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Database: PDB
Entry: 1GX7
LinkDB: 1GX7
Original site: 1GX7 
HEADER    OXIDOREDUCTASE                          28-MAR-02   1GX7              
TITLE     BEST MODEL OF THE ELECTRON TRANSFER COMPLEX BETWEEN CYTOCHROME C3 AND 
TITLE    2 [FE]-HYDROGENASE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.18.99.1;                                                       
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PERIPLASMIC [FE] HYDROGENASE SMALL SUBUNIT;                
COMPND   7 CHAIN: D;                                                            
COMPND   8 EC: 1.18.99.1;                                                       
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: CYTOCHROME C3;                                             
COMPND  11 CHAIN: E                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;                         
SOURCE   3 ORGANISM_TAXID: 882;                                                 
SOURCE   4 STRAIN: HILDENBOROUGH;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;                         
SOURCE   7 ORGANISM_TAXID: 882;                                                 
SOURCE   8 STRAIN: HILDENBOROUGH;                                               
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;                         
SOURCE  11 ORGANISM_TAXID: 882;                                                 
SOURCE  12 STRAIN: HILDENBOROUGH                                                
KEYWDS    OXIDOREDUCTASE, ELECTRON TRANSFER COMPLEX, HYDROGENASE, MULTIHEME     
KEYWDS   2 CYTOCHROME, SOFT DOCKING, OXIDOREDUCTASE ELECTRON TRANSPORT, 4FE-4S, 
KEYWDS   3 IRON-SULFUR                                                          
EXPDTA    SOLUTION NMR; THEORETICAL MODEL                                       
MDLTYP    MINIMIZED AVERAGE                                                     
AUTHOR    L.ELANTAK,X.MORELLI,O.BORNET,C.HATCHIKIAN,M.CZJZEK,A.DOLLA,           
AUTHOR   2 F.GUERLESQUIN                                                        
REVDAT   3   17-JAN-18 1GX7    1       REMARK                                   
REVDAT   2   24-FEB-09 1GX7    1       VERSN                                    
REVDAT   1   31-JUL-03 1GX7    0                                                
JRNL        AUTH   L.ELANTAK,X.MORELLI,O.BORNET,C.HATCHIKIAN,M.CZJZEK,A.DOLLA,  
JRNL        AUTH 2 F.GUERLESQUIN                                                
JRNL        TITL   THE CYTOCHROME C(3)-[FE]-HYDROGENASE ELECTRON-TRANSFER       
JRNL        TITL 2 COMPLEX: STRUCTURAL MODEL BY NMR RESTRAINED DOCKING          
JRNL        REF    FEBS LETT.                    V. 548     1 2003              
JRNL        REFN                   ISSN 0014-5793                               
JRNL        PMID   12885397                                                     
JRNL        DOI    10.1016/S0014-5793(03)00718-X                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR3.851                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: A MOLECULAR DYNAMICS CALCULATION (AMBER   
REMARK   3  FORCE FIELD) WITH SHAKE RESTRAINTS FOR THE HETEROATOMS WAS          
REMARK   3  PERFORMED HEAT-BATH TEMPERATURE: 280 K INITIAL VELOCITIES FROM A    
REMARK   3  MAXWELL-BOLTZMAN DISTRIBUTION AT 280K. SHAKE RESTRAINTS WITH A      
REMARK   3  TOLERANCE OF 0.0004. THIS IS A MODEL COMPLEX OBTAINED BY NMR-       
REMARK   3  RESTRAINED SOFT DOCKING AND MINIMIZATION.                           
REMARK   4                                                                      
REMARK   4 1GX7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAR-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290009632.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 296                                
REMARK 210  PH                             : 5.9                                
REMARK 210  IONIC STRENGTH                 : 10 MM PHOSPHATE BUFFER             
REMARK 210  PRESSURE                       : 1 ATM                              
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : HSQC                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ                            
REMARK 210  SPECTROMETER MODEL             : DRX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: THE COMPLEX MODEL WAS DETERMINED WITH NMR-RESTRAINED         
REMARK 210  (HSQC) SOFT DOCKING, THEN MINIMIZED BY MOLECULAR DYNAMICS           
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 220                                                                      
REMARK 220 EXPERIMENTAL DETAILS                                                 
REMARK 220  EXPERIMENT TYPE                : THEORETICAL MODELLING              
REMARK 220                                                                      
REMARK 220 REMARK: THIS THEORETICAL MODEL ENTRY WAS NOT ANNOTATED AND NOT       
REMARK 220         VALIDATED BY THE WWPDB STAFF AND THEREFORE MAY NOT CONFORM   
REMARK 220         TO THE PDB FORMAT.                                           
REMARK 225                                                                      
REMARK 225 THEORETICAL MODEL                                                    
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.           
