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Database: PDB
Entry: 3AEB
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Original site: 3AEB 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AEB              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 N-(3-PHENOXY-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 3AEB    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-PHENOXY-PHENYL)-2-TRIFLUOROMETHYL-BENZAMIDE  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 33632                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1693                            
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) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2065                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.74                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.3420                       
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          : 192                                     
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) : 75.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.69000                                             
REMARK   3    B22 (A**2) : 0.44000                                              
REMARK   3    B33 (A**2) : 0.25000                                              
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): 0.421         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.304         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.459        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8882 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12064 ; 1.269 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 4.415 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;32.280 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;16.035 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;14.890 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1309 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6666 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5409 ; 0.136 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8672 ; 0.254 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3473 ; 0.285 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3361 ; 0.498 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    10        A   249                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.6880 -18.5390  17.9210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3658 T22:   0.2105                                     
REMARK   3      T33:   0.3132 T12:  -0.1018                                     
REMARK   3      T13:   0.0203 T23:   0.0370                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7797 L22:   1.1455                                     
REMARK   3      L33:   3.2054 L12:  -0.4152                                     
REMARK   3      L13:  -0.5139 L23:  -0.1197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:  -0.1357 S13:  -0.0830                       
REMARK   3      S21:  -0.0829 S22:  -0.0507 S23:   0.0713                       
REMARK   3      S31:  -0.2099 S32:   0.0753 S33:   0.0468                       
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   250        A   340                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.2100   8.4540  22.7580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4448 T22:   0.1796                                     
REMARK   3      T33:   0.5876 T12:  -0.1469                                     
REMARK   3      T13:   0.0918 T23:  -0.0432                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7113 L22:   2.7334                                     
REMARK   3      L33:   0.6967 L12:   0.9328                                     
REMARK   3      L13:  -1.9227 L23:  -1.1018                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5385 S12:  -0.0541 S13:   0.6010                       
REMARK   3      S21:   0.7892 S22:  -0.1625 S23:   0.0373                       
REMARK   3      S31:  -1.2629 S32:   0.0124 S33:  -0.3760                       
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   341        A   511                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1020 -13.5030  17.7740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3517 T22:   0.3245                                     
REMARK   3      T33:   0.2985 T12:  -0.1581                                     
REMARK   3      T13:   0.0391 T23:   0.0612                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9834 L22:   1.5373                                     
REMARK   3      L33:   3.0739 L12:  -0.1342                                     
REMARK   3      L13:  -0.6797 L23:   0.0141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0075 S12:  -0.1607 S13:   0.1228                       
REMARK   3      S21:  -0.0884 S22:   0.0088 S23:  -0.1094                       
REMARK   3      S31:  -0.3515 S32:   0.6207 S33:  -0.0163                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   512        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7500  -6.4680   4.9240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5309 T22:   0.2709                                     
REMARK   3      T33:   0.3273 T12:  -0.1870                                     
