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Database: PDB
Entry: 3AED
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AED              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 2-IODO-N-PHENYL-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 FRAGMENT: RESIDUES 57-159;                                           
COMPND  24 SYNONYM: SUCCINATE-UBIQUINONE OXIDOREDUCTASE CYTOCHROME B SMALL      
COMPND  25 SUBUNIT, CYBS, SUCCINATE-UBIQUINONE REDUCTASE MEMBRANE ANCHOR        
COMPND  26 SUBUNIT, QPS3, CII-4, SUCCINATE DEHYDROGENASE COMPLEX SUBUNIT D      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: HEART;                                                        
SOURCE   6 TISSUE: MUSCLE;                                                      
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   9 ORGANISM_COMMON: PIG;                                                
SOURCE  10 ORGANISM_TAXID: 9823;                                                
SOURCE  11 ORGAN: HEART;                                                        
SOURCE  12 TISSUE: MUSCLE;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  15 ORGANISM_COMMON: PIG;                                                
SOURCE  16 ORGANISM_TAXID: 9823;                                                
SOURCE  17 ORGAN: HEART;                                                        
SOURCE  18 TISSUE: MUSCLE;                                                      
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  21 ORGANISM_COMMON: PIG;                                                
SOURCE  22 ORGANISM_TAXID: 9823;                                                
SOURCE  23 ORGAN: HEART;                                                        
SOURCE  24 TISSUE: MUSCLE                                                       
KEYWDS    RESPIRATORY COMPLEX II, INHIBITORS, ELECTRON TRANSPORT, IRON, IRON-   
KEYWDS   2 SULFUR, METAL-BINDING, MITOCHONDRION, MITOCHONDRION INNER MEMBRANE,  
KEYWDS   3 OXIDOREDUCTASE, TRANSIT PEPTIDE, TRANSPORT, TRICARBOXYLIC ACID       
KEYWDS   4 CYCLE, HEME, TRANSMEMBRANE, FAD-BINDING PROTEIN, OXIDOREDUCTASE-     
KEYWDS   5 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HARADA,T.SASAKI,M.SHINDO,Y.KIDO,D.K.INAOKA,J.OMORI,A.OSANAI,        
AUTHOR   2 K.SAKAMOTO,J.MAO,S.MATSUOKA,M.INOUE,T.HONMA,A.TANAKA,K.KITA          
REVDAT   1   09-FEB-11 3AED    0                                                
JRNL        AUTH   S.HARADA,T.SASAKI,M.SHINDO,Y.KIDO,D.K.INAOKA,J.OMORI,        
JRNL        AUTH 2 A.OSANAI,K.SAKAMOTO,J.MAO,S.MATSUOKA,M.INOUE,T.HONMA,        
JRNL        AUTH 3 A.TANAKA,K.KITA                                              
JRNL        TITL   CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II  
JRNL        TITL 2 BOUND WITH 2-IODO-N-PHENYL-BENZAMIDE                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 3.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 22600                          
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1162                            
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) : 3.52                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.61                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1434                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
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          : 182                                     
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) : 97.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.12000                                              
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): 0.615         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.447         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.512        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.903                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.870                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8866 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12019 ; 0.932 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 4.539 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;33.911 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;16.573 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;12.925 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1304 ; 0.063 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6655 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5412 ; 0.151 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8677 ; 0.277 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3454 ; 0.220 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3325 ; 0.403 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   259                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5290 -17.5240  18.0780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3993 T22:   0.3794                                     
REMARK   3      T33:   0.3327 T12:  -0.0609                                     
REMARK   3      T13:   0.0137 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2618 L22:   0.8793                                     
REMARK   3      L33:   3.0614 L12:  -0.2403                                     
REMARK   3      L13:  -0.5000 L23:  -0.2910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0356 S12:  -0.1088 S13:  -0.0825                       
REMARK   3      S21:  -0.0862 S22:  -0.0034 S23:   0.0502                       
REMARK   3      S31:  -0.3833 S32:  -0.0060 S33:   0.0390                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   260        A   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1640   8.7770  24.3890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2634 T22:   0.4535                                     
REMARK   3      T33:   0.6053 T12:   0.0091                                     
REMARK   3      T13:   0.2178 T23:   0.0971                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9105 L22:   0.0326                                     
REMARK   3      L33:  -0.3564 L12:   0.9309                                     
REMARK   3      L13:   0.1404 L23:   0.1532                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1295 S12:  -0.0639 S13:   1.0192                       
REMARK   3      S21:   0.2534 S22:  -0.0792 S23:   0.4093                       
REMARK   3      S31:  -0.1844 S32:  -0.0299 S33:  -0.0504                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   350        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9780 -10.7890  11.7040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3298 T22:   0.4744                                     
REMARK   3      T33:   0.3294 T12:  -0.1428                                     
