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Database: PDB
Entry: 3AE9
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AE9              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 N-(3-PENTAFLUOROPHENYLOXY-PHENYL)-2-TRIFLUOROMETHYL-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 3AE9    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 N-(3-PENTAFLUOROPHENYLOXY-PHENYL)-2-              
JRNL        TITL 3 TRIFLUOROMETHYL-BENZAMIDE                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.31 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) : 3.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27275                          
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) : 0.259                           
REMARK   3   R VALUE            (WORKING SET) : 0.257                           
REMARK   3   FREE R VALUE                     : 0.307                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1367                            
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) : 3.31                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1807                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.4340                       
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          : 197                                     
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) : 124.64                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.69000                                              
REMARK   3    B22 (A**2) : -0.48000                                             
REMARK   3    B33 (A**2) : -1.21000                                             
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): 0.602         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.563         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 71.683        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8882 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12046 ; 0.867 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 4.045 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;33.628 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;15.482 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;10.189 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1311 ; 0.055 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6671 ; 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):  5411 ; 0.120 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8676 ; 0.216 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3471 ; 0.111 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3353 ; 0.198 ; 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  : 17                                         
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   260                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8710 -17.5650  18.1040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3897 T22:   1.0880                                     
REMARK   3      T33:   1.2686 T12:  -0.0811                                     
REMARK   3      T13:  -0.0023 T23:   0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6853 L22:   1.4909                                     
REMARK   3      L33:   4.8086 L12:   0.0945                                     
REMARK   3      L13:  -0.5711 L23:  -1.0472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0137 S12:  -0.1385 S13:  -0.0294                       
REMARK   3      S21:   0.0408 S22:  -0.1429 S23:   0.0647                       
REMARK   3      S31:  -0.4070 S32:   0.0793 S33:   0.1292                       
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   261        A   353                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.8640   8.6300  24.8820              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8653 T22:   0.9716                                     
REMARK   3      T33:   1.2779 T12:  -0.2178                                     
REMARK   3      T13:   0.2045 T23:  -0.0895                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9005 L22:   2.3260                                     
REMARK   3      L33:  -0.3569 L12:   0.0715                                     
REMARK   3      L13:   0.4504 L23:  -0.5862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4058 S12:  -0.3683 S13:   0.7241                       
REMARK   3      S21:   0.5377 S22:  -0.1957 S23:   0.5265                       
REMARK   3      S31:  -1.1729 S32:   0.2289 S33:  -0.2101                       
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   354        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1090 -10.9860  11.3330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5661 T22:   1.2468                                     
REMARK   3      T33:   1.2602 T12:  -0.2077                                     
REMARK   3      T13:   0.0863 T23:   0.0868                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4230 L22:   2.5180                                     
REMARK   3      L33:   4.4663 L12:  -0.5873                                     
REMARK   3      L13:  -0.1797 L23:  -0.6294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0336 S12:  -0.0795 S13:   0.1855                       
REMARK   3      S21:  -0.3795 S22:  -0.0381 S23:  -0.2944                       
REMARK   3      S31:  -0.6674 S32:   0.7514 S33:   0.0717                       
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    54                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1120 -11.3060  46.6320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5036 T22:   1.8294                                     
REMARK   3      T33:   1.3188 T12:  -0.4711                                     
REMARK   3      T13:  -0.1954 T23:   0.0278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0600 L22:  14.1350                                     
REMARK   3      L33:   7.2104 L12:  -4.0320                                     
