1.00 24.98           N  
ATOM    682  CA  THR A  91      20.332  -1.653  54.137  1.00 25.08           C  
ATOM    683  C   THR A  91      21.374  -0.784  53.451  1.00 39.03           C  
ATOM    684  O   THR A  91      21.797  -1.052  52.346  1.00 24.96           O  
ATOM    685  CB  THR A  91      20.915  -2.333  55.404  1.00 26.08           C  
ATOM    686  OG1 THR A  91      22.036  -3.142  55.101  1.00 20.83           O  
ATOM    687  CG2 THR A  91      19.843  -3.234  55.988  1.00 26.46           C  
ATOM    688  N   HIS A  92      21.792   0.273  54.118  1.00 27.31           N  
ATOM    689  CA  HIS A  92      22.813   1.166  53.620  1.00 24.33           C  
ATOM    690  C   HIS A  92      22.483   1.753  52.293  1.00 21.85           C  
ATOM    691  O   HIS A  92      23.369   1.761  51.449  1.00 28.36           O  
ATOM    692  CB  HIS A  92      24.173   0.477  53.439  1.00 26.17           C  
ATOM    693  CG  HIS A  92      24.726  -0.145  54.680  1.00 33.93           C  
ATOM    694  ND1 HIS A  92      24.186  -1.325  55.209  1.00 34.78           N  
ATOM    695  CD2 HIS A  92      25.784   0.235  55.460  1.00 30.79           C  
ATOM    696  CE1 HIS A  92      24.909  -1.635  56.279  1.00 34.63           C  
ATOM    697  NE2 HIS A  92      25.882  -0.725  56.458  1.00 29.03           N  
ATOM    698  N   LYS A  93      21.270   2.229  52.131  1.00 23.93           N  
ATOM    699  CA  LYS A  93      20.858   2.802  50.853  1.00 24.10           C  
ATOM    700  C   LYS A  93      20.908   4.327  50.834  1.00 32.13           C  
ATOM    701  O   LYS A  93      20.301   4.952  49.979  1.00 29.15           O  
ATOM    702  CB  LYS A  93      19.479   2.294  50.450  1.00 19.90           C  
ATOM    703  CG  LYS A  93      19.439   0.841  49.994  1.00 23.74           C  
ATOM    704  CD  LYS A  93      20.405   0.583  48.841  1.00 29.66           C  
ATOM    705  CE  LYS A  93      20.304  -0.815  48.292  1.00 44.41           C  
ATOM    706  NZ  LYS A  93      21.474  -1.171  47.455  1.00 35.91           N  
ATOM    707  N   LYS A  94      21.624   4.936  51.786  1.00 27.04           N  
ATOM    708  CA  LYS A  94      21.711   6.402  51.900  1.00 33.71           C  
ATOM    709  C   LYS A  94      22.061   7.170  50.600  1.00 33.21           C  
ATOM    710  O   LYS A  94      21.452   8.183  50.220  1.00 27.87           O  
ATOM    711  CB  LYS A  94      22.649   6.702  53.055  1.00 36.27           C  
ATOM    712  CG  LYS A  94      23.338   8.041  53.089  1.00 48.61           C  
ATOM    713  CD  LYS A  94      24.401   7.941  54.154  1.00100.00           C  
ATOM    714  CE  LYS A  94      25.436   9.042  54.209  1.00100.00           C  
ATOM    715  NZ  LYS A  94      26.390   8.848  55.269  1.00100.00           N  
ATOM    716  N   GLU A  95      23.044   6.667  49.882  1.00 33.75           N  
ATOM    717  CA  GLU A  95      23.474   7.289  48.645  1.00 41.52           C  
ATOM    718  C   GLU A  95      22.438   7.329  47.520  1.00 37.37           C  
ATOM    719  O   GLU A  95      22.561   8.182  46.649  1.00 61.85           O  
ATOM    720  CB  GLU A  95      24.806   6.700  48.167  1.00 33.95           C  
ATOM    721  CG  GLU A  95      25.961   6.995  49.151  1.00 35.18           C  
ATOM    722  CD  GLU A  95      26.287   8.476  49.298  1.00100.00           C  
ATOM    723  OE1 GLU A  95      27.201   9.046  48.724  1.00100.00           O  
ATOM    724  OE2 GLU A  95      25.498   9.103  50.130  1.00100.00           O  
ATOM    725  N   ASP A  96      21.430   6.425  47.544  1.00 31.57           N  
ATOM    726  CA  ASP A  96      20.357   6.353  46.540  1.00 35.62           C  
ATOM    727  C   ASP A  96      19.473   7.581  46.531  1.00 39.09           C  
ATOM    728  O   ASP A  96      18.704   7.839  45.601  1.00 41.37           O  
ATOM    729  CB  ASP A  96      19.392   5.176  46.784  1.00 27.55           C  
ATOM    730  CG  ASP A  96      19.990   3.864  46.389  1.00 35.82           C  
ATOM    731  OD1 ASP A  96      21.188   3.731  46.176  1.00 38.75           O  
ATOM    732  OD2 ASP A  96      19.096   2.891  46.352  1.00 39.18           O  