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND                
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE                   
REMARK 225 RECORDS ARE MEANINGLESS.                                             
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E                               
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: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  FE    FE2 A     5    FE    FE2 A     6              0.90            
REMARK 500   HD1  HIS E    52     O    ALA E    62              1.54            
REMARK 500   O    PRO A    61     HD1  HIS A    62              1.55            
REMARK 500   O    LEU D    76     HD1  HIS D    82              1.58            
REMARK 500   O    GLN A    71     HD1  HIS A    75              1.58            
REMARK 500   O    PHE A   197     HE1  TRP D    92              1.58            
REMARK 500   H    LYS E   102     OXT  GLU E   107              1.59            
REMARK 500   O    PRO E     5     HD1  HIS E    22              1.59            
REMARK 500   O    PRO A   173     HD1  HIS A   196              1.59            
REMARK 500   O    ALA A   140     HD1  HIS A   141              1.60            
REMARK 500   S2   PDT A     4     C    CYN A     8              2.13            
REMARK 500   S1   PDT A     4     C    CMO A    10              2.18            
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    TYR A 311   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    SER A 321   N   -  CA  -  CB  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    CYS A 382   CA  -  CB  -  SG  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ALA A 397   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    GLU D 123   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    GLU E 107   N   -  CA  -  C   ANGL. DEV. = -18.3 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    ALA A  33      -40.26   -168.98                                   
REMARK 500    ASP A  39       -1.43     82.09                                   
REMARK 500    PRO A  57      -97.02    -72.14                                   
REMARK 500    ALA A  65      -50.88   -123.26                                   
REMARK 500    ILE A  67       31.11    -79.08                                   
REMARK 500    GLN A  71      -65.77     68.20                                   
REMARK 500    ASN A  79       69.33     60.43                                   
REMARK 500    GLN A  85       41.64   -151.16                                   
REMARK 500    MET A 105       75.47   -119.29                                   
REMARK 500    PHE A 139       49.94    -89.06                                   
REMARK 500    HIS A 141       60.61   -158.94                                   
REMARK 500    THR A 145        5.56    -68.46                                   
REMARK 500    PHE A 197       78.95   -101.83                                   
REMARK 500    SER A 198       97.04    -34.73                                   
REMARK 500    SER A 202      124.35    -29.99                                   
REMARK 500    THR A 213      -79.67   -119.72                                   
REMARK 500    PRO A 244       39.70    -73.02                                   
REMARK 500    LEU A 246       58.09    -95.52                                   
REMARK 500    SER A 284       28.32    -67.63                                   
REMARK 500    SER A 289       48.31    -89.11                                   
REMARK 500    ALA A 293      -46.51   -159.19                                   
REMARK 500    THR A 294       35.75    -82.24                                   
REMARK 500    ILE A 295       48.23   -163.07                                   
REMARK 500    TYR A 311       42.96    -88.15                                   
REMARK 500    GLU A 312      -68.64   -148.54                                   
REMARK 500    ALA A 313       48.45   -104.19                                   
REMARK 500    SER A 321       47.92    -57.28                                   
REMARK 500    ALA A 326      -54.40   -144.01                                   
REMARK 500    VAL A 327       56.79    -93.54                                   
REMARK 500    ARG A 328       73.82   -167.53                                   
REMARK 500    ALA A 377       73.09   -156.61                                   
REMARK 500    VAL A 394      -52.46   -132.73                                   
REMARK 500    ILE D  39      -70.15    -26.47                                   
REMARK 500    TYR D  75      -56.01   -156.90                                   
REMARK 500    GLU D  77      -48.09     77.73                                   
REMARK 500    LEU D  80      -49.33     67.17                                   
REMARK 500    HIS D  82     -131.24     69.18                                   
