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Database: PDB
Entry: 3AE5
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AE5              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 2-METHYL-N-(3-ISOPROPOXY-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 3AE5    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-METHYL-N-(3-ISOPROPOXY-PHENYL)-BENZAMIDE        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 3.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 76.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18899                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 932                             
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) : 3.41                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.50                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1272                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3700                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.4510                       
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          : 186                                     
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) : 105.54                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : -0.46000                                             
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): 0.733         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.547         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 75.653        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8870 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12025 ; 0.906 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 4.417 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;33.581 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;16.525 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;13.911 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1305 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6660 ; 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):  5411 ; 0.106 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8676 ; 0.196 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3459 ; 0.158 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3332 ; 0.282 ; 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  : 12                                         
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): -15.5270 -17.4960  18.0800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2310 T22:   0.1896                                     
REMARK   3      T33:   0.4560 T12:  -0.0894                                     
REMARK   3      T13:   0.0215 T23:   0.0394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6248 L22:   1.3366                                     
REMARK   3      L33:   3.2041 L12:  -0.1540                                     
REMARK   3      L13:  -0.3929 L23:  -0.2728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0057 S12:  -0.2101 S13:  -0.0386                       
REMARK   3      S21:  -0.0355 S22:  -0.0131 S23:   0.0489                       
REMARK   3      S31:  -0.3039 S32:  -0.0659 S33:   0.0188                       
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): -18.2100   8.7930  24.4480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2913 T22:   0.0387                                     
REMARK   3      T33:   0.7330 T12:   0.0517                                     
REMARK   3      T13:   0.0765 T23:  -0.1219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9711 L22:   1.7976                                     
REMARK   3      L33:   2.8718 L12:   0.2978                                     
REMARK   3      L13:  -1.9636 L23:  -0.0947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3250 S12:  -0.3342 S13:   0.7217                       
REMARK   3      S21:   0.8682 S22:   0.0182 S23:   0.1301                       
REMARK   3      S31:  -1.4303 S32:   0.0877 S33:  -0.3432                       
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):  -2.8680 -10.7310  11.8580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3323 T22:   0.2138                                     
REMARK   3      T33:   0.4215 T12:  -0.1463                                     
REMARK   3      T13:   0.0423 T23:   0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7828 L22:   1.1161                                     
REMARK   3      L33:   2.7066 L12:  -0.1146                                     
REMARK   3      L13:   0.0220 L23:   0.1228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0721 S12:   0.0066 S13:   0.1412                       
REMARK   3      S21:  -0.0602 S22:   0.0215 S23:  -0.1174                       
REMARK   3      S31:  -0.3943 S32:   0.5674 S33:  -0.0936                       
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    46                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.9130 -11.9290  48.2320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8724 T22:   1.1988                                     
REMARK   3      T33:   0.3932 T12:  -0.2135                                     
REMARK   3      T13:  -0.3023 T23:  -0.0428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2589 L22:  -1.8500                                     
REMARK   3      L33:   0.0482 L12:   5.1655                                     
REMARK   3      L13:  -2.5478 L23:   0.3903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3377 S12:  -1.2468 S13:   0.1700                       
REMARK   3      S21:  -0.2369 S22:  -0.4351 S23:  -0.5864                       
REMARK   3      S31:  -0.0780 S32:   1.3150 S33:   0.0974                       
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    47        B   148                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.4550 -17.5070  39.0570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3015 T22:   0.1808                                     
REMARK   3      T33:   0.3180 T12:   0.0039                                     