REMARK   3      T13:   0.0334 T23:   0.0844                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8050 L22:   1.0507                                     
REMARK   3      L33:   2.3936 L12:   0.1136                                     
REMARK   3      L13:  -0.2069 L23:  -0.4673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0281 S12:  -0.0566 S13:   0.1624                       
REMARK   3      S21:  -0.1358 S22:  -0.0135 S23:  -0.1463                       
REMARK   3      S31:  -0.4746 S32:   0.4541 S33:  -0.0146                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     9        B    43                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.9160 -12.2820  48.3910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2462 T22:   1.1502                                     
REMARK   3      T33:   0.5314 T12:  -0.1482                                     
REMARK   3      T13:  -0.1795 T23:  -0.0730                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0160 L22:   7.0885                                     
REMARK   3      L33:   5.9947 L12:   4.1100                                     
REMARK   3      L13:   1.3294 L23:  -0.1248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5442 S12:  -0.4606 S13:  -0.2694                       
REMARK   3      S21:   1.0360 S22:  -0.8529 S23:  -1.1699                       
REMARK   3      S31:  -0.0727 S32:   0.8272 S33:   0.3087                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    44        B   105                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9880 -10.9080  44.5870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4153 T22:   0.4809                                     
REMARK   3      T33:   0.4310 T12:  -0.2062                                     
REMARK   3      T13:  -0.0574 T23:   0.0885                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5736 L22:   1.0223                                     
REMARK   3      L33:   3.0162 L12:   2.0242                                     
REMARK   3      L13:   0.8957 L23:   1.3585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1974 S12:  -0.3436 S13:   0.6396                       
REMARK   3      S21:  -0.2331 S22:   0.0930 S23:  -0.0316                       
REMARK   3      S31:  -0.5901 S32:   0.7597 S33:   0.1044                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   106        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2420 -24.3050  40.2100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4904 T22:   0.2469                                     
REMARK   3      T33:   0.3829 T12:   0.0087                                     
REMARK   3      T13:   0.0349 T23:  -0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1618 L22:   0.5415                                     
REMARK   3      L33:   4.0678 L12:  -0.4259                                     
REMARK   3      L13:  -0.9468 L23:  -0.6171                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0406 S12:   0.2597 S13:   0.0052                       
REMARK   3      S21:   0.0504 S22:  -0.0803 S23:   0.2245                       
REMARK   3      S31:   0.2164 S32:  -0.3624 S33:   0.1208                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     6        C    35                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6410 -30.9230  47.2000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4514 T22:   0.2629                                     
REMARK   3      T33:   0.2992 T12:   0.1637                                     
REMARK   3      T13:   0.0065 T23:   0.1963                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1026 L22:   4.3026                                     
REMARK   3      L33:   4.1453 L12:   4.0150                                     
REMARK   3      L13:   1.2277 L23:   0.8043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1128 S12:   0.0681 S13:  -0.3128                       
REMARK   3      S21:   0.1979 S22:  -0.0414 S23:  -0.5977                       
REMARK   3      S31:   0.3905 S32:   0.4280 S33:   0.1543                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    36        C    68                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1260 -29.5660  74.2010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8663 T22:   0.2814                                     
REMARK   3      T33:   0.3148 T12:   0.0283                                     
REMARK   3      T13:   0.0367 T23:  -0.1210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3507 L22:   0.2779                                     
REMARK   3      L33:   0.5613 L12:  -1.4009                                     
REMARK   3      L13:   1.2247 L23:   0.4187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2008 S12:  -0.2303 S13:  -0.0698                       
REMARK   3      S21:   0.2274 S22:   0.1658 S23:  -0.0117                       
REMARK   3      S31:   0.1146 S32:  -0.2719 S33:   0.0350                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    69        C    89                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.7740 -26.4500  94.9470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4393 T22:   0.4988                                     
REMARK   3      T33:   0.4378 T12:  -0.0217                                     
REMARK   3      T13:   0.0747 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.2394 L22:  15.0455                                     
REMARK   3      L33:  18.1061 L12:  10.3182                                     
REMARK   3      L13:  -4.0927 L23:   0.3966                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8439 S12:  -0.9852 S13:  -0.6563                       
REMARK   3      S21:   2.1332 S22:  -0.2924 S23:  -0.6935                       
REMARK   3      S31:  -1.8671 S32:   0.4120 S33:  -0.5514                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    90        C   120                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.7460 -17.4170  66.7990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8873 T22:   0.3066                                     
REMARK   3      T33:   0.5414 T12:  -0.0462                                     
REMARK   3      T13:   0.0926 T23:  -0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1172 L22:   3.7466                                     
REMARK   3      L33:   5.6414 L12:   1.2807                                     
REMARK   3      L13:  -2.9798 L23:  -2.5822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2739 S12:  -0.1699 S13:   0.0121                       
REMARK   3      S21:   0.5514 S22:  -0.3251 S23:   0.0486                       