REMARK 500    THR D  90     -169.27   -160.23                                   
REMARK 500    ALA D 105       49.13    -84.75                                   
REMARK 500    TYR D 122      -44.37   -132.97                                   
REMARK 500    GLU E  12       51.50   -158.31                                   
REMARK 500    LYS E  15       39.90    -95.29                                   
REMARK 500    SER E  23      -80.82    -25.78                                   
REMARK 500    LYS E  29       -5.81     65.86                                   
REMARK 500    CYS E  30      -59.37     64.85                                   
REMARK 500    ASP E  32       39.21   -141.56                                   
REMARK 500    CYS E  33      -47.16   -168.67                                   
REMARK 500    ASN E  38      -67.86     60.43                                   
REMARK 500    ALA E  49      104.08    -51.10                                   
REMARK 500    ASP E  53      -47.01   -152.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ILE A   36     GLY A   37                  149.74                    
REMARK 500 GLY A   37     CYS A   38                  -92.50                    
REMARK 500 ASN A   68     CYS A   69                 -149.76                    
REMARK 500 GLN A   71     CYS A   72                 -142.21                    
REMARK 500 PHE A  147     THR A  148                 -145.44                    
REMARK 500 THR A  199     CYS A  200                  148.54                    
REMARK 500 MET A  232     PRO A  233                 -129.28                    
REMARK 500 LYS A  247     SER A  248                 -143.09                    
REMARK 500 ARG A  252     ASP A  253                 -147.63                    
REMARK 500 LEU A  330     ASP A  331                  147.39                    
REMARK 500 TYR A  370     HIS A  371                 -133.49                    
REMARK 500 CYS A  384     GLY A  385                 -147.21                    
REMARK 500 GLN A  388     PRO A  389                 -137.36                    
REMARK 500 GLU A  396     ALA A  397                  139.37                    
REMARK 500 PRO D  119     TYR D  120                  119.41                    
REMARK 500 THR E   14     LYS E   15                 -141.74                    
REMARK 500 CYS E   33     HIS E   34                  144.19                    
REMARK 500 ASP E   42     TYR E   43                  147.20                    
REMARK 500 ALA E   62     LYS E   63                 -147.62                    
REMARK 500 LYS E   72     ASN E   73                  145.65                    
REMARK 500 HIS E  106     GLU E  107                 -145.78                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  82         0.09    SIDE CHAIN                              
REMARK 500    ARG A 111         0.08    SIDE CHAIN                              
REMARK 500    TYR A 112         0.10    SIDE CHAIN                              
REMARK 500    TYR A 185         0.10    SIDE CHAIN                              
REMARK 500    TYR A 227         0.14    SIDE CHAIN                              
REMARK 500    TYR A 370         0.16    SIDE CHAIN                              
REMARK 500    TYR D  42         0.06    SIDE CHAIN                              
REMARK 500    TYR D 120         0.09    SIDE CHAIN                              
REMARK 500    TYR D 122         0.07    SIDE CHAIN                              
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                             SF4 A   1  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  76   SG                                                     
REMARK 620 2 SF4 A   1   S2  117.2                                              
REMARK 620 3 SF4 A   1   S3  109.0 107.7                                        
REMARK 620 4 SF4 A   1   S4  106.0 107.6 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   1  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  41   SG                                                     
REMARK 620 2 SF4 A   1   S1  106.6                                              
REMARK 620 3 SF4 A   1   S3  113.7 110.0                                        
REMARK 620 4 SF4 A   1   S4  112.1 104.9 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   1  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  38   SG                                                     
REMARK 620 2 SF4 A   1   S1  111.1                                              
REMARK 620 3 SF4 A   1   S2  111.3 109.5                                        
REMARK 620 4 SF4 A   1   S4  111.3 105.5 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   1  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  35   SG                                                     
REMARK 620 2 SF4 A   1   S1  111.8                                              