REMARK   3      L13:  -1.5344 L23:  -4.6473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2983 S12:  -0.3101 S13:   0.3915                       
REMARK   3      S21:  -0.2214 S22:  -0.8708 S23:  -1.2581                       
REMARK   3      S31:  -0.5609 S32:   1.7558 S33:   0.5725                       
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    55        B    79                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6900 -13.5780  40.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5652 T22:   2.4076                                     
REMARK   3      T33:   1.4587 T12:  -0.4235                                     
REMARK   3      T13:  -0.1100 T23:   0.1822                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.7884 L22:   6.3606                                     
REMARK   3      L33:  -6.2931 L12:  -1.8861                                     
REMARK   3      L13:  -5.4653 L23:   2.9847                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2900 S12:   0.9275 S13:   0.3814                       
REMARK   3      S21:   1.0644 S22:   0.1949 S23:   0.3238                       
REMARK   3      S31:  -0.1861 S32:   0.9412 S33:   0.0950                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    80        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0310 -16.8520  46.8660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6221 T22:   1.6320                                     
REMARK   3      T33:   1.2118 T12:  -0.1699                                     
REMARK   3      T13:  -0.0453 T23:   0.0743                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6200 L22:   0.6682                                     
REMARK   3      L33:   1.5726 L12:   0.2532                                     
REMARK   3      L13:   1.4067 L23:   0.9385                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0088 S12:  -0.9083 S13:   0.7820                       
REMARK   3      S21:  -0.1061 S22:  -0.5218 S23:   0.2257                       
REMARK   3      S31:  -0.2315 S32:   0.5955 S33:   0.5130                       
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   123        B   158                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.2660 -21.5900  28.2810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2950 T22:   1.2836                                     
REMARK   3      T33:   1.3645 T12:   0.0175                                     
REMARK   3      T13:   0.0695 T23:   0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7331 L22:  -0.3520                                     
REMARK   3      L33:  13.7489 L12:  -2.4502                                     
REMARK   3      L13:   0.9686 L23:  -0.9024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3612 S12:   0.4426 S13:  -0.4007                       
REMARK   3      S21:  -0.1380 S22:  -0.2765 S23:   0.2775                       
REMARK   3      S31:  -0.6221 S32:  -0.9953 S33:  -0.0847                       
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   159        B   194                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.3920 -24.5190  44.7410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4874 T22:   1.2844                                     
REMARK   3      T33:   1.9115 T12:  -0.1203                                     
REMARK   3      T13:   0.1227 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7811 L22:  -1.5801                                     
REMARK   3      L33:   9.4277 L12:  -0.0268                                     
REMARK   3      L13:  -3.4680 L23:   1.0696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0516 S12:  -0.5891 S13:   0.4727                       
REMARK   3      S21:   0.1763 S22:  -0.3576 S23:   0.3385                       
REMARK   3      S31:   0.8005 S32:  -0.4356 S33:   0.3060                       
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 :   B   195        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.1240 -25.6990  45.4860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7319 T22:   0.9294                                     
REMARK   3      T33:   1.3235 T12:  -0.0912                                     
REMARK   3      T13:   0.1274 T23:  -0.1743                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8493 L22:   0.0541                                     
REMARK   3      L33:  10.5586 L12:  -1.1735                                     
REMARK   3      L13:  -3.6964 L23:  -1.3972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1384 S12:   0.4504 S13:   0.1111                       
REMARK   3      S21:   0.1045 S22:  -0.0189 S23:   0.3742                       
REMARK   3      S31:   0.7224 S32:  -1.2423 S33:   0.1573                       
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     6        C    39                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0710 -29.3240  48.7280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5384 T22:   1.1915                                     
REMARK   3      T33:   1.4129 T12:   0.0388                                     
REMARK   3      T13:   0.0612 T23:   0.2148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6924 L22:   4.2070                                     
REMARK   3      L33:   8.3262 L12:   0.4073                                     
REMARK   3      L13:  -0.2143 L23:   3.6272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0972 S12:   0.0108 S13:   0.0288                       
REMARK   3      S21:   0.0210 S22:  -0.2429 S23:  -0.0953                       
REMARK   3      S31:   0.5377 S32:   1.0427 S33:   0.3401                       
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    40        C    63                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.7520 -29.5490  73.7830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7488 T22:   0.8452                                     
REMARK   3      T33:   1.2396 T12:  -0.1043                                     
