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Database: PDB
Entry: 1FTC
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Original site: 1FTC 
HEADER    ELECTRON TRANSPORT                      08-JAN-97   1FTC              
TITLE     Y13C MUTANT OF AZOTOBACTER VINELANDII FDI                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERREDOXIN;                                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: CYS 13 MODIFIED TO A PERSULFIDE, [3FE-4S]             
COMPND   7 AND [4FE-4S] CLUSTERS AS IN NATIVE PROTEIN                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AZOTOBACTER VINELANDII;                         
SOURCE   3 ORGANISM_TAXID: 354;                                                 
SOURCE   4 STRAIN: JG100;                                                       
SOURCE   5 EXPRESSION_SYSTEM: AZOTOBACTER VINELANDII;                           
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 354                                         
KEYWDS    ELECTRON TRANSPORT, IRON-SULFUR                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.KEMPER,S.J.LLOYD,G.S.PRASAD,C.D.STOUT,S.FAWCETT,                  
AUTHOR   2 F.A.ARMSTRONG,B.K.BURGESS                                            
REVDAT   3   24-MAR-09 1FTC    1       ATOM   CONECT                            
REVDAT   2   24-FEB-09 1FTC    1       VERSN                                    
REVDAT   1   01-APR-97 1FTC    0                                                
JRNL        AUTH   M.A.KEMPER,C.D.STOUT,S.J.LLOYD,G.S.PRASAD,                   
JRNL        AUTH 2 S.E.FAWCETT,F.A.ARMSTRONG,B.SHEN,B.K.BURGESS                 
JRNL        TITL   Y13C AZOTOBACTER VINELANDII FERREDOXIN I. A                  
JRNL        TITL 2 DESIGNED [FE-S] LIGAND MOTIF CONTAINS A CYSTEINE             
JRNL        TITL 3 PERSULFIDE.                                                  
JRNL        REF    J.BIOL.CHEM.                  V. 272 15620 1997              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   9188450                                                      
JRNL        DOI    10.1074/JBC.272.25.15620                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 8577                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
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   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            : 1670                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.64                           
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) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.55                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.49                            
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:                                           
REMARK   3  NOTE THAT THERE ARE TWO IDENTICAL COPIES OF THE Y13C MUTANT         
REMARK   3  OF FERREDOXIN IN THE ASYMMETRIC UNIT, WITH CHAIN                    
REMARK   3  IDENTIFIERS A AND B, AND EACH COPY HAS A MUTATED RESIDUE AT         
REMARK   3  POSITION 13 ( TYR -> CYS ) WHICH IS FURTHER MODIFIED TO A           
REMARK   3  CYSTEINE PERSULFIDE.                                                
REMARK   4                                                                      
REMARK   4 1FTC 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        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
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                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : XENTRONICS                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XENGEN                             
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9116                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.5                               
REMARK 200  DATA REDUNDANCY                : 2.760                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
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       36.85000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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    HIS A  35   NE2   HIS A  35   CD2    -0.068                       
REMARK 500    HIS A 103   NE2   HIS A 103   CD2    -0.069                       
REMARK 500    HIS B 103   NE2   HIS B 103   CD2    -0.072                       
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  15   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    CYS A  42   CA  -  CB  -  SG  ANGL. DEV. =   7.0 DEGREES          
REMARK 500    TRP A  78   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP A  78   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP A  94   CD1 -  CG  -  CD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    TRP A  94   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A 106   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    TRP B  78   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TRP B  78   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TRP B  78   CG  -  CD2 -  CE3 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    LYS B  85   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    GLU B  92   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    TRP B  94   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP B  94   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG B 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG B 106   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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    THR A   5     -161.80   -110.70                                   
REMARK 500    CYS A  11      -64.83   -108.61                                   
REMARK 500    ASN A  30       26.46   -150.28                                   
REMARK 500    THR B   5     -162.58   -115.28                                   
REMARK 500    ASN B  30       24.41   -143.17                                   
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 107                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 108                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 107                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 108                 
DBREF  1FTC A    1   106  UNP    P00214   FER1_AZOVI       1    106             
DBREF  1FTC B    1   106  UNP    P00214   FER1_AZOVI       1    106             
SEQADV 1FTC CSS A   13  UNP  P00214    TYR    13 ENGINEERED                     
