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Database: PDB
Entry: 4YTP
LinkDB: 4YTP
Original site: 4YTP 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 18-MAR-15   4YTP              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 N-[(4-TERT-BUTYLPHENYL)METHYL]-2-(TRIFLUOROMETHYL)BENZAMIDE          
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-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: SUCCINATE-UBIQUINONE OXIDOREDUCTASE CYTOCHROME B LARGE      
COMPND  18 SUBUNIT,CYBL;                                                        
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] CYTOCHROME B SMALL    
COMPND  21 SUBUNIT, MITOCHONDRIAL;                                              
COMPND  22 CHAIN: D;                                                            
COMPND  23 SYNONYM: CYBS,CII-4,QPS3,SUCCINATE DEHYDROGENASE COMPLEX SUBUNIT D,  
COMPND  24 SUCCINATE-UBIQUINONE OXIDOREDUCTASE CYTOCHROME B SMALL SUBUNIT,      
COMPND  25 SUCCINATE-UBIQUINONE REDUCTASE MEMBRANE ANCHOR SUBUNIT               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   7 ORGANISM_COMMON: PIG;                                                
SOURCE   8 ORGANISM_TAXID: 9823;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  11 ORGANISM_COMMON: PIG;                                                
SOURCE  12 ORGANISM_TAXID: 9823;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  15 ORGANISM_COMMON: PIG;                                                
SOURCE  16 ORGANISM_TAXID: 9823                                                 
KEYWDS    OXIDOREDUCTASE, SUCCINATE DEHYDROGENASE, COMPLEX II, INHIBITOR,       
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HARADA,T.SHIBA,D.SATO,A.YAMAMOTO,M.NAGAHAMA,A.YONE,D.K.INAOKA,      
AUTHOR   2 K.SAKAMOTO,M.INOUE,T.HONMA,K.KITA                                    
REVDAT   1   05-AUG-15 4YTP    0                                                
JRNL        AUTH   D.K.INAOKA,T.SHIBA,D.SATO,E.O.BALOGUN,T.SASAKI,M.NAGAHAMA,   
JRNL        AUTH 2 M.ODA,S.MATSUOKA,J.OHMORI,T.HONMA,M.INOUE,K.KITA,S.HARADA    
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE MOLECULAR DESIGN OF FLUTOLANIL  
JRNL        TITL 2 DERIVATIVES TARGETED FOR FUMARATE RESPIRATION OF PARASITE    
JRNL        TITL 3 MITOCHONDRIA                                                 
JRNL        REF    INT J MOL SCI                 V.  16 15287 2015              
JRNL        REFN                   ESSN 1422-0067                               
JRNL        PMID   26198225                                                     
JRNL        DOI    10.3390/IJMS160715287                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 80.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 25461                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1352                            
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 910                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 41.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 54                           
REMARK   3   BIN FREE R VALUE                    : 0.2900                       
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          : 139                                     
REMARK   3   SOLVENT ATOMS            : 22                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.55000                                              
REMARK   3    B22 (A**2) : -1.16000                                             
REMARK   3    B33 (A**2) : -1.39000                                             
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): 0.531         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.340         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.921        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8826 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8319 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11987 ; 1.227 ; 1.981       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 19128 ; 0.838 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 6.330 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;34.755 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;18.588 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;18.389 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1306 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9945 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2046 ; 0.002 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 4YTP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208092.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
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) : 0.98000                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31105                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51600                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 1ZOY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 5MM HEPES-NAOH, 7% PEG 4000, 200MM       
REMARK 280  SUCROSE, 100MM NACL, 10MM CACL2, 0.5MM EDTA, 3% 1,6-HAXANEDIOL,     
REMARK 280  0.5% N-DECYL-BETA-D-MALTOSIDE, PH 7.4, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 293K                                              