REMARK   3      T13:   0.0569 T23:  -0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6350 L22:   1.2936                                     
REMARK   3      L33:   3.8613 L12:   0.1432                                     
REMARK   3      L13:   0.6978 L23:  -0.3886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1798 S12:  -0.4223 S13:   0.3135                       
REMARK   3      S21:   0.1707 S22:  -0.2043 S23:  -0.0185                       
REMARK   3      S31:  -0.2007 S32:   0.2134 S33:   0.0245                       
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   149        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.9020 -23.7220  43.8550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3322 T22:   0.1400                                     
REMARK   3      T33:   0.4898 T12:   0.0042                                     
REMARK   3      T13:   0.0445 T23:  -0.0701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3162 L22:   2.4159                                     
REMARK   3      L33:   4.8278 L12:   0.2460                                     
REMARK   3      L13:  -1.4005 L23:  -0.2532                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0057 S12:   0.0314 S13:   0.0193                       
REMARK   3      S21:   0.1090 S22:  -0.0347 S23:   0.1931                       
REMARK   3      S31:  -0.1509 S32:  -0.5335 S33:   0.0404                       
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    92                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.5560 -28.8590  69.3940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6667 T22:   0.1461                                     
REMARK   3      T33:   0.4447 T12:   0.0162                                     
REMARK   3      T13:   0.0929 T23:   0.0736                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0641 L22:   0.6153                                     
REMARK   3      L33:   4.2349 L12:  -0.0802                                     
REMARK   3      L13:  -1.0975 L23:   0.3090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0118 S12:  -0.3965 S13:   0.0306                       
REMARK   3      S21:   0.2879 S22:  -0.1862 S23:  -0.1248                       
REMARK   3      S31:  -0.2205 S32:   0.4353 S33:   0.1980                       
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    93        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.5950 -14.6380  67.5490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6622 T22:  -0.0295                                     
REMARK   3      T33:   0.5162 T12:  -0.0054                                     
REMARK   3      T13:   0.1535 T23:  -0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1642 L22:   4.1859                                     
REMARK   3      L33:  11.8179 L12:   0.5983                                     
REMARK   3      L13:  -0.5592 L23:  -3.8881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6461 S12:  -0.0462 S13:   0.2775                       
REMARK   3      S21:   0.4044 S22:  -0.0799 S23:   0.0647                       
REMARK   3      S31:   0.1537 S32:   0.1636 S33:  -0.5663                       
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 :   D    35        D    70                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.1680 -29.3010  66.3200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7136 T22:   0.2887                                     
REMARK   3      T33:   0.6133 T12:  -0.0744                                     
REMARK   3      T13:   0.3802 T23:  -0.0919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6678 L22:   1.4461                                     
REMARK   3      L33:   5.0516 L12:   0.3238                                     
REMARK   3      L13:   4.5373 L23:  -2.3612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4107 S12:   0.1476 S13:  -0.0297                       
REMARK   3      S21:   0.2047 S22:   0.5379 S23:   0.7464                       
REMARK   3      S31:  -0.0009 S32:  -0.8577 S33:  -0.1272                       
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 :   D    71        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.7220 -35.4830  64.4720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9687 T22:   0.0082                                     
REMARK   3      T33:   0.5183 T12:  -0.0129                                     
REMARK   3      T13:   0.0856 T23:   0.1834                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3258 L22:   0.3150                                     
REMARK   3      L33:   9.0312 L12:  -0.0992                                     
REMARK   3      L13:  -0.7548 L23:   0.7543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3792 S12:   0.4016 S13:  -0.6351                       
REMARK   3      S21:  -0.2173 S22:  -0.2789 S23:  -0.1153                       
REMARK   3      S31:   0.1124 S32:   0.4769 S33:   0.6581                       
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 :   D    97        D   124                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.8430 -41.8920  74.9600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2603 T22:   0.1397                                     
REMARK   3      T33:   0.8905 T12:  -0.1380                                     
REMARK   3      T13:   0.2769 T23:   0.3580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1886 L22:  -0.2405                                     
REMARK   3      L33:  14.3246 L12:   1.9928                                     
REMARK   3      L13:  -6.3016 L23:  -0.6087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9532 S12:  -1.6995 S13:  -1.3850                       
REMARK   3      S21:  -0.2909 S22:  -0.8781 S23:  -0.4866                       
REMARK   3      S31:  -1.5663 S32:   1.0119 S33:  -0.0751                       
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   125        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.7420 -25.9820  88.1740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5447 T22:   0.3054                                     