REMARK   3      T13:   0.1966 T23:   0.1155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2613 L22:   3.8241                                     
REMARK   3      L33:   3.7430 L12:  -1.6711                                     
REMARK   3      L13:  -0.7764 L23:  11.5546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2175 S12:  -0.4535 S13:  -0.0990                       
REMARK   3      S21:   0.5760 S22:  -0.0791 S23:   0.1488                       
REMARK   3      S31:   0.6006 S32:   0.2108 S33:   0.2966                       
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 :   C    64        C    89                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.5040 -29.6050  94.0930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5190 T22:   1.3377                                     
REMARK   3      T33:   1.6273 T12:   0.1362                                     
REMARK   3      T13:   0.0162 T23:   0.1298                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6922 L22:   5.6841                                     
REMARK   3      L33:  20.4913 L12:   8.8290                                     
REMARK   3      L13:   1.5838 L23:   3.1150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6423 S12:  -0.9799 S13:  -0.7669                       
REMARK   3      S21:   1.5997 S22:  -0.1240 S23:  -1.0829                       
REMARK   3      S31:  -2.1196 S32:  -0.3889 S33:  -0.5183                       
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 :   C    90        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.1310 -15.1400  69.0000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8937 T22:   0.7829                                     
REMARK   3      T33:   1.1997 T12:   0.0308                                     
REMARK   3      T13:   0.1836 T23:  -0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6598 L22:   6.5812                                     
REMARK   3      L33:  12.1443 L12:   0.7439                                     
REMARK   3      L13:  -1.3285 L23:   0.5952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5079 S12:  -0.0199 S13:   0.0422                       
REMARK   3      S21:   0.5374 S22:  -0.1858 S23:   0.2305                       
REMARK   3      S31:  -0.7297 S32:  -0.0787 S33:  -0.3221                       
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    35        D    72                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.1590 -29.8330  67.1590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9094 T22:   1.1976                                     
REMARK   3      T33:   1.4233 T12:   0.0507                                     
REMARK   3      T13:   0.2973 T23:  -0.0721                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7082 L22:   8.4045                                     
REMARK   3      L33:   3.0871 L12:   4.7612                                     
REMARK   3      L13:   0.8590 L23:  -2.4931                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2593 S12:  -0.1563 S13:  -0.2005                       
REMARK   3      S21:   0.2546 S22:  -0.0784 S23:   0.4361                       
REMARK   3      S31:   0.0251 S32:  -0.6503 S33:   0.3377                       
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    73        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.4090 -36.1010  64.0180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0319 T22:   1.0268                                     
REMARK   3      T33:   1.4010 T12:  -0.0083                                     
REMARK   3      T13:   0.1972 T23:  -0.0197                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9384 L22:   3.2818                                     
REMARK   3      L33:   1.0308 L12:   3.7290                                     
REMARK   3      L13:   5.1992 L23:  -3.8930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0900 S12:   0.8297 S13:  -0.6828                       
REMARK   3      S21:  -0.4940 S22:  -0.2958 S23:  -0.4174                       
REMARK   3      S31:   0.6433 S32:   0.4730 S33:   0.2059                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    97        D   120                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.3950 -42.6400  72.7690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0229 T22:   0.7775                                     
REMARK   3      T33:   1.1912 T12:  -0.0771                                     
REMARK   3      T13:   0.2608 T23:   0.0731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.2496 L22:   5.3808                                     
REMARK   3      L33:  31.2936 L12:  -1.1289                                     
REMARK   3      L13: -14.5419 L23:   2.1095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6683 S12:  -0.2468 S13:  -0.2471                       
REMARK   3      S21:  -0.2711 S22:   0.1837 S23:  -0.0246                       
REMARK   3      S31:   1.5522 S32:   0.3393 S33:   0.4846                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   121        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.3640 -30.5330  88.2790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0265 T22:   1.3632                                     
REMARK   3      T33:   1.4828 T12:  -0.0466                                     
REMARK   3      T13:   0.3377 T23:  -0.0776                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3784 L22:  43.4789                                     
REMARK   3      L33:  19.7044 L12:  15.5888                                     
REMARK   3      L13:   1.6393 L23:  -3.9420                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3179 S12:  -1.7310 S13:   0.1277                       
REMARK   3      S21:  -0.6037 S22:  -2.1440 S23:  -0.2930                       
REMARK   3      S31:  -0.9535 S32:  -1.9780 S33:   1.8261                       
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 3AE9 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029143.                                      
