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Database: PDB
Entry: 1ZOY
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Original site: 1ZOY 
HEADER    OXIDOREDUCTASE                          15-MAY-05   1ZOY              
TITLE     CRYSTAL STRUCTURE OF MITOCHONDRIAL RESPIRATORY COMPLEX II             
TITLE    2 FROM PORCINE HEART AT 2.4 ANGSTROMS                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAD-BINDING PROTEIN;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FLAVOPROTEIN;                                               
COMPND   5 EC: 1.3.5.1;                                                         
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: IRON-SULFUR PROTEIN;                                       
COMPND   8 CHAIN: B;                                                            
COMPND   9 EC: 1.3.5.1;                                                         
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: LARGE CYTOCHROME BINDING PROTEIN;                          
COMPND  12 CHAIN: C;                                                            
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: SMALL CYTOCHROME BINDING PROTEIN;                          
COMPND  15 CHAIN: D                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 TISSUE: PORCINE HEART;                                               
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   8 ORGANISM_COMMON: PIG;                                                
SOURCE   9 ORGANISM_TAXID: 9823;                                                
SOURCE  10 TISSUE: PORCINE HEART;                                               
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  13 ORGANISM_COMMON: PIG;                                                
SOURCE  14 ORGANISM_TAXID: 9823;                                                
SOURCE  15 TISSUE: PORCINE HEART;                                               
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  18 ORGANISM_COMMON: PIG;                                                
SOURCE  19 ORGANISM_TAXID: 9823;                                                
SOURCE  20 TISSUE: PORCINE HEART                                                
KEYWDS    SUCCINATE, UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL                   
KEYWDS   2 RESPIRATORY COMPLEX II, MEMBRANE PROTEIN STRUCTURE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.SUN,X.HUO,Y.ZHAI,A.WANG,J.XU,D.SU,M.BARTLAM,Z.RAO                   
REVDAT   2   24-FEB-09 1ZOY    1       VERSN                                    
REVDAT   1   12-JUL-05 1ZOY    0                                                
JRNL        AUTH   F.SUN,X.HUO,Y.ZHAI,A.WANG,J.XU,D.SU,M.BARTLAM,Z.RAO          
JRNL        TITL   CRYSTAL STRUCTURE OF MITOCHONDRIAL RESPIRATORY               
JRNL        TITL 2 MEMBRANE PROTEIN COMPLEX II                                  
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 121  1043 2005              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   15989954                                                     
JRNL        DOI    10.1016/J.CELL.2005.05.025                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 56559                          
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 SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5757                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 43.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 280                          
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            : 8480                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 213                                     
REMARK   3   SOLVENT ATOMS            : 331                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 69.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.34                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.47                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.41                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.48                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.018                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.81                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.82                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 4.83                            
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        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZOY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032971.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-04; 10-FEB-05               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 19-ID; 19-ID                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.74101; 1.0322                    
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111);         
REMARK 200                                   SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; ADSC             
REMARK 200                                   QUANTUM 315                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60175                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
