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Database: PDB
Entry: 2FJE
LinkDB: 2FJE
Original site: 2FJE 
HEADER    OXIDOREDUCTASE                          02-JAN-06   2FJE              
TITLE     ADENOSINE-5-PHOSPHOSULFATE REDUCTASE OXIDIZED STATE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENYLYLSULFATE REDUCTASE, SUBUNIT A;                      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: APRA;                                                       
COMPND   5 EC: 1.8.99.2;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ADENYLYLSULFATE REDUCTASE, SUBUNIT B;                      
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 SYNONYM: APRB;                                                       
COMPND  10 EC: 1.8.99.2                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   6 ORGANISM_TAXID: 2234                                                 
KEYWDS    APS REDUCTASE, SULFUR CYCLE, OXIDOREDUCTASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.SCHIFFER,G.FRITZ,P.M.KRONECK,U.ERMLER                               
REVDAT   5   14-FEB-24 2FJE    1       REMARK                                   
REVDAT   4   18-OCT-17 2FJE    1       REMARK                                   
REVDAT   3   31-MAR-09 2FJE    1       LINK   ATOM   CONECT                     
REVDAT   2   24-FEB-09 2FJE    1       VERSN                                    
REVDAT   1   28-MAR-06 2FJE    0                                                
JRNL        AUTH   A.SCHIFFER,G.FRITZ,P.M.KRONECK,U.ERMLER                      
JRNL        TITL   REACTION MECHANISM OF THE IRON-SULFUR FLAVOENZYME            
JRNL        TITL 2 ADENOSINE-5'-PHOSPHOSULFATE REDUCTASE BASED ON THE           
JRNL        TITL 3 STRUCTURAL CHARACTERIZATION OF DIFFERENT ENZYMATIC STATES    
JRNL        REF    BIOCHEMISTRY                  V.  45  2960 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   16503650                                                     
JRNL        DOI    10.1021/BI0521689                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 127075                         
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) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6400                            
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            : 12669                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 1111                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : -4.04200                                             
REMARK   3    B33 (A**2) : 4.11200                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 52.83                                                
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  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : COF.PAR                                        
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : CNS_TOPPAR:PROTEIN.TOP                         
REMARK   3  TOPOLOGY FILE  2   : CNS_TOPPAR:DNA-RNA.TOP                         
REMARK   3  TOPOLOGY FILE  3   : CNS_TOPPAR:WATER.TOP                           
REMARK   3  TOPOLOGY FILE  4   : CNS_TOPPAR:ION.TOP                             
REMARK   3  TOPOLOGY FILE  5   : COF.TOP                                        
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000035946.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 138616                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.03800                            
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 37.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6 % PEG 4000, 0.1 M NACL, 0.1 M NAAC     
REMARK 280  PH 4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       36.30000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       96.95000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       96.95000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.75000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HETEROTETRAMER PRESENT          
REMARK 300 IN THE ASYMMETRIC UNIT                                               
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 28120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -206.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D                            
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     MET C  2001                                                      
REMARK 465     MET B   701                                                      
REMARK 465     MET D  2701                                                      
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    ASP A 182   C     LYS A 183   N      -0.234                       
REMARK 500    ASP C2182   C     LYS C2183   N      -0.213                       
