GenomeNet

Database: PDB
Entry: 3AE2
LinkDB: 3AE2
Original site: 3AE2 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AE2              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 2-HYDROXY-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 3AE2    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-HYDROXY-N-PHENYL-BENZAMIDE                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 33385                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1688                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.17                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2195                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 127                          
REMARK   3   BIN FREE R VALUE                    : 0.3410                       
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            : 1                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -0.40000                                             
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): 0.409         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.329         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.194        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8866 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):     2 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12019 ; 1.068 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):     1 ; 0.139 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 5.251 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;35.199 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;18.380 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;16.469 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1304 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6658 ; 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 ; 0.194 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):     2 ; 0.001 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8676 ; 0.371 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3455 ; 0.502 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3326 ; 0.881 ; 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    69                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9030 -26.6130  22.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2664 T22:   0.2360                                     
REMARK   3      T33:   0.4570 T12:  -0.0294                                     
REMARK   3      T13:   0.0444 T23:   0.1068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4305 L22:   2.0416                                     
REMARK   3      L33:   3.4014 L12:  -1.6323                                     
REMARK   3      L13:  -0.8896 L23:   0.5468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1126 S12:  -0.3773 S13:  -0.1654                       
REMARK   3      S21:  -0.1495 S22:   0.0675 S23:  -0.1948                       
REMARK   3      S31:   0.4552 S32:   0.4089 S33:   0.0452                       
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    70        A   260                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6070 -15.2360  16.9130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2338 T22:   0.1603                                     
REMARK   3      T33:   0.3975 T12:  -0.0882                                     
REMARK   3      T13:   0.0256 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9226 L22:   1.3548                                     
REMARK   3      L33:   3.5147 L12:  -0.3540                                     
REMARK   3      L13:  -0.4545 L23:  -0.5172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0038 S12:  -0.0193 S13:   0.0877                       
REMARK   3      S21:  -0.0633 S22:  -0.0244 S23:   0.0558                       
REMARK   3      S31:  -0.3361 S32:   0.0370 S33:   0.0206                       
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   261        A   340                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6980   9.4400  23.1440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9038 T22:   0.0904                                     
REMARK   3      T33:   0.7698 T12:  -0.0844                                     
REMARK   3      T13:   0.1062 T23:  -0.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2700 L22:   2.8451                                     
REMARK   3      L33:   6.2245 L12:   0.8809                                     
REMARK   3      L13:  -2.5401 L23:  -1.2885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6345 S12:  -0.0320 S13:   0.8943                       
REMARK   3      S21:   0.1808 S22:  -0.2263 S23:  -0.0178                       
REMARK   3      S31:  -1.5771 S32:  -0.0147 S33:  -0.4081                       
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 :   A   341        A   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7200 -11.7890  15.2360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2598 T22:   0.2191                                     
REMARK   3      T33:   0.4516 T12:  -0.1268                                     