REMARK   3      T33:   0.5146 T12:  -0.0851                                     
REMARK   3      T13:   0.2040 T23:  -0.1055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  34.9274 L22:  20.4737                                     
REMARK   3      L33: -10.5251 L12:  -4.4364                                     
REMARK   3      L13:   1.0876 L23:  -7.4256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0269 S12:  -2.6982 S13:  -0.3709                       
REMARK   3      S21:   0.7597 S22:  -0.0254 S23:   0.0518                       
REMARK   3      S31:  -0.0789 S32:  -0.4801 S33:  -0.0015                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3AE5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029139.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
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 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19023                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
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     (%) : 77.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0210                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.350                              
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   (%): 65.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 8% 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 8.0, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 298K                                              
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       35.54900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.01150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.90400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.01150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.54900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.90400            
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: 12660 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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      -15.18     67.04                                   
REMARK 500    GLN A  62      -50.16   -128.40                                   
REMARK 500    GLU A  73      -86.40   -129.39                                   
REMARK 500    GLU A  74      134.16   -171.83                                   
REMARK 500    THR A 121     -165.74   -115.22                                   
REMARK 500    LYS A 140      -32.67   -131.23                                   
REMARK 500    ALA A 151       83.12     14.00                                   
REMARK 500    ASP A 152      -17.27     70.50                                   
REMARK 500    ASP A 170       40.57    -88.26                                   
REMARK 500    LEU A 180      -71.20    -78.24                                   
REMARK 500    MET A 285       50.60    -95.59                                   
REMARK 500    GLU A 286      -41.68   -133.83                                   
REMARK 500    LYS A 293     -125.97     64.10                                   
REMARK 500    ILE A 347      -63.80    -92.31                                   
REMARK 500    HIS A 365      -74.41   -140.23                                   
REMARK 500    ALA A 482     -149.86   -117.05                                   
REMARK 500    LYS A 544       62.07   -117.69                                   
REMARK 500    LYS A 556       43.69    -77.11                                   
REMARK 500    GLN A 569      -66.42   -144.21                                   
REMARK 500    GLU A 598     -166.93   -125.65                                   
REMARK 500    SER B  57       56.71    -93.48                                   
REMARK 500    SER B  64      -79.65   -155.18                                   
REMARK 500    ARG B  66       41.15     36.58                                   
REMARK 500    ILE B  69       37.55   -145.49                                   
REMARK 500    CYS B  70      -54.42   -127.24                                   
REMARK 500    CYS B  73       36.51    -90.67                                   
REMARK 500    THR B  91       -6.05    -59.61                                   
REMARK 500    ASP B 110      124.83    -32.21                                   
REMARK 500    LEU B 111      -10.34     72.45                                   
REMARK 500    GLU B 126       78.79     57.05                                   
REMARK 500    LEU B 155      -38.21   -134.29                                   
REMARK 500    CYS B 164      -74.41    -62.04                                   
REMARK 500    ASN B 174       55.45   -116.57                                   
REMARK 500    PHE B 198       32.30    -94.18                                   
REMARK 500    MET B 219       59.64     72.56                                   
REMARK 500    HIS C  29      -90.13    -96.01                                   
REMARK 500    LEU C  80       16.98   -140.25                                   
REMARK 500    CYS C  81       60.67     32.74                                   
REMARK 500    ASP D 123     -159.08   -142.03                                   
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  73   SG                                                     
REMARK 620 2 FES B 302   S1  118.2                                              
REMARK 620 3 FES B 302   S2  122.0  90.4                                        
REMARK 620 4 CYS B  85   SG  102.7 121.9 101.5                                  
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  110.2                                              
REMARK 620 3 SF4 B 303   S3  118.6 105.5                                        
REMARK 620 4 SF4 B 303   S4  111.8 104.9 104.7                                  
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  106.4                                              
REMARK 620 3 F3S B 304   S2  108.5 123.0                                        