SEQADV 1FTC CSS B   13  UNP  P00214    TYR    13 ENGINEERED                     
SEQRES   1 A  106  ALA PHE VAL VAL THR ASP ASN CYS ILE LYS CYS LYS CSS          
SEQRES   2 A  106  THR ASP 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                                                      
SEQRES   1 B  106  ALA PHE VAL VAL THR ASP ASN CYS ILE LYS CYS LYS CSS          
SEQRES   2 B  106  THR ASP CYS VAL GLU VAL CYS PRO VAL ASP CYS PHE TYR          
SEQRES   3 B  106  GLU GLY PRO ASN PHE LEU VAL ILE HIS PRO ASP GLU CYS          
SEQRES   4 B  106  ILE ASP CYS ALA LEU CYS GLU PRO GLU CYS PRO ALA GLN          
SEQRES   5 B  106  ALA ILE PHE SER GLU ASP GLU VAL PRO GLU ASP MET GLN          
SEQRES   6 B  106  GLU PHE ILE GLN LEU ASN ALA GLU LEU ALA GLU VAL TRP          
SEQRES   7 B  106  PRO ASN ILE THR GLU LYS LYS ASP PRO LEU PRO ASP ALA          
SEQRES   8 B  106  GLU ASP TRP ASP GLY VAL LYS GLY LYS LEU GLN HIS LEU          
SEQRES   9 B  106  GLU ARG                                                      
MODRES 1FTC CSS A   13  CYS  S-MERCAPTOCYSTEINE                                 
MODRES 1FTC CSS B   13  CYS  S-MERCAPTOCYSTEINE                                 
HET    CSS  A  13       7                                                       
HET    CSS  B  13       7                                                       
HET    SF4  A 107       8                                                       
HET    F3S  A 108       7                                                       
HET    SF4  B 107       8                                                       
HET    F3S  B 108       7                                                       
HETNAM     CSS S-MERCAPTOCYSTEINE                                               
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
FORMUL   1  CSS    2(C3 H7 N O2 S2)                                             
FORMUL   3  SF4    2(FE4 S4)                                                    
FORMUL   4  F3S    2(FE3 S4)                                                    
HELIX    1   1 ASP A    6  CYS A    8  5                                   3    
HELIX    2   2 ASP A   15  VAL A   19  5                                   5    
HELIX    3   3 LEU A   44  GLU A   48  1                                   5    
HELIX    4   4 GLU A   57  GLU A   59  5                                   3    
HELIX    5   5 GLU A   62  VAL A   77  5                                  16    
HELIX    6   6 ALA A   91  TRP A   94  1                                   4    
HELIX    7   7 LYS A  100  HIS A  103  5                                   4    
HELIX    8   8 ASP B    6  CYS B    8  5                                   3    
HELIX    9   9 ASP B   15  VAL B   19  5                                   5    
HELIX   10  10 LEU B   44  GLU B   48  1                                   5    
HELIX   11  11 GLU B   57  GLU B   59  5                                   3    
HELIX   12  12 GLU B   62  VAL B   77  5                                  16    
HELIX   13  13 ALA B   91  TRP B   94  1                                   4    
HELIX   14  14 LYS B  100  HIS B  103  5                                   4    
SHEET    1   A 2 PHE A   2  VAL A   4  0                                        
SHEET    2   A 2 ILE A  54  SER A  56 -1  N  PHE A  55   O  VAL A   3           
SHEET    1   B 2 PHE A  25  GLU A  27  0                                        
SHEET    2   B 2 LEU A  32  ILE A  34 -1  N  VAL A  33   O  TYR A  26           
SHEET    1   C 2 PHE B   2  VAL B   4  0                                        
SHEET    2   C 2 ILE B  54  SER B  56 -1  N  PHE B  55   O  VAL B   3           
SHEET    1   D 2 PHE B  25  GLU B  27  0                                        
SHEET    2   D 2 LEU B  32  ILE B  34 -1  N  VAL B  33   O  TYR B  26           
LINK         N   CSS A  13                 C   LYS A  12     1555   1555  1.33  
LINK         C   CSS A  13                 N   THR A  14     1555   1555  1.34  
LINK        FE1  SF4 A 107                 SG  CYS A  39     1555   1555  2.28  
LINK        FE2  SF4 A 107                 SG  CYS A  42     1555   1555  2.29  
LINK        FE3  SF4 A 107                 SG  CYS A  45     1555   1555  2.28  
LINK        FE4  SF4 A 107                 SG  CYS A  20     1555   1555  2.26  
LINK        FE1  F3S A 108                 SG  CYS A  16     1555   1555  2.29  
LINK        FE3  F3S A 108                 SG  CYS A  49     1555   1555  2.28  
LINK         N   CSS B  13                 C   LYS B  12     1555   1555  1.32  
LINK         C   CSS B  13                 N   THR B  14     1555   1555  1.32  
LINK        FE1  SF4 B 107                 SG  CYS B  39     1555   1555  2.29  
LINK        FE2  SF4 B 107                 SG  CYS B  42     1555   1555  2.28  
LINK        FE3  SF4 B 107                 SG  CYS B  45     1555   1555  2.27  
LINK        FE4  SF4 B 107                 SG  CYS B  20     1555   1555  2.25  
LINK        FE1  F3S B 108                 SG  CYS B  16     1555   1555  2.25  
LINK        FE3  F3S B 108                 SG  CYS B  49     1555   1555  2.26  
LINK         SG  CYS A   8                FE4  F3S A 108     1555   1555  2.30  
LINK         SG  CYS B   8                FE4  F3S B 108     1555   1555  2.27  
SITE     1 AC1 10 CYS A  20  VAL A  22  CYS A  24  PHE A  25                    
SITE     2 AC1 10 ILE A  34  CYS A  39  ILE A  40  CYS A  42                    
SITE     3 AC1 10 ALA A  43  CYS A  45                                          
SITE     1 AC2 10 VAL A   4  CYS A   8  LYS A  12  CSS A  13                    
SITE     2 AC2 10 THR A  14  ASP A  15  CYS A  16  LEU A  32                    
SITE     3 AC2 10 CYS A  49  ILE A  54                                          
SITE     1 AC3 11 PHE B   2  CYS B  20  VAL B  22  CYS B  24                    
SITE     2 AC3 11 PHE B  25  ILE B  34  CYS B  39  ILE B  40                    
SITE     3 AC3 11 CYS B  42  ALA B  43  CYS B  45                               
SITE     1 AC4  8 VAL B   4  CYS B   8  CSS B  13  THR B  14                    
SITE     2 AC4  8 ASP B  15  CYS B  16  CYS B  49  ILE B  54                    
CRYST1   39.300   73.700   45.100  90.00  98.40  90.00 P 1 21 1      4          
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      0.025445  0.000000  0.003757        0.00000                         
SCALE2      0.000000  0.013569  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022413        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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