REMARK   3      T13:   0.0114 T23:   0.0408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4945 L22:   2.7687                                     
REMARK   3      L33:   2.9620 L12:  -0.6575                                     
REMARK   3      L13:  -0.9127 L23:   0.5772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1138 S12:   0.0771 S13:   0.2098                       
REMARK   3      S21:   0.0556 S22:  -0.1882 S23:   0.0009                       
REMARK   3      S31:  -0.3959 S32:   0.1123 S33:   0.0744                       
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 :   A   430        A   514                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.3110 -15.9690  21.0310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2109 T22:   0.7032                                     
REMARK   3      T33:   0.4331 T12:  -0.1404                                     
REMARK   3      T13:   0.0540 T23:   0.0533                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8839 L22:   2.4039                                     
REMARK   3      L33:   2.2381 L12:  -0.2164                                     
REMARK   3      L13:  -0.6674 L23:   0.1035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1408 S12:  -0.3125 S13:   0.0448                       
REMARK   3      S21:  -0.2818 S22:   0.0010 S23:  -0.3618                       
REMARK   3      S31:  -0.1392 S32:   1.1762 S33:   0.1398                       
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 :   A   515        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8950  -5.9950   4.2220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4776 T22:   0.2716                                     
REMARK   3      T33:   0.4063 T12:  -0.1766                                     
REMARK   3      T13:   0.0955 T23:   0.0492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7910 L22:   1.6559                                     
REMARK   3      L33:   4.0811 L12:  -0.3153                                     
REMARK   3      L13:  -0.2863 L23:  -1.2039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0260 S12:   0.2298 S13:   0.5165                       
REMARK   3      S21:  -0.1914 S22:  -0.1805 S23:  -0.2608                       
REMARK   3      S31:  -0.8916 S32:   0.6028 S33:   0.1544                       
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 :   B     9        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2000 -12.4740  46.0760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2653 T22:   0.7124                                     
REMARK   3      T33:   0.3624 T12:  -0.2724                                     
REMARK   3      T13:  -0.0139 T23:  -0.0320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3648 L22:   3.4691                                     
REMARK   3      L33:   3.5914 L12:   0.2369                                     
REMARK   3      L13:  -0.1055 L23:   0.9177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:  -0.7376 S13:   0.3119                       
REMARK   3      S21:   0.4218 S22:  -0.0877 S23:  -0.3561                       
REMARK   3      S31:  -0.4590 S32:   1.2679 S33:   0.0538                       
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 :   B   107        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3660 -24.4640  40.0670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3323 T22:   0.1233                                     
REMARK   3      T33:   0.4623 T12:  -0.0558                                     
REMARK   3      T13:   0.0651 T23:  -0.0611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4477 L22:   1.0741                                     
REMARK   3      L33:   5.0001 L12:  -0.2841                                     
REMARK   3      L13:  -1.4154 L23:  -0.5364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0295 S12:   0.1872 S13:  -0.0151                       
REMARK   3      S21:   0.0915 S22:  -0.1387 S23:   0.2891                       
REMARK   3      S31:   0.2769 S32:  -0.4061 S33:   0.1682                       
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     6        C    65                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0990 -30.2850  58.2900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7216 T22:   0.2945                                     
REMARK   3      T33:   0.6293 T12:   0.0275                                     
REMARK   3      T13:   0.0950 T23:   0.0788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4336 L22:   0.6644                                     
REMARK   3      L33:   4.4086 L12:   0.2706                                     
REMARK   3      L13:  -1.0335 L23:  -0.6740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2327 S12:  -0.2452 S13:  -0.0262                       
REMARK   3      S21:   0.2576 S22:   0.0276 S23:  -0.0165                       
REMARK   3      S31:   0.5116 S32:   0.8116 S33:   0.2051                       
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    66        C   107                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1870 -24.4570  85.2430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1684 T22:   0.6608                                     