REMARK 620 3 SF4 A   1   S2  110.1 109.2                                        
REMARK 620 4 SF4 A   1   S3  107.6 110.3 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   2  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  72   SG                                                     
REMARK 620 2 SF4 A   2   S2  107.3                                              
REMARK 620 3 SF4 A   2   S3  108.3 110.6                                        
REMARK 620 4 SF4 A   2   S4  115.4 110.3 104.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   2  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  45   SG                                                     
REMARK 620 2 SF4 A   2   S1  105.4                                              
REMARK 620 3 SF4 A   2   S3  112.5 108.2                                        
REMARK 620 4 SF4 A   2   S4  114.9 111.1 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   2  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  66   SG                                                     
REMARK 620 2 SF4 A   2   S1  113.5                                              
REMARK 620 3 SF4 A   2   S2  109.3 103.6                                        
REMARK 620 4 SF4 A   2   S4  107.5 111.8 111.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   2  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  69   SG                                                     
REMARK 620 2 SF4 A   2   S1  112.9                                              
REMARK 620 3 SF4 A   2   S2  112.7 103.2                                        
REMARK 620 4 SF4 A   2   S3  108.3 108.7 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   3  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 234   SG                                                     
REMARK 620 2 SF4 A   3   S2  113.1                                              
REMARK 620 3 SF4 A   3   S3  111.3 111.9                                        
REMARK 620 4 SF4 A   3   S4  105.6 107.2 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   3  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 179   SG                                                     
REMARK 620 2 SF4 A   3   S1  116.3                                              
REMARK 620 3 SF4 A   3   S3  109.1 110.5                                        
REMARK 620 4 SF4 A   3   S4  104.1 108.3 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   3  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 382   SG                                                     
REMARK 620 2 SF4 A   3   S1  108.7                                              
REMARK 620 3 SF4 A   3   S2  108.3 107.4                                        
REMARK 620 4 SF4 A   3   S4  115.1 108.9 108.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A   3  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 378   SG                                                     
REMARK 620 2 SF4 A   3   S1  108.4                                              
REMARK 620 3 SF4 A   3   S2  109.9 106.0                                        
REMARK 620 4 SF4 A   3   S3  111.5 109.5 111.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A   5  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYN A   8   C                                                      
REMARK 620 2 PDT A   4   S1   70.5                                              
REMARK 620 3 CYN A   7   C   145.9  78.8                                        
REMARK 620 4 CMO A  10   C    65.5  67.4 115.7                                  
REMARK 620 5 MET A 232   SD  123.5 164.8  86.2 121.8                            
REMARK 620 6 PDT A   4   S2   61.4  33.6  84.8  93.5 143.9                      
REMARK 620 7 CMO A   9   C   115.7  83.0  44.1 148.4  85.1  64.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A   6  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CMO A   9   C                                                      
REMARK 620 2 CYN A   8   C   117.1                                              
REMARK 620 3 PDT A   4   S1   96.1  57.7                                        
REMARK 620 4 CMO A  10   C   149.4  41.1  55.4                                  
REMARK 620 5 MET A 232   SD  115.9  90.7 143.5  89.1                            
REMARK 620 6 PDT A   4   S2   73.5  54.5  32.1  76.0 140.8                      
REMARK 620 7 CYN A   7   C    71.5 145.9  89.4 114.5 116.1 103.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC E 109  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  70   NE2                                                    
REMARK 620 2 HEC E 109   NA   89.6                                              
REMARK 620 3 HEC E 109   NB   93.2  90.5                                        
REMARK 620 4 HEC E 109   NC   90.1 179.6  89.5                                  
