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Database: PDB
Entry: 2ACZ
LinkDB: 2ACZ
Original site: 2ACZ 
HEADER    OXIDOREDUCTASE/ELECTRON TRANSPORT       19-JUL-05   2ACZ              
TITLE     COMPLEX II (SUCCINATE DEHYDROGENASE) FROM E. COLI WITH ATPENIN A5     
TITLE    2 INHIBITOR CO-CRYSTALLIZED AT THE UBIQUINONE BINDING SITE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT;              
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.3.99.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SUCCINATE DEHYDROGENASE IRON-SULFUR PROTEIN;               
COMPND   8 CHAIN: B;                                                            
COMPND   9 EC: 1.3.99.1;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT;           
COMPND  13 CHAIN: C;                                                            
COMPND  14 SYNONYM: CYTOCHROME B-556;                                           
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR        
COMPND  18 PROTEIN;                                                             
COMPND  19 CHAIN: D;                                                            
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 562;                                                 
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  19 ORGANISM_TAXID: 562;                                                 
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  27 ORGANISM_TAXID: 562;                                                 
SOURCE  28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  30 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  31 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  32 EXPRESSION_SYSTEM_PLASMID: PFAS                                      
KEYWDS    MEMBRANE PROTEIN, AEROBIC REPARATORY COMPLEX II, SQR,                 
KEYWDS   2 SUCCINATE:UBIQUINONE OXIDOREDUCTASE, AA5, AT5, ATPENIN A5, SDH,      
KEYWDS   3 SUCCINATE DEHYDROGENASE, OXIDOREDUCTASE-ELECTRON TRANSPORT COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.HORSEFIELD,V.YANKOVSKAYA,G.SEXTON,W.WHITTINGHAM,K.SHIOMI,S.OMURA,   
AUTHOR   2 B.BYRNE,G.CECCHINI,S.IWATA                                           
REVDAT   5   13-JUL-11 2ACZ    1       VERSN                                    
REVDAT   4   24-FEB-09 2ACZ    1       VERSN                                    
REVDAT   3   04-APR-06 2ACZ    1       JRNL                                     
REVDAT   2   17-JAN-06 2ACZ    1       JRNL   HETSYN                            
REVDAT   1   03-JAN-06 2ACZ    0                                                
JRNL        AUTH   R.HORSEFIELD,V.YANKOVSKAYA,G.SEXTON,W.WHITTINGHAM,K.SHIOMI,  
JRNL        AUTH 2 S.OMURA,B.BYRNE,G.CECCHINI,S.IWATA                           
JRNL        TITL   STRUCTURAL AND COMPUTATIONAL ANALYSIS OF THE QUINONE-BINDING 
JRNL        TITL 2 SITE OF COMPLEX II (SUCCINATE-UBIQUINONE OXIDOREDUCTASE): A  
JRNL        TITL 3 MECHANISM OF ELECTRON TRANSFER AND PROTON CONDUCTION DURING  
JRNL        TITL 4 UBIQUINONE REDUCTION.                                        
JRNL        REF    J.BIOL.CHEM.                  V. 281  7309 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16407191                                                     
JRNL        DOI    10.1074/JBC.M508173200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : -2.000                         
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             : 34114                          
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) : 0.264                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 966                             
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.16                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3760                       
REMARK   3   BIN FREE R VALUE                    : 0.4290                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8297                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 224                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.70                          
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.307 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.310 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.661 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.655 ; 2.500                
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 2ACZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033750.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 170                                
REMARK 200  PH                             : 8.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9393                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34114                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 4.360                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
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) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1NEK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL, CACIUM CHLORIDE, PEG 400, PH   
