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Database: PDB
Entry: 3AEC
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AEC              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 2-IODO-N-(1-METHYLETHYL)-BENZAMID                                    
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 3AEC    0                                                
JRNL        AUTH   S.HARADA,T.SASAKI,M.SHINDO,Y.KIDO,D.K.INAOKA,J.OMORI,        
JRNL        AUTH 2 A.OSANAI,K.SAKAMOTO,J.MAO,S.MATSUOKA,M.INOUE,T.HONMA,        
JRNL        AUTH 3 A.TANAKA,K.KITA                                              
JRNL        TITL   CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II  
JRNL        TITL 2 BOUND WITH 2-IODO-N-(1-METHYLETHYL)-BENZAMID                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20635                          
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) : 0.248                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1044                            
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) : 3.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.70                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1296                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
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          : 172                                     
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) : 92.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.46000                                             
REMARK   3    B22 (A**2) : 0.30000                                              
REMARK   3    B33 (A**2) : 0.16000                                              
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): 0.722         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.570         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 80.878        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.892                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.850                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8856 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12007 ; 0.857 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 4.109 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;34.273 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;15.961 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;11.184 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1305 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6644 ; 0.002 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5412 ; 0.091 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8677 ; 0.168 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3444 ; 0.129 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3313 ; 0.232 ; 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): -16.1540 -17.6460  18.0330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5522 T22:   0.5090                                     
REMARK   3      T33:   0.5063 T12:  -0.0935                                     
REMARK   3      T13:   0.0341 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1076 L22:   1.4483                                     
REMARK   3      L33:   3.7833 L12:  -0.2911                                     
REMARK   3      L13:  -0.2003 L23:  -0.2571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0212 S12:  -0.1196 S13:  -0.0807                       
REMARK   3      S21:  -0.0363 S22:   0.0039 S23:   0.0784                       
REMARK   3      S31:  -0.2227 S32:   0.0473 S33:   0.0173                       
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   348                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7720   8.6700  24.4790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9965 T22:   0.3321                                     
REMARK   3      T33:   0.7753 T12:  -0.0948                                     
REMARK   3      T13:   0.0777 T23:  -0.1458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4853 L22:   0.9462                                     
REMARK   3      L33:   4.3308 L12:   0.4766                                     
REMARK   3      L13:  -2.3586 L23:  -1.8573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1025 S12:  -0.1994 S13:   0.4591                       
REMARK   3      S21:   0.4278 S22:  -0.1250 S23:  -0.0484                       
REMARK   3      S31:  -1.1766 S32:  -0.2764 S33:   0.0225                       
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   349        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6370 -10.9100  11.8190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6518 T22:   0.5941                                     
REMARK   3      T33:   0.4938 T12:  -0.1571                                     
REMARK   3      T13:   0.0466 T23:   0.0561                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7173 L22:   1.2215                                     
REMARK   3      L33:   1.9840 L12:  -0.2519                                     
REMARK   3      L13:  -0.5874 L23:  -0.3545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0650 S12:   0.0698 S13:   0.0778                       
REMARK   3      S21:  -0.0970 S22:  -0.0601 S23:  -0.1158                       
REMARK   3      S31:  -0.4360 S32:   0.6017 S33:  -0.0048                       
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   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5530 -12.2290  46.1780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4967 T22:   1.1072                                     
REMARK   3      T33:   0.5436 T12:  -0.2335                                     
REMARK   3      T13:  -0.0672 T23:  -0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3339 L22:   3.9044                                     