REMARK 620 5 HEC E 109   ND   87.7  89.7 179.1  90.3                            
REMARK 620 6 HIS E 106   NE2 177.7  88.2  87.5  92.2  91.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC E 110  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  35   NE2                                                    
REMARK 620 2 HEC E 110   NA   89.5                                              
REMARK 620 3 HEC E 110   NB   91.4  89.9                                        
REMARK 620 4 HEC E 110   NC   89.7 179.2  89.9                                  
REMARK 620 5 HEC E 110   ND   88.6  90.3 179.8  89.9                            
REMARK 620 6 HIS E  52   NE2 176.9  88.1  90.5  92.7  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC E 111  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  22   NE2                                                    
REMARK 620 2 HEC E 111   NA   93.5                                              
REMARK 620 3 HEC E 111   NB   90.9  90.0                                        
REMARK 620 4 HEC E 111   NC   90.5 176.0  89.8                                  
REMARK 620 5 HEC E 111   ND   89.1  89.6 179.6  90.7                            
REMARK 620 6 HIS E  34   NE2 176.6  88.4  91.9  87.6  88.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC E 112  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  25   NE2                                                    
REMARK 620 2 HEC E 112   NA   84.2                                              
REMARK 620 3 HEC E 112   NB   90.4  90.0                                        
REMARK 620 4 HEC E 112   NC   93.0 177.2  90.0                                  
REMARK 620 5 HEC E 112   ND   90.4  90.3 179.2  89.8                            
REMARK 620 6 HIS E  83   NE2 175.3  91.9  92.2  90.9  87.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDT A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 109                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 110                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 111                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 112                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HFE   RELATED DB: PDB                                   
REMARK 900 1.6 A RESOLUTION STRUCTURE OF THE FE- ONLY HYDROGENASE FROM          
REMARK 900 DESULFOVIBRIO DESULFURICANS                                          
REMARK 900 RELATED ID: 1A2I   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS ( HILDENBOROUGH)        
REMARK 900 FERROCYTOCHROME C3, NMR, 20 STRUCTURES                               
REMARK 900 RELATED ID: 1MDV   RELATED DB: PDB                                   
REMARK 900 KEY ROLE OF PHENYLALANINE 20 IN CYTOCHROME C3: STRUCTURE, STABILITY  
REMARK 900 AND FUNCTION STUDIES                                                 
REMARK 900 RELATED ID: 2CTH   RELATED DB: PDB                                   
REMARK 900 CYTOCHROME C3 FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH              
REMARK 900 RELATED ID: 2CYM   RELATED DB: PDB                                   
REMARK 900 CYTOCHROME C3                                                        
DBREF  1GX7 A   27   397  UNP    P07598   PHFL_DESVH      27    397             
DBREF  1GX7 D   36   123  UNP    P07603   PHFS_DESVH      36    123             
DBREF  1GX7 E    1   107  UNP    P00131   CYC3_DESVH      23    129             
SEQRES   1 A  371  PHE VAL GLN ILE ASP GLU ALA LYS CYS ILE GLY CYS ASP          
SEQRES   2 A  371  THR CYS SER GLN TYR CYS PRO THR ALA ALA ILE PHE GLY          
SEQRES   3 A  371  GLU MET GLY GLU PRO HIS SER ILE PRO HIS ILE GLU ALA          
SEQRES   4 A  371  CYS ILE ASN CYS GLY GLN CYS LEU THR HIS CYS PRO GLU          
SEQRES   5 A  371  ASN ALA ILE TYR GLU ALA GLN SER TRP VAL PRO GLU VAL          
SEQRES   6 A  371  GLU LYS LYS LEU LYS ASP GLY LYS VAL LYS CYS ILE ALA          
SEQRES   7 A  371  MET PRO ALA PRO ALA VAL ARG TYR ALA LEU GLY ASP ALA          
SEQRES   8 A  371  PHE GLY MET PRO VAL GLY SER VAL THR THR GLY LYS MET          
SEQRES   9 A  371  LEU ALA ALA LEU GLN LYS LEU GLY PHE ALA HIS CYS TRP          
SEQRES  10 A  371  ASP THR GLU PHE THR ALA ASP VAL THR ILE TRP GLU GLU          
SEQRES  11 A  371  GLY SER GLU PHE VAL GLU ARG LEU THR LYS LYS SER ASP          
SEQRES  12 A  371  MET PRO LEU PRO GLN PHE THR SER CYS CYS PRO GLY TRP          
SEQRES  13 A  371  GLN LYS TYR ALA GLU THR TYR TYR PRO GLU LEU LEU PRO          
SEQRES  14 A  371  HIS PHE SER THR CYS LYS SER PRO ILE GLY MET ASN GLY          
SEQRES  15 A  371  ALA LEU ALA LYS THR TYR GLY ALA GLU ARG MET LYS TYR          
SEQRES  16 A  371  ASP PRO LYS GLN VAL TYR THR VAL SER ILE MET PRO CYS          
SEQRES  17 A  371  ILE ALA LYS LYS TYR GLU GLY LEU ARG PRO GLU LEU LYS          
SEQRES  18 A  371  SER SER GLY MET ARG ASP ILE ASP ALA THR LEU THR THR          