REMARK   3      T13:   0.0760 T23:   0.0731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1362 L22:   0.9693                                     
REMARK   3      L33:   3.4009 L12:  -0.3581                                     
REMARK   3      L13:  -0.0361 L23:  -0.3725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0167 S12:   0.1557 S13:   0.4042                       
REMARK   3      S21:  -0.2681 S22:  -0.0786 S23:  -0.1436                       
REMARK   3      S31:  -0.7634 S32:   0.5010 S33:   0.0619                       
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     9        B   105                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5250 -11.7830  45.9800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3394 T22:   0.6135                                     
REMARK   3      T33:   0.2615 T12:  -0.3087                                     
REMARK   3      T13:  -0.0703 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7673 L22:   3.5908                                     
REMARK   3      L33:   4.1879 L12:  -0.4753                                     
REMARK   3      L13:  -0.6227 L23:   0.7474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0180 S12:  -0.5262 S13:   0.3568                       
REMARK   3      S21:   0.1142 S22:  -0.0277 S23:  -0.3472                       
REMARK   3      S31:  -0.5594 S32:   1.1166 S33:   0.0457                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   106        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2080 -24.3650  40.2110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4500 T22:   0.1796                                     
REMARK   3      T33:   0.3805 T12:  -0.0497                                     
REMARK   3      T13:   0.0596 T23:  -0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6642 L22:   0.6288                                     
REMARK   3      L33:   4.2025 L12:  -0.5401                                     
REMARK   3      L13:  -0.7575 L23:  -0.8586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0259 S12:   0.1362 S13:  -0.0889                       
REMARK   3      S21:  -0.0097 S22:  -0.0841 S23:   0.2424                       
REMARK   3      S31:   0.1440 S32:  -0.2948 S33:   0.1100                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     6        C    35                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6360 -31.1710  47.2810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7429 T22:   0.4618                                     
REMARK   3      T33:   0.2185 T12:   0.1921                                     
REMARK   3      T13:   0.2355 T23:   0.2068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4170 L22:  10.1647                                     
REMARK   3      L33:   5.3006 L12:   1.4998                                     
REMARK   3      L13:   3.2402 L23:   4.0278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1189 S12:  -0.3986 S13:  -0.3691                       
REMARK   3      S21:   1.3163 S22:  -0.1684 S23:  -0.0879                       
REMARK   3      S31:   1.7619 S32:   1.1715 S33:   0.2873                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    36        C    65                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.7230 -28.6850  72.6330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7288 T22:   0.1844                                     
REMARK   3      T33:   0.3867 T12:  -0.0679                                     
REMARK   3      T13:   0.1711 T23:   0.0782                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7832 L22:   5.9778                                     
REMARK   3      L33:   1.4430 L12:   0.0079                                     
REMARK   3      L13:   0.4062 L23:  -1.8287                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2113 S12:  -0.1555 S13:  -0.0753                       
REMARK   3      S21:   0.4149 S22:  -0.2005 S23:  -0.3721                       
REMARK   3      S31:   0.0277 S32:   0.2979 S33:   0.4118                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    66        C    90                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.4010 -28.1810  94.3730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1585 T22:   0.7829                                     
REMARK   3      T33:   0.4963 T12:   0.0650                                     
REMARK   3      T13:   0.1930 T23:   0.1314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.1184 L22:  12.7404                                     
REMARK   3      L33:   8.1950 L12:   7.1227                                     
REMARK   3      L13:   1.6729 L23:   0.9461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3922 S12:  -0.5950 S13:  -0.4613                       
REMARK   3      S21:   1.3766 S22:  -0.4171 S23:  -0.8797                       
REMARK   3      S31:  -1.4458 S32:   0.4067 S33:   0.0249                       
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    91        C   111                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.6310 -18.9220  70.6220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6422 T22:   0.0558                                     
REMARK   3      T33:   0.4174 T12:  -0.0139                                     
REMARK   3      T13:   0.1509 T23:  -0.0258                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0073 L22:   2.5872                                     