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  58     -134.94   -112.68                                   
REMARK 500    ASP A  78       86.01     71.26                                   
REMARK 500    GLU A 141      -70.04    -93.47                                   
REMARK 500    ALA A 213       46.68   -141.66                                   
REMARK 500    ALA A 229        2.71    -65.37                                   
REMARK 500    ASP A 268      -54.43     69.02                                   
REMARK 500    MET A 365      -28.65   -155.05                                   
REMARK 500    HIS A 398     -131.87    -93.70                                   
REMARK 500    PHE A 448     -157.29     55.44                                   
REMARK 500    ALA A 529       41.04   -108.96                                   
REMARK 500    ALA C2058     -129.36   -114.20                                   
REMARK 500    ASP C2078       85.04     73.37                                   
REMARK 500    GLU C2141      -70.87    -93.83                                   
REMARK 500    ALA C2229        1.52    -64.57                                   
REMARK 500    ASP C2268      -52.03     69.34                                   
REMARK 500    MET C2365      -28.94   -154.66                                   
REMARK 500    HIS C2398     -131.40    -96.74                                   
REMARK 500    PHE C2448     -158.49     56.85                                   
REMARK 500    ASN C2473       66.60   -155.62                                   
REMARK 500    ALA C2529       40.79   -108.95                                   
REMARK 500    CYS B 713       76.15     62.64                                   
REMARK 500    LYS B 714     -114.05    -14.32                                   
REMARK 500    LEU B 716      171.30    -56.88                                   
REMARK 500    GLU B 743       74.78   -154.71                                   
REMARK 500    GLU D2743       74.69   -160.05                                   
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 B1110  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 710   SG                                                     
REMARK 620 2 SF4 B1110   S2  116.4                                              
REMARK 620 3 SF4 B1110   S3  117.5 101.6                                        
REMARK 620 4 SF4 B1110   S4  116.7  99.9 102.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1110  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 721   SG                                                     
REMARK 620 2 SF4 B1110   S1  108.7                                              
REMARK 620 3 SF4 B1110   S2  119.8 101.9                                        
REMARK 620 4 SF4 B1110   S4  113.6 106.1 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1100  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 725   SG                                                     
REMARK 620 2 SF4 B1100   S2  111.7                                              
REMARK 620 3 SF4 B1100   S3  114.5 103.0                                        
REMARK 620 4 SF4 B1100   S4  119.2 104.8 101.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1100  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 747   SG                                                     
REMARK 620 2 SF4 B1100   S1   99.6                                              
REMARK 620 3 SF4 B1100   S3  118.8 104.8                                        
REMARK 620 4 SF4 B1100   S4  120.8 104.4 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1100  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 750   SG                                                     
REMARK 620 2 SF4 B1100   S1  119.5                                              
REMARK 620 3 SF4 B1100   S2  100.8 102.9                                        
REMARK 620 4 SF4 B1100   S4  119.7 103.9 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1100  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 753   SG                                                     
REMARK 620 2 SF4 B1100   S1  110.6                                              
REMARK 620 3 SF4 B1100   S2  111.6 104.7                                        
REMARK 620 4 SF4 B1100   S3  117.2 103.5 108.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B1110  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 757   SG                                                     
REMARK 620 2 SF4 B1110   S1  112.8                                              
REMARK 620 3 SF4 B1110   S2  116.2 100.9                                        