SEQRES  19 A  371  ARG GLU LEU ALA TYR MET ILE LYS LYS ALA GLY ILE ASP          
SEQRES  20 A  371  PHE ALA LYS LEU PRO ASP GLY LYS ARG ASP SER LEU MET          
SEQRES  21 A  371  GLY GLU SER THR GLY GLY ALA THR ILE PHE GLY VAL THR          
SEQRES  22 A  371  GLY GLY VAL MET GLU ALA ALA LEU ARG PHE ALA TYR GLU          
SEQRES  23 A  371  ALA VAL THR GLY LYS LYS PRO ASP SER TRP ASP PHE LYS          
SEQRES  24 A  371  ALA VAL ARG GLY LEU ASP GLY ILE LYS GLU ALA THR VAL          
SEQRES  25 A  371  ASN VAL GLY GLY THR ASP VAL LYS VAL ALA VAL VAL HIS          
SEQRES  26 A  371  GLY ALA LYS ARG PHE LYS GLN VAL CYS ASP ASP VAL LYS          
SEQRES  27 A  371  ALA GLY LYS SER PRO TYR HIS PHE ILE GLU TYR MET ALA          
SEQRES  28 A  371  CYS PRO GLY GLY CYS VAL CYS GLY GLY GLY GLN PRO VAL          
SEQRES  29 A  371  MET PRO GLY VAL LEU GLU ALA                                  
SEQRES   1 D   88  VAL LYS GLN ILE LYS ASP TYR MET LEU ASP ARG ILE ASN          
SEQRES   2 D   88  GLY VAL TYR GLY ALA ASP ALA LYS PHE PRO VAL ARG ALA          
SEQRES   3 D   88  SER GLN ASP ASN THR GLN VAL LYS ALA LEU TYR LYS SER          
SEQRES   4 D   88  TYR LEU GLU LYS PRO LEU GLY HIS LYS SER HIS ASP LEU          
SEQRES   5 D   88  LEU HIS THR HIS TRP PHE ASP LYS SER LYS GLY VAL LYS          
SEQRES   6 D   88  GLU LEU THR THR ALA GLY LYS LEU PRO ASN PRO ARG ALA          
SEQRES   7 D   88  SER GLU PHE GLU GLY PRO TYR PRO TYR GLU                      
SEQRES   1 E  107  ALA PRO LYS ALA PRO ALA ASP GLY LEU LYS MET GLU ALA          
SEQRES   2 E  107  THR LYS GLN PRO VAL VAL PHE ASN HIS SER THR HIS LYS          
SEQRES   3 E  107  SER VAL LYS CYS GLY ASP CYS HIS HIS PRO VAL ASN GLY          
SEQRES   4 E  107  LYS GLU ASP TYR ARG LYS CYS GLY THR ALA GLY CYS HIS          
SEQRES   5 E  107  ASP SER MET ASP LYS LYS ASP LYS SER ALA LYS GLY TYR          
SEQRES   6 E  107  TYR HIS VAL MET HIS ASP LYS ASN THR LYS PHE LYS SER          
SEQRES   7 E  107  CYS VAL GLY CYS HIS VAL GLU VAL ALA GLY ALA ASP ALA          
SEQRES   8 E  107  ALA LYS LYS LYS ASP LEU THR GLY CYS LYS LYS SER LYS          
SEQRES   9 E  107  CYS HIS GLU                                                  
HET    SF4  A   1       8                                                       
HET    SF4  A   2       8                                                       
HET    SF4  A   3       8                                                       
HET    PDT  A   4       5                                                       
HET    FE2  A   5       1                                                       
HET    FE2  A   6       1                                                       
HET    CYN  A   7       2                                                       
HET    CYN  A   8       2                                                       
HET    CMO  A   9       2                                                       
HET    CMO  A  10       2                                                       
HET    HEC  E 109      47                                                       
HET    HEC  E 110      47                                                       
HET    HEC  E 111      47                                                       
HET    HEC  E 112      47                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     PDT 1,3-PROPANEDITHIOL                                               
HETNAM     FE2 FE (II) ION                                                      
HETNAM     CYN CYANIDE ION                                                      
HETNAM     CMO CARBON MONOXIDE                                                  
HETNAM     HEC HEME C                                                           
FORMUL   4  SF4    3(FE4 S4)                                                    
FORMUL   7  PDT    C3 H8 S2                                                     
FORMUL   8  FE2    2(FE 2+)                                                     
FORMUL  10  CYN    2(C N 1-)                                                    
FORMUL  12  CMO    2(C O)                                                       
FORMUL  14  HEC    4(C34 H34 FE N4 O4)                                          
HELIX    1   1 THR A   40  CYS A   45  5                                   6    
HELIX    2   2 TRP A   87  ASP A   97  1                                  11    
HELIX    3   3 ALA A  107  GLY A  115  1                                   9    
HELIX    4   4 ASP A  116  GLY A  119  5                                   4    
HELIX    5   5 THR A  126  LEU A  137  1                                  12    
HELIX    6   6 ASP A  144  THR A  165  1                                  22    
HELIX    7   7 CYS A  179  TYR A  190  1                                  12    
HELIX    8   8 PRO A  191  PHE A  197  5                                   7    
HELIX    9   9 SER A  202  LYS A  212  1                                  11    