REMARK   3      L33:   4.0994 L12:   0.2013                                     
REMARK   3      L13:  -0.1574 L23:   1.2025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1067 S12:  -0.7594 S13:   0.4341                       
REMARK   3      S21:   0.3036 S22:  -0.1445 S23:  -0.3739                       
REMARK   3      S31:  -0.3441 S32:   1.2307 S33:   0.0378                       
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   107        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2450 -24.2350  40.0940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7165 T22:   0.4014                                     
REMARK   3      T33:   0.6489 T12:  -0.0129                                     
REMARK   3      T13:   0.0093 T23:  -0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9831 L22:   0.1409                                     
REMARK   3      L33:   4.8302 L12:  -0.8463                                     
REMARK   3      L13:  -1.4160 L23:  -0.8366                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0256 S12:   0.1554 S13:  -0.1276                       
REMARK   3      S21:  -0.1332 S22:   0.0122 S23:   0.2473                       
REMARK   3      S31:   0.1302 S32:  -0.6825 S33:   0.0134                       
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 :   C     6        C    47                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.0490 -28.3250  51.4830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8911 T22:   0.4719                                     
REMARK   3      T33:   0.4965 T12:   0.0296                                     
REMARK   3      T13:   0.0220 T23:   0.2597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2029 L22:   2.6285                                     
REMARK   3      L33:   5.8110 L12:  -1.0358                                     
REMARK   3      L13:  -2.5986 L23:   3.1320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0291 S12:   0.1544 S13:  -0.1161                       
REMARK   3      S21:   0.3749 S22:   0.1252 S23:  -0.0865                       
REMARK   3      S31:  -0.1235 S32:   0.8510 S33:  -0.1543                       
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    48        C   106                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.1920 -27.2840  84.3750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2874 T22:   0.4303                                     
REMARK   3      T33:   0.4500 T12:  -0.0127                                     
REMARK   3      T13:   0.1409 T23:   0.0434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0844 L22:   5.8499                                     
REMARK   3      L33:   9.9826 L12:   2.4026                                     
REMARK   3      L13:  -1.0016 L23:  -3.8458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0920 S12:  -1.0272 S13:  -0.1412                       
REMARK   3      S21:   1.0720 S22:  -0.1474 S23:  -0.3469                       
REMARK   3      S31:  -0.6738 S32:   0.4760 S33:   0.0554                       
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   107        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.6340 -12.9350  65.6630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8482 T22:   0.0339                                     
REMARK   3      T33:   0.7371 T12:   0.0106                                     
REMARK   3      T13:   0.1190 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5006 L22:   6.4151                                     
REMARK   3      L33:  22.6394 L12:   2.3213                                     
REMARK   3      L13:  -5.1226 L23:   0.6324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6890 S12:   0.3276 S13:   0.0842                       
REMARK   3      S21:   0.3952 S22:  -0.0622 S23:   0.2594                       
REMARK   3      S31:  -1.0672 S32:  -0.6822 S33:  -0.6268                       
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    67                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.6850 -28.8400  65.2490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6289 T22:   0.7127                                     
REMARK   3      T33:   0.5839 T12:   0.0590                                     
REMARK   3      T13:   0.0137 T23:   0.1573                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0822 L22:   8.9335                                     
REMARK   3      L33:  17.4591 L12:   2.3154                                     
REMARK   3      L13:  -2.7534 L23:   1.5244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0461 S12:   0.0453 S13:  -0.1615                       
REMARK   3      S21:  -0.0987 S22:   0.2811 S23:   0.3507                       
REMARK   3      S31:  -0.9138 S32:   0.4581 S33:  -0.3272                       
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    68        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.1090 -35.4440  66.3630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0399 T22:   0.1457                                     
REMARK   3      T33:   0.7114 T12:  -0.0574                                     
REMARK   3      T13:   0.1666 T23:   0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1542 L22:   2.2726                                     
REMARK   3      L33:   7.0111 L12:   1.2182                                     
REMARK   3      L13:   2.1779 L23:  -1.6643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0161 S12:   0.0802 S13:  -0.6772                       
REMARK   3      S21:   0.1493 S22:  -0.3406 S23:   0.2312                       
REMARK   3      S31:   0.1841 S32:   0.2412 S33:   0.3567                       