REMARK 620 4 F3S B 304   S3  119.8 100.2  99.6                                  
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  65   SG                                                     
REMARK 620 2 FES B 302   S1  118.7                                              
REMARK 620 3 FES B 302   S2  107.1  90.3                                        
REMARK 620 N                    1     2                                         
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  101.2                                              
REMARK 620 3 SF4 B 303   S3  111.1 106.3                                        
REMARK 620 4 SF4 B 303   S4  126.9 104.9 104.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 221   SG                                                     
REMARK 620 2 F3S B 304   S1  110.8                                              
REMARK 620 3 F3S B 304   S3  123.7 100.2                                        
REMARK 620 4 F3S B 304   S4  100.4 122.5 100.5                                  
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 C 101   NE2                                                    
REMARK 620 2 HEM C1305   NA   93.2                                              
REMARK 620 3 HEM C1305   NB  105.1  88.7                                        
REMARK 620 4 HEM C1305   NC   89.9 176.8  89.6                                  
REMARK 620 5 HEM C1305   ND   79.1  90.6 175.8  90.9                            
REMARK 620 6 HIS D  79   NE2 169.0  82.1  84.9  95.1  90.9                      
REMARK 620 N                    1     2     3     4     5                       
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   90.9                                              
REMARK 620 3 F3S B 304   S3   85.9 100.1                                        
REMARK 620 4 F3S B 304   S4   92.2 158.8 101.0                                  
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   90.9                                              
REMARK 620 3 SF4 B 303   S2  125.1 105.2                                        
REMARK 620 4 SF4 B 303   S4  121.2 105.0 104.9                                  
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 FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 701                 
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 EPH D 1306                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRN D 1201                
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: 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: 3AED   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  3AE5 A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AE5 B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AE5 C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AE5 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    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    MLI  A 701       7                                                       
HET    HEM  C1305      43                                                       
HET    EPH  D1306      44                                                       
HET    MRN  D1201      20                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     MLI MALONATE ION                                                     
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-                
HETNAM   2 EPH  PHOSPHATIDYLETHANOLAMINE                                        
HETNAM     MRN 2-METHYL-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE                   
HETSYN     HEM HEME                                                             
HETSYN     MRN 2-METHYL-N-(3-ISOPROPOXY-PHENYL)-BENZAMIDE                       
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  FES    FE2 S2                                                       
FORMUL   7  SF4    FE4 S4                                                       
FORMUL   8  F3S    FE3 S4                                                       
FORMUL   9  MLI    C3 H2 O4 2-                                                  
FORMUL  10  HEM    C34 H32 FE N4 O4                                             
FORMUL  11  EPH    C39 H68 N O8 P                                               
FORMUL  12  MRN    C17 H19 N O2                                                 
HELIX    1   1 GLY A   29  GLY A   42  1                                  14    
HELIX    2   2 PHE A   52  ALA A   61  5                                  10    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  ASN A  113  1                                  21    
HELIX    5   5 ARG A  153  LEU A  167  1                                  15    
HELIX    6   6 TYR A  217  TYR A  221  5                                   5    
HELIX    7   7 GLY A  232  ALA A  241  1                                  10    
HELIX    8   8 GLU A  267  GLY A  273  1                                   7    
HELIX    9   9 ALA A  292  ALA A  296  5                                   5    
HELIX   10  10 SER A  297  GLU A  311  1                                  15    
HELIX   11  11 PRO A  330  LEU A  338  1                                   9    
HELIX   12  12 PRO A  339  PHE A  348  1                                  10    
HELIX   13  13 ASN A  413  CYS A  433  1                                  21    
HELIX   14  14 GLY A  447  ALA A  460  1                                  14    
HELIX   15  15 THR A  466  ALA A  481  1                                  16    
HELIX   16  16 VAL A  486  GLY A  502  1                                  17    
HELIX   17  17 ASP A  503  GLN A  505  5                                   3    
HELIX   18  18 ASN A  517  ARG A  543  1                                  27    
HELIX   19  19 MET B   43  GLU B   54  1                                  12    
HELIX   20  20 LEU B  115  ILE B  125  1                                  11    
HELIX   21  21 SER B  145  LYS B  151  1                                   7    
HELIX   22  22 CYS B  164  SER B  167  5                                   4    