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     (%) : 85.1                               
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.12500                            
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) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SAD; SINGLE WAVELENGTH                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD COMBINED WITH MR         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1NEK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: N-NONYL-D-MALTOSIDE, N-DECYL-D-          
REMARK 280  MALTOSIDE, HEPES, PEG 4000, 1,6-HEXANEDIOL, NACL, CACL2,            
REMARK 280  SUCROSE, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  290.0K                                                              
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       35.11900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      146.94800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.77850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      146.94800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.11900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.77850            
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: 19430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -155.0 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: 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    CYS B  73   CB    CYS B  73   SG     -0.107                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  11       21.52     37.98                                   
REMARK 500    ALA A  67      119.35   -173.41                                   
REMARK 500    ALA A  68       59.27    -69.62                                   
REMARK 500    LYS A 137       53.91     31.39                                   
REMARK 500    ALA A 151     -117.42     50.28                                   
REMARK 500    TYR A 217       44.03   -142.17                                   
REMARK 500    ARG A 219        1.14    -62.57                                   
REMARK 500    ASP A 247       37.93     38.56                                   
REMARK 500    PHE A 250       93.31    -65.05                                   
REMARK 500    ILE A 258      129.66    -39.14                                   
REMARK 500    THR A 266      144.92    -27.43                                   
REMARK 500    GLU A 286      -18.26    174.97                                   
REMARK 500    ALA A 289       87.80   -159.25                                   
REMARK 500    LYS A 293     -139.93     50.73                                   
REMARK 500    LEU A 295       64.07   -113.74                                   
REMARK 500    SER A 304      -70.34    -67.26                                   
REMARK 500    ARG A 313       39.49   -143.82                                   
REMARK 500    PRO A 317      -74.44    -16.25                                   
REMARK 500    HIS A 321     -162.96   -125.12                                   
REMARK 500    VAL A 322     -161.08   -129.92                                   
REMARK 500    LEU A 326      -18.20   -140.33                                   
REMARK 500    LYS A 355       11.64   -143.20                                   
REMARK 500    HIS A 365      -59.24   -142.60                                   
REMARK 500    SER A 403       72.19     62.85                                   
REMARK 500    ASN A 408      119.49   -166.84                                   
REMARK 500    PRO A 444       -3.71    -57.16                                   
REMARK 500    ALA A 482     -151.20    -87.22                                   
REMARK 500    LEU A 504       -9.94    -52.61                                   
REMARK 500    ARG A 512       16.76   -140.40                                   
REMARK 500    TRP A 516       63.58     36.26                                   
REMARK 500    LYS A 556       31.38    -80.53                                   
REMARK 500    TYR A 564        0.43    -67.18                                   
REMARK 500    GLN A 569      -58.38    166.10                                   
REMARK 500    ASN A 608      104.46   -167.25                                   
REMARK 500    SER A 621      141.66   -170.61                                   
REMARK 500    TRP B  19      113.80   -174.36                                   
REMARK 500    ASP B  22       32.14    -98.84                                   
REMARK 500    THR B  24      132.02    -31.22                                   
REMARK 500    SER B  64      -75.25   -166.44                                   
REMARK 500    ALA B  74      112.86    -16.55                                   
REMARK 500    LYS B 109      134.44   -178.40                                   
REMARK 500    ASP B 110     -119.37     42.30                                   
REMARK 500    TYR B 213        3.89    -61.32                                   
REMARK 500    HIS C  29      -91.96   -131.84                                   
REMARK 500    LEU C  80       38.98   -154.67                                   
REMARK 500    CYS C  81       14.85     46.86                                   
REMARK 500    LEU C  82      100.36    -25.75                                   
REMARK 500    THR C  85       47.73    -83.41                                   