REMARK 280  8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       69.37950            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       40.05627            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      173.95767            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       69.37950            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       40.05627            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      173.95767            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       69.37950            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       40.05627            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      173.95767            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       69.37950            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       40.05627            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      173.95767            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       69.37950            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       40.05627            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      173.95767            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       69.37950            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       40.05627            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      173.95767            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       80.11255            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      347.91533            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       80.11255            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      347.91533            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       80.11255            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      347.91533            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       80.11255            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      347.91533            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       80.11255            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      347.91533            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       80.11255            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      347.91533            
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 63630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 110430 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -565.0 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 350   BIOMT1   2 -0.500000 -0.866025  0.000000      208.13850            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      120.16882            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000      240.33764            
REMARK 350   BIOMT3   3  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 D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ASP A  110                                                       
REMARK 475     ASP A  111                                                       
REMARK 475     GLY A  112                                                       
REMARK 475     ARG A  113                                                       
REMARK 475     ILE A  114                                                       
REMARK 475     TYR A  115                                                       
REMARK 475     GLN A  116                                                       
REMARK 475     SER A  563                                                       
REMARK 475     GLU A  564                                                       
REMARK 475     SER A  565                                                       
REMARK 475     MET A  566                                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  117   N    CA                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLY D    41     OA3  CDN C   132              1.91            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    SER A  44   C     HIS A  45   N       0.242                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 278   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    PRO A 546   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    CYS B  60   CA  -  CB  -  SG  ANGL. DEV. =   6.8 DEGREES          
REMARK 500    PRO B  85   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    CYS B 212   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  15       57.08   -108.73                                   
REMARK 500    SER A  29       45.87    -84.38                                   
REMARK 500    PRO A  41      -40.53    -24.80                                   
REMARK 500    SER A  44      147.52    -35.29                                   
REMARK 500    GLN A  50      -71.45   -119.40                                   
REMARK 500    ALA A  56       83.89    -64.52                                   
REMARK 500    GLU A  62      152.52    -48.79                                   
REMARK 500    ASP A  77       47.16     81.19                                   
REMARK 500    ILE A  79      -10.08   -140.28                                   
REMARK 500    PRO A 105       40.60    -59.86                                   