REMARK   3      T33:   0.8344 T12:  -0.1206                                     
REMARK   3      T13:   0.1034 T23:   0.0322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1645 L22:   4.5392                                     
REMARK   3      L33:   6.0116 L12:  -0.2955                                     
REMARK   3      L13:   0.4505 L23:  -4.0753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1901 S12:  -0.5478 S13:   0.0484                       
REMARK   3      S21:   1.2332 S22:  -0.1510 S23:  -0.0822                       
REMARK   3      S31:  -1.2423 S32:   0.6925 S33:  -0.0392                       
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   108        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.7700 -13.1220  65.7120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6550 T22:   0.1404                                     
REMARK   3      T33:   0.5806 T12:   0.0873                                     
REMARK   3      T13:   0.2458 T23:  -0.0139                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4967 L22:   6.5950                                     
REMARK   3      L33:   9.6562 L12:   1.7518                                     
REMARK   3      L13:   1.3828 L23:   1.0339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3149 S12:  -0.1277 S13:  -0.1521                       
REMARK   3      S21:   0.3589 S22:  -0.1197 S23:   0.0995                       
REMARK   3      S31:  -1.0785 S32:  -0.6318 S33:  -0.1952                       
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    71                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6720 -29.8810  66.6460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3497 T22:   0.1205                                     
REMARK   3      T33:   0.4457 T12:   0.0193                                     
REMARK   3      T13:   0.1905 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4485 L22:   4.6745                                     
REMARK   3      L33:  13.1683 L12:   0.9683                                     
REMARK   3      L13:  -1.9797 L23:   2.2755                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3457 S12:   0.0146 S13:  -0.5721                       
REMARK   3      S21:   0.1500 S22:  -0.0199 S23:   0.3984                       
REMARK   3      S31:  -0.5216 S32:  -0.6708 S33:   0.3656                       
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    72        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2600 -36.1660  64.1730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7023 T22:   0.1586                                     
REMARK   3      T33:   0.6524 T12:  -0.0052                                     
REMARK   3      T13:   0.1977 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1409 L22:  -0.1006                                     
REMARK   3      L33:   6.5634 L12:   1.5044                                     
REMARK   3      L13:  -2.8826 L23:  -3.1257                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2703 S12:   0.0316 S13:  -0.5307                       
REMARK   3      S21:  -0.2551 S22:  -0.1769 S23:  -0.0895                       
REMARK   3      S31:   0.9470 S32:   0.7586 S33:   0.4472                       
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    97        D   124                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2720 -42.5090  74.8730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8047 T22:   0.0273                                     
REMARK   3      T33:   0.6171 T12:  -0.0127                                     
REMARK   3      T13:   0.2108 T23:   0.0825                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4550 L22:   3.6766                                     
REMARK   3      L33:  10.5105 L12:  -1.5618                                     
REMARK   3      L13:  -8.0375 L23:   2.0989                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0806 S12:  -0.0738 S13:  -0.7984                       
REMARK   3      S21:  -0.1012 S22:  -0.2718 S23:  -0.0101                       
REMARK   3      S31:   0.0521 S32:  -0.1733 S33:   0.3524                       
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   125        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5420 -26.7000  88.3120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2261 T22:   0.4997                                     
REMARK   3      T33:   0.3718 T12:   0.0192                                     
REMARK   3      T13:   0.1493 T23:   0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  29.7554 L22:   7.1288                                     
REMARK   3      L33:   2.2491 L12:  -1.4710                                     
REMARK   3      L13:  -6.9737 L23:  -0.1653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0215 S12:  -0.9905 S13:   0.1204                       
REMARK   3      S21:   1.7852 S22:  -0.7750 S23:   0.7014                       
REMARK   3      S31:  -0.8816 S32:  -0.8578 S33:  -0.2465                       
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 3AE2 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 RCSB029136.                                      