REMARK   3      S31:  -0.7718 S32:   0.5758 S33:   0.0512                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   121        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.4240 -10.9290  72.0770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8151 T22:   0.2114                                     
REMARK   3      T33:   0.5702 T12:  -0.0650                                     
REMARK   3      T13:   0.0780 T23:  -0.2168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5985 L22:   7.7901                                     
REMARK   3      L33:  -2.3679 L12:  -3.3988                                     
REMARK   3      L13:   0.6018 L23:   1.7526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2900 S12:   0.3460 S13:  -0.2800                       
REMARK   3      S21:   0.3460 S22:  -0.1865 S23:   0.3876                       
REMARK   3      S31:   0.1378 S32:   0.1509 S33:  -0.1035                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    35        D    67                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.7950 -28.9280  65.2330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4481 T22:   0.3641                                     
REMARK   3      T33:   0.5373 T12:   0.0252                                     
REMARK   3      T13:   0.2098 T23:  -0.1533                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9450 L22:   4.3767                                     
REMARK   3      L33:   9.7392 L12:   1.6372                                     
REMARK   3      L13:   2.0891 L23:  -0.6623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2687 S12:   0.0236 S13:  -0.2598                       
REMARK   3      S21:  -0.0404 S22:  -0.0199 S23:  -0.0208                       
REMARK   3      S31:  -0.4423 S32:  -0.6472 S33:   0.2885                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    68        D    97                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.7510 -35.6820  66.2710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8399 T22:   0.0410                                     
REMARK   3      T33:   0.4063 T12:  -0.0441                                     
REMARK   3      T13:   0.0206 T23:   0.0463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6425 L22:   2.2477                                     
REMARK   3      L33:   4.7660 L12:   0.2229                                     
REMARK   3      L13:   1.1565 L23:  -1.3115                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0101 S12:   0.0994 S13:  -0.6169                       
REMARK   3      S21:  -0.2512 S22:  -0.2636 S23:  -0.0225                       
REMARK   3      S31:   0.2872 S32:   0.3992 S33:   0.2534                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    98        D   122                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.0060 -42.3040  74.4990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7665 T22:   0.2399                                     
REMARK   3      T33:   0.4333 T12:   0.1104                                     
REMARK   3      T13:   0.3477 T23:   0.1654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2768 L22:   5.9438                                     
REMARK   3      L33:   2.1784 L12:   2.5666                                     
REMARK   3      L13:   3.4785 L23:  -0.1911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1672 S12:  -0.3306 S13:  -0.1396                       
REMARK   3      S21:  -0.7081 S22:  -0.2958 S23:  -0.4063                       
REMARK   3      S31:   0.4932 S32:  -0.1027 S33:   0.1286                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   123        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.9730 -27.5730  88.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3771 T22:   1.0342                                     
REMARK   3      T33:   1.0244 T12:   0.0107                                     
REMARK   3      T13:  -0.1719 T23:  -0.4317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6018 L22:  -3.1377                                     
REMARK   3      L33:  25.5432 L12:  -7.1741                                     
REMARK   3      L13: -20.4452 L23:   9.1870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1605 S12:   0.2947 S13:  -0.3807                       
REMARK   3      S21:  -0.1664 S22:  -1.0291 S23:   0.8625                       
REMARK   3      S31:  -0.9062 S32:  -1.1347 S33:   1.1896                       
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 U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3AED COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029147.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22670                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.16400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9640                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.580                              
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: PDB ENTRY 1ZOY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 6% 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 7.2, 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       35.76150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.54350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.03700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.54350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.76150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.03700            
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: 12790 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THESE COMPLEX FORMS MITOCHONDRIAL RESPIRATORY COMPLEX II.            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     LYS B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     ALA B   250                                                      
REMARK 465     SER B   251                                                      
REMARK 465     ALA B   252                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     ALA D    34                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  11      -23.23     65.00                                   
REMARK 500    LYS A 137       53.95     38.74                                   
REMARK 500    ALA A 151       73.90     30.22                                   
REMARK 500    ASP A 152       -1.69     72.42                                   
REMARK 500    ASP A 170       44.36    -89.96                                   
REMARK 500    ARG A 219        8.15    -68.00                                   
REMARK 500    ASN A 278     -156.40    -87.15                                   
REMARK 500    TYR A 288      -64.47   -102.35                                   
REMARK 500    LYS A 293     -121.90     60.32                                   
REMARK 500    ARG A 313       45.58    -88.69                                   