REMARK 500    PHE A 106      156.13    -48.51                                   
REMARK 500    ASP A 110     -130.78    164.77                                   
REMARK 500    ILE A 114       30.35   -151.16                                   
REMARK 500    PRO A 118     -118.05    -44.46                                   
REMARK 500    ALA A 131     -147.75   -137.07                                   
REMARK 500    ARG A 133       -3.01   -140.16                                   
REMARK 500    ALA A 137       73.90   -104.80                                   
REMARK 500    ALA A 138     -136.03     69.20                                   
REMARK 500    ASN A 156       25.37    -79.75                                   
REMARK 500    HIS A 157       50.42     35.90                                   
REMARK 500    LEU A 167      -71.16    -93.37                                   
REMARK 500    VAL A 178       59.65   -116.89                                   
REMARK 500    ALA A 201       49.18   -147.12                                   
REMARK 500    ALA A 205       42.83   -177.57                                   
REMARK 500    HIS A 216       -5.20    -59.49                                   
REMARK 500    ASN A 218       84.57    -60.56                                   
REMARK 500    PRO A 232      176.29    -52.96                                   
REMARK 500    ASP A 235       34.15     16.62                                   
REMARK 500    MET A 236        5.70    -57.41                                   
REMARK 500    THR A 254      124.40    -24.05                                   
REMARK 500    ARG A 271       75.11   -102.76                                   
REMARK 500    PHE A 272      -13.47    -45.55                                   
REMARK 500    PRO A 278      -63.28    -27.12                                   
REMARK 500    LYS A 281     -138.89     35.77                                   
REMARK 500    GLU A 296       -3.31    -58.53                                   
REMARK 500    CYS A 303      152.31    -40.16                                   
REMARK 500    LEU A 327       40.07   -152.24                                   
REMARK 500    HIS A 339       45.67     27.25                                   
REMARK 500    PRO A 348       93.59    -69.82                                   
REMARK 500    HIS A 354      -96.20   -127.31                                   
REMARK 500    MET A 357      -80.40    -52.80                                   
REMARK 500    SER A 393       37.27     76.01                                   
REMARK 500    ASN A 398      107.18   -160.78                                   
REMARK 500    GLU A 425      -38.11    -39.51                                   
REMARK 500    ALA A 428      160.22    -44.28                                   
REMARK 500    ASP A 431      175.99    -53.60                                   
REMARK 500    ARG A 446      -71.53    -57.43                                   
REMARK 500    CYS A 466      -74.65    -48.70                                   
REMARK 500    MET A 467      -29.25    -37.69                                   
REMARK 500    SER A 472     -156.61    -65.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     101 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS C   7        24.9      L          L   OUTSIDE RANGE           
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                             HEB C 130  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  84   NE2                                                    
REMARK 620 2 HEB C 130   NA   82.0                                              
REMARK 620 3 HEB C 130   NB   84.8  89.7                                        
REMARK 620 4 HEB C 130   NC   96.8 177.3  92.6                                  
REMARK 620 5 HEB C 130   ND   96.2  90.5 179.0  87.2                            
REMARK 620 6 HIS D  71   NE2 176.2  94.3  94.7  87.0  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  63   OD2                                                    
REMARK 620 2 FES B 302   S1   82.1                                              
REMARK 620 3 FES B 302   S2  173.1 102.3                                        
REMARK 620 4 CYS B  75   SG   97.9 124.7  84.2                                  
REMARK 620 5 ASP B  63   OD1  54.3 130.9 119.4  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  55   SG                                                     
REMARK 620 2 FES B 302   S1  128.0                                              
REMARK 620 3 FES B 302   S2   99.5 106.5                                        
REMARK 620 4 CYS B  60   SG  110.4  95.3 118.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 155   SG                                                     
REMARK 620 2 SF4 B 303   S2  106.1                                              
REMARK 620 3 SF4 B 303   S3  111.0  99.0                                        
REMARK 620 4 SF4 B 303   S4  128.0 102.7 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 149   SG                                                     
REMARK 620 2 SF4 B 303   S1   48.0                                              