REMARK   3      L33:  14.1810 L12:   0.4752                                     
REMARK   3      L13:   0.0251 L23:  -1.0646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1410 S12:  -0.0921 S13:   0.0005                       
REMARK   3      S21:   0.4325 S22:  -0.2583 S23:  -0.1146                       
REMARK   3      S31:  -0.5974 S32:   0.1918 S33:   0.1174                       
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   112        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.5960 -11.8460  66.9670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6261 T22:   0.0901                                     
REMARK   3      T33:   0.4090 T12:   0.0890                                     
REMARK   3      T13:   0.1649 T23:  -0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1455 L22:   5.7875                                     
REMARK   3      L33:  15.3227 L12:   1.8605                                     
REMARK   3      L13:  -0.1110 L23:   1.6952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4233 S12:   0.0130 S13:   0.2964                       
REMARK   3      S21:   0.5391 S22:   0.2800 S23:   0.1191                       
REMARK   3      S31:  -1.4541 S32:   0.2392 S33:  -0.7033                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    35        D    71                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.4540 -29.6020  66.6490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6304 T22:   0.3173                                     
REMARK   3      T33:   0.5908 T12:   0.0541                                     
REMARK   3      T13:   0.3246 T23:   0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1414 L22:   4.0864                                     
REMARK   3      L33:  11.0794 L12:   3.0560                                     
REMARK   3      L13:   0.0294 L23:   0.1153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5836 S12:   0.0950 S13:  -0.4610                       
REMARK   3      S21:  -0.1322 S22:  -0.2308 S23:   0.6615                       
REMARK   3      S31:  -0.5059 S32:  -0.5671 S33:   0.8144                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    72        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6060 -35.8310  64.2120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7118 T22:   0.1098                                     
REMARK   3      T33:   0.4527 T12:  -0.0212                                     
REMARK   3      T13:   0.1548 T23:   0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.3848 L22:   0.2080                                     
REMARK   3      L33:   5.8432 L12:  -1.4428                                     
REMARK   3      L13:  -2.8331 L23:  -0.7262                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8141 S12:   0.0007 S13:  -0.6535                       
REMARK   3      S21:   0.0103 S22:   0.1255 S23:  -0.0854                       
REMARK   3      S31:   0.9624 S32:   0.4360 S33:   0.6887                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    97        D   120                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.1390 -42.5490  72.3410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7518 T22:   0.0424                                     
REMARK   3      T33:   0.4648 T12:  -0.0086                                     
REMARK   3      T13:   0.2693 T23:   0.1268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.3406 L22:   6.1039                                     
REMARK   3      L33:  11.9481 L12:  -0.9339                                     
REMARK   3      L13:  -9.2960 L23:   1.7909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3264 S12:  -0.5711 S13:  -0.8989                       
REMARK   3      S21:  -0.2887 S22:  -0.0695 S23:  -0.2935                       
REMARK   3      S31:   0.4584 S32:   0.5062 S33:   0.3959                       
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   121        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.8990 -30.4160  87.8960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1800 T22:   0.3242                                     
REMARK   3      T33:   0.3193 T12:   0.0062                                     
REMARK   3      T13:   0.2715 T23:   0.0580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9271 L22:  -6.6902                                     
REMARK   3      L33:   1.8185 L12:   0.3996                                     
REMARK   3      L13:  -0.1214 L23:  -4.5194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0209 S12:  -1.0393 S13:   0.0232                       
REMARK   3      S21:   0.7212 S22:  -0.3816 S23:   0.5091                       
REMARK   3      S31:  -1.2310 S32:  -1.0064 S33:   0.3607                       
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 3AEB 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 RCSB029145.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33711                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
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     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.660                              
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   (%): 65.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 8% PEG 4000, 200MM      
