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Entry: 3SFD
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HEADER    OXIDOREDUCTASE                          13-JUN-11   3SFD              
TITLE     CRYSTAL STRUCTURE OF PORCINE MITOCHONDRIAL RESPIRATORY COMPLEX II     
TITLE    2 BOUND WITH OXALOACETATE AND PENTACHLOROPHENOL                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, 
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: FLAVOPROTEIN SUBUNIT OF COMPLEX II, FP;                     
COMPND   6 EC: 1.3.5.1;                                                         
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT,  
COMPND   9 MITOCHONDRIAL;                                                       
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: IRON-SULF PROTEIN, IRON-SULFUR SUBUNIT OF COMPLEX II, IP;   
COMPND  12 EC: 1.3.5.1;                                                         
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT,           
COMPND  15 MITOCHONDRIAL;                                                       
COMPND  16 CHAIN: C;                                                            
COMPND  17 SYNONYM: CYTOCHROME B BINDING PROTEIN, CYBL, SUCCINATE-UBIQUINONE    
COMPND  18 OXIDOREDUCTASE CYTOCHROME B LARGE SUBUNIT;                           
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] CYTOCHROME B SMALL    
COMPND  21 SUBUNIT, MITOCHONDRIAL;                                              
COMPND  22 CHAIN: D;                                                            
COMPND  23 FRAGMENT: UNP RESIDUES 57-153;                                       
COMPND  24 SYNONYM: CYTOCHROME B BINDING PROTEIN, CYBS, CII-4, QPS3, SUCCINATE  
COMPND  25 DEHYDROGENASE COMPLEX SUBUNIT D, SUCCINATE-UBIQUINONE OXIDOREDUCTASE 
COMPND  26 CYTOCHROME B SMALL SUBUNIT, SUCCINATE-UBIQUINONE REDUCTASE MEMBRANE  
COMPND  27 ANCHOR SUBUNIT                                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIGS;                                               
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   7 ORGANISM_COMMON: PIGS;                                               
SOURCE   8 ORGANISM_TAXID: 9823;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  11 ORGANISM_COMMON: PIGS;                                               
SOURCE  12 ORGANISM_TAXID: 9823;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  15 ORGANISM_COMMON: PIGS;                                               
SOURCE  16 ORGANISM_TAXID: 9823                                                 
KEYWDS    SUCCINATE, UBIQUINONE OXIDOREDUCTASE, OXIDOREDUCTASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.J.ZHOU,Y.J.ZHAI,M.LIU,F.SUN                                         
REVDAT   1   07-SEP-11 3SFD    0                                                
JRNL        AUTH   Q.ZHOU,Y.ZHAI,J.LOU,M.LIU,X.PANG,F.SUN                       
JRNL        TITL   THIABENDAZOLE INHIBITS UBIQUINONE REDUCTION ACTIVITY OF      
JRNL        TITL 2 MITOCHONDRIAL RESPIRATORY COMPLEX II VIA A WATER MOLECULE    
JRNL        TITL 3 MEDIATED BINDING FEATURE.                                    