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                             : 7.2                                
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   : 33467                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2880                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.160                              
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   (%): 65.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 7% PEG 4000, 200MM      
REMARK 280  SUCROSE, 100MM NACL, 10MM CACL2, 0.5MM EDTA, 3% 1,6-HAXANEDIOL,     
REMARK 280  0.5% N-DECYL-BETA-D-MALTOSIDE, PH 7.2, 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       35.92750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.30750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.10050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.30750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.92750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.10050            
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: 12600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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      -13.17     66.39                                   
REMARK 500    SER A  56      150.20    -49.17                                   
REMARK 500    GLN A  62      -53.27   -140.57                                   
REMARK 500    MET A  72      -76.57    -88.32                                   
REMARK 500    HIS A 145       79.11   -117.38                                   
REMARK 500    ALA A 151     -137.51     57.01                                   
REMARK 500    ASP A 170       39.78    -83.24                                   
REMARK 500    LEU A 180      -66.77    -92.81                                   
REMARK 500    THR A 256       77.72   -112.28                                   
REMARK 500    ARG A 283       87.54    -68.66                                   
REMARK 500    LYS A 293     -132.93     57.18                                   
REMARK 500    ARG A 313       47.78    -93.34                                   
REMARK 500    HIS A 321     -168.16   -123.26                                   
REMARK 500    HIS A 365      -57.25   -143.43                                   
REMARK 500    CYS A 401       82.62   -153.45                                   
REMARK 500    SER A 403       76.52     29.42                                   
REMARK 500    LYS A 544       63.65   -102.76                                   
REMARK 500    GLN A 569      -96.24    -40.88                                   
REMARK 500    ASN A 608      108.53   -160.53                                   
REMARK 500    ARG B  10       81.79   -165.24                                   
REMARK 500    SER B  64      -62.99   -144.11                                   
REMARK 500    ASP B 110     -126.00     43.72                                   
REMARK 500    GLU B 126       69.86     60.13                                   
REMARK 500    HIS C  29      -83.41   -120.92                                   
REMARK 500    ASP D  95      -72.96    -92.62                                   
REMARK 500    LYS D 135       36.46    -77.95                                   
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  65   SG                                                     
REMARK 620 2 FES B 302   S1  125.9                                              
REMARK 620 3 FES B 302   S2  111.1  91.9                                        
REMARK 620 4 CYS B  70   SG  113.1  98.1 115.1                                  
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 C 101   NE2                                                    
REMARK 620 2 HEM C1305   NA   90.6                                              
REMARK 620 3 HEM C1305   NB   93.6  89.7                                        
REMARK 620 4 HEM C1305   NC   88.2 178.3  89.2                                  
REMARK 620 5 HEM C1305   ND   88.0  91.0 178.3  90.2                            
REMARK 620 6 HIS D  79   NE2 175.4  86.7  82.7  94.4  95.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  112.5                                              
REMARK 620 3 FES B 302   S2  128.5  92.2                                        
REMARK 620 4 CYS B  85   SG  106.3 119.0  98.7                                  
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  112.6                                              
REMARK 620 3 F3S B 304   S3  123.0  98.8                                        
REMARK 620 4 F3S B 304   S4  103.5 120.4  99.1                                  
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   98.1                                              
REMARK 620 3 F3S B 304   S2  107.8 121.0                                        
REMARK 620 4 F3S B 304   S3  133.4  98.8  99.8                                  
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  118.4                                              
REMARK 620 3 SF4 B 303   S2  114.3 105.9                                        
REMARK 620 4 SF4 B 303   S4  107.7 103.1 106.2                                  
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   87.1                                              
REMARK 620 3 F3S B 304   S3   90.6 101.2                                        