REMARK 500    CYS A 315       74.77   -119.27                                   
REMARK 500    ALA A 349      -36.39   -134.71                                   
REMARK 500    HIS A 365      -59.88   -133.42                                   
REMARK 500    GLN A 386     -167.12   -126.60                                   
REMARK 500    ASN A 445       54.89   -108.51                                   
REMARK 500    THR A 463      -16.27   -140.54                                   
REMARK 500    ALA A 482     -164.48    -73.84                                   
REMARK 500    TRP A 516       70.86     42.64                                   
REMARK 500    LYS A 544       56.10   -109.22                                   
REMARK 500    PRO A 567      151.03    -49.48                                   
REMARK 500    SER A 621      125.08   -170.29                                   
REMARK 500    ILE B  55      -62.30    -95.37                                   
REMARK 500    LEU B  59       95.42    -61.04                                   
REMARK 500    SER B  64      -70.39   -137.50                                   
REMARK 500    ALA B  74      114.09    -39.36                                   
REMARK 500    ASN B  92       98.49    -66.44                                   
REMARK 500    HIS B 104       62.81     37.17                                   
REMARK 500    LYS B 109      129.22   -178.64                                   
REMARK 500    ASP B 110       87.74     30.22                                   
REMARK 500    LEU B 111       -1.38     72.01                                   
REMARK 500    GLU B 126       74.01     56.47                                   
REMARK 500    GLU B 134       41.00   -103.80                                   
REMARK 500    PHE B 198       39.41    -94.92                                   
REMARK 500    TYR B 213       32.99    -84.73                                   
REMARK 500    THR B 217       56.31     37.07                                   
REMARK 500    MET B 219        8.53     80.56                                   
REMARK 500    THR B 244       60.26   -109.63                                   
REMARK 500    ASN C  23       33.30    -86.02                                   
REMARK 500    HIS C  29      -73.72   -131.79                                   
REMARK 500    CYS C  81       61.01     23.57                                   
REMARK 500    ALA C 142       47.95   -101.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EPH D 1306                                                       
REMARK 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 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  70   SG                                                     
REMARK 620 2 FES B 302   S1  106.7                                              
REMARK 620 3 FES B 302   S2  124.5  91.3                                        
REMARK 620 4 CYS B  65   SG  114.3 114.1 104.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C1305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  79   NE2                                                    
REMARK 620 2 HEM C1305   NA   97.2                                              
REMARK 620 3 HEM C1305   NB   91.6  89.3                                        
REMARK 620 4 HEM C1305   NC   88.1 174.6  90.0                                  
REMARK 620 5 HEM C1305   ND   89.6  90.9 178.8  89.7                            
REMARK 620 6 HIS C 101   NE2 168.5  89.0  98.2  85.8  80.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 164   SG                                                     
REMARK 620 2 SF4 B 303   S1  109.4                                              
REMARK 620 3 SF4 B 303   S2  124.0 105.4                                        
REMARK 620 4 SF4 B 303   S3  105.4 105.2 106.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 303   S2  105.6                                              
REMARK 620 3 SF4 B 303   S3  106.7 106.1                                        
REMARK 620 4 SF4 B 303   S4  127.3 104.9 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1   88.4                                              
REMARK 620 3 FES B 302   S2  157.1  91.4                                        
REMARK 620 4 CYS B  85   SG  101.4 131.4  95.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 161   SG                                                     
REMARK 620 2 SF4 B 303   S1  107.3                                              
REMARK 620 3 SF4 B 303   S3  123.8 105.5                                        
REMARK 620 4 SF4 B 303   S4  109.1 104.9 104.8                                  
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 221   SG                                                     
REMARK 620 2 F3S B 304   S1  103.8                                              
REMARK 620 3 F3S B 304   S3  128.2 100.1                                        
REMARK 620 4 F3S B 304   S4  103.9 123.4  99.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 168   SG                                                     
REMARK 620 2 F3S B 304   S2   87.0                                              
REMARK 620 3 F3S B 304   S3   83.7 100.4                                        
REMARK 620 4 F3S B 304   S4   96.7 159.3 100.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 225   SG                                                     
REMARK 620 2 SF4 B 303   S1   96.0                                              
REMARK 620 3 SF4 B 303   S2  117.9 105.6                                        
REMARK 620 4 SF4 B 303   S4  124.6 105.0 104.9                                  
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 215   SG                                                     
REMARK 620 2 F3S B 304   S1   96.3                                              
REMARK 620 3 F3S B 304   S2  105.8 118.3                                        
REMARK 620 4 F3S B 304   S3  138.0 100.1  99.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOL C 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ABV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE4   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE8   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE9   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEB   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEC   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEE   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEF   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX WITH AN EMPTY QUINONE-BINDING               
REMARK 900 POCKET                                                               
REMARK 900 RELATED ID: 3AEG   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF CHAIN D IS REFERRED IN REF 2 IN A5GZW8, UNIPROT.     