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       35.71450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.40850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.00400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.40850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.71450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.00400            
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: 16760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 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     MET A   -41                                                      
REMARK 465     SER A   -40                                                      
REMARK 465     GLY A   -39                                                      
REMARK 465     VAL A   -38                                                      
REMARK 465     ARG A   -37                                                      
REMARK 465     ALA A   -36                                                      
REMARK 465     VAL A   -35                                                      
REMARK 465     SER A   -34                                                      
REMARK 465     ARG A   -33                                                      
REMARK 465     LEU A   -32                                                      
REMARK 465     LEU A   -31                                                      
REMARK 465     ARG A   -30                                                      
REMARK 465     ALA A   -29                                                      
REMARK 465     ARG A   -28                                                      
REMARK 465     ARG A   -27                                                      
REMARK 465     LEU A   -26                                                      
REMARK 465     ALA A   -25                                                      
REMARK 465     LEU A   -24                                                      
REMARK 465     THR A   -23                                                      
REMARK 465     TRP A   -22                                                      
REMARK 465     ALA A   -21                                                      
REMARK 465     GLN A   -20                                                      
REMARK 465     PRO A   -19                                                      
REMARK 465     ALA A   -18                                                      
REMARK 465     ALA A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     PRO A   -15                                                      
REMARK 465     ILE A   -14                                                      
REMARK 465     GLY A   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     ARG A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     PHE A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     PHE A    -7                                                      
REMARK 465     THR A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     LYS A    -1                                                      
REMARK 465     ARG A     0                                                      
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     MET B   -27                                                      
REMARK 465     ALA B   -26                                                      
REMARK 465     ALA B   -25                                                      
REMARK 465     VAL B   -24                                                      
REMARK 465     VAL B   -23                                                      
REMARK 465     ALA B   -22                                                      
REMARK 465     VAL B   -21                                                      
REMARK 465     SER B   -20                                                      
REMARK 465     LEU B   -19                                                      
REMARK 465     LYS B   -18                                                      
REMARK 465     ARG B   -17                                                      
REMARK 465     TRP B   -16                                                      
REMARK 465     PHE B   -15                                                      
REMARK 465     PRO B   -14                                                      
REMARK 465     ALA B   -13                                                      
REMARK 465     THR B   -12                                                      
REMARK 465     THR B   -11                                                      
REMARK 465     LEU B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     ALA B    -7                                                      
REMARK 465     CYS B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     ALA B    -3                                                      
REMARK 465     CYS B    -2                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     GLY B     0                                                      
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     ALA B   252                                                      
REMARK 465     MET C   -25                                                      
REMARK 465     ALA C   -24                                                      
REMARK 465     ALA C   -23                                                      