REMARK 620 4 F3S B 304   S4   95.8 157.6 101.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 161   SG                                                     
REMARK 620 2 SF4 B 303   S1   96.6                                              
REMARK 620 3 SF4 B 303   S3  129.7 105.9                                        
REMARK 620 4 SF4 B 303   S4  112.1 103.1 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 303   S2  116.5                                              
REMARK 620 3 SF4 B 303   S3   88.2 106.2                                        
REMARK 620 4 SF4 B 303   S4  129.9 105.7 105.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 164   SG                                                     
REMARK 620 2 SF4 B 303   S1   98.6                                              
REMARK 620 3 SF4 B 303   S2  123.4 105.8                                        
REMARK 620 4 SF4 B 303   S3  115.2 105.5 106.2                                  
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 SLI C 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: 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: 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  3AE2 A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AE2 B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AE2 C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AE2 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    SLI  C1201      16                                                       
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     SLI 2-HYDROXY-N-PHENYLBENZAMIDE                                      
HETSYN     HEM HEME                                                             
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  FES    FE2 S2                                                       
FORMUL   7  SF4    FE4 S4                                                       
FORMUL   8  F3S    FE3 S4                                                       
FORMUL   9  MLI    C3 H2 O4 2-                                                  
FORMUL  10  HEM    C34 H32 FE N4 O4                                             
FORMUL  11  EPH    C39 H68 N O8 P                                               
FORMUL  12  SLI    C13 H11 N O2                                                 
FORMUL  13  HOH   *(H2 O)                                                       
HELIX    1   1 GLY A   28  ALA A   41  1                                  14    
HELIX    2   2 PHE A   52  ALA A   61  5                                  10    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  GLY A  115  1                                  23    
HELIX    5   5 ARG A  153  LEU A  167  1                                  15    
HELIX    6   6 TYR A  217  TYR A  221  5                                   5    
HELIX    7   7 GLY A  232  ALA A  241  1                                  10    
HELIX    8   8 GLU A  267  GLY A  273  1                                   7    
HELIX    9   9 PHE A  284  ALA A  289  1                                   6    
HELIX   10  10 ALA A  292  ALA A  296  5                                   5    
HELIX   11  11 SER A  297  GLU A  311  1                                  15    
HELIX   12  12 PRO A  330  LEU A  338  1                                   9    
HELIX   13  13 LEU A  338  GLY A  350  1                                  13    
HELIX   14  14 ASN A  413  GLU A  431  1                                  19    
HELIX   15  15 GLY A  447  PHE A  459  1                                  13    
HELIX   16  16 THR A  466  ALA A  481  1                                  16    
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 PRO A  575  HIS A  579  5                                   5    
HELIX   20  20 ASN B   38  CYS B   40  5                                   3    
HELIX   21  21 MET B   43  ILE B   55  1                                  13    
HELIX   22  22 LEU B  115  SER B  124  1                                  10    
HELIX   23  23 ASP B  133  GLU B  137  5                                   5    
HELIX   24  24 SER B  145  LYS B  151  1                                   7    
HELIX   25  25 CYS B  164  SER B  167  5                                   4    
HELIX   26  26 CYS B  168  GLY B  175  1                                   8    
HELIX   27  27 LEU B  179  ILE B  192  1                                  14    
HELIX   28  28 PHE B  198  LYS B  205  1                                   8    
HELIX   29  29 MET B  219  CYS B  225  1                                   7    
HELIX   30  30 ASN B  230  TYR B  245  1                                  16    
HELIX   31  31 THR C    7  GLY C   21  1                                  15    
HELIX   32  32 SER C   36  LEU C   66  1                                  31    
HELIX   33  33 ASN C   69  CYS C   81  1                                  13    
HELIX   34  34 PRO C   84  LEU C  113  1                                  30    
HELIX   35  35 THR C  118  ALA C  142  1                                  25    
HELIX   36  36 LYS D   37  ASN D   63  1                                  27    
HELIX   37  37 CYS D   65  VAL D   92  1                                  28    
HELIX   38  38 ASP D   95  ASP D  123  1                                  29    
HELIX   39  39 VAL D  124  LYS D  135  1                                  12    