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   : 27349                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
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     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7830                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.980                              
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   (%): 66.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 6% PEG 4000, 200MM      
REMARK 280  SUCROSE, 100MM NACL, 10MM CACL2, 0.5MM EDTA, 3% 1,6-HAXANEDIOL,     
REMARK 280  0.5% N-DECYL-BETA-D-MALTOSIDE, PH 7.2, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.30450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.82300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.12450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.82300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.30450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.12450            
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: 12780 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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      -17.72     65.23                                   
REMARK 500    PRO A  53      -37.65    -37.85                                   
REMARK 500    ALA A  68       51.31    -91.12                                   
REMARK 500    ARG A 146       24.40   -145.48                                   
REMARK 500    ALA A 151     -134.48     57.85                                   
REMARK 500    ARG A 153       47.83   -109.76                                   
REMARK 500    ASP A 170       47.11    -78.71                                   
REMARK 500    PHE A 174       74.64   -105.20                                   
REMARK 500    TYR A 288      -61.52    -91.60                                   
REMARK 500    LYS A 293     -130.31     61.40                                   
REMARK 500    ALA A 296     -159.82   -104.99                                   
REMARK 500    HIS A 365      -53.47   -135.81                                   
REMARK 500    ALA A 481       54.43    -90.55                                   
REMARK 500    ALA A 482     -155.73    -79.10                                   
REMARK 500    TRP A 516       72.21     49.16                                   
REMARK 500    LYS A 544       54.32    -98.66                                   
REMARK 500    GLN A 569      -20.08     71.47                                   
REMARK 500    GLN A 577       31.27    -87.62                                   
REMARK 500    SER A 621      117.94   -165.95                                   
REMARK 500    SER B  64      -80.88   -149.05                                   
REMARK 500    ASP B 110     -137.13     49.08                                   
REMARK 500    GLU B 126       82.32     59.94                                   
REMARK 500    ASP B 193       97.80    -66.23                                   
REMARK 500    SER B 194        1.23    -63.30                                   
REMARK 500    ASN C  23       32.15    -87.01                                   
REMARK 500    HIS C  29      -74.00   -121.89                                   
REMARK 500    SER C  79      -71.73   -103.70                                   
REMARK 500    CYS C  81     -128.96     54.48                                   
REMARK 500    ALA C 142       77.51   -100.21                                   
REMARK 500    ASP D 123     -149.53    -88.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EPH D 1306                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  114.4                                              
REMARK 620 3 FES B 302   S2  125.9  89.8                                        
REMARK 620 4 CYS B  85   SG  106.1 118.6 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  70   SG                                                     
REMARK 620 2 FES B 302   S1  108.0                                              
REMARK 620 3 FES B 302   S2  111.6  89.8                                        
REMARK 620 4 CYS B  65   SG  108.5 124.4 113.4                                  
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  106.5                                              
REMARK 620 3 SF4 B 303   S3  119.9 105.3                                        
REMARK 620 4 SF4 B 303   S4  114.1 104.8 105.1                                  
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  109.2                                              
REMARK 620 3 SF4 B 303   S2  112.9 105.3                                        
REMARK 620 4 SF4 B 303   S3  117.8 105.2 105.4                                  
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 168   SG                                                     
REMARK 620 2 F3S B 304   S1  111.1                                              
REMARK 620 3 F3S B 304   S3  116.1  99.6                                        