REMARK 465     LEU C   -22                                                      
REMARK 465     LEU C   -21                                                      
REMARK 465     LEU C   -20                                                      
REMARK 465     ARG C   -19                                                      
REMARK 465     HIS C   -18                                                      
REMARK 465     VAL C   -17                                                      
REMARK 465     GLY C   -16                                                      
REMARK 465     ARG C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     CYS C   -13                                                      
REMARK 465     LEU C   -12                                                      
REMARK 465     ARG C   -11                                                      
REMARK 465     ALA C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     LEU C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     PRO C    -6                                                      
REMARK 465     GLN C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     CYS C    -3                                                      
REMARK 465     ILE C    -2                                                      
REMARK 465     ARG C    -1                                                      
REMARK 465     ASN C     0                                                      
REMARK 465     ALA C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     MET D   -22                                                      
REMARK 465     ALA D   -21                                                      
REMARK 465     THR D   -20                                                      
REMARK 465     LEU D   -19                                                      
REMARK 465     TRP D   -18                                                      
REMARK 465     ARG D   -17                                                      
REMARK 465     LEU D   -16                                                      
REMARK 465     SER D   -15                                                      
REMARK 465     VAL D   -14                                                      
REMARK 465     LEU D   -13                                                      
REMARK 465     CYS D   -12                                                      
REMARK 465     GLY D   -11                                                      
REMARK 465     ALA D   -10                                                      
REMARK 465     ARG D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     GLY D    -6                                                      
REMARK 465     ALA D    -5                                                      
REMARK 465     LEU D    -4                                                      
REMARK 465     VAL D    -3                                                      
REMARK 465     LEU D    -2                                                      
REMARK 465     ARG D    -1                                                      
REMARK 465     THR D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     VAL D     3                                                      
REMARK 465     ARG D     4                                                      
REMARK 465     PRO D     5                                                      
REMARK 465     ALA D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     VAL D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     PHE D    11                                                      
REMARK 465     LEU D    12                                                      
REMARK 465     GLN D    13                                                      
REMARK 465     ASP D    14                                                      
REMARK 465     ARG D    15                                                      
REMARK 465     HIS D    16                                                      
REMARK 465     THR D    17                                                      
REMARK 465     PRO D    18                                                      
REMARK 465     GLY D    19                                                      
REMARK 465     TRP D    20                                                      
REMARK 465     CYS D    21                                                      
REMARK 465     GLY D    22                                                      
REMARK 465     VAL D    23                                                      
REMARK 465     GLN D    24                                                      
REMARK 465     HIS D    25                                                      
REMARK 465     ILE D    26                                                      
REMARK 465     HIS D    27                                                      
REMARK 465     LEU D    28                                                      
REMARK 465     SER D    29                                                      
REMARK 465     PRO D    30                                                      
REMARK 465     SER D    31                                                      
REMARK 465     HIS D    32                                                      
REMARK 465     GLN D    33                                                      