REMARK 500    LEU C  86      -38.15   -160.26                                   
REMARK 500    ALA C 141        1.78    -67.93                                   
REMARK 500    LYS D  37       52.15   -108.56                                   
REMARK 500    ALA D  96      -74.17    -42.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EPH D 1306                                                       
REMARK 610     EPH D 1307                                                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C SSEQI                                                      
REMARK 615     UQ1 B 1201                                                       
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 HIS D  79   NE2 160.0                                              
REMARK 620 N                    1                                               
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 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1307                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ1 B 1201                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ZP0   RELATED DB: PDB                                   
REMARK 900 MITOCHONDRIAL RESPIRATORY COMPLEX II BOUND WITH 3-                   
REMARK 900 NITROPROPIONATE AND 2-THENOYLTRIFLUOROACETONE                        
DBREF  1ZOY A   17   557  UNP    Q0QF01   Q0QF01_PIG       1    541             
DBREF  1ZOY B    1   251  UNP    Q007T0   DHSB_PIG        29    279             
DBREF  1ZOY C    4   143  PDB    1ZOY     1ZOY             4    143             
DBREF  1ZOY D   34   136  UNP    A5GZW8   DHSD_PIG        57    159             
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    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    HEM  C1305      43                                                       
HET    EPH  D1306      44                                                       
HET    EPH  D1307      36                                                       
HET    UQ1  B1201      18                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-                
HETNAM   2 EPH  PHOSPHATIDYLETHANOLAMINE                                        
HETNAM     UQ1 UBIQUINONE-1                                                     
HETSYN     HEM HEME                                                             
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  FES    FE2 S2                                                       
FORMUL   7  SF4    FE4 S4                                                       
FORMUL   8  F3S    FE3 S4                                                       
FORMUL   9  HEM    C34 H32 FE N4 O4                                             
FORMUL  10  EPH    2(C39 H68 N O8 P)                                            
FORMUL  12  UQ1    C14 H18 O4                                                   
FORMUL  13  HOH   *331(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  GLY A  273  1                                   7    
HELIX    9   9 SER A  297  GLY A  312  1                                  16    
HELIX   10  10 GLU A  332  ARG A  337  1                                   6    
HELIX   11  11 LEU A  338  GLY A  350  1                                  13    
HELIX   12  12 ASN A  413  CYS A  433  1                                  21    
HELIX   13  13 GLY A  447  PHE A  459  1                                  13    
HELIX   14  14 THR A  466  ALA A  481  1                                  16    
HELIX   15  15 VAL A  486  LEU A  504  1                                  19    
HELIX   16  16 ASN A  517  ARG A  543  1                                  27    
HELIX   17  17 PRO A  575  HIS A  579  5                                   5    
HELIX   18  18 ASN B   38  CYS B   40  5                                   3    
HELIX   19  19 MET B   43  GLU B   54  1                                  12    
HELIX   20  20 LEU B  115  ILE B  125  1                                  11    
HELIX   21  21 SER B  145  LYS B  151  1                                   7    
HELIX   22  22 CYS B  164  SER B  167  5                                   4    
HELIX   23  23 CYS B  168  GLY B  175  1                                   8    
HELIX   24  24 LEU B  179  ILE B  192  1                                  14    
HELIX   25  25 PHE B  198  LYS B  205  1                                   8    
HELIX   26  26 CYS B  221  CYS B  225  5                                   5    
HELIX   27  27 ASN B  230  ALA B  243  1                                  14    
HELIX   28  28 THR C    7  GLY C   21  1                                  15    
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  141  1                                  24    
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  HIS D  122  1                                  29    
HELIX   36  36 GLY D  125  LYS D  135  1                                  11    
SHEET    1   A 4 VAL A  15  GLU A  19  0                                        
SHEET    2   A 4 ILE A 202  ARG A 206  1  O  ILE A 202   N  VAL A  16           
SHEET    3   A 4 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    4   A 4 TYR A 177  GLU A 185 -1  N  LEU A 183   O  GLY A 191           