JRNL        REF    PROTEIN CELL                  V.   2   531 2011              
JRNL        REFN                   ISSN 1674-800X                               
JRNL        PMID   21822798                                                     
JRNL        DOI    10.1007/S13238-011-1079-1                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 75.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 38294                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2055                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 188                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 5.17                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 12                           
REMARK   3   BIN FREE R VALUE                    : 0.4390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8480                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 136                                     
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.29000                                             
REMARK   3    B22 (A**2) : -0.53000                                             
REMARK   3    B33 (A**2) : 0.83000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.398         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.272         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.057        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.860                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8820 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11970 ; 1.237 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 5.374 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;35.518 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;18.555 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;16.793 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1303 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6653 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5409 ; 0.361 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8673 ; 0.672 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3411 ; 0.644 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3280 ; 1.100 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3SFD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-JUN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066134.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50419                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 8.200                              
REMARK 200  R MERGE                    (I) : 0.13600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ZOY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5% N-NONYL-D-MALTOSIDE, 1.7MM N-       
REMARK 280  DECYL-D-MALTOSIDE, 25MM HEPES, 5% PEG 4000, 3% 1,6-HEXANEDIOL,      
REMARK 280  100MM NACL, 10MM CACL2, 200MM SUCROSE, PH 7.2, VAPOR DIFFUSION,     
REMARK 280  HANGING DROP, TEMPERATURE 290K                                      
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       35.15500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      146.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.68000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      146.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.15500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.68000            
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 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: 17290 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     LYS B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     ALA B   250                                                      
REMARK 465     SER B   251                                                      
REMARK 465     VAL B   252                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     ALA D    34                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  11      -36.38     63.29                                   
REMARK 500    ALA A  67      139.06   -171.39                                   
REMARK 500    MET A  72      -74.10    -76.48                                   
REMARK 500    GLU A  73     -167.67   -105.41                                   
REMARK 500    ALA A 151      -90.39     39.40                                   
REMARK 500    ASP A 170       33.84    -82.38                                   
REMARK 500    THR A 266      150.87    -47.89                                   
REMARK 500    GLU A 286      -22.79   -163.06                                   
REMARK 500    LYS A 293     -129.05     60.98                                   
REMARK 500    LEU A 295       51.11    -97.83                                   
REMARK 500    LYS A 319       73.18     64.91                                   
REMARK 500    ASP A 320       26.94   -158.38                                   
REMARK 500    LEU A 326      -14.62   -141.38                                   