REMARK 465     ALA D    34                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL D 100    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A  28   N   -  CA  -  C   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PRO A 567   C   -  N   -  CD  ANGL. DEV. = -12.9 DEGREES          
REMARK 500    PRO B 181   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  11       -0.35     60.95                                   
REMARK 500    ASN A  44       96.24    -63.80                                   
REMARK 500    GLN A  62      -41.70   -130.95                                   
REMARK 500    ALA A  67      119.67   -173.65                                   
REMARK 500    MET A  72      -70.34    -82.12                                   
REMARK 500    GLU A  73     -158.60   -101.10                                   
REMARK 500    LYS A 137       59.74     36.47                                   
REMARK 500    VAL A 150       76.81   -107.25                                   
REMARK 500    ALA A 151     -103.04     49.87                                   
REMARK 500    LEU A 180      -63.91    -99.94                                   
REMARK 500    ASP A 247       29.08     43.14                                   
REMARK 500    ASP A 294       14.27     85.91                                   
REMARK 500    ARG A 313       49.44   -107.24                                   
REMARK 500    LYS A 355       21.04   -144.93                                   
REMARK 500    HIS A 365      -48.33   -147.75                                   
REMARK 500    ASN A 374      171.53    -59.89                                   
REMARK 500    LYS A 438      109.03    -51.51                                   
REMARK 500    ALA A 482     -162.68    -71.13                                   
REMARK 500    CYS A 494      -71.11    -57.57                                   
REMARK 500    ASP A 503        2.94    -67.57                                   
REMARK 500    LYS A 544       71.67   -118.51                                   
REMARK 500    ILE A 568     -110.61    -92.91                                   
REMARK 500    GLN A 569     -116.75     65.18                                   
REMARK 500    GLU A 598     -161.39   -116.47                                   
REMARK 500    ASN A 608      110.94   -164.36                                   
REMARK 500    THR A 614      107.75    -51.33                                   
REMARK 500    SER A 621      134.71   -176.97                                   
REMARK 500    ARG B  10       91.40   -170.23                                   
REMARK 500    LYS B  23       79.26   -155.92                                   
REMARK 500    ILE B  55      -89.26    -86.39                                   
REMARK 500    SER B  64      -74.73   -158.51                                   
REMARK 500    ARG B  66       18.95     42.48                                   
REMARK 500    CYS B  70      -35.47   -132.33                                   
REMARK 500    CYS B  73       30.76    -96.54                                   
REMARK 500    LYS B 109      144.52   -173.88                                   
REMARK 500    ASP B 110     -111.60     39.39                                   
REMARK 500    GLU B 126       64.04     66.12                                   
REMARK 500    LYS B 139      -45.74   -141.25                                   
REMARK 500    ASN B 174       39.65   -146.54                                   
REMARK 500    HIS C  29      -86.46   -145.51                                   
REMARK 500    CYS C  81       57.45     29.87                                   
REMARK 500    LEU C 117       53.60   -105.64                                   
REMARK 500    ASP D 123     -168.65   -162.19                                   
REMARK 500    LYS D 135      -36.72    -38.38                                   
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                             FES B 301  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 FES B 301   S1  131.3                                              
REMARK 620 3 FES B 301   S2   93.5  94.4                                        
REMARK 620 4 CYS B  70   SG   91.1 130.4 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 301  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 301   S1   95.6                                              
REMARK 620 3 FES B 301   S2  119.5  93.6                                        
REMARK 620 4 CYS B  85   SG  114.1 128.2 105.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 302   S1  145.4                                              
REMARK 620 3 SF4 B 302   S3  120.4  87.2                                        
REMARK 620 4 SF4 B 302   S4  111.2  88.0  88.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 302  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 161   SG                                                     
REMARK 620 2 SF4 B 302   S1  143.5                                              
REMARK 620 3 SF4 B 302   S2  106.3  85.9                                        
REMARK 620 4 SF4 B 302   S4  126.5  88.1  85.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 164   SG                                                     
REMARK 620 2 SF4 B 302   S2  112.6                                              