HELIX   10  10 THR A  213  MET A  219  1                                   7    
HELIX   11  11 ASP A  222  LYS A  224  5                                   3    
HELIX   12  12 ILE A  235  LEU A  242  1                                   8    
HELIX   13  13 THR A  259  ALA A  270  1                                  12    
HELIX   14  14 ASP A  273  LEU A  277  5                                   5    
HELIX   15  15 GLY A  300  TYR A  311  1                                  12    
HELIX   16  16 GLY A  352  LYS A  354  5                                   3    
HELIX   17  17 ARG A  355  ALA A  365  1                                  11    
HELIX   18  18 GLY A  381  GLY A  385  5                                   5    
HELIX   19  19 GLN D   38  ALA D   55  1                                  18    
HELIX   20  20 ASN D   65  SER D   74  1                                  10    
HELIX   21  21 LYS D   83  LEU D   88  1                                   6    
HELIX   22  22 LYS D   97  LEU D  102  1                                   6    
HELIX   23  23 ARG D  112  PHE D  116  5                                   5    
HELIX   24  24 GLY E   64  ASP E   71  1                                   8    
HELIX   25  25 SER E   78  GLY E   88  1                                  11    
HELIX   26  26 ALA E   91  GLY E   99  1                                   9    
SHEET    1  AA 2 VAL A  28  ILE A  30  0                                        
SHEET    2  AA 2 ILE A  81  GLU A  83 -1  O  TYR A  82   N  GLN A  29           
SHEET    1  AB 3 LYS A 101  MET A 105  0                                        
SHEET    2  AB 3 VAL A 226  ILE A 231  1  O  TYR A 227   N  ILE A 103           
SHEET    3  AB 3 ALA A 256  LEU A 258  1  O  ALA A 256   N  SER A 230           
SHEET    1  AC 4 GLN A 174  PHE A 175  0                                        
SHEET    2  AC 4 PHE A 372  TYR A 375  1  N  ILE A 373   O  GLN A 174           
SHEET    3  AC 4 ASP A 344  VAL A 350  1  O  ALA A 348   N  GLU A 374           
SHEET    4  AC 4 ILE A 333  ASN A 339 -1  O  LYS A 334   N  VAL A 349           
SHEET    1  EA 2 LEU E   9  MET E  11  0                                        
SHEET    2  EA 2 VAL E  18  PHE E  20 -1  O  VAL E  18   N  MET E  11           
LINK        FE1  SF4 A   1                 SG  CYS A  76     1555   1555  2.22  
LINK        FE2  SF4 A   1                 SG  CYS A  41     1555   1555  2.21  
LINK        FE3  SF4 A   1                 SG  CYS A  38     1555   1555  2.25  
LINK        FE4  SF4 A   1                 SG  CYS A  35     1555   1555  2.21  
LINK        FE1  SF4 A   2                 SG  CYS A  72     1555   1555  2.19  
LINK        FE2  SF4 A   2                 SG  CYS A  45     1555   1555  2.24  
LINK        FE3  SF4 A   2                 SG  CYS A  66     1555   1555  2.22  
LINK        FE4  SF4 A   2                 SG  CYS A  69     1555   1555  2.19  
LINK        FE1  SF4 A   3                 SG  CYS A 234     1555   1555  2.26  
LINK        FE2  SF4 A   3                 SG  CYS A 179     1555   1555  2.27  
LINK        FE3  SF4 A   3                 SG  CYS A 382     1555   1555  2.27  
LINK        FE4  SF4 A   3                 SG  CYS A 378     1555   1555  2.22  
LINK        FE   FE2 A   5                 C   CYN A   8     1555   1555  1.41  
LINK        FE   FE2 A   5                 S1  PDT A   4     1555   1555  2.29  
LINK        FE   FE2 A   5                 C   CYN A   7     1555   1555  2.16  
LINK        FE   FE2 A   5                 C   CMO A  10     1555   1555  1.42  
LINK        FE   FE2 A   5                 SD  MET A 232     1555   1555  1.78  
LINK        FE   FE2 A   5                 S2  PDT A   4     1555   1555  2.41  
LINK        FE   FE2 A   5                 C   CMO A   9     1555   1555  2.16  
LINK        FE   FE2 A   6                 C   CMO A   9     1555   1555  1.37  
LINK        FE   FE2 A   6                 C   CYN A   8     1555   1555  2.16  
LINK        FE   FE2 A   6                 S1  PDT A   4     1555   1555  2.47  
LINK        FE   FE2 A   6                 C   CMO A  10     1555   1555  2.19  
LINK        FE   FE2 A   6                 SD  MET A 232     1555   1555  1.78  
LINK        FE   FE2 A   6                 S2  PDT A   4     1555   1555  2.45  
LINK        FE   FE2 A   6                 C   CYN A   7     1555   1555  1.40  
LINK         C   CYN A   7                 C   CMO A   9     1555   1555  1.62  
LINK         C   CYN A   8                 C   CMO A  10     1555   1555  1.53  
LINK         SG  CYS E  30                 CAB HEC E 111     1555   1555  1.82  
LINK         SG  CYS E  33                 CAC HEC E 111     1555   1555  1.83  
LINK         SG  CYS E  46                 CAB HEC E 110     1555   1555  1.82  
LINK         SG  CYS E  51                 CAC HEC E 110     1555   1555  1.83  