DBREF  3AED A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AED B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AED C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AED D   34   136  UNP    A5GZW8   DHSD_PIG        57    159             
SEQRES   1 A  622  SER SER ALA LYS VAL SER ASP ALA ILE SER THR GLN TYR          
SEQRES   2 A  622  PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY          
SEQRES   3 A  622  ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER          
SEQRES   4 A  622  GLU ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE          
SEQRES   5 A  622  PRO THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE          
SEQRES   6 A  622  ASN ALA ALA LEU GLY ASN MET GLU GLU ASP ASN TRP ARG          
SEQRES   7 A  622  TRP HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU          
SEQRES   8 A  622  GLY ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA          
SEQRES   9 A  622  PRO ALA SER VAL VAL GLU LEU GLU ASN TYR GLY MET PRO          
SEQRES  10 A  622  PHE SER ARG THR GLU ASP GLY LYS ILE TYR GLN ARG ALA          
SEQRES  11 A  622  PHE GLY GLY GLN SER LEU LYS PHE GLY LYS GLY GLY GLN          
SEQRES  12 A  622  ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS          
SEQRES  13 A  622  SER LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR          
SEQRES  14 A  622  ASP THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU          
SEQRES  15 A  622  LEU MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU          
SEQRES  16 A  622  CYS ILE GLU ASP GLY SER ILE HIS ARG ILE ARG ALA ARG          
SEQRES  17 A  622  ASN THR VAL VAL ALA THR GLY GLY TYR GLY ARG THR TYR          
SEQRES  18 A  622  PHE SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY          
SEQRES  19 A  622  THR ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP          
SEQRES  20 A  622  LEU GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY          
SEQRES  21 A  622  ALA GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY          
SEQRES  22 A  622  GLY ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU          
SEQRES  23 A  622  ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP          
SEQRES  24 A  622  VAL VAL SER ARG SER MET THR LEU GLU ILE ARG GLU GLY          
SEQRES  25 A  622  ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN          
SEQRES  26 A  622  LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA VAL ARG LEU          
SEQRES  27 A  622  PRO GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL          
SEQRES  28 A  622  ASP VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL          
SEQRES  29 A  622  HIS TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY          
SEQRES  30 A  622  GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP GLN VAL VAL          
SEQRES  31 A  622  PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA CYS ALA SER          
SEQRES  32 A  622  VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU          
SEQRES  33 A  622  ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU SER ILE          
SEQRES  34 A  622  ALA GLU SER CYS ARG PRO GLY ASP LYS VAL PRO SER ILE          
SEQRES  35 A  622  LYS PRO ASN ALA GLY GLU GLU SER VAL MET ASN LEU ASP          
SEQRES  36 A  622  LYS LEU ARG PHE ALA ASN GLY THR ILE ARG THR SER GLU          
SEQRES  37 A  622  LEU ARG LEU SER MET GLN LYS SER MET GLN SER HIS ALA          
SEQRES  38 A  622  ALA VAL PHE ARG VAL GLY SER VAL LEU GLN GLU GLY CYS          
SEQRES  39 A  622  GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU GLN HIS LEU          
SEQRES  40 A  622  LYS THR PHE ASP ARG GLY MET VAL TRP ASN THR ASP LEU          
SEQRES  41 A  622  VAL GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA          
SEQRES  42 A  622  LEU GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER          
SEQRES  43 A  622  ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS GLU ARG VAL          
SEQRES  44 A  622  ASP GLU TYR ASP TYR SER LYS PRO ILE GLN GLY GLN GLN          
SEQRES  45 A  622  LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS HIS THR LEU          
SEQRES  46 A  622  SER TYR VAL ASP VAL LYS THR GLY LYS VAL SER LEU GLU          
SEQRES  47 A  622  TYR ARG PRO VAL ILE ASP LYS THR LEU ASN GLU ALA ASP          
SEQRES  48 A  622  CYS ALA THR VAL PRO PRO ALA ILE ARG SER TYR                  
SEQRES   1 B  252  ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE LYS LYS          
SEQRES   2 B  252  PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR GLY ASP          