REMARK 620 3 SF4 B 302   S3  133.6  87.1                                        
REMARK 620 4 SF4 B 302   S4  132.4  85.2  88.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 215   SG                                                     
REMARK 620 2 F3S B 303   S1  124.0                                              
REMARK 620 3 F3S B 303   S2   89.0 137.1                                        
REMARK 620 4 F3S B 303   S3  126.3  91.4  88.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 221   SG                                                     
REMARK 620 2 F3S B 303   S2  104.9                                              
REMARK 620 3 F3S B 303   S3  112.9  88.3                                        
REMARK 620 4 F3S B 303   S4  103.3 149.5  91.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 302  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 225   SG                                                     
REMARK 620 2 SF4 B 302   S1  117.5                                              
REMARK 620 3 SF4 B 302   S2  111.0  85.8                                        
REMARK 620 4 SF4 B 302   S3  149.4  87.4  86.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 301  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 101   NE2                                                    
REMARK 620 2 HEM C 301   NA   87.4                                              
REMARK 620 3 HEM C 301   NB   98.9  90.3                                        
REMARK 620 4 HEM C 301   NC   92.1 179.2  90.3                                  
REMARK 620 5 HEM C 301   ND   82.0  89.3 179.0  90.1                            
REMARK 620 6 HIS D  79   NE2 170.1  88.8  90.3  91.6  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 168   SG                                                     
REMARK 620 2 F3S B 303   S1  102.5                                              
REMARK 620 3 F3S B 303   S3  112.1  91.6                                        
REMARK 620 4 F3S B 303   S4  117.8 135.0  91.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FES B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue F3S B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue E23 C 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4YSX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YSY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YSZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YT0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YTM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YTN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4YXD   RELATED DB: PDB                                   
DBREF  4YTP A  -41   622  UNP    Q0QF01   SDHA_PIG         1    664             
DBREF  4YTP B  -27   252  UNP    Q007T0   SDHB_PIG         1    280             
DBREF  4YTP C  -25   143  UNP    D0VWV4   C560_PIG         1    169             
DBREF  4YTP D  -22   136  UNP    A5GZW8   DHSD_PIG         1    159             
SEQRES   1 A  664  MET SER GLY VAL ARG ALA VAL SER ARG LEU LEU ARG ALA          
SEQRES   2 A  664  ARG ARG LEU ALA LEU THR TRP ALA GLN PRO ALA ALA SER          
SEQRES   3 A  664  PRO ILE GLY ALA ARG SER PHE HIS PHE THR VAL ASP GLY          
SEQRES   4 A  664  ASN LYS ARG SER SER ALA LYS VAL SER ASP ALA ILE SER          
SEQRES   5 A  664  THR GLN TYR PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL          
SEQRES   6 A  664  VAL VAL GLY ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE          
SEQRES   7 A  664  GLY LEU SER GLU ALA GLY PHE ASN THR ALA CYS VAL THR          
SEQRES   8 A  664  LYS LEU PHE PRO THR ARG SER HIS THR VAL ALA ALA GLN          
SEQRES   9 A  664  GLY GLY ILE ASN ALA ALA LEU GLY ASN MET GLU GLU ASP          
SEQRES  10 A  664  ASN TRP ARG TRP HIS PHE TYR ASP THR VAL LYS GLY SER          
SEQRES  11 A  664  ASP TRP LEU GLY ASP GLN ASP ALA ILE HIS TYR MET THR          
SEQRES  12 A  664  GLU GLN ALA PRO ALA SER VAL VAL GLU LEU GLU ASN TYR          
SEQRES  13 A  664  GLY MET PRO PHE SER ARG THR GLU ASP GLY LYS ILE TYR          
SEQRES  14 A  664  GLN ARG ALA PHE GLY GLY GLN SER LEU LYS PHE GLY LYS          
SEQRES  15 A  664  GLY GLY GLN ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG          
SEQRES  16 A  664  THR GLY HIS SER LEU LEU HIS THR LEU TYR GLY ARG SER          
SEQRES  17 A  664  LEU ARG TYR ASP THR SER TYR PHE VAL GLU TYR PHE ALA          
SEQRES  18 A  664  LEU ASP LEU LEU MET GLU ASN GLY GLU CYS ARG GLY VAL          
SEQRES  19 A  664  ILE ALA LEU CYS ILE GLU ASP GLY SER ILE HIS ARG ILE          
SEQRES  20 A  664  ARG ALA ARG ASN THR VAL VAL ALA THR GLY GLY TYR GLY          
SEQRES  21 A  664  ARG THR TYR PHE SER CYS THR SER ALA HIS THR SER THR          
SEQRES  22 A  664  GLY ASP GLY THR ALA MET VAL THR ARG ALA GLY LEU PRO          
SEQRES  23 A  664  CYS GLN ASP LEU GLU PHE VAL GLN PHE HIS PRO THR GLY          
SEQRES  24 A  664  ILE TYR GLY ALA GLY CYS LEU ILE THR GLU GLY CYS ARG          
SEQRES  25 A  664  GLY GLU GLY GLY ILE LEU ILE ASN SER GLN GLY GLU ARG          
SEQRES  26 A  664  PHE MET GLU ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA          
SEQRES  27 A  664  SER ARG ASP VAL VAL SER ARG SER MET THR LEU GLU ILE          
SEQRES  28 A  664  ARG GLU GLY ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL          
