GenomeNet

Database: PDB
Entry: 2FDN
LinkDB: 2FDN
Original site: 2FDN 
HEADER    ELECTRON TRANSPORT                      01-OCT-97   2FDN              
TITLE     2[4FE-4S] FERREDOXIN FROM CLOSTRIDIUM ACIDI-URICI                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERREDOXIN;                                                
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACIDURICI;                          
SOURCE   3 ORGANISM_TAXID: 1556;                                                
SOURCE   4 ATCC: 7906                                                           
KEYWDS    ELECTRON TRANSPORT, IRON-SULFUR, 4FE-4S                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.DAUTER,K.S.WILSON,L.C.SIEKER,J.MEYER,J.M.MOULIS                     
REVDAT   4   24-MAR-09 2FDN    1       ATOM   CONECT                            
REVDAT   3   24-FEB-09 2FDN    1       VERSN                                    
REVDAT   2   05-JAN-00 2FDN    1       REMARK                                   
REVDAT   1   08-APR-98 2FDN    0                                                
JRNL        AUTH   Z.DAUTER,K.S.WILSON,L.C.SIEKER,J.MEYER,J.M.MOULIS            
JRNL        TITL   ATOMIC RESOLUTION (0.94 A) STRUCTURE OF                      
JRNL        TITL 2 CLOSTRIDIUM ACIDURICI FERREDOXIN. DETAILED                   
JRNL        TITL 3 GEOMETRY OF [4FE-4S] CLUSTERS IN A PROTEIN.                  
JRNL        REF    BIOCHEMISTRY                  V.  36 16065 1997              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9405040                                                      
JRNL        DOI    10.1021/BI972155Y                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.D.DUEE,E.FANCHON,J.VICAT,L.C.SIEKER,J.MEYER,               
REMARK   1  AUTH 2 J.M.MOULIS                                                   
REMARK   1  TITL   REFINED CRYSTAL STRUCTURE OF THE 2[4FE-4S]                   
REMARK   1  TITL 2 FERREDOXIN FROM CLOSTRIDIUM ACIDURICI AT 1.84 A              
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    J.MOL.BIOL.                   V. 243   683 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.94 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELX                                                
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.94                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.100                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 47452                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.087                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 37200                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 381                                           
REMARK   3   NUCLEIC ACID ATOMS : NULL                                          
REMARK   3   HETEROGEN ATOMS    : 16                                            
REMARK   3   SOLVENT ATOMS      : 96                                            
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 472.00                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 272.00                  
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 6                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 5145                    
REMARK   3   NUMBER OF RESTRAINTS                     : 5081                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.027                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.038                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.017                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.360                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.033                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.075                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: SHELX SWAT                                            
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NO RESTRAINTS ON [4FE-4S] CLUSTERS        
REMARK   4                                                                      
REMARK   4 2FDN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6-7.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.883                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : 0.07300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: TAKEN FROM PDB ENTRY         
REMARK 200  1FDN                                                                
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 55-60% AMMONIUM SULFATE, 100 MM          
REMARK 280  TRISMALEATE PH 6.6-7.0 MIXED 1:1 WITH 10 MG/ML PROTEIN              
REMARK 280  SOLUTION.                                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.41000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       16.97500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.11500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       16.97500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       18.70500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       16.97500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       56.11500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       16.97500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       16.97500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       18.70500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       37.41000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 149  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ILE A   4   C     ASN A   5   N       0.158                       
REMARK 500    SER A  10   CA    SER A  10   CB      0.426                       
REMARK 500    SER A  24   CA    SER A  24   CB      0.150                       
REMARK 500    VAL A  31   CA    VAL A  31   CB      0.167                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A   6   CA  -  C   -  N   ANGL. DEV. =  18.3 DEGREES          
REMARK 500    GLU A   6   O   -  C   -  N   ANGL. DEV. = -23.4 DEGREES          
REMARK 500    ALA A   7   C   -  N   -  CA  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    SER A  10   CB  -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    SER A  24   CB  -  CA  -  C   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    SER A  24   N   -  CA  -  CB  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ASP A  27   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ASP A  28   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    ARG A  29   CD  -  NE  -  CZ  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    TYR A  30   C   -  N   -  CA  ANGL. DEV. = -17.9 DEGREES          
REMARK 500    VAL A  31   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    VAL A  31   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    VAL A  31   CA  -  CB  -  CG2 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  27      -70.17    -57.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 61                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 62                  
DBREF  2FDN A    1    55  UNP    P00198   FER_CLOAC        1     55             
SEQRES   1 A   55  ALA TYR VAL ILE ASN GLU ALA CYS ILE SER CYS GLY ALA          
SEQRES   2 A   55  CYS GLU PRO GLU CYS PRO VAL ASN ALA ILE SER SER GLY          
SEQRES   3 A   55  ASP ASP ARG TYR VAL ILE ASP ALA ASP THR CYS ILE ASP          
SEQRES   4 A   55  CYS GLY ALA CYS ALA GLY VAL CYS PRO VAL ASP ALA PRO          
SEQRES   5 A   55  VAL GLN ALA                                                  
HET    SF4  A  61       8                                                       
HET    SF4  A  62       8                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
FORMUL   2  SF4    2(FE4 S4)                                                    
FORMUL   4  HOH   *94(H2 O)                                                     
HELIX    1   1 GLU A   15  GLU A   17  5                                   3    
HELIX    2   2 ALA A   42  VAL A   46  1                                   5    
SHEET    1   A 2 TYR A   2  ILE A   4  0                                        
SHEET    2   A 2 PRO A  52  GLN A  54 -1  N  VAL A  53   O  VAL A   3           
LINK        FE1  SF4 A  61                 SG  CYS A   8     1555   1555  2.26  
LINK        FE2  SF4 A  61                 SG  CYS A  11     1555   1555  2.27  
LINK        FE3  SF4 A  61                 SG  CYS A  14     1555   1555  2.23  
LINK        FE4  SF4 A  61                 SG  CYS A  47     1555   1555  2.25  
LINK        FE1  SF4 A  62                 SG  CYS A  37     1555   1555  2.28  
LINK        FE2  SF4 A  62                 SG  CYS A  40     1555   1555  2.28  
LINK        FE3  SF4 A  62                 SG  CYS A  43     1555   1555  2.26  
LINK        FE4  SF4 A  62                 SG  CYS A  18     1555   1555  2.28  
SITE     1 AC1  7 CYS A   8  ILE A   9  CYS A  11  GLY A  12                    
SITE     2 AC1  7 CYS A  14  TYR A  30  CYS A  47                               
SITE     1 AC2  8 CYS A  18  VAL A  20  ILE A  32  CYS A  37                    
SITE     2 AC2  8 ILE A  38  CYS A  40  GLY A  41  CYS A  43                    
CRYST1   33.950   33.950   74.820  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.029455  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.029455  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013365        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system