SEQRES   3 B  252  LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU ASN ASN          
SEQRES   4 B  252  CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS          
SEQRES   5 B  252  ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG SER CYS          
SEQRES   6 B  252  ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ASN          
SEQRES   7 B  252  GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE ASP THR          
SEQRES   8 B  252  ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU PRO HIS          
SEQRES   9 B  252  MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU SER ASN          
SEQRES  10 B  252  PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS          
SEQRES  11 B  252  LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN TYR LEU          
SEQRES  12 B  252  GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY LEU TYR          
SEQRES  13 B  252  GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO          
SEQRES  14 B  252  SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA          
SEQRES  15 B  252  VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG          
SEQRES  16 B  252  ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU GLN ASP          
SEQRES  17 B  252  PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS          
SEQRES  18 B  252  THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA          
SEQRES  19 B  252  ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU          
SEQRES  20 B  252  LYS LYS ALA SER ALA                                          
SEQRES   1 C  140  LEU GLY THR THR ALA LYS GLU GLU MET GLU ARG PHE TRP          
SEQRES   2 C  140  ASN LYS ASN LEU GLY SER ASN ARG PRO LEU SER PRO HIS          
SEQRES   3 C  140  ILE THR ILE TYR ARG TRP SER LEU PRO MET ALA MET SER          
SEQRES   4 C  140  ILE CYS HIS ARG GLY THR GLY ILE ALA LEU SER ALA GLY          
SEQRES   5 C  140  VAL SER LEU PHE GLY LEU SER ALA LEU LEU LEU PRO GLY          
SEQRES   6 C  140  ASN PHE GLU SER HIS LEU GLU LEU VAL LYS SER LEU CYS          
SEQRES   7 C  140  LEU GLY PRO THR LEU ILE TYR THR ALA LYS PHE GLY ILE          
SEQRES   8 C  140  VAL PHE PRO LEU MET TYR HIS THR TRP ASN GLY ILE ARG          
SEQRES   9 C  140  HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU THR ILE PRO          
SEQRES  10 C  140  GLN LEU THR GLN SER GLY VAL VAL VAL LEU ILE LEU THR          
SEQRES  11 C  140  VAL LEU SER SER VAL GLY LEU ALA ALA MET                      
SEQRES   1 D  103  ALA SER SER LYS ALA ALA SER LEU HIS TRP THR GLY GLU          
SEQRES   2 D  103  ARG VAL VAL SER VAL LEU LEU LEU GLY LEU LEU PRO ALA          
SEQRES   3 D  103  ALA TYR LEU ASN PRO CYS SER ALA MET ASP TYR SER LEU          
SEQRES   4 D  103  ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY ILE GLY          
SEQRES   5 D  103  GLN VAL VAL THR ASP TYR VAL ARG GLY ASP ALA LEU GLN          
SEQRES   6 D  103  LYS ALA ALA LYS ALA GLY LEU LEU ALA LEU SER ALA PHE          
SEQRES   7 D  103  THR PHE ALA GLY LEU CYS TYR PHE ASN TYR HIS ASP VAL          
SEQRES   8 D  103  GLY ILE CYS LYS ALA VAL ALA MET LEU TRP LYS LEU              
HET    FAD  A 700      53                                                       
HET    MLI  A 701       7                                                       
HET    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    HEM  C1305      43                                                       
HET    BOL  C1201      16                                                       
HET    EPH  D1306      44                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     MLI MALONATE ION                                                     
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     BOL 2-IODO-N-PHENYLBENZAMIDE                                         
HETNAM     EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-                
HETNAM   2 EPH  PHOSPHATIDYLETHANOLAMINE                                        
HETSYN     HEM HEME                                                             
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  MLI    C3 H2 O4 2-                                                  
FORMUL   7  FES    FE2 S2                                                       
FORMUL   8  SF4    FE4 S4                                                       
FORMUL   9  F3S    FE3 S4                                                       
FORMUL  10  HEM    C34 H32 FE N4 O4                                             