REMARK 620 4 SF4 B1110   S3  111.3 106.8 108.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3110  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2710   SG                                                     
REMARK 620 2 SF4 D3110   S2  117.4                                              
REMARK 620 3 SF4 D3110   S3  116.1 102.1                                        
REMARK 620 4 SF4 D3110   S4  115.7 100.8 102.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3110  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2713   SG                                                     
REMARK 620 2 SF4 D3110   S1   98.2                                              
REMARK 620 3 SF4 D3110   S3  121.8 107.4                                        
REMARK 620 4 SF4 D3110   S4  118.0 102.7 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3110  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2721   SG                                                     
REMARK 620 2 SF4 D3110   S1  108.0                                              
REMARK 620 3 SF4 D3110   S2  121.5 102.4                                        
REMARK 620 4 SF4 D3110   S4  111.4 106.2 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3100  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2725   SG                                                     
REMARK 620 2 SF4 D3100   S1  105.8                                              
REMARK 620 3 SF4 D3100   S2  115.7 103.0                                        
REMARK 620 4 SF4 D3100   S4  118.9 106.6 105.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3100  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2747   SG                                                     
REMARK 620 2 SF4 D3100   S2  121.9                                              
REMARK 620 3 SF4 D3100   S3  101.2 102.1                                        
REMARK 620 4 SF4 D3100   S4  121.0 103.7 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3100  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2750   SG                                                     
REMARK 620 2 SF4 D3100   S1   99.8                                              
REMARK 620 3 SF4 D3100   S3  121.8 104.1                                        
REMARK 620 4 SF4 D3100   S4  118.5 105.5 104.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3100  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2753   SG                                                     
REMARK 620 2 SF4 D3100   S1  109.4                                              
REMARK 620 3 SF4 D3100   S2  118.4 104.3                                        
REMARK 620 4 SF4 D3100   S3  111.5 104.6 107.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 D3110  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D2757   SG                                                     
REMARK 620 2 SF4 D3110   S1  112.4                                              
REMARK 620 3 SF4 D3110   S2  120.4 100.2                                        
REMARK 620 4 SF4 D3110   S3  110.5 104.9 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 3000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1100                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 3100                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 3110                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JNR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1JNZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FJA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2FJB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FJD   RELATED DB: PDB                                   
DBREF  2FJE A    1   643  UNP    O28603   O28603_ARCFU     1    643             
DBREF  2FJE C 2001  2643  UNP    O28603   O28603_ARCFU     1    643             
DBREF  2FJE B  701   850  UNP    O28604   O28604_ARCFU     1    150             
DBREF  2FJE D 2701  2850  UNP    O28604   O28604_ARCFU     1    150             
SEQRES   1 A  643  MET VAL TYR TYR PRO LYS LYS TYR GLU LEU TYR LYS ALA          
SEQRES   2 A  643  ASP GLU VAL PRO THR GLU VAL VAL GLU THR ASP ILE LEU          
SEQRES   3 A  643  ILE ILE GLY GLY GLY PHE SER GLY CYS GLY ALA ALA TYR          
SEQRES   4 A  643  GLU ALA ALA TYR TRP ALA LYS LEU GLY GLY LEU LYS VAL          
SEQRES   5 A  643  THR LEU VAL GLU LYS ALA ALA VAL GLU ARG SER GLY ALA          
SEQRES   6 A  643  VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR ILE ASP          
SEQRES   7 A  643  LEU THR GLY ARG SER GLU ARG GLN ASN THR LEU GLU ASP          
SEQRES   8 A  643  TYR VAL ARG TYR VAL THR LEU ASP MET MET GLY LEU ALA          
SEQRES   9 A  643  ARG GLU ASP LEU VAL ALA ASP TYR ALA ARG HIS VAL ASP          
SEQRES  10 A  643  GLY THR VAL HIS LEU PHE GLU LYS TRP GLY LEU PRO ILE          