HELIX   23  23 CYS B  168  ASN B  174  1                                   7    
HELIX   24  24 GLY B  180  TRP B  190  1                                  11    
HELIX   25  25 PHE B  198  ALA B  204  1                                   7    
HELIX   26  26 LYS B  205  GLN B  207  5                                   3    
HELIX   27  27 CYS B  221  CYS B  225  5                                   5    
HELIX   28  28 ASN B  230  TYR B  245  1                                  16    
HELIX   29  29 THR C    7  LEU C   20  1                                  14    
HELIX   30  30 SER C   36  LEU C   66  1                                  31    
HELIX   31  31 ASN C   69  SER C   79  1                                  11    
HELIX   32  32 THR C   85  GLY C  114  1                                  30    
HELIX   33  33 THR C  118  ALA C  142  1                                  25    
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 ASP D   95  ASP D  123  1                                  29    
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 204   N  VAL A  16           
SHEET    3   A 4 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    4   A 4 TYR A 177  GLU A 185 -1  N  PHE A 178   O  LEU A 195           
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  VAL A  48           
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 386  ALA A 395  1  O  TYR A 394   N  THR A 210           
SHEET    6   B 6 GLN A 378  VAL A 383 -1  N  VAL A 379   O  VAL A 390           
SHEET    1   C 3 ILE A  65  ASN A  66  0                                        
SHEET    2   C 3 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  ARG A 600   N  HIS A 583           
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  VAL A 360   N  VAL A 322           
SHEET    1   G 2 ILE A 371  PRO A 372  0                                        
SHEET    2   G 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   H 2 ILE A 464  ARG A 465  0                                        
SHEET    2   H 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   I 2 PHE A 484  ARG A 485  0                                        
SHEET    2   I 2 ALA A 551  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    1   J 5 HIS B  29  ASP B  36  0                                        
SHEET    2   J 5 ILE B  11  ARG B  18 -1  N  ARG B  18   O  HIS B  29           
SHEET    3   J 5 SER B  97  TYR B 100  1  O  ILE B  99   N  ALA B  15           
SHEET    4   J 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   J 5 GLY B  80  LEU B  83 -1  O  THR B  82   N  MET B  75           
SHEET    1   K 2 VAL B 107  LYS B 109  0                                        
SHEET    2   K 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  LYS B 109           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  2.01  
LINK         SG  CYS B  73                FE2  FES B 302     1555   1555  1.92  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.06  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.14  
LINK         SG  CYS B  65                FE1  FES B 302     1555   1555  2.28  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.29  
LINK         SG  CYS B 221                FE3  F3S B 304     1555   1555  2.32  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.32  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.35  
LINK         SG  CYS B  85                FE2  FES B 302     1555   1555  2.57  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.63  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.69  
SITE     1 AC1 33 GLY A  26  ALA A  27  GLY A  28  ALA A  30                    
SITE     2 AC1 33 THR A  49  LYS A  50  LEU A  51  SER A  56                    
SITE     3 AC1 33 HIS A  57  THR A  58  ALA A  60  ALA A  61                    
SITE     4 AC1 33 GLN A  62  GLY A  63  GLY A  64  TYR A 177                    
SITE     5 AC1 33 PHE A 178  ALA A 179  ALA A 213  THR A 214                    
SITE     6 AC1 33 GLY A 215  THR A 225  SER A 226  ASP A 233                    
SITE     7 AC1 33 LEU A 264  HIS A 365  TYR A 366  GLU A 398                    
SITE     8 AC1 33 ARG A 409  ALA A 412  SER A 414  LEU A 415                    
SITE     9 AC1 33 MLI A 701                                                     
SITE     1 AC2  7 SER B  64  CYS B  65  ARG B  66  CYS B  70                    
SITE     2 AC2  7 GLY B  71  CYS B  73  CYS B  85                               
SITE     1 AC3  8 CYS B 158  ILE B 159  CYS B 161  ALA B 162                    
SITE     2 AC3  8 CYS B 164  ALA B 182  CYS B 225  PRO B 226                    
SITE     1 AC4  9 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC4  9 HIS B 216  THR B 217  MET B 219  ASN B 220                    
SITE     3 AC4  9 CYS B 221                                                     
SITE     1 AC5 11 GLY A  63  PHE A 131  HIS A 254  LEU A 264                    
SITE     2 AC5 11 THR A 266  GLU A 267  ARG A 298  HIS A 365                    
SITE     3 AC5 11 ARG A 409  ALA A 412  FAD A 700                               
SITE     1 AC6 14 HIS C  45  ARG C  46  GLY C  49  LEU C  52                    
SITE     2 AC6 14 SER C  53  HIS C 101  HIS C 108  ARG D  47                    
SITE     3 AC6 14 SER D  50  LEU D  53  LEU D  54  LEU D  57                    
SITE     4 AC6 14 HIS D  79  GLY D  83                                          
SITE     1 AC7  5 ALA D  60  TYR D  61  CYS D 127  VAL D 130                    
SITE     2 AC7  5 TRP D 134                                                     
SITE     1 AC8  7 TRP B 173  ILE C  30  TRP C  35  MET C  39                    
SITE     2 AC8  7 SER C  42  ARG C  46  TYR D  91                               
CRYST1   71.098   83.808  294.023  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      0.014065  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011932  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003401        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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