REMARK 620 3 SF4 B 303   S3  107.3 103.4                                        
REMARK 620 4 SF4 B 303   S4   53.9 101.1 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 216   SG                                                     
REMARK 620 2 SF4 B 303   S1   50.3                                              
REMARK 620 3 SF4 B 303   S2  112.7 107.4                                        
REMARK 620 4 SF4 B 303   S4   52.1 102.2 105.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 152   SG                                                     
REMARK 620 2 SF4 B 303   S1  118.7                                              
REMARK 620 3 SF4 B 303   S2  122.6 108.9                                        
REMARK 620 4 SF4 B 303   S3   97.5 103.0 101.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 206   SG                                                     
REMARK 620 2 F3S B 304   S1   91.0                                              
REMARK 620 3 F3S B 304   S2   98.9  80.6                                        
REMARK 620 4 F3S B 304   S3  150.2 107.4 106.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 212   SG                                                     
REMARK 620 2 F3S B 304   S1  131.6                                              
REMARK 620 3 F3S B 304   S3   98.9 104.9                                        
REMARK 620 4 F3S B 304   S4  110.5 110.2  91.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 159   SG                                                     
REMARK 620 2 F3S B 304   S2  114.3                                              
REMARK 620 3 F3S B 304   S3  114.4 106.7                                        
REMARK 620 4 F3S B 304   S4  110.6 115.5  93.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OAA A 589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEB C 130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT5 C 131                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDN C 132                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NEK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF COMPLEX II WITH UBIQUINONE BOUND                
REMARK 900 RELATED ID: 1NEN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF COMPLEX II WITH DINITROPHENOL BOUND             
REMARK 900 RELATED ID: 2AD0   RELATED DB: PDB                                   
REMARK 900 THEORETICAL MODEL OF COMPLEX II WITH CARBOXIN DOCKED USING           
REMARK 900 PROTEIN-LIGAND DOCKING                                               
DBREF  2ACZ A    1   588  UNP    P10444   DHSA_ECOLI       1    588             
DBREF  2ACZ B    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2ACZ C    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2ACZ D    1   115  UNP    P10445   DHSD_ECOLI       1    115             
SEQRES   1 A  588  MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE          
SEQRES   2 A  588  GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE          
SEQRES   3 A  588  SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL          
SEQRES   4 A  588  PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY          
SEQRES   5 A  588  ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP          
SEQRES   6 A  588  GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR          
SEQRES   7 A  588  ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR          
SEQRES   8 A  588  GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU          
SEQRES   9 A  588  PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG          
SEQRES  10 A  588  PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN          
SEQRES  11 A  588  ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS          
SEQRES  12 A  588  ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN          
SEQRES  13 A  588  HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU          
SEQRES  14 A  588  VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA          
SEQRES  15 A  588  LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA          
SEQRES  16 A  588  ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE          
SEQRES  17 A  588  TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP          
SEQRES  18 A  588  GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN          
SEQRES  19 A  588  ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA          
SEQRES  20 A  588  GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU          
SEQRES  21 A  588  GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET          
SEQRES  22 A  588  GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG          
SEQRES  23 A  588  ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU          
SEQRES  24 A  588  GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS          
SEQRES  25 A  588  LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER          
SEQRES  26 A  588  ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA          
SEQRES  27 A  588  HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO          
SEQRES  28 A  588  THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL          