SEQRES  11 A  643  TRP LYS THR PRO ASP GLY LYS TYR VAL ARG GLU GLY GLN          
SEQRES  12 A  643  TRP GLN ILE MET ILE HIS GLY GLU SER TYR LYS PRO ILE          
SEQRES  13 A  643  ILE ALA GLU ALA ALA LYS MET ALA VAL GLY GLU GLU ASN          
SEQRES  14 A  643  ILE TYR GLU ARG VAL PHE ILE PHE GLU LEU LEU LYS ASP          
SEQRES  15 A  643  LYS ASN ASP PRO ASN ALA VAL ALA GLY ALA VAL GLY PHE          
SEQRES  16 A  643  SER VAL ARG GLU PRO LYS PHE TYR VAL PHE LYS ALA LYS          
SEQRES  17 A  643  ALA VAL ILE LEU ALA THR GLY GLY ALA THR LEU LEU PHE          
SEQRES  18 A  643  ARG PRO ARG SER THR GLY GLU ALA ALA GLY ARG THR TRP          
SEQRES  19 A  643  TYR ALA ILE PHE ASP THR GLY SER GLY TYR TYR MET GLY          
SEQRES  20 A  643  LEU LYS ALA GLY ALA MET LEU THR GLN PHE GLU HIS ARG          
SEQRES  21 A  643  PHE ILE PRO PHE ARG PHE LYS ASP GLY TYR GLY PRO VAL          
SEQRES  22 A  643  GLY ALA TRP PHE LEU PHE PHE LYS CYS LYS ALA LYS ASN          
SEQRES  23 A  643  ALA TYR GLY GLU GLU TYR ILE LYS THR ARG ALA ALA GLU          
SEQRES  24 A  643  LEU GLU LYS TYR LYS PRO TYR GLY ALA ALA GLN PRO ILE          
SEQRES  25 A  643  PRO THR PRO LEU ARG ASN HIS GLN VAL MET LEU GLU ILE          
SEQRES  26 A  643  MET ASP GLY ASN GLN PRO ILE TYR MET HIS THR GLU GLU          
SEQRES  27 A  643  ALA LEU ALA GLU LEU ALA GLY GLY ASP LYS LYS LYS LEU          
SEQRES  28 A  643  LYS HIS ILE TYR GLU GLU ALA PHE GLU ASP PHE LEU ASP          
SEQRES  29 A  643  MET THR VAL SER GLN ALA LEU LEU TRP ALA CYS GLN ASN          
SEQRES  30 A  643  ILE ASP PRO GLN GLU GLN PRO SER GLU ALA ALA PRO ALA          
SEQRES  31 A  643  GLU PRO TYR ILE MET GLY SER HIS SER GLY GLU ALA GLY          
SEQRES  32 A  643  PHE TRP VAL CYS GLY PRO GLU ASP LEU MET PRO GLU GLU          
SEQRES  33 A  643  TYR ALA LYS LEU PHE PRO LEU LYS TYR ASN ARG MET THR          
SEQRES  34 A  643  THR VAL LYS GLY LEU PHE ALA ILE GLY ASP CYS ALA GLY          
SEQRES  35 A  643  ALA ASN PRO HIS LYS PHE SER SER GLY SER PHE THR GLU          
SEQRES  36 A  643  GLY ARG ILE ALA ALA LYS ALA ALA VAL ARG PHE ILE LEU          
SEQRES  37 A  643  GLU GLN LYS PRO ASN PRO GLU ILE ASP ASP ALA VAL VAL          
SEQRES  38 A  643  GLU GLU LEU LYS LYS LYS ALA TYR ALA PRO MET GLU ARG          
SEQRES  39 A  643  PHE MET GLN TYR LYS ASP LEU SER THR ALA ASP ASP VAL          
SEQRES  40 A  643  ASN PRO GLU TYR ILE LEU PRO TRP GLN GLY LEU VAL ARG          
SEQRES  41 A  643  LEU GLN LYS ILE MET ASP GLU TYR ALA ALA GLY ILE ALA          
SEQRES  42 A  643  THR ILE TYR LYS THR ASN GLU LYS MET LEU GLN ARG ALA          
SEQRES  43 A  643  LEU GLU LEU LEU ALA PHE LEU LYS GLU ASP LEU GLU LYS          
SEQRES  44 A  643  LEU ALA ALA ARG ASP LEU HIS GLU LEU MET ARG ALA TRP          
SEQRES  45 A  643  GLU LEU VAL HIS ARG VAL TRP THR ALA GLU ALA HIS VAL          
SEQRES  46 A  643  ARG HIS MET LEU PHE ARG LYS GLU THR ARG TRP PRO GLY          
SEQRES  47 A  643  TYR TYR TYR ARG THR ASP TYR PRO GLU LEU ASN ASP GLU          
SEQRES  48 A  643  GLU TRP LYS CYS PHE VAL CYS SER LYS TYR ASP ALA GLU          
SEQRES  49 A  643  LYS ASP GLU TRP THR PHE GLU LYS VAL PRO TYR VAL GLN          
SEQRES  50 A  643  VAL ILE GLU TRP SER PHE                                      
SEQRES   1 C  643  MET VAL TYR TYR PRO LYS LYS TYR GLU LEU TYR LYS ALA          
SEQRES   2 C  643  ASP GLU VAL PRO THR GLU VAL VAL GLU THR ASP ILE LEU          
SEQRES   3 C  643  ILE ILE GLY GLY GLY PHE SER GLY CYS GLY ALA ALA TYR          
SEQRES   4 C  643  GLU ALA ALA TYR TRP ALA LYS LEU GLY GLY LEU LYS VAL          
SEQRES   5 C  643  THR LEU VAL GLU LYS ALA ALA VAL GLU ARG SER GLY ALA          
SEQRES   6 C  643  VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR ILE ASP          
SEQRES   7 C  643  LEU THR GLY ARG SER GLU ARG GLN ASN THR LEU GLU ASP          
SEQRES   8 C  643  TYR VAL ARG TYR VAL THR LEU ASP MET MET GLY LEU ALA          
SEQRES   9 C  643  ARG GLU ASP LEU VAL ALA ASP TYR ALA ARG HIS VAL ASP          
SEQRES  10 C  643  GLY THR VAL HIS LEU PHE GLU LYS TRP GLY LEU PRO ILE          
SEQRES  11 C  643  TRP LYS THR PRO ASP GLY LYS TYR VAL ARG GLU GLY GLN          
SEQRES  12 C  643  TRP GLN ILE MET ILE HIS GLY GLU SER TYR LYS PRO ILE          
SEQRES  13 C  643  ILE ALA GLU ALA ALA LYS MET ALA VAL GLY GLU GLU ASN          
SEQRES  14 C  643  ILE TYR GLU ARG VAL PHE ILE PHE GLU LEU LEU LYS ASP          
SEQRES  15 C  643  LYS ASN ASP PRO ASN ALA VAL ALA GLY ALA VAL GLY PHE          
SEQRES  16 C  643  SER VAL ARG GLU PRO LYS PHE TYR VAL PHE LYS ALA LYS          
SEQRES  17 C  643  ALA VAL ILE LEU ALA THR GLY GLY ALA THR LEU LEU PHE          
SEQRES  18 C  643  ARG PRO ARG SER THR GLY GLU ALA ALA GLY ARG THR TRP          
SEQRES  19 C  643  TYR ALA ILE PHE ASP THR GLY SER GLY TYR TYR MET GLY          