REMARK 620 4 F3S B 304   S4  113.5 115.4 100.0                                  
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   91.2                                              
REMARK 620 3 HEM C1305   NB   96.7  89.1                                        
REMARK 620 4 HEM C1305   NC   85.6 176.7  90.6                                  
REMARK 620 5 HEM C1305   ND   84.4  90.9 178.9  89.4                            
REMARK 620 6 HIS D  79   NE2 172.0  96.8  84.6  86.5  94.4                      
REMARK 620 N                    1     2     3     4     5                       
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  119.6                                              
REMARK 620 3 F3S B 304   S2   92.5 116.4                                        
REMARK 620 4 F3S B 304   S3  128.2  99.8  99.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 303   S2  109.1                                              
REMARK 620 3 SF4 B 303   S3  104.0 105.3                                        
REMARK 620 4 SF4 B 303   S4  126.4 105.3 104.9                                  
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  104.3                                              
REMARK 620 3 SF4 B 303   S2  118.4 105.3                                        
REMARK 620 4 SF4 B 303   S4  117.2 104.8 105.3                                  
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 FD8 C 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ABV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE4   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE8   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 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  3AE9 A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AE9 B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AE9 C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AE9 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    FD8  C1201      31                                                       
HET    EPH  D1306      44                                                       
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     FD8 N-[3-(PENTAFLUOROPHENOXY)PHENYL]-2-(TRIFLUOROMETHYL)             
HETNAM   2 FD8  BENZAMIDE                                                       
HETNAM     EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-                
HETNAM   2 EPH  PHOSPHATIDYLETHANOLAMINE                                        
HETSYN     HEM HEME                                                             
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  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  FD8    C20 H9 F8 N O2                                               
FORMUL  12  EPH    C39 H68 N O8 P                                               
HELIX    1   1 GLY A   28  GLY A   42  1                                  15    
HELIX    2   2 SER A   56  ALA A   61  5                                   6    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  GLN A  103  1                                  11    
HELIX    5   5 GLN A  103  GLY A  115  1                                  13    
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 ASP A  233  ARG A  240  1                                   8    
HELIX    9   9 GLU A  267  GLY A  273  1                                   7    
HELIX   10  10 PHE A  284  ALA A  289  1                                   6    
HELIX   11  11 SER A  297  GLY A  312  1                                  16    
HELIX   12  12 PRO A  330  ARG A  337  1                                   8    
HELIX   13  13 PRO A  339  PHE A  348  1                                  10    
HELIX   14  14 ASN A  413  CYS A  433  1                                  21    
HELIX   15  15 GLY A  447  PHE A  459  1                                  13    
HELIX   16  16 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 MET B   43  GLU B   54  1                                  12    
HELIX   20  20 LEU B  115  SER B  124  1                                  10    
HELIX   21  21 SER B  145  GLU B  150  1                                   6    
HELIX   22  22 LYS B  151  ASP B  153  5                                   3    
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  ILE B  192  1                                  13    
HELIX   26  26 PHE B  198  LYS B  205  1                                   8    
HELIX   27  27 MET B  219  CYS B  225  1                                   7    
HELIX   28  28 ASN B  230  THR B  244  1                                  15    
HELIX   29  29 THR C    7  LEU C   20  1                                  14    
HELIX   30  30 SER C   36  LEU C   61  1                                  26    
HELIX   31  31 LEU C   61  LEU C   66  1                                   6    
HELIX   32  32 ASN C   69  LYS C   78  1                                  10    
HELIX   33  33 THR C   85  ASP C  112  1                                  28    
