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Database: PDB
Entry: 3AE7
LinkDB: 3AE7
Original site: 3AE7 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AE7              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 2-IODO-N-(3-ISOPROPOXY-PHENYL)-BENZAMIDE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, 
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: FLAVOPROTEIN SUBUNIT OF COMPLEX II, FP;                     
COMPND   6 EC: 1.3.5.1;                                                         
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT,  
COMPND   9 MITOCHONDRIAL;                                                       
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: IRON-SULFUR SUBUNIT OF COMPLEX II, IP;                      
COMPND  12 EC: 1.3.5.1;                                                         
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT,           
COMPND  15 MITOCHONDRIAL;                                                       
COMPND  16 CHAIN: C;                                                            
COMPND  17 SYNONYM: SUCCINATE-UBIQUINONE OXIDOREDUCTASE CYTOCHROME B LARGE      
COMPND  18 SUBUNIT, CYBL;                                                       
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] CYTOCHROME B SMALL    
COMPND  21 SUBUNIT, MITOCHONDRIAL;                                              
COMPND  22 CHAIN: D;                                                            
COMPND  23 FRAGMENT: RESIDUES 57-159;                                           
COMPND  24 SYNONYM: SUCCINATE-UBIQUINONE OXIDOREDUCTASE CYTOCHROME B SMALL      
COMPND  25 SUBUNIT, CYBS, SUCCINATE-UBIQUINONE REDUCTASE MEMBRANE ANCHOR        
COMPND  26 SUBUNIT, QPS3, CII-4, SUCCINATE DEHYDROGENASE COMPLEX SUBUNIT D      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: HEART;                                                        
SOURCE   6 TISSUE: MUSCLE;                                                      
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   9 ORGANISM_COMMON: PIG;                                                
SOURCE  10 ORGANISM_TAXID: 9823;                                                
SOURCE  11 ORGAN: HEART;                                                        
SOURCE  12 TISSUE: MUSCLE;                                                      
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  15 ORGANISM_COMMON: PIG;                                                
SOURCE  16 ORGANISM_TAXID: 9823;                                                
SOURCE  17 ORGAN: HEART;                                                        
SOURCE  18 TISSUE: MUSCLE;                                                      
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE  21 ORGANISM_COMMON: PIG;                                                
SOURCE  22 ORGANISM_TAXID: 9823;                                                
SOURCE  23 ORGAN: HEART;                                                        
SOURCE  24 TISSUE: MUSCLE                                                       
KEYWDS    RESPIRATORY COMPLEX II, INHIBITORS, ELECTRON TRANSPORT, IRON, IRON-   
KEYWDS   2 SULFUR, METAL-BINDING, MITOCHONDRION, MITOCHONDRION INNER MEMBRANE,  
KEYWDS   3 OXIDOREDUCTASE, TRANSIT PEPTIDE, TRANSPORT, TRICARBOXYLIC ACID       
KEYWDS   4 CYCLE, HEME, TRANSMEMBRANE, FAD-BINDING PROTEIN, OXIDOREDUCTASE-     
KEYWDS   5 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HARADA,T.SASAKI,M.SHINDO,Y.KIDO,D.K.INAOKA,J.OMORI,A.OSANAI,        
AUTHOR   2 K.SAKAMOTO,J.MAO,S.MATSUOKA,M.INOUE,T.HONMA,A.TANAKA,K.KITA          
REVDAT   1   09-FEB-11 3AE7    0                                                
JRNL        AUTH   S.HARADA,T.SASAKI,M.SHINDO,Y.KIDO,D.K.INAOKA,J.OMORI,        
JRNL        AUTH 2 A.OSANAI,K.SAKAMOTO,J.MAO,S.MATSUOKA,M.INOUE,T.HONMA,        
JRNL        AUTH 3 A.TANAKA,K.KITA                                              
JRNL        TITL   CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II  
JRNL        TITL 2 BOUND WITH 2-IODO-N-(3-ISOPROPOXY-PHENYL)-BENZAMIDE          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.62 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.62                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 20118                          
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) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.305                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1046                            
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) : 3.62                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.71                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1077                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3610                       
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          : 135                                     
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) : 145.11                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.42000                                              
REMARK   3    B22 (A**2) : 0.62000                                              
REMARK   3    B33 (A**2) : -1.04000                                             
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): 0.765         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.587         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 81.032        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.906                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.860                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8821 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11970 ; 0.844 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 3.872 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;33.189 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;14.857 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;12.043 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1304 ; 0.052 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6644 ; 0.002 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5410 ; 0.087 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8675 ; 0.156 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3411 ; 0.069 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3278 ; 0.120 ; 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   191                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8520 -17.8930 -17.4100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5536 T22:   0.5629                                     