REMARK 500    MET A 346      -76.24    -68.92                                   
REMARK 500    LYS A 355      -52.74   -125.63                                   
REMARK 500    HIS A 365      -59.07   -134.84                                   
REMARK 500    ASN A 374      168.63    -41.60                                   
REMARK 500    SER A 403       63.03     31.36                                   
REMARK 500    LYS A 438      101.57    -57.91                                   
REMARK 500    ALA A 481       50.62   -140.32                                   
REMARK 500    ALA A 482     -159.83    -88.75                                   
REMARK 500    LYS A 544       66.61   -115.10                                   
REMARK 500    GLN A 569      -55.66    174.11                                   
REMARK 500    GLN A 577       29.58    -76.67                                   
REMARK 500    ARG A 581       72.51    -68.87                                   
REMARK 500    ASN A 608      117.09   -165.92                                   
REMARK 500    THR B  24       93.88     43.03                                   
REMARK 500    ILE B  55      -69.37   -102.68                                   
REMARK 500    SER B  64      -70.32   -153.00                                   
REMARK 500    GLU B  67       -1.94   -143.02                                   
REMARK 500    CYS B  73      -82.87    -61.32                                   
REMARK 500    ALA B  74       87.34     39.68                                   
REMARK 500    HIS B 104       51.13     37.77                                   
REMARK 500    LYS B 109      135.70   -176.36                                   
REMARK 500    ASP B 110     -106.23     45.40                                   
REMARK 500    GLN B 144      115.93   -163.06                                   
REMARK 500    LYS B 151        5.23    -62.02                                   
REMARK 500    HIS C  29      -87.80   -131.58                                   
REMARK 500    THR C  85       51.06    -97.00                                   
REMARK 500    LEU C  86      -20.55   -160.27                                   
REMARK 500    LYS D  37       40.84   -107.24                                   
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                             HEM C1305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 101   NE2                                                    
REMARK 620 2 HEM C1305   NA   99.1                                              
REMARK 620 3 HEM C1305   NB   99.1  89.8                                        
REMARK 620 4 HEM C1305   NC   87.8 173.0  90.3                                  
REMARK 620 5 HEM C1305   ND   87.0  89.2 173.8  90.0                            
REMARK 620 6 HIS D  79   NE2 161.3  95.1  92.9  77.9  81.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  144.7                                              
REMARK 620 3 FES B 302   S2  104.0  93.4                                        
REMARK 620 4 CYS B  85   SG  106.5  96.4 108.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  70   SG                                                     
REMARK 620 2 FES B 302   S1  119.4                                              
REMARK 620 3 FES B 302   S2  105.5  93.3                                        
REMARK 620 4 CYS B  65   SG  119.0 100.7 116.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 215   SG                                                     
REMARK 620 2 F3S B 304   S1  104.5                                              
REMARK 620 3 F3S B 304   S3  128.5  96.4                                        
REMARK 620 4 F3S B 304   S4  105.3 130.0  95.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 221   SG                                                     
REMARK 620 2 F3S B 304   S1  106.0                                              
REMARK 620 3 F3S B 304   S2  107.4 131.0                                        
REMARK 620 4 F3S B 304   S3  118.2  96.5  98.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 164   SG                                                     
REMARK 620 2 SF4 B 303   S1  112.4                                              
REMARK 620 3 SF4 B 303   S2  121.3 103.3                                        
REMARK 620 4 SF4 B 303   S3  105.6 103.5 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 225   SG                                                     
REMARK 620 2 SF4 B 303   S1  108.4                                              
REMARK 620 3 SF4 B 303   S2  126.3 103.6                                        
REMARK 620 4 SF4 B 303   S4  107.0 105.0 104.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 168   SG                                                     
REMARK 620 2 F3S B 304   S2   95.2                                              
REMARK 620 3 F3S B 304   S3   97.4 100.4                                        