REMARK 280  SUCROSE, 100MM NACL, 10MM CACL2, 0.5MM EDTA, 3% 1,6-HAXANEDIOL,     
REMARK 280  0.5% N-DECYL-BETA-D-MALTOSIDE, PH 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       35.85400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.35350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.12750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.35350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.85400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.12750            
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: 12710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 121     -164.41   -111.95                                   
REMARK 500    ALA A 151     -131.95     54.32                                   
REMARK 500    ASP A 170       39.06    -95.55                                   
REMARK 500    ARG A 283       91.41    -62.20                                   
REMARK 500    LYS A 293     -138.22     61.05                                   
REMARK 500    GLU A 311       35.68    -98.40                                   
REMARK 500    ARG A 313       48.50    -93.23                                   
REMARK 500    LYS A 355      -44.74   -130.33                                   
REMARK 500    HIS A 365      -70.75   -132.26                                   
REMARK 500    ALA A 460      102.69    -55.30                                   
REMARK 500    ALA A 482     -150.49    -87.75                                   
REMARK 500    LYS A 544       61.08   -110.50                                   
REMARK 500    GLN A 569      -72.42    -41.93                                   
REMARK 500    ILE B  55      -73.94    -93.48                                   
REMARK 500    SER B  64      -78.66   -154.11                                   
REMARK 500    ARG B  66       -6.99     70.99                                   
REMARK 500    ASP B 110     -127.67     53.84                                   
REMARK 500    GLU B 126       72.74     54.75                                   
REMARK 500    ALA B 162        7.29     80.26                                   
REMARK 500    HIS C  29      -68.12   -124.61                                   
REMARK 500    SER C  79      -73.84   -107.24                                   
REMARK 500    LEU C 117       38.50    -98.02                                   
REMARK 500    ASP D 123     -155.61   -102.71                                   
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   89.1                                              
REMARK 620 3 HEM C1305   NB   97.4  90.4                                        
REMARK 620 4 HEM C1305   NC   89.3 178.5  89.6                                  
REMARK 620 5 HEM C1305   ND   84.3  89.8 178.3  90.3                            
REMARK 620 6 HIS D  79   NE2 174.2  90.0  88.3  91.6  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 FES B 302   S1  135.8                                              
REMARK 620 3 FES B 302   S2  103.3  90.1                                        
REMARK 620 4 CYS B  70   SG  107.1 107.4 109.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 215   SG                                                     
REMARK 620 2 F3S B 304   S1  101.8                                              
REMARK 620 3 F3S B 304   S2  109.9 121.9                                        
REMARK 620 4 F3S B 304   S3  126.2  98.8  99.7                                  
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 161   SG                                                     
REMARK 620 2 SF4 B 303   S1  122.7                                              
REMARK 620 3 SF4 B 303   S2  118.0 105.4                                        
REMARK 620 4 SF4 B 303   S3   99.2 104.1 104.9                                  
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 164   SG                                                     
REMARK 620 2 SF4 B 303   S1  117.7                                              
REMARK 620 3 SF4 B 303   S3  101.0 103.7                                        
REMARK 620 4 SF4 B 303   S4  119.9 106.3 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  107.3                                              
REMARK 620 3 FES B 302   S2  130.9  90.4                                        
REMARK 620 4 CYS B  85   SG  106.1 121.4 102.1                                  
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  114.7                                              
REMARK 620 3 F3S B 304   S3  122.9  98.9                                        
REMARK 620 4 F3S B 304   S4  100.3 120.4 100.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 303   S1   97.4                                              
REMARK 620 3 SF4 B 303   S2  127.0 105.0                                        
REMARK 620 4 SF4 B 303   S4  113.9 106.3 105.0                                  
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 225   SG                                                     
REMARK 620 2 SF4 B 303   S2  111.1                                              
REMARK 620 3 SF4 B 303   S3  108.6 104.4                                        
REMARK 620 4 SF4 B 303   S4  119.8 105.0 106.7                                  
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   88.6                                              