ATOM    733  N   LEU A  97      19.540   8.309  47.622  1.00 37.98           N  
ATOM    734  CA  LEU A  97      18.712   9.473  47.728  1.00 48.93           C  
ATOM    735  C   LEU A  97      19.372  10.737  47.209  1.00 46.76           C  
ATOM    736  O   LEU A  97      20.572  10.968  47.316  1.00 81.73           O  
ATOM    737  CB  LEU A  97      18.069   9.644  49.116  1.00 29.69           C  
ATOM    738  CG  LEU A  97      17.550   8.316  49.692  1.00 44.74           C  
ATOM    739  CD1 LEU A  97      17.006   8.500  51.103  1.00 44.12           C  
ATOM    740  CD2 LEU A  97      16.487   7.658  48.821  1.00 55.19           C  
ATOM    741  N   TYR A  98      18.523  11.529  46.601  1.00 76.74           N  
ATOM    742  CA  TYR A  98      18.825  12.827  46.049  1.00100.00           C  
ATOM    743  C   TYR A  98      17.575  13.690  46.087  1.00100.00           C  
ATOM    744  O   TYR A  98      17.130  14.087  44.987  1.00100.00           O  
ATOM    745  CB  TYR A  98      19.649  12.969  44.709  1.00100.00           C  
ATOM    746  CG  TYR A  98      19.454  12.021  43.530  1.00 85.80           C  
ATOM    747  CD1 TYR A  98      18.258  11.344  43.278  1.00 61.42           C  
ATOM    748  CD2 TYR A  98      20.505  11.832  42.616  1.00 69.58           C  
ATOM    749  CE1 TYR A  98      18.118  10.510  42.175  1.00100.00           C  
ATOM    750  CE2 TYR A  98      20.403  10.976  41.525  1.00100.00           C  
ATOM    751  CZ  TYR A  98      19.197  10.302  41.295  1.00100.00           C  
ATOM    752  OH  TYR A  98      19.057   9.456  40.220  1.00100.00           O  
ATOM    753  OXT TYR A  98      17.011  13.925  47.196  1.00 66.18           O  
TER     754      TYR A  98                                                      
HETATM  755 FE1  FES A 100      18.042  10.068  60.599  1.00 25.21          FE  
HETATM  756 FE2  FES A 100      16.955   7.610  60.644  1.00 22.70          FE  
HETATM  757  S1  FES A 100      18.927   8.243  61.353  1.00 21.98           S  
HETATM  758  S2  FES A 100      16.116   9.447  59.695  1.00 23.57           S  
HETATM  759  O   HOH A 200      20.346   1.836  59.071  1.00 21.55           O  
HETATM  760  O   HOH A 201      15.442  -7.358  70.096  1.00 20.90           O  
HETATM  761  O   HOH A 202      23.536   0.634  64.960  1.00 26.43           O  
HETATM  762  O   HOH A 203      20.334   1.176  56.397  1.00 24.83           O  
HETATM  763  O   HOH A 204       6.719   5.466  62.517  1.00 36.65           O  
HETATM  764  O   HOH A 205       8.572   2.670  51.206  1.00 30.34           O  
HETATM  765  O   HOH A 206      11.622   0.810  69.159  1.00 28.68           O  
HETATM  766  O   HOH A 207      22.816  -5.162  56.696  1.00 29.81           O  
HETATM  767  O   HOH A 208      25.996   2.336  63.881  1.00 43.23           O  
HETATM  768  O   HOH A 209      12.261 -11.867  56.287  1.00 30.11           O  
HETATM  769  O   HOH A 210      18.390 -12.698  65.959  1.00 28.37           O  
HETATM  770  O   HOH A 211      21.462  -8.291  45.044  1.00 45.14           O  
HETATM  771  O   HOH A 212      22.441  -3.013  50.241  1.00 29.46           O  
HETATM  772  O   HOH A 213      21.821   3.855  54.773  1.00 35.63           O  
HETATM  773  O   HOH A 214      25.492  -4.691  57.672  1.00 38.10           O  
HETATM  774  O   HOH A 215      23.246  -7.957  56.024  1.00 35.60           O  
HETATM  775  O   HOH A 216      20.583  -7.443  73.372  1.00 54.77           O  
HETATM  776  O   HOH A 217      16.894  11.363  68.506  1.00 55.80           O  
HETATM  777  O   HOH A 218       4.013  -0.408  66.628  1.00 82.34           O  
HETATM  778  O   HOH A 219       4.066   4.350  56.933  1.00 47.30           O  
HETATM  779  O   HOH A 220       7.084  13.042  46.238  1.00 47.95           O  
HETATM  780  O   HOH A 221      25.716   0.459  50.208  1.00 36.44           O  
HETATM  781  O   HOH A 222      25.805   7.659  64.824  1.00 32.41           O  
HETATM  782  O   HOH A 223      24.810  -3.910  68.168  1.00 37.14           O  
HETATM  783  O   HOH A 224       3.605  -2.994  63.535  1.00 41.06           O  
HETATM  784  O   HOH A 225       5.245  -0.404  53.384  1.00 37.74           O  