REMARK 620 4 F3S B 304   S4   85.9 162.2  97.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 161   SG                                                     
REMARK 620 2 SF4 B 303   S1  102.0                                              
REMARK 620 3 SF4 B 303   S3  115.6 103.9                                        
REMARK 620 4 SF4 B 303   S4  121.5 104.5 107.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 303   S2  116.1                                              
REMARK 620 3 SF4 B 303   S3   99.8 108.6                                        
REMARK 620 4 SF4 B 303   S4  121.4 103.4 106.7                                  
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 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OAA A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PCI D 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZOY   RELATED DB: PDB                                   
REMARK 900 STRUCTURE WITH SUCCINATE DEHYDROGENATION INHIBITOR                   
REMARK 900 (OXALOACETATE) AND UBIQUINONE REDUCTION INHIBITOR                    
REMARK 900 (PENTACHLOROPHENOL) BOUND                                            
REMARK 900 RELATED ID: 1ZP0   RELATED DB: PDB                                   
REMARK 900 DIFFERENT INHIBITORS AT THE Q-SITE                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE DISCREPANCIES ARE THE NATURAL VARIATIONS FROM DIFFERENT PIGS     
DBREF  3SFD A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3SFD B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3SFD C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3SFD D   34   136  UNP    A5GZW8   DHSD_PIG        57    159             
SEQADV 3SFD VAL B  252  UNP  Q007T0    ALA   280 SEE REMARK 999                 
SEQADV 3SFD ALA D  100  UNP  A5GZW8    VAL   123 SEE REMARK 999                 
SEQRES   1 A  622  SER SER ALA LYS VAL SER ASP ALA ILE SER THR GLN TYR          
SEQRES   2 A  622  PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY          
SEQRES   3 A  622  ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER          
SEQRES   4 A  622  GLU ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE          
SEQRES   5 A  622  PRO THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE          
SEQRES   6 A  622  ASN ALA ALA LEU GLY ASN MET GLU GLU ASP ASN TRP ARG          
SEQRES   7 A  622  TRP HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU          
SEQRES   8 A  622  GLY ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA          
SEQRES   9 A  622  PRO ALA SER VAL VAL GLU LEU GLU ASN TYR GLY MET PRO          
SEQRES  10 A  622  PHE SER ARG THR GLU ASP GLY LYS ILE TYR GLN ARG ALA          
SEQRES  11 A  622  PHE GLY GLY GLN SER LEU LYS PHE GLY LYS GLY GLY GLN          
SEQRES  12 A  622  ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS          
SEQRES  13 A  622  SER LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR          
SEQRES  14 A  622  ASP THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU          
SEQRES  15 A  622  LEU MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU          
SEQRES  16 A  622  CYS ILE GLU ASP GLY SER ILE HIS ARG ILE ARG ALA ARG          
SEQRES  17 A  622  ASN THR VAL VAL ALA THR GLY GLY TYR GLY ARG THR TYR          
SEQRES  18 A  622  PHE SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY          
SEQRES  19 A  622  THR ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP          
SEQRES  20 A  622  LEU GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY          
SEQRES  21 A  622  ALA GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY          
SEQRES  22 A  622  GLY ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU          
SEQRES  23 A  622  ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP          
SEQRES  24 A  622  VAL VAL SER ARG SER MET THR LEU GLU ILE ARG GLU GLY          
SEQRES  25 A  622  ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN          
SEQRES  26 A  622  LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA VAL ARG LEU          
SEQRES  27 A  622  PRO GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL          
SEQRES  28 A  622  ASP VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL          
SEQRES  29 A  622  HIS TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY          
SEQRES  30 A  622  GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP GLN VAL VAL          
SEQRES  31 A  622  PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA CYS ALA SER          
SEQRES  32 A  622  VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU          
SEQRES  33 A  622  ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU SER ILE          
SEQRES  34 A  622  ALA GLU SER CYS ARG PRO GLY ASP LYS VAL PRO SER ILE          
SEQRES  35 A  622  LYS PRO ASN ALA GLY GLU GLU SER VAL MET ASN LEU ASP          