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  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 180   O  ILE A 193           
SHEET    1   B 6 SER A 172  VAL A 175  0                                        
SHEET    2   B 6 THR A  45  THR A  49  1  N  THR A  45   O  SER A 172           
SHEET    3   B 6 ALA A  22  VAL A  25  1  N  VAL A  24   O  VAL A  48           
SHEET    4   B 6 ASN A 209  VAL A 212  1  O  VAL A 211   N  VAL A  23           
SHEET    5   B 6 GLN A 386  ALA A 395  1  O  TYR A 394   N  VAL A 212           
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 GLN A 143  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    3   C 3 GLN A 128  SER A 135 -1  N  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  ASP A 589 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 LYS A 594  PRO A 601 -1  O  ARG A 600   N  HIS A 583           
SHEET    1   E 4 VAL A 251  ILE A 258  0                                        
SHEET    2   E 4 ILE A 358  ASN A 367 -1  O  TYR A 366   N  GLN A 252           
SHEET    3   E 4 VAL A 322  GLN A 325 -1  N  VAL A 322   O  VAL A 360           
SHEET    4   E 4 ILE A 275  ILE A 277 -1  N  ILE A 275   O  GLN A 325           
SHEET    1   F 2 ILE A 371  PRO A 372  0                                        
SHEET    2   F 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   G 2 ILE A 464  ARG A 465  0                                        
SHEET    2   G 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   H 2 PHE A 484  ARG A 485  0                                        
SHEET    2   H 2 ALA A 551  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    1   I 5 HIS B  29  ASP B  36  0                                        
SHEET    2   I 5 ILE B  11  ARG B  18 -1  N  ARG B  18   O  HIS B  29           
SHEET    3   I 5 SER B  97  TYR B 100  1  O  SER B  97   N  ALA B  15           
SHEET    4   I 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   I 5 GLY B  80  LEU B  83 -1  O  THR B  82   N  MET B  75           
SHEET    1   J 2 VAL B 107  LYS B 109  0                                        
SHEET    2   J 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  LYS B 109           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  1.95  
LINK         SG  CYS B  65                FE2  FES B 302     1555   1555  2.03  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.10  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.20  
LINK         SG  CYS B  73                FE1  FES B 302     1555   1555  2.22  
LINK         SG  CYS B  70                FE2  FES B 302     1555   1555  2.22  
LINK         SG  CYS B 221                FE3  F3S B 304     1555   1555  2.23  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.25  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.31  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.32  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.33  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.38  
LINK         SG  CYS B 164                FE4  SF4 B 303     1555   1555  2.39  
LINK         SG  CYS B  85                FE1  FES B 302     1555   1555  2.45  
SITE     1 AC1 36 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 36 ALA A  30  VAL A  48  THR A  49  LYS A  50                    
SITE     3 AC1 36 LEU A  51  SER A  56  HIS A  57  THR A  58                    
SITE     4 AC1 36 ALA A  60  ALA A  61  GLN A  62  GLY A  63                    
SITE     5 AC1 36 GLY A  64  TYR A 177  PHE A 178  ALA A 179                    
SITE     6 AC1 36 THR A 214  GLY A 215  THR A 225  ASP A 233                    
SITE     7 AC1 36 LEU A 264  HIS A 365  TYR A 366  GLY A 397                    
SITE     8 AC1 36 GLU A 398  ARG A 409  ALA A 412  ASN A 413                    
SITE     9 AC1 36 SER A 414  LEU A 415  LEU A 418  MLI A 701                    
SITE     1 AC2  8 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC2  8 CYS B  70  GLY B  71  CYS B  73  CYS B  85                    
SITE     1 AC3  8 CYS B 158  ILE B 159  LEU B 160  CYS B 161                    
SITE     2 AC3  8 CYS B 163  CYS B 164  CYS B 225  PRO B 226                    
SITE     1 AC4 10 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC4 10 HIS B 216  THR B 217  ILE B 218  MET B 219                    
SITE     3 AC4 10 ASN B 220  CYS B 221                                          
SITE     1 AC5 12 GLN A  62  GLY A  63  PHE A 131  HIS A 254                    
SITE     2 AC5 12 LEU A 264  THR A 266  GLU A 267  ARG A 298                    
SITE     3 AC5 12 HIS A 365  ARG A 409  ALA A 412  FAD A 700                    
SITE     1 AC6 13 HIS C  45  ARG C  46  GLY C  49  LEU C  52                    
SITE     2 AC6 13 SER C  53  HIS C 101  HIS C 108  SLI C1201                    
SITE     3 AC6 13 ARG D  47  LEU D  53  LEU D  54  HIS D  79                    
SITE     4 AC6 13 GLY D  83                                                     
SITE     1 AC7  2 TYR D  61  TRP D 134                                          
SITE     1 AC8  7 HIS B 216  HOH B1202  SER C  42  ILE C  43                    
SITE     2 AC8  7 ARG C  46  HEM C1305  TYR D  91                               
CRYST1   71.855   84.201  294.615  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      0.013917  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011876  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003394        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system