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): -36.8810 -42.0510  75.1390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1392 T22:   0.2742                                     
REMARK   3      T33:   0.7578 T12:  -0.0285                                     
REMARK   3      T13:   0.2537 T23:   0.2065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4533 L22:   6.1754                                     
REMARK   3      L33:  22.3815 L12:  -1.4955                                     
REMARK   3      L13: -12.2388 L23:   5.0736                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0688 S12:  -0.7801 S13:   0.1371                       
REMARK   3      S21:   0.0537 S22:   0.2972 S23:  -0.8124                       
REMARK   3      S31:   0.6590 S32:   0.0499 S33:  -0.3660                       
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): -42.0140 -26.3370  88.4730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3137 T22:   0.4731                                     
REMARK   3      T33:   0.9588 T12:  -0.0346                                     
REMARK   3      T13:   0.0999 T23:   0.0736                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  36.0313 L22:  33.1170                                     
REMARK   3      L33:  12.1283 L12:  -0.6746                                     
REMARK   3      L13: -12.2028 L23:  12.3283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.4674 S12:  -2.0795 S13:   2.3572                       
REMARK   3      S21:  -1.0722 S22:  -0.4162 S23:   2.2929                       
REMARK   3      S31:  -1.2862 S32:  -1.7525 S33:  -1.0512                       
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 3AEC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029146.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.30001                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20826                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.16000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.4310                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.520                              
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   (%): 65.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
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       35.48300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.62700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.99700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.62700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.48300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.99700            
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: 12950 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS B    73    FE2   FES B   302              1.87            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  11      -22.64     65.23                                   
REMARK 500    ARG A  55       32.39    -89.71                                   
REMARK 500    SER A  56     -138.60    -76.69                                   
REMARK 500    ALA A  68       57.44    -91.31                                   
REMARK 500    TRP A  90       17.63     59.30                                   
REMARK 500    THR A 121     -169.90   -112.63                                   
REMARK 500    ARG A 146       24.98   -140.91                                   
REMARK 500    VAL A 150       58.52   -107.57                                   
REMARK 500    ALA A 151       72.50     43.68                                   
REMARK 500    ASP A 152      -17.41     69.72                                   
REMARK 500    ARG A 153       52.12   -114.53                                   
REMARK 500    MET A 285       45.92    -78.47                                   
REMARK 500    TYR A 288      -60.81    -96.82                                   
REMARK 500    LYS A 293     -133.77     49.69                                   
REMARK 500    ARG A 313       44.18   -102.28                                   
REMARK 500    ASP A 320      -36.16   -134.68                                   
REMARK 500    HIS A 365      -72.30   -131.54                                   
REMARK 500    ALA A 481       55.33    -95.62                                   
REMARK 500    TRP A 516       74.94     46.97                                   
REMARK 500    PHE A 555       77.26   -111.41                                   
REMARK 500    GLN A 569      -73.24   -159.35                                   
REMARK 500    GLN A 577       32.74    -91.69                                   
REMARK 500    ASP B  22       54.70   -102.27                                   
REMARK 500    THR B  24       95.06     54.61                                   
REMARK 500    ASN B  39       46.09   -104.56                                   
REMARK 500    GLU B  54      -60.37   -133.93                                   
REMARK 500    SER B  64      -83.54   -161.86                                   
REMARK 500    ARG B  66       40.75     38.86                                   
REMARK 500    ILE B  69       -0.29   -141.22                                   
REMARK 500    CYS B  73       46.15    -79.41                                   
REMARK 500    LYS B 109      133.88   -171.78                                   
REMARK 500    ASP B 110       85.43     26.37                                   
REMARK 500    GLU B 126       79.16     58.79                                   
REMARK 500    ASP B 133       76.67   -103.83                                   
REMARK 500    LYS B 139      -35.27   -136.92                                   
REMARK 500    LEU B 155      -44.90   -135.47                                   
REMARK 500    PHE B 198       49.37    -83.93                                   