SEQRES  36 A  622  LYS LEU ARG PHE ALA ASN GLY THR ILE ARG THR SER GLU          
SEQRES  37 A  622  LEU ARG LEU SER MET GLN LYS SER MET GLN SER HIS ALA          
SEQRES  38 A  622  ALA VAL PHE ARG VAL GLY SER VAL LEU GLN GLU GLY CYS          
SEQRES  39 A  622  GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU GLN HIS LEU          
SEQRES  40 A  622  LYS THR PHE ASP ARG GLY MET VAL TRP ASN THR ASP LEU          
SEQRES  41 A  622  VAL GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA          
SEQRES  42 A  622  LEU GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER          
SEQRES  43 A  622  ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS GLU ARG VAL          
SEQRES  44 A  622  ASP GLU TYR ASP TYR SER LYS PRO ILE GLN GLY GLN GLN          
SEQRES  45 A  622  LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS HIS THR LEU          
SEQRES  46 A  622  SER TYR VAL ASP VAL LYS THR GLY LYS VAL SER LEU GLU          
SEQRES  47 A  622  TYR ARG PRO VAL ILE ASP LYS THR LEU ASN GLU ALA ASP          
SEQRES  48 A  622  CYS ALA THR VAL PRO PRO ALA ILE ARG SER TYR                  
SEQRES   1 B  252  ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE LYS LYS          
SEQRES   2 B  252  PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR GLY ASP          
SEQRES   3 B  252  LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU ASN ASN          
SEQRES   4 B  252  CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS          
SEQRES   5 B  252  ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG SER CYS          
SEQRES   6 B  252  ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ASN          
SEQRES   7 B  252  GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE ASP THR          
SEQRES   8 B  252  ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU PRO HIS          
SEQRES   9 B  252  MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU SER ASN          
SEQRES  10 B  252  PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS          
SEQRES  11 B  252  LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN TYR LEU          
SEQRES  12 B  252  GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY LEU TYR          
SEQRES  13 B  252  GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO          
SEQRES  14 B  252  SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA          
SEQRES  15 B  252  VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG          
SEQRES  16 B  252  ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU GLN ASP          
SEQRES  17 B  252  PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS          
SEQRES  18 B  252  THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA          
SEQRES  19 B  252  ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU          
SEQRES  20 B  252  LYS LYS ALA SER VAL                                          
SEQRES   1 C  140  LEU GLY THR THR ALA LYS GLU GLU MET GLU ARG PHE TRP          
SEQRES   2 C  140  ASN LYS ASN LEU GLY SER ASN ARG PRO LEU SER PRO HIS          
SEQRES   3 C  140  ILE THR ILE TYR ARG TRP SER LEU PRO MET ALA MET SER          
SEQRES   4 C  140  ILE CYS HIS ARG GLY THR GLY ILE ALA LEU SER ALA GLY          
SEQRES   5 C  140  VAL SER LEU PHE GLY LEU SER ALA LEU LEU LEU PRO GLY          
SEQRES   6 C  140  ASN PHE GLU SER HIS LEU GLU LEU VAL LYS SER LEU CYS          
SEQRES   7 C  140  LEU GLY PRO THR LEU ILE TYR THR ALA LYS PHE GLY ILE          
SEQRES   8 C  140  VAL PHE PRO LEU MET TYR HIS THR TRP ASN GLY ILE ARG          
SEQRES   9 C  140  HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU THR ILE PRO          
SEQRES  10 C  140  GLN LEU THR GLN SER GLY VAL VAL VAL LEU ILE LEU THR          
SEQRES  11 C  140  VAL LEU SER SER VAL GLY LEU ALA ALA MET                      
SEQRES   1 D  103  ALA SER SER LYS ALA ALA SER LEU HIS TRP THR GLY GLU          
SEQRES   2 D  103  ARG VAL VAL SER VAL LEU LEU LEU GLY LEU LEU PRO ALA          
SEQRES   3 D  103  ALA TYR LEU ASN PRO CYS SER ALA MET ASP TYR SER LEU          
SEQRES   4 D  103  ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY ILE GLY          
SEQRES   5 D  103  GLN VAL VAL THR ASP TYR VAL ARG GLY ASP ALA LEU GLN          
SEQRES   6 D  103  LYS ALA ALA LYS ALA GLY LEU LEU ALA LEU SER ALA PHE          
SEQRES   7 D  103  THR PHE ALA GLY LEU CYS TYR PHE ASN TYR HIS ASP VAL          
SEQRES   8 D  103  GLY ILE CYS LYS ALA VAL ALA MET LEU TRP LYS LEU              
HET    FAD  A 700      53                                                       
HET    OAA  A 701       9                                                       
HET    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    HEM  C1305      43                                                       
HET    PCI  D   1      12                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     OAA OXALOACETATE ION                                                 