FORMUL  11  BOL    C13 H10 I N O                                                
FORMUL  12  EPH    C39 H68 N O8 P                                               
HELIX    1   1 GLY A   28  ALA A   41  1                                  14    
HELIX    2   2 SER A   56  ALA A   61  5                                   6    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  GLY A  115  1                                  23    
HELIX    5   5 ARG A  153  LEU A  167  1                                  15    
HELIX    6   6 TYR A  217  TYR A  221  5                                   5    
HELIX    7   7 GLY A  232  ARG A  240  1                                   9    
HELIX    8   8 GLU A  267  GLU A  272  1                                   6    
HELIX    9   9 ARG A  283  ARG A  287  5                                   5    
HELIX   10  10 ALA A  292  ALA A  296  5                                   5    
HELIX   11  11 SER A  297  GLY A  312  1                                  16    
HELIX   12  12 PRO A  330  LEU A  338  1                                   9    
HELIX   13  13 PRO A  339  PHE A  348  1                                  10    
HELIX   14  14 ASN A  413  CYS A  433  1                                  21    
HELIX   15  15 GLY A  447  PHE A  459  1                                  13    
HELIX   16  16 ARG A  465  ALA A  481  1                                  17    
HELIX   17  17 VAL A  486  ASP A  503  1                                  18    
HELIX   18  18 ASN A  517  ARG A  543  1                                  27    
HELIX   19  19 MET B   43  ILE B   55  1                                  13    
HELIX   20  20 LEU B  115  ILE B  125  1                                  11    
HELIX   21  21 SER B  145  LYS B  151  1                                   7    
HELIX   22  22 ALA B  162  CYS B  168  1                                   7    
HELIX   23  23 CYS B  168  ASN B  174  1                                   7    
HELIX   24  24 GLY B  180  ILE B  192  1                                  13    
HELIX   25  25 PHE B  198  LYS B  205  1                                   8    
HELIX   26  26 MET B  219  CYS B  225  1                                   7    
HELIX   27  27 ASN B  230  THR B  244  1                                  15    
HELIX   28  28 THR C    7  GLY C   21  1                                  15    
HELIX   29  29 SER C   36  LEU C   64  1                                  29    
HELIX   30  30 ASN C   69  LYS C   78  1                                  10    
HELIX   31  31 SER C   79  CYS C   81  5                                   3    
HELIX   32  32 GLY C   83  LEU C  113  1                                  31    
HELIX   33  33 THR C  118  ALA C  141  1                                  24    
HELIX   34  34 LYS D   37  ASN D   63  1                                  27    
HELIX   35  35 CYS D   65  VAL D   92  1                                  28    
HELIX   36  36 GLY D   94  ASP D  123  1                                  30    
HELIX   37  37 GLY D  125  LYS D  135  1                                  11    
SHEET    1   A 4 VAL A  15  GLU A  19  0                                        
SHEET    2   A 4 ILE A 202  ARG A 206  1  O  ARG A 206   N  HIS A  18           
SHEET    3   A 4 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    4   A 4 TYR A 177  GLU A 185 -1  N  LEU A 183   O  ARG A 190           
SHEET    1   B 6 SER A 172  VAL A 175  0                                        
SHEET    2   B 6 THR A  45  THR A  49  1  N  CYS A  47   O  PHE A 174           
SHEET    3   B 6 ALA A  22  VAL A  25  1  N  VAL A  24   O  ALA A  46           
SHEET    4   B 6 ASN A 209  VAL A 212  1  O  VAL A 211   N  VAL A  23           
SHEET    5   B 6 GLN A 388  ALA A 395  1  O  TYR A 394   N  THR A 210           
SHEET    6   B 6 GLN A 378  ARG A 381 -1  N  VAL A 379   O  VAL A 390           
SHEET    1   C 3 ILE A  65  ASN A  66  0                                        
SHEET    2   C 3 CYS A 147  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    3   C 3 GLN A 128  ARG A 129 -1  N  ARG A 129   O  CYS A 147           
SHEET    1   D 3 CYS A 245  GLN A 246  0                                        
SHEET    2   D 3 LYS A 582  VAL A 588 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 VAL A 595  PRO A 601 -1  O  GLU A 598   N  LEU A 585           
SHEET    1   E 2 VAL A 251  HIS A 254  0                                        
SHEET    2   E 2 THR A 363  ASN A 367 -1  O  TYR A 366   N  GLN A 252           