LINK         SG  CYS E  79                 CAB HEC E 112     1555   1555  1.82  
LINK         SG  CYS E  82                 CAC HEC E 112     1555   1555  1.83  
LINK         SG  CYS E 100                 CAB HEC E 109     1555   1555  1.83  
LINK         SG  CYS E 105                 CAC HEC E 109     1555   1555  1.82  
LINK        FE   HEC E 109                 NE2 HIS E  70     1555   1555  2.21  
LINK        FE   HEC E 109                 NE2 HIS E 106     1555   1555  2.28  
LINK        FE   HEC E 110                 NE2 HIS E  35     1555   1555  2.17  
LINK        FE   HEC E 110                 NE2 HIS E  52     1555   1555  2.17  
LINK        FE   HEC E 111                 NE2 HIS E  22     1555   1555  2.24  
LINK        FE   HEC E 111                 NE2 HIS E  34     1555   1555  2.21  
LINK        FE   HEC E 112                 NE2 HIS E  25     1555   1555  2.20  
LINK        FE   HEC E 112                 NE2 HIS E  83     1555   1555  2.20  
CISPEP   1 LEU A  172    PRO A  173          0         1.72                     
CISPEP   2 LEU D  108    PRO D  109          0         5.83                     
SITE     1 AC1  7 PDT A   4  FE2 A   6  CYN A   7  CYN A   8                    
SITE     2 AC1  7 CMO A   9  CMO A  10  MET A 232                               
SITE     1 AC2  7 PDT A   4  FE2 A   5  CYN A   7  CYN A   8                    
SITE     2 AC2  7 CMO A   9  CMO A  10  MET A 232                               
SITE     1 AC3  9 PDT A   4  FE2 A   5  FE2 A   6  CYN A   8                    
SITE     2 AC3  9 CMO A   9  CMO A  10  PRO A 203  ILE A 204                    
SITE     3 AC3  9 MET A 232                                                     
SITE     1 AC4 10 PDT A   4  FE2 A   5  FE2 A   6  CYN A   7                    
SITE     2 AC4 10 CMO A   9  CMO A  10  ALA A 107  PRO A 108                    
SITE     3 AC4 10 ALA A 109  MET A 232                                          
SITE     1 AC5 12 LYS A  34  CYS A  35  ILE A  36  CYS A  38                    
SITE     2 AC5 12 ASP A  39  CYS A  41  SER A  42  HIS A  58                    
SITE     3 AC5 12 HIS A  75  CYS A  76  ILE A  81  HEC E 109                    
SITE     1 AC6  9 TYR A  44  CYS A  45  ILE A  50  ALA A  65                    
SITE     2 AC6  9 CYS A  66  ILE A  67  CYS A  69  GLY A  70                    
SITE     3 AC6  9 CYS A  72                                                     
SITE     1 AC7 10 CYS A  69  CYS A 179  PRO A 180  CYS A 234                    
SITE     2 AC7 10 MET A 376  ALA A 377  CYS A 378  CYS A 382                    
SITE     3 AC7 10 GLY A 385  GLY A 386                                          
SITE     1 AC8 11 FE2 A   5  FE2 A   6  CYN A   7  CYN A   8                    
SITE     2 AC8 11 CMO A   9  CMO A  10  PRO A 203  PHE A 296                    
SITE     3 AC8 11 GLY A 297  MET A 376  CYS A 382                               
SITE     1 AC9  9 PDT A   4  FE2 A   5  FE2 A   6  CYN A   7                    
SITE     2 AC9  9 CYN A   8  CMO A  10  MET A 232  PRO A 233                    
SITE     3 AC9  9 LYS A 237                                                     
SITE     1 BC1  9 PDT A   4  FE2 A   5  FE2 A   6  CYN A   7                    
SITE     2 BC1  9 CYN A   8  CMO A   9  PRO A 108  THR A 145                    
SITE     3 BC1  9 MET A 232                                                     
SITE     1 BC2 19 SF4 A   1  ILE A  36  CYS A  38  MET A  54                    
SITE     2 BC2 19 MET E  11  GLU E  12  ALA E  13  THR E  14                    
SITE     3 BC2 19 LYS E  15  GLN E  16  VAL E  18  TYR E  65                    
SITE     4 BC2 19 HIS E  70  CYS E  79  VAL E  80  LEU E  97                    
SITE     5 BC2 19 CYS E 100  CYS E 105  HIS E 106                               
SITE     1 BC3 17 HIS E  34  HIS E  35  PRO E  36  VAL E  37                    
SITE     2 BC3 17 ASN E  38  ASP E  42  CYS E  46  THR E  48                    
SITE     3 BC3 17 CYS E  51  HIS E  52  SER E  61  ALA E  62                    
SITE     4 BC3 17 HIS E  67  VAL E  68  THR E  74  LYS E  75                    
SITE     5 BC3 17 PHE E  76                                                     
SITE     1 BC4 15 PRO E   2  LYS E   3  ALA E   4  PHE E  20                    
SITE     2 BC4 15 HIS E  22  HIS E  25  LYS E  26  CYS E  30                    
SITE     3 BC4 15 CYS E  33  HIS E  34  ARG E  44  LYS E  45                    
SITE     4 BC4 15 CYS E  46  GLY E  47  HEC E 112                               
SITE     1 BC5 14 VAL E  19  PHE E  20  ASN E  21  SER E  23                    
SITE     2 BC5 14 THR E  24  HIS E  25  CYS E  33  MET E  69                    
SITE     3 BC5 14 CYS E  79  CYS E  82  HIS E  83  LYS E 104                    
SITE     4 BC5 14 CYS E 105  HEC E 111                                          
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system