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     PCI PENTACHLOROPHENOL                                                
HETSYN     HEM HEME                                                             
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  OAA    C4 H3 O5 1-                                                  
FORMUL   7  FES    FE2 S2                                                       
FORMUL   8  SF4    FE4 S4                                                       
FORMUL   9  F3S    FE3 S4                                                       
FORMUL  10  HEM    C34 H32 FE N4 O4                                             
FORMUL  11  PCI    C6 H CL5 O                                                   
FORMUL  12  HOH   *130(H2 O)                                                    
HELIX    1   1 GLY A   28  ALA A   41  1                                  14    
HELIX    2   2 PHE A   52  ALA A   61  5                                  10    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  GLY A  115  1                                  23    
HELIX    5   5 ARG A  153  LEU A  167  1                                  15    
HELIX    6   6 TYR A  217  TYR A  221  5                                   5    
HELIX    7   7 GLY A  232  ALA A  241  1                                  10    
HELIX    8   8 GLU A  267  GLU A  272  1                                   6    
HELIX    9   9 ALA A  292  ALA A  296  5                                   5    
HELIX   10  10 SER A  297  GLY A  312  1                                  16    
HELIX   11  11 PRO A  330  LEU A  338  1                                   9    
HELIX   12  12 LEU A  338  PHE A  348  1                                  11    
HELIX   13  13 ASN A  413  CYS A  433  1                                  21    
HELIX   14  14 GLY A  447  PHE A  459  1                                  13    
HELIX   15  15 THR A  466  ALA A  481  1                                  16    
HELIX   16  16 VAL A  486  ASP A  503  1                                  18    
HELIX   17  17 ASN A  517  ARG A  543  1                                  27    
HELIX   18  18 PRO A  575  HIS A  579  5                                   5    
HELIX   19  19 ASN B   38  CYS B   40  5                                   3    
HELIX   20  20 MET B   43  ILE B   55  1                                  13    
HELIX   21  21 LEU B  115  ILE B  125  1                                  11    
HELIX   22  22 SER B  145  LYS B  151  1                                   7    
HELIX   23  23 CYS B  168  GLY B  175  1                                   8    
HELIX   24  24 GLY B  180  ILE B  192  1                                  13    
HELIX   25  25 PHE B  198  LYS B  205  1                                   8    
HELIX   26  26 MET B  219  CYS B  225  1                                   7    
HELIX   27  27 ASN B  230  TYR B  245  1                                  16    
HELIX   28  28 THR C    7  LEU C   20  1                                  14    
HELIX   29  29 SER C   36  LEU C   66  1                                  31    
HELIX   30  30 ASN C   69  SER C   79  1                                  11    
HELIX   31  31 GLY C   83  LEU C  113  1                                  31    
HELIX   32  32 THR C  118  ALA C  142  1                                  25    
HELIX   33  33 LYS D   37  ASN D   63  1                                  27    
HELIX   34  34 CYS D   65  VAL D   92  1                                  28    
HELIX   35  35 GLY D   94  ASP D  123  1                                  30    
HELIX   36  36 GLY D  125  LYS D  135  1                                  11    
SHEET    1   A 6 SER A 172  VAL A 175  0                                        
SHEET    2   A 6 THR A  45  THR A  49  1  N  CYS A  47   O  PHE A 174           
SHEET    3   A 6 VAL A  15  VAL A  25  1  N  VAL A  24   O  ALA A  46           
SHEET    4   A 6 ILE A 202  VAL A 212  1  O  VAL A 211   N  VAL A  25           
SHEET    5   A 6 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    6   A 6 TYR A 177  GLU A 185 -1  N  LEU A 183   O  ARG A 190           
SHEET    1   B 6 SER A 172  VAL A 175  0                                        
SHEET    2   B 6 THR A  45  THR A  49  1  N  CYS A  47   O  PHE A 174           
SHEET    3   B 6 VAL A  15  VAL A  25  1  N  VAL A  24   O  ALA A  46           
SHEET    4   B 6 ILE A 202  VAL A 212  1  O  VAL A 211   N  VAL A  25           
SHEET    5   B 6 GLN A 386  ALA A 395  1  O  TYR A 394   N  THR A 210           
SHEET    6   B 6 GLN A 378  VAL A 383 -1  N  VAL A 379   O  VAL A 390           
SHEET    1   C 3 ILE A  65  ASN A  66  0                                        
SHEET    2   C 3 GLN A 143  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    3   C 3 GLN A 128  SER A 135 -1  N  GLN A 134   O  ALA A 144           
SHEET    1   D 3 CYS A 245  GLN A 246  0                                        