SEQRES  29 A  664  TYR LEU GLN LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA          
SEQRES  30 A  664  VAL ARG LEU PRO GLY ILE SER GLU THR ALA MET ILE PHE          
SEQRES  31 A  664  ALA GLY VAL ASP VAL THR LYS GLU PRO ILE PRO VAL LEU          
SEQRES  32 A  664  PRO THR VAL HIS TYR ASN MET GLY GLY ILE PRO THR ASN          
SEQRES  33 A  664  TYR LYS GLY GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP          
SEQRES  34 A  664  GLN VAL VAL PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA          
SEQRES  35 A  664  CYS ALA SER VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN          
SEQRES  36 A  664  SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA          
SEQRES  37 A  664  LEU SER ILE ALA GLU SER CYS ARG PRO GLY ASP LYS VAL          
SEQRES  38 A  664  PRO SER ILE LYS PRO ASN ALA GLY GLU GLU SER VAL MET          
SEQRES  39 A  664  ASN LEU ASP LYS LEU ARG PHE ALA ASN GLY THR ILE ARG          
SEQRES  40 A  664  THR SER GLU LEU ARG LEU SER MET GLN LYS SER MET GLN          
SEQRES  41 A  664  SER HIS ALA ALA VAL PHE ARG VAL GLY SER VAL LEU GLN          
SEQRES  42 A  664  GLU GLY CYS GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU          
SEQRES  43 A  664  GLN HIS LEU LYS THR PHE ASP ARG GLY MET VAL TRP ASN          
SEQRES  44 A  664  THR ASP LEU VAL GLU THR LEU GLU LEU GLN ASN LEU MET          
SEQRES  45 A  664  LEU CYS ALA LEU GLN THR ILE TYR GLY ALA GLU ALA ARG          
SEQRES  46 A  664  LYS GLU SER ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS          
SEQRES  47 A  664  GLU ARG VAL ASP GLU TYR ASP TYR SER LYS PRO ILE GLN          
SEQRES  48 A  664  GLY GLN GLN LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS          
SEQRES  49 A  664  HIS THR LEU SER TYR VAL ASP VAL LYS THR GLY LYS VAL          
SEQRES  50 A  664  SER LEU GLU TYR ARG PRO VAL ILE ASP LYS THR LEU ASN          
SEQRES  51 A  664  GLU ALA ASP CYS ALA THR VAL PRO PRO ALA ILE ARG SER          
SEQRES  52 A  664  TYR                                                          
SEQRES   1 B  280  MET ALA ALA VAL VAL ALA VAL SER LEU LYS ARG TRP PHE          
SEQRES   2 B  280  PRO ALA THR THR LEU GLY GLY ALA CYS LEU GLN ALA CYS          
SEQRES   3 B  280  ARG GLY ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE          
SEQRES   4 B  280  LYS LYS PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR          
SEQRES   5 B  280  GLY ASP LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU          
SEQRES   6 B  280  ASN ASN CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS          
SEQRES   7 B  280  ILE LYS ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG          
SEQRES   8 B  280  SER CYS ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN          
SEQRES   9 B  280  ILE ASN GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE          
SEQRES  10 B  280  ASP THR ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU          
SEQRES  11 B  280  PRO HIS MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU          
SEQRES  12 B  280  SER ASN PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR          
SEQRES  13 B  280  LEU LYS LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN          
SEQRES  14 B  280  TYR LEU GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY          
SEQRES  15 B  280  LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER          
SEQRES  16 B  280  CYS PRO SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY          
SEQRES  17 B  280  PRO ALA VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP          
SEQRES  18 B  280  SER ARG ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU          
SEQRES  19 B  280  GLN ASP PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET          
SEQRES  20 B  280  ASN CYS THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY          
SEQRES  21 B  280  LYS ALA ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR          
SEQRES  22 B  280  LYS GLU LYS LYS ALA SER ALA                                  
SEQRES   1 C  169  MET ALA ALA LEU LEU LEU ARG HIS VAL GLY ARG HIS CYS          
SEQRES   2 C  169  LEU ARG ALA HIS LEU SER PRO GLN LEU CYS ILE ARG ASN          
SEQRES   3 C  169  ALA VAL PRO LEU GLY THR THR ALA LYS GLU GLU MET GLU          
SEQRES   4 C  169  ARG PHE TRP ASN LYS ASN LEU GLY SER ASN ARG PRO LEU          
SEQRES   5 C  169  SER PRO HIS ILE THR ILE TYR ARG TRP SER LEU PRO MET          
SEQRES   6 C  169  ALA MET SER ILE CYS HIS ARG GLY THR GLY ILE ALA LEU          
SEQRES   7 C  169  SER ALA GLY VAL SER LEU PHE GLY LEU SER ALA LEU LEU          
SEQRES   8 C  169  LEU PRO GLY ASN PHE GLU SER HIS LEU GLU LEU VAL LYS          
SEQRES   9 C  169  SER LEU CYS LEU GLY PRO THR LEU ILE TYR THR ALA LYS          
SEQRES  10 C  169  PHE GLY ILE VAL PHE PRO LEU MET TYR HIS THR TRP ASN          
SEQRES  11 C  169  GLY ILE ARG HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU          
SEQRES  12 C  169  THR ILE PRO GLN LEU THR GLN SER GLY VAL VAL VAL LEU          
SEQRES  13 C  169  ILE LEU THR VAL LEU SER SER VAL GLY LEU ALA ALA MET          
SEQRES   1 D  159  MET ALA THR LEU TRP ARG LEU SER VAL LEU CYS GLY ALA          
SEQRES   2 D  159  ARG GLY GLY GLY ALA LEU VAL LEU ARG THR SER VAL VAL          
SEQRES   3 D  159  ARG PRO ALA HIS VAL SER ALA PHE LEU GLN ASP ARG HIS          