SHEET    1   F 3 ILE A 275  ILE A 277  0                                        
SHEET    2   F 3 VAL A 322  GLN A 325 -1  O  GLN A 325   N  ILE A 275           
SHEET    3   F 3 ILE A 358  VAL A 360 -1  O  ILE A 358   N  LEU A 324           
SHEET    1   G 2 ILE A 371  PRO A 372  0                                        
SHEET    2   G 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   H 5 HIS B  29  ASP B  36  0                                        
SHEET    2   H 5 ILE B  11  ARG B  18 -1  N  ILE B  16   O  GLN B  31           
SHEET    3   H 5 SER B  97  TYR B 100  1  O  ILE B  99   N  ALA B  15           
SHEET    4   H 5 MET B  75  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   H 5 GLY B  80  THR B  82 -1  O  GLY B  80   N  ILE B  77           
SHEET    1   I 2 VAL B 107  LYS B 109  0                                        
SHEET    2   I 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  ILE B 108           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  1.98  
LINK         SG  CYS B  70                FE2  FES B 302     1555   1555  1.99  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.15  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.17  
LINK         SG  CYS B 164                FE4  SF4 B 303     1555   1555  2.20  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.22  
LINK         SG  CYS B  73                FE1  FES B 302     1555   1555  2.23  
LINK         SG  CYS B  65                FE2  FES B 302     1555   1555  2.25  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.30  
LINK         SG  CYS B  85                FE1  FES B 302     1555   1555  2.51  
LINK         SG  CYS B 221                FE3  F3S B 304     1555   1555  2.51  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.67  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.70  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.70  
SITE     1 AC1 37 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 37 ALA A  30  VAL A  48  THR A  49  LYS A  50                    
SITE     3 AC1 37 LEU A  51  SER A  56  HIS A  57  THR A  58                    
SITE     4 AC1 37 ALA A  60  ALA A  61  GLN A  62  GLY A  63                    
SITE     5 AC1 37 GLY A  64  TYR A 177  PHE A 178  ALA A 179                    
SITE     6 AC1 37 ALA A 213  THR A 214  GLY A 215  THR A 225                    
SITE     7 AC1 37 ASP A 233  LEU A 264  HIS A 365  TYR A 366                    
SITE     8 AC1 37 GLY A 397  GLU A 398  ARG A 409  ALA A 412                    
SITE     9 AC1 37 ASN A 413  SER A 414  LEU A 415  LEU A 418                    
SITE    10 AC1 37 MLI A 701                                                     
SITE     1 AC2 11 GLN A  62  GLY A  63  PHE A 131  HIS A 254                    
SITE     2 AC2 11 LEU A 264  THR A 266  GLU A 267  ARG A 298                    
SITE     3 AC2 11 HIS A 365  ARG A 409  FAD A 700                               
SITE     1 AC3  9 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC3  9 ILE B  69  CYS B  70  GLY B  71  CYS B  73                    
SITE     3 AC3  9 CYS B  85                                                     
SITE     1 AC4  9 CYS B 158  ILE B 159  LEU B 160  CYS B 161                    
SITE     2 AC4  9 ALA B 162  CYS B 164  ALA B 182  CYS B 225                    
SITE     3 AC4  9 PRO B 226                                                     
SITE     1 AC5  9 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC5  9 HIS B 216  THR B 217  MET B 219  ASN B 220                    
SITE     3 AC5  9 CYS B 221                                                     
SITE     1 AC6 16 HIS C  45  ARG C  46  GLY C  49  LEU C  52                    
SITE     2 AC6 16 SER C  53  HIS C 101  THR C 102  HIS C 108                    
SITE     3 AC6 16 ARG D  47  SER D  50  LEU D  53  LEU D  54                    
SITE     4 AC6 16 LEU D  57  HIS D  79  GLY D  83  ILE D  84                    
SITE     1 AC7  8 SER B 170  TRP B 173  HIS B 216  ILE C  30                    
SITE     2 AC7  8 MET C  39  SER C  42  ARG C  46  TYR D  91                    
SITE     1 AC8  8 PHE C  59  LEU C 140  MET C 143  LEU D  57                    
SITE     2 AC8  8 TYR D  61  VAL D 130  ALA D 131  TRP D 134                    
CRYST1   71.523   84.074  295.087  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      0.013982  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011894  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003389        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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