REMARK 620 3 F3S B 304   S3   90.4 100.8                                        
REMARK 620 4 F3S B 304   S4   93.7 157.6 101.5                                  
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 F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 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 F7A C 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ABV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE4   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE8   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE9   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 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  3AEB A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AEB B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AEB C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AEB 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    F3S  B 304       7                                                       
HET    SF4  B 303       8                                                       
HET    MLI  A 701       7                                                       
HET    HEM  C1305      43                                                       
HET    F7A  C1201      26                                                       
HET    EPH  D1306      44                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     MLI MALONATE ION                                                     
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     F7A N-(3-PHENOXYPHENYL)-2-(TRIFLUOROMETHYL)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  F3S    FE3 S4                                                       
FORMUL   8  SF4    FE4 S4                                                       
FORMUL   9  MLI    C3 H2 O4 2-                                                  
FORMUL  10  HEM    C34 H32 FE N4 O4                                             
FORMUL  11  F7A    C20 H14 F3 N O2                                              
FORMUL  12  EPH    C39 H68 N O8 P                                               
HELIX    1   1 GLY A   28  ALA A   41  1                                  14    
HELIX    2   2 PHE A   52  ALA A   61  5                                  10    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  GLY A  115  1                                  23    
HELIX    5   5 LYS A  137  LYS A  140  5                                   4    
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  GLU A  272  1                                   6    
HELIX   10  10 PHE A  284  ALA A  289  1                                   6    
HELIX   11  11 ALA A  292  ALA A  296  5                                   5    
HELIX   12  12 SER A  297  GLU A  311  1                                  15    
HELIX   13  13 PRO A  330  LEU A  338  1                                   9    
HELIX   14  14 LEU A  338  GLY A  350  1                                  13    
HELIX   15  15 ASN A  413  CYS A  433  1                                  21    
HELIX   16  16 GLY A  447  PHE A  459  1                                  13    
HELIX   17  17 THR A  466  ALA A  481  1                                  16    
HELIX   18  18 VAL A  486  GLY A  502  1                                  17    
HELIX   19  19 ASP A  503  GLN A  505  5                                   3    
HELIX   20  20 ASN A  517  ARG A  543  1                                  27    
HELIX   21  21 PRO A  575  HIS A  579  5                                   5    
HELIX   22  22 ASN B   38  CYS B   40  5                                   3    
HELIX   23  23 MET B   43  GLU B   54  1                                  12    
HELIX   24  24 LEU B  115  SER B  124  1                                  10    
HELIX   25  25 SER B  145  LYS B  151  1                                   7    
HELIX   26  26 ALA B  162  CYS B  168  1                                   7    
HELIX   27  27 CYS B  168  GLY B  175  1                                   8    
HELIX   28  28 LEU B  179  ILE B  192  1                                  14    
HELIX   29  29 PHE B  198  LYS B  205  1                                   8    
HELIX   30  30 MET B  219  CYS B  225  1                                   7    
HELIX   31  31 ASN B  230  TYR B  245  1                                  16    
HELIX   32  32 THR C    7  GLY C   21  1                                  15    
HELIX   33  33 SER C   36  LEU C   66  1                                  31    
HELIX   34  34 ASN C   69  LYS C   78  1                                  10    
HELIX   35  35 GLY C   83  LEU C  113  1                                  31    
HELIX   36  36 THR C  118  ALA C  142  1                                  25    
HELIX   37  37 LYS D   37  ASN D   63  1                                  27    
HELIX   38  38 CYS D   65  VAL D   92  1                                  28    
HELIX   39  39 GLY D   94  ASP D  123  1                                  30    
HELIX   40  40 GLY D  125  LYS D  135  1                                  11    
SHEET    1   A 4 VAL A  15  GLU A  19  0                                        
SHEET    2   A 4 ILE A 202  ARG A 206  1  O  ARG A 204   N  HIS A  18           
SHEET    3   A 4 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    4   A 4 TYR A 177  GLU A 185 -1  N  LEU A 183   O  ARG A 190           
SHEET    1   B 6 SER A 172  VAL A 175  0                                        