SEQRES   4 D  159  THR PRO GLY TRP CYS GLY VAL GLN HIS ILE HIS LEU SER          
SEQRES   5 D  159  PRO SER HIS GLN ALA SER SER LYS ALA ALA SER LEU HIS          
SEQRES   6 D  159  TRP THR GLY GLU ARG VAL VAL SER VAL LEU LEU LEU GLY          
SEQRES   7 D  159  LEU LEU PRO ALA ALA TYR LEU ASN PRO CYS SER ALA MET          
SEQRES   8 D  159  ASP TYR SER LEU ALA ALA ALA LEU THR LEU HIS GLY HIS          
SEQRES   9 D  159  TRP GLY ILE GLY GLN VAL VAL THR ASP TYR VAL ARG GLY          
SEQRES  10 D  159  ASP ALA LEU GLN LYS VAL ALA LYS ALA GLY LEU LEU ALA          
SEQRES  11 D  159  LEU SER ALA PHE THR PHE ALA GLY LEU CYS TYR PHE ASN          
SEQRES  12 D  159  TYR HIS ASP VAL GLY ILE CYS LYS ALA VAL ALA MET LEU          
SEQRES  13 D  159  TRP LYS LEU                                                  
HET    FAD  A 701      53                                                       
HET    FES  B 301       4                                                       
HET    SF4  B 302       8                                                       
HET    F3S  B 303       7                                                       
HET    HEM  C 301      43                                                       
HET    E23  C 302      24                                                       
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     E23 N-(4-TERT-BUTYLBENZYL)-2-(TRIFLUOROMETHYL)BENZAMIDE              
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  E23    C19 H20 F3 N O                                               
FORMUL  11  HOH   *22(H2 O)                                                     
HELIX    1 AA1 GLY A   28  ALA A   41  1                                  14    
HELIX    2 AA2 PHE A   52  SER A   56  5                                   5    
HELIX    3 AA3 HIS A   57  ALA A   61  5                                   5    
HELIX    4 AA4 ASN A   76  SER A   88  1                                  13    
HELIX    5 AA5 ASP A   93  ASN A  113  1                                  21    
HELIX    6 AA6 LYS A  137  LYS A  140  5                                   4    
HELIX    7 AA7 ARG A  153  LEU A  167  1                                  15    
HELIX    8 AA8 TYR A  217  TYR A  221  5                                   5    
HELIX    9 AA9 GLY A  232  ARG A  240  1                                   9    
HELIX   10 AB1 GLU A  267  GLU A  272  1                                   6    
HELIX   11 AB2 PHE A  284  ALA A  289  1                                   6    
HELIX   12 AB3 SER A  297  GLU A  311  1                                  15    
HELIX   13 AB4 PRO A  330  LEU A  338  1                                   9    
HELIX   14 AB5 LEU A  338  GLY A  350  1                                  13    
HELIX   15 AB6 ASN A  413  CYS A  433  1                                  21    
HELIX   16 AB7 GLY A  447  PHE A  459  1                                  13    
HELIX   17 AB8 THR A  466  ALA A  481  1                                  16    
HELIX   18 AB9 VAL A  486  ASP A  503  1                                  18    
HELIX   19 AC1 ASN A  517  ARG A  543  1                                  27    
HELIX   20 AC2 PRO A  575  HIS A  579  5                                   5    
HELIX   21 AC3 ASN B   38  CYS B   40  5                                   3    
HELIX   22 AC4 MET B   43  GLU B   54  1                                  12    
HELIX   23 AC5 LEU B  115  SER B  124  1                                  10    
HELIX   24 AC6 SER B  145  LYS B  151  1                                   7    
HELIX   25 AC7 CYS B  164  SER B  167  5                                   4    
HELIX   26 AC8 CYS B  168  ASN B  174  1                                   7    
HELIX   27 AC9 GLY B  180  ILE B  192  1                                  13    
HELIX   28 AD1 PHE B  198  LYS B  205  1                                   8    
HELIX   29 AD2 MET B  219  CYS B  225  1                                   7    
HELIX   30 AD3 ASN B  230  TYR B  245  1                                  16    
HELIX   31 AD4 THR C    7  GLY C   21  1                                  15    
HELIX   32 AD5 SER C   36  LEU C   66  1                                  31    
HELIX   33 AD6 ASN C   69  SER C   79  1                                  11    
HELIX   34 AD7 GLY C   83  LEU C  113  1                                  31    
HELIX   35 AD8 THR C  118  ALA C  141  1                                  24    
HELIX   36 AD9 LYS D   37  ASN D   63  1                                  27    
HELIX   37 AE1 CYS D   65  VAL D   92  1                                  28    
HELIX   38 AE2 GLY D   94  ASP D  123  1                                  30    
HELIX   39 AE3 GLY D  125  LEU D  136  1                                  12    
SHEET    1 AA1 6 SER A 172  VAL A 175  0                                        
SHEET    2 AA1 6 THR A  45  THR A  49  1  N  THR A  45   O  SER A 172           
SHEET    3 AA1 6 VAL A  15  VAL A  25  1  N  ALA A  22   O  ALA A  46           
SHEET    4 AA1 6 ILE A 202  VAL A 212  1  O  VAL A 211   N  VAL A  25           
SHEET    5 AA1 6 CYS A 189  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    6 AA1 6 TYR A 177  MET A 184 -1  N  LEU A 183   O  ARG A 190           
SHEET    1 AA2 6 SER A 172  VAL A 175  0                                        
SHEET    2 AA2 6 THR A  45  THR A  49  1  N  THR A  45   O  SER A 172           