SEQRES  29 A  588  THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP          
SEQRES  30 A  588  VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA          
SEQRES  31 A  588  CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN          
SEQRES  32 A  588  SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY          
SEQRES  33 A  588  LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU          
SEQRES  34 A  588  ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP          
SEQRES  35 A  588  ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP          
SEQRES  36 A  588  PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN          
SEQRES  37 A  588  HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA          
SEQRES  38 A  588  LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU          
SEQRES  39 A  588  LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN          
SEQRES  40 A  588  THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET          
SEQRES  41 A  588  GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG          
SEQRES  42 A  588  THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO          
SEQRES  43 A  588  ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR          
SEQRES  44 A  588  LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN          
SEQRES  45 A  588  MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE          
SEQRES  46 A  588  ARG THR TYR                                                  
SEQRES   1 B  238  MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP          
SEQRES   2 B  238  VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU          
SEQRES   3 B  238  ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU          
SEQRES   4 B  238  ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG          
SEQRES   5 B  238  ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU          
SEQRES   6 B  238  ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO          
SEQRES   7 B  238  ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE          
SEQRES   8 B  238  ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL          
SEQRES   9 B  238  VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE          
SEQRES  10 B  238  LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA          
SEQRES  11 B  238  ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU          
SEQRES  12 B  238  ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER          
SEQRES  13 B  238  THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE          
SEQRES  14 B  238  ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU          
SEQRES  15 B  238  ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP          
SEQRES  16 B  238  GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER          
SEQRES  17 B  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 B  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 B  238  GLN ARG ASN ALA                                              
SEQRES   1 C  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 C  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 C  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 C  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 C  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 C  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 C  129  THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS          
SEQRES   8 C  129  MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU          
SEQRES   9 C  129  ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR          
SEQRES  10 C  129  VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP              
SEQRES   1 D  115  MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL          
SEQRES   2 D  115  HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU          
SEQRES   3 D  115  THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR          
SEQRES   4 D  115  SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE          
SEQRES   5 D  115  ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU          
SEQRES   6 D  115  PHE SER ILE LEU ILE HIS ALA TRP ILE GLY MET TRP GLN          
SEQRES   7 D  115  VAL LEU THR ASP TYR VAL LYS PRO LEU ALA LEU ARG LEU          
SEQRES   8 D  115  MET LEU GLN LEU VAL ILE VAL VAL ALA LEU VAL VAL TYR          
SEQRES   9 D  115  VAL ILE TYR GLY PHE VAL VAL VAL TRP GLY VAL                  
HET    OAA  A 589       9                                                       
HET    FAD  A 601      53                                                       
HET    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    HEB  C 130      43                                                       
HET    AT5  C 131      23                                                       
HET    CDN  C 132      77                                                       
HETNAM     OAA OXALOACETATE ION                                                 
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEB HEME B/C                                                         
HETNAM     AT5 3-[(2S,4S,5R)-5,6-DICHLORO-2,4-DIMETHYL-1-OXOHEXYL]-4-           