REMARK   3      T33:   0.8826 T12:   0.0686                                     
REMARK   3      T13:   0.0294 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5878 L22:   1.2936                                     
REMARK   3      L33:   3.9478 L12:  -0.3418                                     
REMARK   3      L13:  -0.0784 L23:   0.7305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0476 S12:   0.2716 S13:  -0.0428                       
REMARK   3      S21:   0.0449 S22:   0.0739 S23:  -0.0530                       
REMARK   3      S31:  -0.2372 S32:   0.1387 S33:  -0.0263                       
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   192        A   261                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5410 -16.1390 -20.1670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4153 T22:   0.6593                                     
REMARK   3      T33:   0.8981 T12:   0.1360                                     
REMARK   3      T13:   0.0234 T23:  -0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8395 L22:   4.4001                                     
REMARK   3      L33:   4.2835 L12:   2.0674                                     
REMARK   3      L13:   0.4171 L23:   1.0641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1182 S12:   0.2205 S13:   0.1100                       
REMARK   3      S21:  -0.7414 S22:  -0.0124 S23:   0.2082                       
REMARK   3      S31:  -0.6490 S32:  -0.5811 S33:   0.1306                       
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   262        A   354                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4760   8.7620 -24.9950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5298 T22:   0.4433                                     
REMARK   3      T33:   1.1238 T12:   0.1249                                     
REMARK   3      T13:   0.0968 T23:   0.1495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9738 L22:   2.0643                                     
REMARK   3      L33:  -1.3816 L12:  -0.8679                                     
REMARK   3      L13:   0.9550 L23:   0.2038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1262 S12:   0.2349 S13:   0.5710                       
REMARK   3      S21:  -0.6227 S22:   0.0372 S23:  -0.1259                       
REMARK   3      S31:  -0.6720 S32:  -0.1859 S33:   0.0890                       
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   355        A   429                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3140 -13.9510 -11.3520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6249 T22:   0.6276                                     
REMARK   3      T33:   0.9548 T12:   0.1174                                     
REMARK   3      T13:   0.0783 T23:  -0.0377                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4396 L22:   3.9500                                     
REMARK   3      L33:   0.5203 L12:   0.3434                                     
REMARK   3      L13:   0.3414 L23:   2.0526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0868 S12:  -0.0438 S13:   0.2152                       
REMARK   3      S21:  -0.0788 S22:  -0.0167 S23:   0.0690                       
REMARK   3      S31:  -0.2231 S32:  -0.0421 S33:  -0.0701                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   430        A   511                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1770 -15.3110 -20.6290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3655 T22:   1.0153                                     
REMARK   3      T33:   0.7026 T12:   0.1964                                     
REMARK   3      T13:   0.0824 T23:  -0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7096 L22:   4.3838                                     
REMARK   3      L33:   2.1424 L12:  -0.2472                                     
REMARK   3      L13:  -0.1889 L23:  -0.1875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1705 S12:   0.3868 S13:  -0.0234                       
REMARK   3      S21:   0.2461 S22:   0.1484 S23:   0.6902                       
REMARK   3      S31:  -0.1944 S32:  -0.9696 S33:   0.0221                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   512        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6490  -6.3540  -5.0150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6680 T22:   0.5442                                     
REMARK   3      T33:   0.9250 T12:   0.2352                                     
REMARK   3      T13:   0.0688 T23:  -0.0705                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5779 L22:   0.9866                                     
REMARK   3      L33:   3.8372 L12:   0.5307                                     
REMARK   3      L13:  -0.4375 L23:   0.0305                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1232 S12:  -0.2923 S13:   0.4466                       
REMARK   3      S21:   0.2976 S22:  -0.2235 S23:   0.2948                       
REMARK   3      S31:  -0.8342 S32:  -0.6932 S33:   0.1003                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     9        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0130 -11.8980 -46.1910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5476 T22:   1.0473                                     
REMARK   3      T33:   0.8052 T12:   0.1847                                     
REMARK   3      T13:  -0.0202 T23:   0.0715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4018 L22:   2.7166                                     
REMARK   3      L33:   5.0539 L12:  -0.4363                                     
REMARK   3      L13:   0.3336 L23:  -1.2014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0476 S12:   0.8534 S13:   0.4551                       
REMARK   3      S21:  -0.1777 S22:  -0.0195 S23:   0.0538                       
REMARK   3      S31:  -0.3757 S32:  -0.9494 S33:   0.0671                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   107        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.7730 -24.0980 -39.9600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7469 T22:   0.4744                                     
REMARK   3      T33:   0.9866 T12:   0.0034                                     
REMARK   3      T13:  -0.0038 T23:   0.0585                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7763 L22:  -0.2102                                     
REMARK   3      L33:   4.5813 L12:   0.5262                                     
REMARK   3      L13:  -2.3423 L23:   0.8352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0467 S12:   0.1329 S13:   0.0367                       