SHEET    3 AA2 6 VAL A  15  VAL A  25  1  N  ALA A  22   O  ALA A  46           
SHEET    4 AA2 6 ILE A 202  VAL A 212  1  O  VAL A 211   N  VAL A  25           
SHEET    5 AA2 6 GLN A 386  ALA A 395  1  O  TYR A 394   N  THR A 210           
SHEET    6 AA2 6 GLN A 378  VAL A 383 -1  N  VAL A 383   O  GLN A 386           
SHEET    1 AA3 3 ILE A  65  ASN A  66  0                                        
SHEET    2 AA3 3 GLN A 143  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    3 AA3 3 GLN A 128  SER A 135 -1  N  ARG A 129   O  CYS A 147           
SHEET    1 AA4 3 CYS A 245  GLN A 246  0                                        
SHEET    2 AA4 3 LYS A 582  ASP A 589 -1  O  SER A 586   N  CYS A 245           
SHEET    3 AA4 3 LYS A 594  PRO A 601 -1  O  ARG A 600   N  HIS A 583           
SHEET    1 AA5 2 GLN A 252  HIS A 254  0                                        
SHEET    2 AA5 2 THR A 363  TYR A 366 -1  O  TYR A 366   N  GLN A 252           
SHEET    1 AA6 3 ILE A 275  ILE A 277  0                                        
SHEET    2 AA6 3 VAL A 322  GLN A 325 -1  O  GLN A 325   N  ILE A 275           
SHEET    3 AA6 3 ILE A 358  VAL A 360 -1  O  ILE A 358   N  LEU A 324           
SHEET    1 AA7 2 ILE A 371  PRO A 372  0                                        
SHEET    2 AA7 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1 AA8 2 ILE A 464  ARG A 465  0                                        
SHEET    2 AA8 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1 AA9 2 PHE A 484  ARG A 485  0                                        
SHEET    2 AA9 2 ALA A 551  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    1 AB1 5 HIS B  29  ASP B  36  0                                        
SHEET    2 AB1 5 ILE B  11  ARG B  18 -1  N  ILE B  16   O  GLN B  31           
SHEET    3 AB1 5 SER B  97  TYR B 100  1  O  SER B  97   N  ALA B  15           
SHEET    4 AB1 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5 AB1 5 ASN B  81  LEU B  83 -1  O  THR B  82   N  MET B  75           
SHEET    1 AB2 2 VAL B 107  LYS B 109  0                                        
SHEET    2 AB2 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  LYS B 109           
LINK         SG  CYS B  65                FE2  FES B 301     1555   1555  2.27  
LINK         SG  CYS B  70                FE2  FES B 301     1555   1555  2.15  
LINK         SG  CYS B  73                FE1  FES B 301     1555   1555  2.34  
LINK         SG  CYS B  85                FE1  FES B 301     1555   1555  2.13  
LINK         SG  CYS B 158                FE2  SF4 B 302     1555   1555  2.16  
LINK         SG  CYS B 161                FE3  SF4 B 302     1555   1555  2.32  
LINK         SG  CYS B 164                FE1  SF4 B 302     1555   1555  2.07  
LINK         SG  CYS B 215                FE1  F3S B 303     1555   1555  2.50  
LINK         SG  CYS B 221                FE4  F3S B 303     1555   1555  2.29  
LINK         SG  CYS B 225                FE4  SF4 B 302     1555   1555  2.45  
LINK         NE2 HIS C 101                FE   HEM C 301     1555   1555  2.29  
LINK         NE2 HIS D  79                FE   HEM C 301     1555   1555  2.30  
LINK         SG  CYS B 168                FE3  F3S B 303     1555   1555  1.83  
SITE     1 AC1 33 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 33 ALA A  30  VAL A  48  THR A  49  LYS A  50                    
SITE     3 AC1 33 LEU A  51  SER A  56  HIS A  57  THR A  58                    
SITE     4 AC1 33 ALA A  61  GLN A  62  GLY A  63  GLY A  64                    
SITE     5 AC1 33 TYR A 177  PHE A 178  ALA A 179  THR A 214                    
SITE     6 AC1 33 GLY A 215  THR A 225  ASP A 233  LEU A 264                    
SITE     7 AC1 33 HIS A 365  TYR A 366  GLU A 398  ARG A 409                    
SITE     8 AC1 33 ALA A 412  ASN A 413  SER A 414  LEU A 415                    
SITE     9 AC1 33 LEU A 418                                                     
SITE     1 AC2  6 SER B  64  CYS B  65  CYS B  70  GLY B  71                    
SITE     2 AC2  6 CYS B  73  CYS B  85                                          
SITE     1 AC3  7 CYS B 158  ILE B 159  CYS B 161  ALA B 162                    
SITE     2 AC3  7 CYS B 164  CYS B 225  PRO B 226                               
SITE     1 AC4  8 CYS B 168  TYR B 178  CYS B 215  HIS B 216                    
SITE     2 AC4  8 ILE B 218  MET B 219  ASN B 220  CYS B 221                    
SITE     1 AC5 15 HIS C  45  ARG C  46  GLY C  49  LEU C  52                    
SITE     2 AC5 15 SER C  53  VAL C  56  HIS C 101  THR C 102                    
SITE     3 AC5 15 HIS C 108  ARG D  47  SER D  50  LEU D  53                    
SITE     4 AC5 15 LEU D  54  HIS D  79  GLY D  83                               
SITE     1 AC6  9 PRO B 169  SER B 170  TRP B 173  HIS B 216                    
SITE     2 AC6  9 ILE C  30  SER C  42  ARG C  46  ASP D  90                    
SITE     3 AC6  9 TYR D  91                                                     
CRYST1   71.429   84.008  294.817  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      0.014000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011904  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003392        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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