REMARK 500    GLN B 207       40.87    -79.04                                   
REMARK 500    THR C   7     -169.96   -107.52                                   
REMARK 500    HIS C  29      -89.29   -106.45                                   
REMARK 500    CYS C  81      121.69    -38.05                                   
REMARK 500    ALA C 142       40.69   -105.67                                   
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                             HEM C1305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 101   NE2                                                    
REMARK 620 2 HEM C1305   NA   96.3                                              
REMARK 620 3 HEM C1305   NB   96.3  88.5                                        
REMARK 620 4 HEM C1305   NC   84.5 177.9  89.5                                  
REMARK 620 5 HEM C1305   ND   88.4  91.4 175.3  90.6                            
REMARK 620 6 HIS D  79   NE2 172.5  88.9  89.2  90.4  86.1                      
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  70   SG                                                     
REMARK 620 2 FES B 302   S1  104.3                                              
REMARK 620 3 FES B 302   S2  116.5  90.7                                        
REMARK 620 4 CYS B  65   SG  109.0 123.0 112.7                                  
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  123.9                                              
REMARK 620 3 SF4 B 303   S3  107.4 105.3                                        
REMARK 620 4 SF4 B 303   S4  109.0 104.5 105.3                                  
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   97.9                                              
REMARK 620 3 SF4 B 303   S3  103.9 106.0                                        
REMARK 620 4 SF4 B 303   S4  136.2 104.7 105.1                                  
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  102.2                                              
REMARK 620 3 F3S B 304   S2  101.5 122.0                                        
REMARK 620 4 F3S B 304   S3  134.5 100.3  99.1                                  
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  106.2                                              
REMARK 620 3 F3S B 304   S3  123.8 100.3                                        
REMARK 620 4 F3S B 304   S4  104.7 123.5 100.1                                  
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   97.4                                              
REMARK 620 3 SF4 B 303   S2  132.0 105.1                                        
REMARK 620 4 SF4 B 303   S4  109.6 104.7 105.0                                  
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   93.0                                              
REMARK 620 3 SF4 B 303   S2  107.5 104.9                                        
REMARK 620 4 SF4 B 303   S3  136.0 105.1 106.0                                  
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   83.6                                              
REMARK 620 3 F3S B 304   S3   88.9  99.5                                        
REMARK 620 4 F3S B 304   S4   98.3 160.0 100.5                                  
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 HEM C 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EBM 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: 3AE2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE4   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE8   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE9   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEB   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 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  3AEC A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AEC B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AEC C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AEC 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    HEM  C1305      43                                                       
HET    EPH  D1306      44                                                       
HET    EBM  C1201      13                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-                
HETNAM   2 EPH  PHOSPHATIDYLETHANOLAMINE                                        
HETNAM     EBM 2-IODO-N-(1-METHYLETHYL)BENZAMIDE                                
HETSYN     HEM HEME                                                             
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  FES    FE2 S2                                                       
FORMUL   7  SF4    FE4 S4                                                       
FORMUL   8  F3S    FE3 S4                                                       
FORMUL   9  HEM    C34 H32 FE N4 O4                                             
FORMUL  10  EPH    C39 H68 N O8 P                                               
FORMUL  11  EBM    C10 H12 I N O                                                
HELIX    1   1 GLY A   28  GLY A   42  1                                  15    
HELIX    2   2 PHE A   52  SER A   56  5                                   5    
HELIX    3   3 HIS A   57  ALA A   61  5                                   5    
HELIX    4   4 ASN A   76  SER A   88  1                                  13    
HELIX    5   5 ASP A   93  GLY A  115  1                                  23    
HELIX    6   6 ARG A  153  LEU A  167  1                                  15    
HELIX    7   7 TYR A  217  TYR A  221  5                                   5    
HELIX    8   8 GLY A  232  ALA A  241  1                                  10    
HELIX    9   9 GLU A  267  GLY A  273  1                                   7    