SEQRES  20 C  643  LEU LYS ALA GLY ALA MET LEU THR GLN PHE GLU HIS ARG          
SEQRES  21 C  643  PHE ILE PRO PHE ARG PHE LYS ASP GLY TYR GLY PRO VAL          
SEQRES  22 C  643  GLY ALA TRP PHE LEU PHE PHE LYS CYS LYS ALA LYS ASN          
SEQRES  23 C  643  ALA TYR GLY GLU GLU TYR ILE LYS THR ARG ALA ALA GLU          
SEQRES  24 C  643  LEU GLU LYS TYR LYS PRO TYR GLY ALA ALA GLN PRO ILE          
SEQRES  25 C  643  PRO THR PRO LEU ARG ASN HIS GLN VAL MET LEU GLU ILE          
SEQRES  26 C  643  MET ASP GLY ASN GLN PRO ILE TYR MET HIS THR GLU GLU          
SEQRES  27 C  643  ALA LEU ALA GLU LEU ALA GLY GLY ASP LYS LYS LYS LEU          
SEQRES  28 C  643  LYS HIS ILE TYR GLU GLU ALA PHE GLU ASP PHE LEU ASP          
SEQRES  29 C  643  MET THR VAL SER GLN ALA LEU LEU TRP ALA CYS GLN ASN          
SEQRES  30 C  643  ILE ASP PRO GLN GLU GLN PRO SER GLU ALA ALA PRO ALA          
SEQRES  31 C  643  GLU PRO TYR ILE MET GLY SER HIS SER GLY GLU ALA GLY          
SEQRES  32 C  643  PHE TRP VAL CYS GLY PRO GLU ASP LEU MET PRO GLU GLU          
SEQRES  33 C  643  TYR ALA LYS LEU PHE PRO LEU LYS TYR ASN ARG MET THR          
SEQRES  34 C  643  THR VAL LYS GLY LEU PHE ALA ILE GLY ASP CYS ALA GLY          
SEQRES  35 C  643  ALA ASN PRO HIS LYS PHE SER SER GLY SER PHE THR GLU          
SEQRES  36 C  643  GLY ARG ILE ALA ALA LYS ALA ALA VAL ARG PHE ILE LEU          
SEQRES  37 C  643  GLU GLN LYS PRO ASN PRO GLU ILE ASP ASP ALA VAL VAL          
SEQRES  38 C  643  GLU GLU LEU LYS LYS LYS ALA TYR ALA PRO MET GLU ARG          
SEQRES  39 C  643  PHE MET GLN TYR LYS ASP LEU SER THR ALA ASP ASP VAL          
SEQRES  40 C  643  ASN PRO GLU TYR ILE LEU PRO TRP GLN GLY LEU VAL ARG          
SEQRES  41 C  643  LEU GLN LYS ILE MET ASP GLU TYR ALA ALA GLY ILE ALA          
SEQRES  42 C  643  THR ILE TYR LYS THR ASN GLU LYS MET LEU GLN ARG ALA          
SEQRES  43 C  643  LEU GLU LEU LEU ALA PHE LEU LYS GLU ASP LEU GLU LYS          
SEQRES  44 C  643  LEU ALA ALA ARG ASP LEU HIS GLU LEU MET ARG ALA TRP          
SEQRES  45 C  643  GLU LEU VAL HIS ARG VAL TRP THR ALA GLU ALA HIS VAL          
SEQRES  46 C  643  ARG HIS MET LEU PHE ARG LYS GLU THR ARG TRP PRO GLY          
SEQRES  47 C  643  TYR TYR TYR ARG THR ASP TYR PRO GLU LEU ASN ASP GLU          
SEQRES  48 C  643  GLU TRP LYS CYS PHE VAL CYS SER LYS TYR ASP ALA GLU          
SEQRES  49 C  643  LYS ASP GLU TRP THR PHE GLU LYS VAL PRO TYR VAL GLN          
SEQRES  50 C  643  VAL ILE GLU TRP SER PHE                                      
SEQRES   1 B  150  MET PRO SER PHE VAL ASN PRO GLU LYS CYS ASP GLY CYS          
SEQRES   2 B  150  LYS ALA LEU GLU ARG THR ALA CYS GLU TYR ILE CYS PRO          
SEQRES   3 B  150  ASN ASP LEU MET THR LEU ASP LYS GLU LYS MET LYS ALA          
SEQRES   4 B  150  TYR ASN ARG GLU PRO ASP MET CYS TRP GLU CYS TYR SER          
SEQRES   5 B  150  CYS VAL LYS MET CYS PRO GLN GLY ALA ILE ASP VAL ARG          
SEQRES   6 B  150  GLY TYR VAL ASP TYR SER PRO LEU GLY GLY ALA CYS VAL          
SEQRES   7 B  150  PRO MET ARG GLY THR SER ASP ILE MET TRP THR VAL LYS          
SEQRES   8 B  150  TYR ARG ASN GLY LYS VAL LEU ARG PHE LYS PHE ALA ILE          
SEQRES   9 B  150  ARG THR THR PRO TRP GLY SER ILE GLN PRO PHE GLU GLY          
SEQRES  10 B  150  PHE PRO GLU PRO THR GLU GLU ALA LEU LYS SER GLU LEU          
SEQRES  11 B  150  LEU ALA GLY GLU PRO GLU ILE ILE GLY THR SER GLU PHE          
SEQRES  12 B  150  PRO GLN VAL LYS LYS LYS ALA                                  
SEQRES   1 D  150  MET PRO SER PHE VAL ASN PRO GLU LYS CYS ASP GLY CYS          
SEQRES   2 D  150  LYS ALA LEU GLU ARG THR ALA CYS GLU TYR ILE CYS PRO          
SEQRES   3 D  150  ASN ASP LEU MET THR LEU ASP LYS GLU LYS MET LYS ALA          
SEQRES   4 D  150  TYR ASN ARG GLU PRO ASP MET CYS TRP GLU CYS TYR SER          
SEQRES   5 D  150  CYS VAL LYS MET CYS PRO GLN GLY ALA ILE ASP VAL ARG          
SEQRES   6 D  150  GLY TYR VAL ASP TYR SER PRO LEU GLY GLY ALA CYS VAL          
SEQRES   7 D  150  PRO MET ARG GLY THR SER ASP ILE MET TRP THR VAL LYS          
SEQRES   8 D  150  TYR ARG ASN GLY LYS VAL LEU ARG PHE LYS PHE ALA ILE          
SEQRES   9 D  150  ARG THR THR PRO TRP GLY SER ILE GLN PRO PHE GLU GLY          
SEQRES  10 D  150  PHE PRO GLU PRO THR GLU GLU ALA LEU LYS SER GLU LEU          
SEQRES  11 D  150  LEU ALA GLY GLU PRO GLU ILE ILE GLY THR SER GLU PHE          
SEQRES  12 D  150  PRO GLN VAL LYS LYS LYS ALA                                  
HET    FAD  A1000      53                                                       
HET    FAD  C3000      53                                                       
HET    SF4  B1100       8                                                       
HET    SF4  B1110       8                                                       