SHEET    2   D 3 LYS A 582  SER A 586 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 LEU A 597  PRO A 601 -1  O  GLU A 598   N  LEU A 585           
SHEET    1   E 4 VAL A 251  ILE A 258  0                                        
SHEET    2   E 4 ILE A 358  ASN A 367 -1  O  TYR A 366   N  GLN A 252           
SHEET    3   E 4 VAL A 322  GLN A 325 -1  N  LEU A 324   O  ILE A 358           
SHEET    4   E 4 ILE A 275  ILE A 277 -1  N  ILE A 275   O  GLN A 325           
SHEET    1   F 2 ILE A 371  PRO A 372  0                                        
SHEET    2   F 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   G 2 ILE A 464  ARG A 465  0                                        
SHEET    2   G 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   H 5 HIS B  29  ASP B  36  0                                        
SHEET    2   H 5 ILE B  11  ARG B  18 -1  N  ILE B  16   O  GLN B  31           
SHEET    3   H 5 SER B  97  TYR B 100  1  O  SER B  97   N  ALA B  15           
SHEET    4   H 5 MET B  75  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   H 5 GLY B  80  THR B  82 -1  O  GLY B  80   N  ILE B  77           
SHEET    1   I 2 VAL B 107  LYS B 109  0                                        
SHEET    2   I 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  ILE B 108           
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  1.98  
LINK         SG  CYS B  73                FE1  FES B 302     1555   1555  2.04  
LINK         SG  CYS B  70                FE2  FES B 302     1555   1555  2.05  
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  2.12  
LINK         SG  CYS B 215                FE3  F3S B 304     1555   1555  2.18  
LINK         SG  CYS B 221                FE1  F3S B 304     1555   1555  2.25  
LINK         SG  CYS B  65                FE2  FES B 302     1555   1555  2.26  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.27  
LINK         SG  CYS B 164                FE4  SF4 B 303     1555   1555  2.28  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.38  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.39  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.41  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.53  
LINK         SG  CYS B  85                FE1  FES B 302     1555   1555  2.61  
SITE     1 AC1 41 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 41 ALA A  30  VAL A  48  THR A  49  LYS A  50                    
SITE     3 AC1 41 LEU A  51  SER A  56  HIS A  57  THR A  58                    
SITE     4 AC1 41 ALA A  60  ALA A  61  GLN A  62  GLY A  63                    
SITE     5 AC1 41 GLY A  64  TYR A 177  PHE A 178  ALA A 179                    
SITE     6 AC1 41 ALA A 213  THR A 214  GLY A 215  THR A 225                    
SITE     7 AC1 41 ASP A 233  LEU A 264  HIS A 365  TYR A 366                    
SITE     8 AC1 41 GLU A 398  ARG A 409  ALA A 412  ASN A 413                    
SITE     9 AC1 41 SER A 414  LEU A 415  LEU A 418  HOH A 623                    
SITE    10 AC1 41 HOH A 642  HOH A 650  HOH A 658  HOH A 671                    
SITE    11 AC1 41 OAA A 701                                                     
SITE     1 AC2 13 GLN A  62  GLY A  63  PHE A 131  HIS A 254                    
SITE     2 AC2 13 LEU A 264  THR A 266  GLU A 267  ARG A 298                    
SITE     3 AC2 13 HIS A 365  ARG A 409  GLY A 411  ALA A 412                    
SITE     4 AC2 13 FAD A 700                                                     
SITE     1 AC3  9 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC3  9 CYS B  70  GLY B  71  SER B  72  CYS B  73                    
SITE     3 AC3  9 CYS B  85                                                     
SITE     1 AC4  9 CYS B 158  ILE B 159  CYS B 161  ALA B 162                    
SITE     2 AC4  9 CYS B 163  CYS B 164  ALA B 182  CYS B 225                    
SITE     3 AC4  9 PRO B 226                                                     
SITE     1 AC5 10 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC5 10 HIS B 216  THR B 217  MET B 219  ASN B 220                    
SITE     3 AC5 10 CYS B 221  ILE B 235                                          
SITE     1 AC6 14 HIS C  45  ARG C  46  LEU C  52  SER C  53                    
SITE     2 AC6 14 HIS C 101  THR C 102  HIS C 108  HOH C 146                    
SITE     3 AC6 14 HOH C 152  LEU D  76  HIS D  79  GLY D  83                    
SITE     4 AC6 14 ILE D  84  GLN D  86                                          
SITE     1 AC7  8 PRO B 169  TRP B 173  ILE B 218  TRP C  35                    
SITE     2 AC7  8 MET C  39  SER C  42  ARG C  46  TYR D  91                    
CRYST1   70.310   83.360  293.100  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014223  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011996  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003412        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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