HELIX   10  10 SER A  297  GLY A  312  1                                  16    
HELIX   11  11 PRO A  330  LEU A  338  1                                   9    
HELIX   12  12 LEU A  338  PHE A  348  1                                  11    
HELIX   13  13 ASN A  413  GLU A  431  1                                  19    
HELIX   14  14 GLY A  447  PHE A  459  1                                  13    
HELIX   15  15 THR A  466  ALA A  481  1                                  16    
HELIX   16  16 VAL A  486  ASP A  503  1                                  18    
HELIX   17  17 ASN A  517  ARG A  543  1                                  27    
HELIX   18  18 PRO A  575  HIS A  579  5                                   5    
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 ASP B  133  GLU B  137  5                                   5    
HELIX   22  22 SER B  145  LYS B  151  1                                   7    
HELIX   23  23 CYS B  164  SER B  167  5                                   4    
HELIX   24  24 CYS B  168  ASN B  174  1                                   7    
HELIX   25  25 GLY B  180  TRP B  190  1                                  11    
HELIX   26  26 PHE B  198  LYS B  205  1                                   8    
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 LYS C    9  LEU C   20  1                                  12    
HELIX   30  30 SER C   36  LEU C   66  1                                  31    
HELIX   31  31 ASN C   69  LEU C   80  1                                  12    
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 ALA D   38  GLY D   55  1                                  18    
HELIX   35  35 LEU D   56  ASN D   63  1                                   8    
HELIX   36  36 CYS D   65  VAL D   92  1                                  28    
HELIX   37  37 ASP D   95  HIS D  122  1                                  28    
HELIX   38  38 GLY D  125  LYS D  135  1                                  11    
SHEET    1   A 6 SER A 172  VAL A 175  0                                        
SHEET    2   A 6 THR A  45  THR A  49  1  N  CYS A  47   O  PHE A 174           
SHEET    3   A 6 VAL A  15  VAL A  25  1  N  ALA A  22   O  ALA A  46           
SHEET    4   A 6 ILE A 202  VAL A 212  1  O  VAL A 211   N  VAL A  23           
SHEET    5   A 6 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    6   A 6 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 VAL A  15  VAL A  25  1  N  ALA A  22   O  ALA A  46           
SHEET    4   B 6 ILE A 202  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 HIS A 145  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    3   C 3 GLN A 128  ALA A 130 -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  HIS A 365   N  GLN A 252           
SHEET    1   F 3 ILE A 275  ILE A 277  0                                        
SHEET    2   F 3 VAL A 322  GLN A 325 -1  O  GLN A 325   N  ILE A 275           
SHEET    3   F 3 ILE A 358  VAL A 360 -1  O  ILE A 358   N  LEU A 324           
SHEET    1   G 2 ILE A 371  PRO A 372  0                                        
SHEET    2   G 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   H 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  LYS B  12   O  ILE B  35           
SHEET    3   J 5 SER B  97  TYR B 100  1  O  SER B  97   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 ASN B  81  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  ILE B 108           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  2.01  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.08  
LINK         SG  CYS B  70                FE1  FES B 302     1555   1555  2.11  
LINK         SG  CYS B  65                FE1  FES B 302     1555   1555  2.17  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.26  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.32  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.42  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.44  
LINK         SG  CYS B 221                FE3  F3S B 304     1555   1555  2.46  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.60  
LINK         SG  CYS B 164                FE4  SF4 B 303     1555   1555  2.61  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.68  
SITE     1 AC1 30 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 30 ALA A  30  THR A  49  LYS A  50  LEU A  51                    
SITE     3 AC1 30 SER A  56  HIS A  57  THR A  58  ALA A  60                    
SITE     4 AC1 30 ALA A  61  GLN A  62  GLY A  63  GLY A  64                    
SITE     5 AC1 30 TYR A 177  PHE A 178  ALA A 179  THR A 214                    
SITE     6 AC1 30 GLY A 215  THR A 225  SER A 226  ASP A 233                    
SITE     7 AC1 30 GLU A 398  ARG A 409  ALA A 412  SER A 414                    
SITE     8 AC1 30 LEU A 415  LEU A 418                                          
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  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 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 HIS B 216  HIS C  45  ARG C  46  GLY C  49                    
SITE     2 AC5 12 LEU C  52  SER C  53  HIS C 101  HIS C 108                    
SITE     3 AC5 12 LEU D  53  LEU D  57  HIS D  79  GLY D  83                    
SITE     1 AC6  8 LEU C 140  ALA D  60  TYR D  61  LEU D  62                    
SITE     2 AC6  8 PRO D  64  CYS D 127  ALA D 131  TRP D 134                    
SITE     1 AC7  8 SER B 170  TRP B 173  HIS B 216  ILE B 218                    
SITE     2 AC7  8 SER C  42  ARG C  46  ASP D  90  TYR D  91                    
CRYST1   70.966   83.994  295.254  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      0.014091  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003387        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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