HETNAM   2 AT5  HYDROXY-5,6-DIMETHOXY-2(1H)-PYRIDINONE                          
HETNAM     CDN CARDIOLIPIN                                                      
HETSYN     HEB HYBRID BETWEEN B AND C TYPE HEMES (PROTOPORPHYRIN IX             
HETSYN   2 HEB  CONTAINING FE)                                                  
HETSYN     AT5 ATPENIN A5; AA5                                                  
FORMUL   5  OAA    C4 H3 O5 1-                                                  
FORMUL   6  FAD    C27 H33 N9 O15 P2                                            
FORMUL   7  FES    FE2 S2                                                       
FORMUL   8  SF4    FE4 S4                                                       
FORMUL   9  F3S    FE3 S4                                                       
FORMUL  10  HEB    C34 H34 FE N4 O4                                             
FORMUL  11  AT5    C15 H21 CL2 N O5                                             
FORMUL  12  CDN    C58 H120 O17 P2                                              
HELIX    1   1 GLY A   16  SER A   29  1                                  14    
HELIX    2   2 PHE A   40  ALA A   49  5                                  10    
HELIX    3   3 ASN A   64  ASP A   77  1                                  14    
HELIX    4   4 ASP A   81  HIS A  101  1                                  21    
HELIX    5   5 ARG A  140  ASN A  156  1                                  17    
HELIX    6   6 GLY A  222  ILE A  227  1                                   6    
HELIX    7   7 GLU A  255  GLY A  261  1                                   7    
HELIX    8   8 ARG A  271  ALA A  277  1                                   7    
HELIX    9   9 ALA A  280  ALA A  284  5                                   5    
HELIX   10  10 GLY A  285  GLU A  296  1                                  12    
HELIX   11  11 GLY A  319  LEU A  327  1                                   9    
HELIX   12  12 LEU A  327  ALA A  338  1                                  12    
HELIX   13  13 GLY A  402  GLN A  426  1                                  25    
HELIX   14  14 SER A  433  ASN A  450  1                                  18    
HELIX   15  15 ASP A  455  PHE A  471  1                                  17    
HELIX   16  16 GLU A  476  LEU A  494  1                                  19    
HELIX   17  17 LYS A  495  ALA A  497  5                                   3    
HELIX   18  18 ASN A  507  ARG A  533  1                                  27    
HELIX   19  19 MET B   34  ASP B   46  1                                  13    
HELIX   20  20 CYS B   75  THR B   77  5                                   3    
HELIX   21  21 PRO B   78  ASN B   83  5                                   6    
HELIX   22  22 MET B  107  ILE B  117  1                                  11    
HELIX   23  23 MET B  136  GLU B  141  1                                   6    
HELIX   24  24 LYS B  142  ASP B  144  5                                   3    
HELIX   25  25 CYS B  155  SER B  158  5                                   4    
HELIX   26  26 CYS B  159  ASN B  165  1                                   7    
HELIX   27  27 GLY B  171  ILE B  183  1                                  13    
HELIX   28  28 GLU B  189  GLY B  196  1                                   8    
HELIX   29  29 MET B  210  CYS B  216  1                                   7    
HELIX   30  30 ASN B  221  ASN B  237  1                                  17    
HELIX   31  31 PRO C   21  SER C   53  1                                  33    
HELIX   32  32 SER C   54  SER C   67  1                                  14    
HELIX   33  33 SER C   67  PHE C   96  1                                  30    
HELIX   34  34 THR C  102  TRP C  129  1                                  28    
HELIX   35  35 ASN D   11  ALA D   38  1                                  28    
HELIX   36  36 THR D   44  PHE D   52  1                                   9    
HELIX   37  37 SER D   54  VAL D   84  1                                  31    
HELIX   38  38 PRO D   86  GLY D  114  1                                  29    
SHEET    1   A 6 THR A 159  SER A 162  0                                        
SHEET    2   A 6 ALA A  34  SER A  37  1  N  LEU A  35   O  PHE A 161           
SHEET    3   A 6 VAL A  11  ILE A  13  1  N  VAL A  12   O  ALA A  34           
SHEET    4   A 6 THR A 198  LEU A 200  1  O  VAL A 199   N  VAL A  11           
SHEET    5   A 6 ASP A 377  ALA A 385  1  O  GLY A 382   N  THR A 198           
SHEET    6   A 6 GLN A 367  VAL A 371 -1  N  ALA A 368   O  VAL A 380           
SHEET    1   B 3 ILE A  53  THR A  54  0                                        
SHEET    2   B 3 ALA A 132  ALA A 135 -1  O  ALA A 135   N  ILE A  53           
SHEET    3   B 3 SER A 123  ASN A 125 -1  N  LYS A 124   O  THR A 134           
SHEET    1   C 3 TRP A 164  LYS A 171  0                                        
SHEET    2   C 3 VAL A 177  CYS A 184 -1  O  LEU A 183   N  TYR A 165           
SHEET    3   C 3 VAL A 190  PHE A 193 -1  O  PHE A 193   N  CYS A 180           
SHEET    1   D 4 TRP A 239  ILE A 246  0                                        
SHEET    2   D 4 ILE A 347  MET A 356 -1  O  HIS A 354   N  GLN A 240           