HET    SF4  D3100       8                                                       
HET    SF4  D3110       8                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
FORMUL   5  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   7  SF4    4(FE4 S4)                                                    
FORMUL  11  HOH   *1111(H2 O)                                                   
HELIX    1   1 LYS A   12  VAL A   16  5                                   5    
HELIX    2   2 GLY A   31  LYS A   46  1                                  16    
HELIX    3   3 THR A   88  MET A  100  1                                  13    
HELIX    4   4 ARG A  105  TRP A  126  1                                  22    
HELIX    5   5 SER A  152  GLY A  166  1                                  15    
HELIX    6   6 GLY A  227  ARG A  232  5                                   6    
HELIX    7   7 GLY A  241  GLY A  251  1                                  11    
HELIX    8   8 VAL A  273  PHE A  279  1                                   7    
HELIX    9   9 GLU A  291  ARG A  296  1                                   6    
HELIX   10  10 ALA A  297  LYS A  304  5                                   8    
HELIX   11  11 PRO A  305  ALA A  309  5                                   5    
HELIX   12  12 PRO A  313  ASP A  327  1                                  15    
HELIX   13  13 HIS A  335  GLY A  345  1                                  11    
HELIX   14  14 ASP A  347  ASP A  364  1                                  18    
HELIX   15  15 THR A  366  GLN A  376  1                                  11    
HELIX   16  16 PRO A  414  LYS A  419  1                                   6    
HELIX   17  17 GLY A  438  ALA A  441  5                                   4    
HELIX   18  18 LYS A  447  LYS A  471  1                                  25    
HELIX   19  19 ASP A  477  LYS A  499  1                                  23    
HELIX   20  20 ASP A  500  SER A  502  5                                   3    
HELIX   21  21 LEU A  513  ALA A  529  1                                  17    
HELIX   22  22 GLY A  531  ILE A  535  5                                   5    
HELIX   23  23 ASN A  539  GLU A  558  1                                  20    
HELIX   24  24 ASP A  564  ARG A  591  1                                  28    
HELIX   25  30 LYS C 2012  VAL C 2016  5                                   5    
HELIX   26  31 GLY C 2031  ALA C 2045  1                                  15    
HELIX   27  32 LYS C 2046  GLY C 2048  5                                   3    
HELIX   28  33 THR C 2088  MET C 2100  1                                  13    
HELIX   29  34 ARG C 2105  TRP C 2126  1                                  22    
HELIX   30  35 SER C 2152  GLY C 2166  1                                  15    
HELIX   31  36 GLY C 2227  ARG C 2232  5                                   6    
HELIX   32  37 GLY C 2241  GLY C 2251  1                                  11    
HELIX   33  38 VAL C 2273  PHE C 2279  1                                   7    
HELIX   34  39 GLU C 2291  ARG C 2296  1                                   6    
HELIX   35  40 ALA C 2297  GLU C 2301  5                                   5    
HELIX   36  41 PRO C 2305  ALA C 2309  5                                   5    
HELIX   37  42 PRO C 2313  GLY C 2328  1                                  16    
HELIX   38  43 HIS C 2335  GLY C 2345  1                                  11    
HELIX   39  44 ASP C 2347  ASP C 2364  1                                  18    
HELIX   40  45 THR C 2366  GLN C 2376  1                                  11    
HELIX   41  46 PRO C 2414  LYS C 2419  1                                   6    
HELIX   42  47 GLY C 2438  ALA C 2441  5                                   4    
HELIX   43  48 LYS C 2447  LYS C 2471  1                                  25    
HELIX   44  49 ASP C 2477  LYS C 2499  1                                  23    
HELIX   45  50 ASP C 2500  SER C 2502  5                                   3    
HELIX   46  51 LEU C 2513  ALA C 2529  1                                  17    
HELIX   47  52 GLY C 2531  ILE C 2535  5                                   5    
HELIX   48  53 ASN C 2539  GLU C 2558  1                                  20    
HELIX   49  54 ASP C 2564  ARG C 2591  1                                  28    
HELIX   50  25 THR B  719  CYS B  725  1                                   7    
HELIX   51  26 GLU B  743  CYS B  747  5                                   5    
HELIX   52  27 TYR B  751  CYS B  757  1                                   7    
HELIX   53  28 GLU B  824  SER B  828  5                                   5    
HELIX   54  29 PRO B  835  GLY B  839  5                                   5    
