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Database: PDB
Entry: 1D3W
LinkDB: 1D3W
Original site: 1D3W 
HEADER    ELECTRON TRANSPORT                      01-OCT-99   1D3W              
TITLE     CRYSTAL STRUCTURE OF FERREDOXIN 1 D15E MUTANT FROM                    
TITLE    2 AZOTOBACTER VINELANDII AT 1.7 ANGSTROM RESOLUTION.                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERREDOXIN 1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AZOTOBACTER VINELANDII;                         
SOURCE   3 ORGANISM_TAXID: 354;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 OTHER_DETAILS: THE SEQUENCE WAS MUTATED BY SITE DIRECTED             
SOURCE   7 MUTAGENESIS USING BIORAD MUTAGENE 2 KIT.                             
KEYWDS    BETA SHEET, PROTEIN MONOMER, IRON-SULPHUR PROTEIN,                    
KEYWDS   2 FERREDOXIN, ELECTRON TRANSPORT                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.CHEN,J.HIRST,R.CAMBA,C.A.BONAGURA,C.D.STOUT,B.K.BURGES,             
AUTHOR   2 F.A.ARMSTRONG                                                        
REVDAT   3   24-FEB-09 1D3W    1       VERSN                                    
REVDAT   2   05-APR-05 1D3W    1       COMPND SOURCE MASTER JRNL                
REVDAT   2 2                   1       REMARK CRYST1 CONECT                     
REVDAT   1   14-OCT-99 1D3W    0                                                
JRNL        AUTH   K.CHEN,J.HIRST,R.CAMBA,C.A.BONAGURA,C.D.STOUT,               
JRNL        AUTH 2 B.K.BURGESS,F.A.ARMSTRONG                                    
JRNL        TITL   ATOMICALLY DEFINED MECHANISM FOR PROTON TRANSFER             
JRNL        TITL 2 TO A BURIED REDOX CENTRE IN A PROTEIN.                       
JRNL        REF    NATURE                        V. 405   814 2000              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   10866206                                                     
JRNL        DOI    10.1038/35015610                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 10561                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 528                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 992                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 420                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.90                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1D3W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009771.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
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                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16030                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 13.810                             
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: .4M TRIS PH 7.8, 1.2 M AMMONIUM          
REMARK 280  SULPHATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.26750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       27.68500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       27.68500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.13375            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       27.68500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       27.68500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.40125            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       27.68500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       27.68500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       23.13375            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       27.68500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       27.68500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       69.40125            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       46.26750            
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: 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    THR A   5     -167.82   -105.01                                   
REMARK 500    LYS A  10       -3.39     76.36                                   
REMARK 500    ASN A  30       32.30   -145.76                                   
REMARK 500    ALA A  43       -2.10     62.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 217        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH A 246        DISTANCE =  5.36 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 107                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 108                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FDD   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF FERREDOXIN I D15N MUTANT AT 1.9           
REMARK 900 ANGSTROM RESOLUTION.                                                 
REMARK 900 RELATED ID: 1BOT   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF FERREDOXIN I D15K, K84D MUTANT            
REMARK 900 AT 2.1 ANGSTROM RESOLUTION.                                          
REMARK 900 RELATED ID: 6FDR   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF DITHIONITE REDUCED FERREDOXIN I           
REMARK 900 WILDTYPE FROM AZOTOBACTER VINELANDII AT 1.4 ANGSTROM                 
REMARK 900 RESOLUTION.                                                          
REMARK 900 RELATED ID: 7FDR   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF FERREDOXIN           
REMARK 900 I WILDTYPE FROM AZOTOBACTER VINELANDII AT 1.4 ANGSTROM               
REMARK 900 RESOLUTION.                                                          
DBREF  1D3W A    1   106  UNP    P00214   FER1_AZOVI       2    107             
SEQADV 1D3W GLU A   15  UNP  P00214    ASP    15 ENGINEERED MUTATION            
SEQRES   1 A  106  ALA PHE VAL VAL THR ASP ASN CYS ILE LYS CYS LYS TYR          
SEQRES   2 A  106  THR GLU CYS VAL GLU VAL CYS PRO VAL ASP CYS PHE TYR          
SEQRES   3 A  106  GLU GLY PRO ASN PHE LEU VAL ILE HIS PRO ASP GLU CYS          
SEQRES   4 A  106  ILE ASP CYS ALA LEU CYS GLU PRO GLU CYS PRO ALA GLN          
SEQRES   5 A  106  ALA ILE PHE SER GLU ASP GLU VAL PRO GLU ASP MET GLN          
SEQRES   6 A  106  GLU PHE ILE GLN LEU ASN ALA GLU LEU ALA GLU VAL TRP          
SEQRES   7 A  106  PRO ASN ILE THR GLU LYS LYS ASP PRO LEU PRO ASP ALA          
SEQRES   8 A  106  GLU ASP TRP ASP GLY VAL LYS GLY LYS LEU GLN HIS LEU          
SEQRES   9 A  106  GLU ARG                                                      
HET    SF4  A 107       8                                                       
HET    F3S  A 108       7                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
FORMUL   2  SF4    FE4 S4                                                       
FORMUL   3  F3S    FE3 S4                                                       
FORMUL   4  HOH   *140(H2 O)                                                    
HELIX    1   1 ASP A    6  ILE A    9  5                                   4    
HELIX    2   2 CYS A   45  CYS A   49  5                                   5    
HELIX    3   3 ASP A   58  VAL A   60  5                                   3    
HELIX    4   4 PRO A   61  MET A   64  5                                   4    
HELIX    5   5 GLN A   65  TRP A   78  1                                  14    
HELIX    6   6 ASP A   90  ASP A   95  1                                   6    
HELIX    7   7 GLY A   99  LEU A  104  5                                   6    
SHEET    1   A 2 PHE A   2  VAL A   4  0                                        
SHEET    2   A 2 ILE A  54  SER A  56 -1  O  PHE A  55   N  VAL A   3           
SHEET    1   B 2 PHE A  25  GLY A  28  0                                        
SHEET    2   B 2 PHE A  31  ILE A  34 -1  O  PHE A  31   N  GLY A  28           
LINK         SG  CYS A   8                FE3  F3S A 108     1555   1555  2.28  
LINK         SG  CYS A  16                FE1  F3S A 108     1555   1555  2.28  
LINK         SG  CYS A  20                FE4  SF4 A 107     1555   1555  2.28  
LINK         SG  CYS A  39                FE1  SF4 A 107     1555   1555  2.29  
LINK         SG  CYS A  42                FE2  SF4 A 107     1555   1555  2.31  
LINK         SG  CYS A  45                FE3  SF4 A 107     1555   1555  2.29  
LINK         SG  CYS A  49                FE4  F3S A 108     1555   1555  2.27  
SITE     1 AC1 11 PHE A   2  CYS A  20  VAL A  22  CYS A  24                    
SITE     2 AC1 11 PHE A  25  ILE A  34  CYS A  39  ILE A  40                    
SITE     3 AC1 11 CYS A  42  ALA A  43  CYS A  45                               
SITE     1 AC2  9 CYS A   8  LYS A  12  TYR A  13  THR A  14                    
SITE     2 AC2  9 GLU A  15  CYS A  16  LEU A  32  CYS A  49                    
SITE     3 AC2  9 PRO A  50                                                     
CRYST1   55.370   55.370   92.535  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.018060  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010807        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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