SHEET    1   B 6 SER A 172  VAL A 175  0                                        
SHEET    2   B 6 THR A  45  THR A  49  1  N  THR A  45   O  SER A 172           
SHEET    3   B 6 ALA A  22  VAL A  25  1  N  VAL A  24   O  VAL A  48           
SHEET    4   B 6 ASN A 209  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 383   O  GLN A 386           
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 HIS A 583  VAL A 588 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 VAL A 595  ARG A 600 -1  O  GLU A 598   N  LEU A 585           
SHEET    1   E 2 VAL A 251  HIS A 254  0                                        
SHEET    2   E 2 THR A 363  ASN A 367 -1  O  TYR A 366   N  GLN A 252           
SHEET    1   F 2 ILE A 275  ILE A 277  0                                        
SHEET    2   F 2 TYR A 323  GLN A 325 -1  O  GLN A 325   N  ILE A 275           
SHEET    1   G 2 ILE A 371  PRO A 372  0                                        
SHEET    2   G 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   H 2 ILE A 464  ARG A 465  0                                        
SHEET    2   H 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   I 5 HIS B  29  ASP B  36  0                                        
SHEET    2   I 5 ILE B  11  ARG B  18 -1  N  PHE B  14   O  TYR B  33           
SHEET    3   I 5 VAL B  96  TYR B 100  1  O  SER B  97   N  ALA B  15           
SHEET    4   I 5 MET B  75  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   I 5 GLY B  80  THR B  82 -1  O  GLY B  80   N  ILE B  77           
SHEET    1   J 2 VAL B 107  LYS B 109  0                                        
SHEET    2   J 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  ILE B 108           
LINK         C8M FAD A 700                 NE2 HIS A  57     1555   1555  1.71  
LINK        FE2  FES B 302                 SG  CYS B  65     1555   1555  2.31  
LINK        FE2  FES B 302                 SG  CYS B  70     1555   1555  2.19  
LINK        FE1  FES B 302                 SG  CYS B  73     1555   1555  2.33  
LINK        FE1  FES B 302                 SG  CYS B  85     1555   1555  2.49  
LINK        FE2  SF4 B 303                 SG  CYS B 158     1555   1555  2.24  
LINK        FE4  SF4 B 303                 SG  CYS B 161     1555   1555  2.40  
LINK        FE1  SF4 B 303                 SG  CYS B 164     1555   1555  2.28  
LINK        FE3  SF4 B 303                 SG  CYS B 225     1555   1555  2.44  
LINK        FE4  F3S B 304                 SG  CYS B 168     1555   1555  2.45  
LINK        FE1  F3S B 304                 SG  CYS B 215     1555   1555  2.36  
LINK        FE3  F3S B 304                 SG  CYS B 221     1555   1555  2.19  
LINK        FE   HEM C1305                 NE2 HIS C 101     1555   1555  2.23  
LINK        FE   HEM C1305                 NE2 HIS D  79     1555   1555  2.18  
SITE     1 AC1 43 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 43 ALA A  30  VAL A  48  THR A  49  LYS A  50                    
SITE     3 AC1 43 LEU A  51  SER A  56  HIS A  57  THR A  58                    
SITE     4 AC1 43 ALA A  60  ALA A  61  GLN A  62  GLY A  63                    
SITE     5 AC1 43 GLY A  64  TYR A 177  PHE A 178  ALA A 179                    
SITE     6 AC1 43 ALA A 213  THR A 214  GLY A 215  THR A 225                    
SITE     7 AC1 43 ASP A 233  LEU A 264  HIS A 365  TYR A 366                    
SITE     8 AC1 43 GLY A 397  GLU A 398  ARG A 409  ALA A 412                    
SITE     9 AC1 43 ASN A 413  SER A 414  LEU A 415  LEU A 418                    
SITE    10 AC1 43 HOH A 703  HOH A 705  HOH A 769  HOH A 790                    
SITE    11 AC1 43 HOH A 796  HOH A 847  HOH A 886                               
SITE     1 AC2  8 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC2  8 CYS B  70  GLY B  71  CYS B  73  CYS B  85                    
SITE     1 AC3  6 CYS B 158  CYS B 161  ALA B 162  CYS B 164                    
SITE     2 AC3  6 CYS B 225  PRO B 226                                          
SITE     1 AC4  9 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC4  9 HIS B 216  MET B 219  ASN B 220  CYS B 221                    
SITE     3 AC4  9 HOH B1260                                                     
SITE     1 AC5 16 HOH B1211  HOH B1249  ARG C  46  GLY C  49                    
SITE     2 AC5 16 LEU C  52  SER C  53  HIS C 101  THR C 102                    
SITE     3 AC5 16 GLY C 105  HIS C 108  LEU D  53  LEU D  57                    
SITE     4 AC5 16 HIS D  79  GLY D  83  VAL D  87  HOH D1309                    
SITE     1 AC6  6 ALA D  60  TYR D  61  PRO D  64  LEU D  72                    
SITE     2 AC6  6 TRP D 134  HOH D1326                                          
SITE     1 AC7  7 LEU C 135  GLY C 139  ALA C 142  MET C 143                    
SITE     2 AC7  7 LYS D  99  ALA D 103  HOH D1324                               
SITE     1 AC8  6 TRP B 173  ILE B 218  HOH B1272  TRP C  35                    
SITE     2 AC8  6 ILE C  43  TYR D  91                                          
CRYST1   70.238   83.557  293.896  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      0.014237  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011968  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003403        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system