HELIX   55  55 THR D 2719  CYS D 2725  1                                   7    
HELIX   56  56 GLU D 2743  CYS D 2747  5                                   5    
HELIX   57  57 TYR D 2751  CYS D 2757  1                                   7    
HELIX   58  58 THR D 2822  LYS D 2827  1                                   6    
HELIX   59  59 PRO D 2835  GLY D 2839  5                                   5    
SHEET    1   A 4 THR A  18  GLU A  22  0                                        
SHEET    2   A 4 PHE A 202  LYS A 206  1  O  PHE A 202   N  GLU A  19           
SHEET    3   A 4 VAL A 189  SER A 196 -1  N  ALA A 192   O  PHE A 205           
SHEET    4   A 4 VAL A 174  LYS A 181 -1  N  LEU A 180   O  ALA A 190           
SHEET    1   B 5 ILE A 170  GLU A 172  0                                        
SHEET    2   B 5 VAL A  52  GLU A  56  1  N  GLU A  56   O  TYR A 171           
SHEET    3   B 5 ILE A  25  ILE A  28  1  N  ILE A  27   O  THR A  53           
SHEET    4   B 5 ALA A 209  LEU A 212  1  O  ILE A 211   N  LEU A  26           
SHEET    5   B 5 LEU A 434  ALA A 436  1  O  PHE A 435   N  VAL A 210           
SHEET    1   C 2 LEU A  70  ILE A  73  0                                        
SHEET    2   C 2 ILE A 146  GLY A 150 -1  O  ILE A 146   N  ILE A  73           
SHEET    1   D 4 GLY A 403  PHE A 404  0                                        
SHEET    2   D 4 LEU A 254  THR A 255 -1  N  THR A 255   O  GLY A 403           
SHEET    3   D 4 CYS A 615  ASP A 622 -1  O  SER A 619   N  LEU A 254           
SHEET    4   D 4 GLU A 627  PRO A 634 -1  O  VAL A 633   N  PHE A 616           
SHEET    1   E 4 PHE A 264  PHE A 266  0                                        
SHEET    2   E 4 SER A 385  PRO A 389 -1  O  ALA A 388   N  ARG A 265           
SHEET    3   E 4 ILE A 332  MET A 334 -1  N  MET A 334   O  SER A 385           
SHEET    4   E 4 ALA A 284  LYS A 285 -1  N  LYS A 285   O  TYR A 333           
SHEET    1   F 2 LYS A 537  THR A 538  0                                        
SHEET    2   F 2 TYR A 601  ARG A 602  1  O  TYR A 601   N  THR A 538           
SHEET    1   G 2 SER B 703  VAL B 705  0                                        
SHEET    2   G 2 ILE B 762  VAL B 764 -1  O  ASP B 763   N  PHE B 704           
SHEET    1   H 2 MET B 730  ASP B 733  0                                        
SHEET    2   H 2 LYS B 738  ASN B 741 -1  O  LYS B 738   N  ASP B 733           
SHEET    1   I 3 ALA B 776  ARG B 781  0                                        
SHEET    2   I 3 ASP B 785  LYS B 791 -1  O  THR B 789   N  VAL B 778           
SHEET    3   I 3 VAL B 797  ALA B 803 -1  O  LEU B 798   N  VAL B 790           
SHEET    1   J 4 THR C2018  GLU C2022  0                                        
SHEET    2   J 4 PHE C2202  LYS C2206  1  O  PHE C2202   N  GLU C2019           
SHEET    3   J 4 ASP C2185  SER C2196 -1  N  ALA C2192   O  PHE C2205           
SHEET    4   J 4 VAL C2174  ASP C2182 -1  N  LEU C2180   O  ALA C2190           
SHEET    1   K 5 ILE C2170  TYR C2171  0                                        
SHEET    2   K 5 VAL C2052  VAL C2055  1  N  LEU C2054   O  TYR C2171           
SHEET    3   K 5 ILE C2025  ILE C2028  1  N  ILE C2025   O  THR C2053           
SHEET    4   K 5 ALA C2209  LEU C2212  1  O  ILE C2211   N  LEU C2026           
SHEET    5   K 5 LEU C2434  ALA C2436  1  O  PHE C2435   N  VAL C2210           
SHEET    1   L 2 LEU C2070  ILE C2073  0                                        
SHEET    2   L 2 ILE C2146  GLY C2150 -1  O  ILE C2146   N  ILE C2073           
SHEET    1   M 4 GLY C2403  PHE C2404  0                                        
SHEET    2   M 4 LEU C2254  THR C2255 -1  N  THR C2255   O  GLY C2403           
SHEET    3   M 4 CYS C2615  ASP C2622 -1  O  SER C2619   N  LEU C2254           
SHEET    4   M 4 GLU C2627  PRO C2634 -1  O  VAL C2633   N  PHE C2616           
SHEET    1   N 4 PHE C2264  PHE C2266  0                                        
SHEET    2   N 4 SER C2385  PRO C2389 -1  O  ALA C2388   N  ARG C2265           
SHEET    3   N 4 ILE C2332  MET C2334 -1  N  MET C2334   O  SER C2385           
SHEET    4   N 4 ALA C2284  LYS C2285 -1  N  LYS C2285   O  TYR C2333           
SHEET    1   O 2 LYS C2537  THR C2538  0                                        
SHEET    2   O 2 TYR C2601  ARG C2602  1  O  TYR C2601   N  THR C2538           
SHEET    1   P 2 SER D2703  VAL D2705  0                                        
SHEET    2   P 2 ILE D2762  VAL D2764 -1  O  ASP D2763   N  PHE D2704           
SHEET    1   Q 2 MET D2730  ASP D2733  0                                        
SHEET    2   Q 2 LYS D2738  ASN D2741 -1  O  LYS D2738   N  ASP D2733           
SHEET    1   R 3 ALA D2776  ARG D2781  0                                        