SHEET    2   B 6 THR A  45  THR A  49  1  N  CYS A  47   O  SER A 172           
SHEET    3   B 6 ALA A  22  VAL A  25  1  N  VAL A  24   O  VAL A  48           
SHEET    4   B 6 ASN A 209  VAL A 212  1  O  VAL A 211   N  VAL A  25           
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 3 ILE A  65  ASN A  66  0                                        
SHEET    2   C 3 GLN A 143  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    3   C 3 GLN A 128  SER A 135 -1  N  GLN A 134   O  ALA A 144           
SHEET    1   D 3 CYS A 245  GLN A 246  0                                        
SHEET    2   D 3 LYS A 582  ASP A 589 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 LYS A 594  PRO A 601 -1  O  GLU A 598   N  LEU A 585           
SHEET    1   E 4 VAL A 251  ILE A 258  0                                        
SHEET    2   E 4 ILE A 358  ASN A 367 -1  O  TYR A 366   N  GLN A 252           
SHEET    3   E 4 VAL A 322  GLN A 325 -1  N  VAL A 322   O  VAL A 360           
SHEET    4   E 4 ILE A 275  ILE A 277 -1  N  ILE A 275   O  GLN A 325           
SHEET    1   F 2 ILE A 371  PRO A 372  0                                        
SHEET    2   F 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   G 2 ILE A 464  ARG A 465  0                                        
SHEET    2   G 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   H 2 PHE A 484  ARG A 485  0                                        
SHEET    2   H 2 ALA A 551  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    1   I 5 HIS B  29  ASP B  36  0                                        
SHEET    2   I 5 ILE B  11  ARG B  18 -1  N  ARG B  18   O  HIS B  29           
SHEET    3   I 5 SER B  97  TYR B 100  1  O  ILE B  99   N  ALA B  15           
SHEET    4   I 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   I 5 GLY B  80  LEU B  83 -1  O  GLY B  80   N  ILE B  77           
SHEET    1   J 2 VAL B 107  LYS B 109  0                                        
SHEET    2   J 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  LYS B 109           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  1.94  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.12  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.15  
LINK         SG  CYS B  65                FE2  FES B 302     1555   1555  2.20  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.21  
LINK         SG  CYS B  70                FE2  FES B 302     1555   1555  2.24  
LINK         SG  CYS B 161                FE4  SF4 B 303     1555   1555  2.29  
LINK         SG  CYS B 164                FE2  SF4 B 303     1555   1555  2.29  
LINK         SG  CYS B  73                FE1  FES B 302     1555   1555  2.29  
LINK         SG  CYS B 221                FE3  F3S B 304     1555   1555  2.29  
LINK         SG  CYS B 158                FE3  SF4 B 303     1555   1555  2.31  
LINK         SG  CYS B  85                FE1  FES B 302     1555   1555  2.39  
LINK         SG  CYS B 225                FE1  SF4 B 303     1555   1555  2.40  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.47  
SITE     1 AC1 35 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 35 ALA A  30  VAL A  48  THR A  49  LYS A  50                    
SITE     3 AC1 35 LEU A  51  SER A  56  HIS A  57  THR A  58                    
SITE     4 AC1 35 ALA A  61  GLN A  62  GLY A  63  GLY A  64                    
SITE     5 AC1 35 TYR A 177  PHE A 178  ALA A 179  ALA A 213                    
SITE     6 AC1 35 THR A 214  GLY A 215  THR A 225  ASP A 233                    
SITE     7 AC1 35 LEU A 264  HIS A 365  TYR A 366  GLU A 398                    
SITE     8 AC1 35 ARG A 409  ALA A 412  ASN A 413  SER A 414                    
SITE     9 AC1 35 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 10 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC3 10 HIS B 216  THR B 217  ILE B 218  MET B 219                    
SITE     3 AC3 10 ASN B 220  CYS B 221                                          
SITE     1 AC4  9 CYS B 158  ILE B 159  LEU B 160  CYS B 161                    
SITE     2 AC4  9 ALA B 162  CYS B 164  ALA B 182  CYS B 225                    
SITE     3 AC4  9 PRO B 226                                                     
SITE     1 AC5 11 GLY A  63  PHE A 131  HIS A 254  LEU A 264                    
SITE     2 AC5 11 THR A 266  GLU A 267  ARG A 298  HIS A 365                    
SITE     3 AC5 11 ARG A 409  ALA A 412  FAD A 700                               
SITE     1 AC6 15 HIS C  45  ARG C  46  GLY C  49  LEU C  52                    
SITE     2 AC6 15 SER C  53  HIS C 101  THR C 102  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 11 PRO B 169  SER B 170  TRP B 173  HIS B 216                    
SITE     2 AC7 11 ILE C  30  TRP C  35  MET C  39  SER C  42                    
SITE     3 AC7 11 ARG C  46  ASP D  90  TYR D  91                               
SITE     1 AC8  6 LEU D  57  TYR D  61  CYS D 127  VAL D 130                    
SITE     2 AC8  6 ALA D 131  TRP D 134                                          
CRYST1   71.708   84.255  294.707  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      0.013945  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011869  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003393        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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