HETATM  785  O   HOH A 226       6.744  -9.339  69.815  1.00 67.26           O  
HETATM  786  O   HOH A 227      13.528   6.502  66.435  1.00 51.31           O  
HETATM  787  O   HOH A 228       3.643   7.203  48.166  1.00 61.32           O  
HETATM  788  O   HOH A 229       1.675  -1.476  56.832  1.00 54.10           O  
HETATM  789  O   HOH A 230      24.400   4.324  50.474  1.00 37.23           O  
HETATM  790  O   HOH A 231      20.593 -13.257  63.774  1.00 54.57           O  
HETATM  791  O   HOH A 232      20.053   0.639  45.218  1.00 42.71           O  
HETATM  792  O   HOH A 233       6.653  12.228  52.351  1.00 47.87           O  
HETATM  793  O   HOH A 234      27.166  -6.189  57.274  1.00 51.86           O  
HETATM  794  O   HOH A 235       9.985  13.429  61.827  1.00 50.86           O  
HETATM  795  O   HOH A 236       5.309   5.607  67.189  1.00 53.30           O  
HETATM  796  O   HOH A 237      18.424  16.223  57.275  1.00 62.87           O  
HETATM  797  O   HOH A 238      26.160   5.149  63.213  1.00 39.41           O  
HETATM  798  O   HOH A 239      27.548   1.492  60.685  1.00 90.51           O  
HETATM  799  O   HOH A 240      18.545  -5.049  43.840  1.00 47.66           O  
HETATM  800  O   HOH A 241       6.770   2.189  52.933  1.00 47.13           O  
HETATM  801  O   HOH A 242      24.275  -3.290  70.737  1.00 62.61           O  
HETATM  802  O   HOH A 243      -0.736  -9.341  68.144  1.00 72.11           O  
HETATM  803  O   HOH A 244      10.261 -12.874  53.966  1.00 56.99           O  
HETATM  804  O   HOH A 245       5.169   3.783  54.186  1.00 48.52           O  
HETATM  805  O   HOH A 246      19.089  -0.445  70.582  1.00 53.35           O  
HETATM  806  O   HOH A 247       6.013 -13.563  61.129  1.00 63.64           O  
HETATM  807  O   HOH A 248       4.325 -11.803  57.294  1.00 51.40           O  
HETATM  808  O   HOH A 249       5.381  -7.605  49.406  1.00 53.71           O  
HETATM  809  O   HOH A 250      24.868  -2.545  50.298  1.00 54.36           O  
HETATM  810  O   HOH A 251      27.860  -5.688  64.508  1.00 58.82           O  
HETATM  811  O   HOH A 252      10.810 -11.429  49.102  1.00 62.61           O  
HETATM  812  O   HOH A 253      21.648  -4.215  73.868  1.00 62.34           O  
HETATM  813  O   HOH A 254      25.300 -13.416  55.601  1.00 61.77           O  
HETATM  814  O   HOH A 255      13.278  14.142  50.193  1.00 55.61           O  
HETATM  815  O   HOH A 256       4.515   8.643  44.060  1.00 60.78           O  
HETATM  816  O   HOH A 257      27.182   9.075  63.190  1.00 74.98           O  
HETATM  817  O   HOH A 258      13.097   1.805  43.221  1.00 54.62           O  
HETATM  818  O   HOH A 259       9.149   2.886  69.515  1.00 56.56           O  
HETATM  819  O   HOH A 260       1.666   7.792  63.650  1.00 70.12           O  
HETATM  820  O   HOH A 261       3.379  10.572  63.653  1.00 58.53           O  
HETATM  821  O   HOH A 262      16.206  13.225  49.161  1.00 44.99           O  
HETATM  822  O   HOH A 263       0.318 -12.147  68.376  1.00 84.35           O  
HETATM  823  O   HOH A 264      14.758 -16.409  64.134  1.00 96.04           O  
HETATM  824  O   HOH A 265      12.166  -0.486  71.715  1.00 77.62           O  
HETATM  825  O   HOH A 266      24.389 -11.511  65.933  1.00 61.60           O  
HETATM  826  O   HOH A 267       1.493   2.974  57.517  1.00 74.40           O  
CONECT  323  755                                                                
CONECT  354  755                                                                
CONECT  373  756                                                                
CONECT  597  756                                                                
CONECT  755  323  354  757  758                                                 
CONECT  756  373  597  757  758                                                 
CONECT  757  755  756                                                           
CONECT  758  755  756                                                           
MASTER      286    0    1    4    7    0    2    6  822    1    8    8          
END                                                                             