SHEET    3   D 4 ALA A 311  LYS A 314 -1  N  ALA A 311   O  VAL A 349           
SHEET    4   D 4 TYR A 263  LEU A 265 -1  N  TYR A 263   O  LYS A 314           
SHEET    1   E 2 ILE A 360  PRO A 361  0                                        
SHEET    2   E 2 ALA A 390  CYS A 391  1  O  CYS A 391   N  ILE A 360           
SHEET    1   F 2 PHE A 474  ARG A 475  0                                        
SHEET    2   F 2 SER A 541  ARG A 542  1  O  SER A 541   N  ARG A 475           
SHEET    1   G 5 ARG B  19  LEU B  25  0                                        
SHEET    2   G 5 LEU B   3  ARG B   9 -1  N  PHE B   5   O  TYR B  23           
SHEET    3   G 5 ILE B  89  ARG B  92  1  O  ILE B  89   N  SER B   6           
SHEET    4   G 5 GLY B  64  MET B  67 -1  N  ASN B  66   O  ARG B  92           
SHEET    5   G 5 LYS B  70  LEU B  73 -1  O  GLY B  72   N  LEU B  65           
SHEET    1   H 2 VAL B  99  ARG B 101  0                                        
SHEET    2   H 2 VAL B 104  VAL B 105 -1  O  VAL B 104   N  ILE B 100           
LINK         C8M FAD A 601                 NE2 HIS A  45     1555   1555  1.38  
LINK        FE   HEB C 130                 NE2 HIS C  84     1555   1555  2.22  
LINK        FE   HEB C 130                 NE2 HIS D  71     1555   1555  2.24  
LINK        FE1  FES B 302                 OD2 ASP B  63     1555   1555  2.22  
LINK        FE1  FES B 302                 SG  CYS B  75     1555   1555  2.58  
LINK        FE2  FES B 302                 SG  CYS B  55     1555   1555  2.33  
LINK        FE2  FES B 302                 SG  CYS B  60     1555   1555  2.54  
LINK        FE1  SF4 B 303                 SG  CYS B 155     1555   1555  2.45  
LINK        FE2  SF4 B 303                 SG  CYS B 149     1555   1555  4.88  
LINK        FE3  SF4 B 303                 SG  CYS B 216     1555   1555  4.97  
LINK        FE4  SF4 B 303                 SG  CYS B 152     1555   1555  2.42  
LINK        FE1  F3S B 304                 SG  CYS B 206     1555   1555  2.59  
LINK        FE3  F3S B 304                 SG  CYS B 212     1555   1555  2.38  
LINK        FE4  F3S B 304                 SG  CYS B 159     1555   1555  2.34  
LINK         OD1 ASP B  63                FE1  FES B 302     1555   1555  2.52  
SITE     1 AC1 12 GLY A  51  PHE A 126  HIS A 242  LEU A 252                    
SITE     2 AC1 12 THR A 254  GLU A 255  ARG A 286  HIS A 354                    
SITE     3 AC1 12 ARG A 399  GLY A 401  GLY A 402  FAD A 601                    
SITE     1 AC2 32 GLY A  14  ALA A  15  GLY A  16  GLY A  17                    
SITE     2 AC2 32 ALA A  18  SER A  37  LYS A  38  VAL A  39                    
SITE     3 AC2 32 SER A  44  HIS A  45  THR A  46  SER A  48                    
SITE     4 AC2 32 ALA A  49  GLN A  50  GLY A  51  GLY A  52                    
SITE     5 AC2 32 TRP A 164  TYR A 165  ALA A 166  ALA A 201                    
SITE     6 AC2 32 THR A 202  GLY A 203  ASN A 214  ASP A 221                    
SITE     7 AC2 32 TYR A 355  GLU A 388  ARG A 399  GLY A 402                    
SITE     8 AC2 32 SER A 404  LEU A 405  LEU A 408  OAA A 589                    
SITE     1 AC3  9 SER B  54  CYS B  55  ARG B  56  GLY B  58                    
SITE     2 AC3  9 VAL B  59  CYS B  60  GLY B  61  ASP B  63                    
SITE     3 AC3  9 CYS B  75                                                     
SITE     1 AC4  8 CYS B 149  ILE B 150  CYS B 152  ALA B 153                    
SITE     2 AC4  8 CYS B 154  CYS B 155  CYS B 216  PRO B 217                    
SITE     1 AC5 10 CYS B 159  PRO B 172  CYS B 206  HIS B 207                    
SITE     2 AC5 10 SER B 208  ILE B 209  MET B 210  ASN B 211                    
SITE     3 AC5 10 CYS B 212  THR B 223                                          
SITE     1 AC6 17 HIS B 207  HIS C  30  ARG C  31  THR C  37                    
SITE     2 AC6 17 PHE C  38  HIS C  84  VAL C  85  GLY C  88                    
SITE     3 AC6 17 CDN C 132  ARG D  20  ALA D  23  THR D  27                    
SITE     4 AC6 17 ILE D  68  HIS D  71  GLY D  75  MET D  76                    
SITE     5 AC6 17 GLN D  78                                                     
SITE     1 AC7 12 PRO B 160  TRP B 164  HIS B 207  ILE B 209                    
SITE     2 AC7 12 LEU C  15  PHE C  20  ALA C  24  SER C  27                    
SITE     3 AC7 12 ILE C  28  ARG C  31  ASP D  82  TYR D  83                    
SITE     1 AC8 18 LEU C  44  SER C  51  ALA C  61  SER C  62                    
SITE     2 AC8 18 MET C  65  MET C  74  LEU C  78  VAL C 115                    
SITE     3 AC8 18 LEU C 123  ALA C 124  VAL C 126  LEU C 127                    
SITE     4 AC8 18 TRP C 129  HEB C 130  ILE D  30  GLY D  41                    
SITE     5 AC8 18 LEU D  43  ILE D  68                                          
CRYST1  138.759  138.759  521.873  90.00  90.00 120.00 H 3 2        18          
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      0.007207  0.004161  0.000000        0.00000                         
SCALE2      0.000000  0.008322  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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