SHEET    2   R 3 ASP D2785  LYS D2791 -1  O  LYS D2791   N  ALA D2776           
SHEET    3   R 3 VAL D2797  ALA D2803 -1  O  LEU D2798   N  VAL D2790           
LINK         SG  CYS B 710                FE1  SF4 B1110     1555   1555  2.50  
LINK         SG  CYS B 721                FE3  SF4 B1110     1555   1555  2.47  
LINK         SG  CYS B 725                FE1  SF4 B1100     1555   1555  2.40  
LINK         SG  CYS B 747                FE2  SF4 B1100     1555   1555  2.38  
LINK         SG  CYS B 750                FE3  SF4 B1100     1555   1555  2.38  
LINK         SG  CYS B 753                FE4  SF4 B1100     1555   1555  2.40  
LINK         SG  CYS B 757                FE4  SF4 B1110     1555   1555  2.48  
LINK         SG  CYS D2710                FE1  SF4 D3110     1555   1555  2.42  
LINK         SG  CYS D2713                FE2  SF4 D3110     1555   1555  2.44  
LINK         SG  CYS D2721                FE3  SF4 D3110     1555   1555  2.45  
LINK         SG  CYS D2725                FE3  SF4 D3100     1555   1555  2.41  
LINK         SG  CYS D2747                FE1  SF4 D3100     1555   1555  2.36  
LINK         SG  CYS D2750                FE2  SF4 D3100     1555   1555  2.35  
LINK         SG  CYS D2753                FE4  SF4 D3100     1555   1555  2.42  
LINK         SG  CYS D2757                FE4  SF4 D3110     1555   1555  2.37  
CISPEP   1 LYS A  304    PRO A  305          0        -0.09                     
CISPEP   2 GLN A  310    PRO A  311          0        -0.03                     
CISPEP   3 GLN A  330    PRO A  331          0         0.20                     
CISPEP   4 LYS C 2304    PRO C 2305          0         0.07                     
CISPEP   5 GLN C 2310    PRO C 2311          0         0.02                     
CISPEP   6 GLN C 2330    PRO C 2331          0         0.08                     
CISPEP   7 GLU B  834    PRO B  835          0        -0.01                     
CISPEP   8 GLU D 2834    PRO D 2835          0         0.27                     
SITE     1 AC1 37 GLY A  29  GLY A  30  GLY A  31  PHE A  32                    
SITE     2 AC1 37 SER A  33  GLU A  56  LYS A  57  SER A  63                    
SITE     3 AC1 37 GLY A  64  ALA A  65  VAL A  66  LEU A  70                    
SITE     4 AC1 37 ALA A  72  ILE A  73  ASN A  74  PHE A 175                    
SITE     5 AC1 37 ILE A 176  ALA A 213  THR A 214  GLY A 215                    
SITE     6 AC1 37 TRP A 234  TYR A 235  ALA A 236  ASP A 239                    
SITE     7 AC1 37 SER A 242  MET A 365  SER A 397  GLY A 438                    
SITE     8 AC1 37 ASP A 439  PHE A 448  SER A 449  SER A 452                    
SITE     9 AC1 37 HOH A5045  HOH A5121  HOH A5319  HOH A5324                    
SITE    10 AC1 37 HOH A5747                                                     
SITE     1 AC2 38 GLY C2029  GLY C2030  GLY C2031  PHE C2032                    
SITE     2 AC2 38 SER C2033  GLU C2056  LYS C2057  SER C2063                    
SITE     3 AC2 38 GLY C2064  ALA C2065  VAL C2066  LEU C2070                    
SITE     4 AC2 38 ALA C2072  ILE C2073  ASN C2074  PHE C2175                    
SITE     5 AC2 38 ILE C2176  ALA C2213  THR C2214  GLY C2215                    
SITE     6 AC2 38 TRP C2234  TYR C2235  ALA C2236  ASP C2239                    
SITE     7 AC2 38 SER C2242  MET C2365  SER C2397  GLY C2438                    
SITE     8 AC2 38 ASP C2439  PHE C2448  SER C2449  SER C2452                    
SITE     9 AC2 38 HOH C5008  HOH C5048  HOH C5059  HOH C5197                    
SITE    10 AC2 38 HOH C5323  HOH C5642                                          
SITE     1 AC3  8 SER B 703  CYS B 725  ASN B 741  CYS B 747                    
SITE     2 AC3  8 TRP B 748  CYS B 750  TYR B 751  CYS B 753                    
SITE     1 AC4  8 CYS B 710  ASP B 711  CYS B 713  THR B 719                    
SITE     2 AC4  8 ALA B 720  CYS B 721  CYS B 757  ILE B 762                    
SITE     1 AC5 10 SER D2703  CYS D2725  PRO D2726  ASN D2741                    
SITE     2 AC5 10 CYS D2747  TRP D2748  CYS D2750  TYR D2751                    
SITE     3 AC5 10 SER D2752  CYS D2753                                          
SITE     1 AC6  9 CYS D2710  ASP D2711  CYS D2713  THR D2719                    
SITE     2 AC6  9 ALA D2720  CYS D2721  ALA D2739  CYS D2757                    
SITE     3 AC6  9 ILE D2762                                                     
CRYST1   72.600  113.500  193.900  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013774  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008811  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005157        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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