HELIX   34  34 THR C  118  ALA C  142  1                                  25    
HELIX   35  35 ALA D   38  ASN D   63  1                                  26    
HELIX   36  36 CYS D   65  VAL D   92  1                                  28    
HELIX   37  37 GLY D   94  HIS D  122  1                                  29    
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 CYS A 189  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    6   A 6 TYR A 177  MET A 184 -1  N  LEU A 183   O  ARG A 190           
SHEET    1   B 6 SER A 172  VAL A 175  0                                        
SHEET    2   B 6 THR A  45  THR A  49  1  N  CYS A  47   O  PHE A 174           
SHEET    3   B 6 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  ARG A 381   O  GLN A 388           
SHEET    1   C 2 ILE A  65  ASN A  66  0                                        
SHEET    2   C 2 CYS A 147  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    1   D 2 ALA A 130  SER A 135  0                                        
SHEET    2   D 2 GLN A 143  HIS A 145 -1  O  ALA A 144   N  PHE A 131           
SHEET    1   E 3 CYS A 245  GLN A 246  0                                        
SHEET    2   E 3 LYS A 582  ASP A 589 -1  O  SER A 586   N  CYS A 245           
SHEET    3   E 3 LYS A 594  PRO A 601 -1  O  GLU A 598   N  LEU A 585           
SHEET    1   F 4 VAL A 251  ILE A 258  0                                        
SHEET    2   F 4 ILE A 358  ASN A 367 -1  O  TYR A 366   N  GLN A 252           
SHEET    3   F 4 VAL A 322  GLN A 325 -1  N  VAL A 322   O  VAL A 360           
SHEET    4   F 4 ILE A 275  ILE A 277 -1  N  ILE A 275   O  GLN A 325           
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 VAL B  96  TYR B 100  1  O  ILE B  99   N  ALA B  15           
SHEET    4   J 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   J 5 GLY B  80  LEU B  83 -1  O  GLY B  80   N  ILE B  77           
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  2.06  
LINK         SG  CYS B  73                FE2  FES B 302     1555   1555  2.03  
LINK         SG  CYS B  70                FE1  FES B 302     1555   1555  2.11  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.12  
LINK         SG  CYS B 164                FE4  SF4 B 303     1555   1555  2.14  
LINK         SG  CYS B 168                FE3  F3S B 304     1555   1555  2.16  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.21  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.23  
LINK         SG  CYS B  65                FE1  FES B 302     1555   1555  2.28  
LINK         SG  CYS B  85                FE2  FES B 302     1555   1555  2.50  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.55  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.61  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.62  
SITE     1 AC1 31 GLY A  26  GLY A  28  GLY A  29  ALA A  30                    
SITE     2 AC1 31 THR A  49  LYS A  50  LEU A  51  SER A  56                    
SITE     3 AC1 31 HIS A  57  THR A  58  ALA A  60  ALA A  61                    
SITE     4 AC1 31 GLN A  62  GLY A  63  GLY A  64  PHE A 178                    
SITE     5 AC1 31 ALA A 179  THR A 214  GLY A 215  ASP A 233                    
SITE     6 AC1 31 HIS A 365  TYR A 366  GLY A 397  GLU A 398                    
SITE     7 AC1 31 ARG A 409  ALA A 412  ASN A 413  SER A 414                    
SITE     8 AC1 31 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 ALA B 162  CYS B 164  CYS B 225  PRO B 226                    
SITE     1 AC4  9 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC4  9 HIS B 216  ILE B 218  MET B 219  ASN B 220                    
SITE     3 AC4  9 CYS B 221                                                     
SITE     1 AC5  9 GLY A  63  PHE A 131  HIS A 254  LEU A 264                    
SITE     2 AC5  9 THR A 266  GLU A 267  ARG A 298  HIS A 365                    
SITE     3 AC5  9 FAD A 700                                                     
SITE     1 AC6 15 HIS B 216  HIS C  45  ARG C  46  GLY C  49                    
SITE     2 AC6 15 LEU C  52  SER C  53  HIS C 101  HIS C 108                    
SITE     3 AC6 15 ARG D  47  SER D  50  LEU D  53  LEU D  54                    
SITE     4 AC6 15 LEU D  57  HIS D  79  GLY D  83                               
SITE     1 AC7  9 PRO B 169  SER B 170  TRP B 173  HIS B 216                    
SITE     2 AC7  9 ILE C  30  SER C  42  ILE C  43  ARG C  46                    
SITE     3 AC7  9 TYR D  91                                                     
SITE     1 AC8  4 MET C 143  TYR D  61  CYS D 127  TRP D 134                    
CRYST1   72.609   84.249  295.646  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      0.013772  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011870  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003382        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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