REMARK   3      S21:   0.0685 S22:   0.0397 S23:  -0.2211                       
REMARK   3      S31:   0.2741 S32:   0.3495 S33:   0.0070                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     6        C    35                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1390 -30.9910 -47.2770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6141 T22:   0.7872                                     
REMARK   3      T33:   0.7978 T12:  -0.0422                                     
REMARK   3      T13:   0.1582 T23:  -0.1557                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3714 L22:  13.5938                                     
REMARK   3      L33:   4.8147 L12:  -3.3705                                     
REMARK   3      L13:   2.3456 L23:  -1.0706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1428 S12:   0.1136 S13:  -0.2584                       
REMARK   3      S21:  -0.7120 S22:  -0.4924 S23:   0.0004                       
REMARK   3      S31:   0.3660 S32:  -0.3752 S33:   0.3497                       
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    36        C    63                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9350 -26.8860 -71.4100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0502 T22:   0.1294                                     
REMARK   3      T33:   1.0652 T12:   0.0307                                     
REMARK   3      T13:   0.0171 T23:   0.1102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1198 L22:  -4.8800                                     
REMARK   3      L33:   3.6552 L12:   1.3669                                     
REMARK   3      L13:   4.2330 L23:  -5.2146                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8696 S12:  -0.5933 S13:  -0.3434                       
REMARK   3      S21:  -1.2228 S22:  -0.0502 S23:   1.3902                       
REMARK   3      S31:  -0.8537 S32:   0.2885 S33:   0.9198                       
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    64        C    89                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0240 -29.3570 -93.4750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5560 T22:   1.0771                                     
REMARK   3      T33:   0.9621 T12:   0.0737                                     
REMARK   3      T13:   0.0115 T23:  -0.1715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1743 L22:  -3.4725                                     
REMARK   3      L33:   6.7318 L12:   2.3772                                     
REMARK   3      L13:  -2.8030 L23:  -0.4683                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2827 S12:   0.4991 S13:   0.0395                       
REMARK   3      S21:  -0.1557 S22:   0.0801 S23:   0.3104                       
REMARK   3      S31:  -0.4200 S32:  -0.2564 S33:   0.2026                       
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    90        C   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.4620 -17.4290 -66.6090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8575 T22:   0.4269                                     
REMARK   3      T33:   0.8967 T12:  -0.0317                                     
REMARK   3      T13:   0.1512 T23:   0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8447 L22:   5.2479                                     
REMARK   3      L33:  10.6785 L12:  -1.9245                                     
REMARK   3      L13:  -6.6734 L23:   3.1884                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1123 S12:  -0.0495 S13:   0.1961                       
REMARK   3      S21:  -0.5745 S22:  -0.1417 S23:  -0.5142                       
REMARK   3      S31:  -0.6253 S32:  -0.4705 S33:   0.0294                       
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   121        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0260 -10.8750 -71.7750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6125 T22:   0.1332                                     
REMARK   3      T33:   1.0925 T12:   0.1949                                     
REMARK   3      T13:   0.3339 T23:   0.1375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.5624 L22:   3.6979                                     
REMARK   3      L33:  30.8921 L12:   3.9017                                     
REMARK   3      L13: -15.0950 L23:   3.3716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5181 S12:  -0.2884 S13:  -0.7357                       
REMARK   3      S21:  -0.1893 S22:  -0.3277 S23:  -0.5559                       
REMARK   3      S31:   1.7900 S32:  -0.3386 S33:   0.8458                       
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    96                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.5420 -31.9120 -65.4590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8086 T22:   0.3792                                     
REMARK   3      T33:   0.9045 T12:   0.0113                                     
REMARK   3      T13:   0.1825 T23:  -0.0388                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4905 L22:   3.6619                                     
REMARK   3      L33:   4.4107 L12:  -0.6657                                     
REMARK   3      L13:  -1.2704 L23:   0.2920                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0339 S12:  -0.4669 S13:  -0.4653                       
REMARK   3      S21:  -0.5571 S22:  -0.1697 S23:  -0.2285                       
REMARK   3      S31:   0.0020 S32:   0.4546 S33:   0.1358                       
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    97        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7710 -37.1020 -78.5720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8150 T22:   0.5588                                     
REMARK   3      T33:   0.9976 T12:  -0.0218                                     
REMARK   3      T13:   0.4684 T23:  -0.1989                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3458 L22:   1.6110                                     
REMARK   3      L33:   1.7755 L12:   0.0731                                     
REMARK   3      L13:   2.1932 L23:  -2.5706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6388 S12:   0.2865 S13:   0.0952                       
REMARK   3      S21:   0.1437 S22:  -0.7737 S23:  -0.0650                       
REMARK   3      S31:  -0.7291 S32:   0.3810 S33:   0.1349                       
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 3AE7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029141.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98000                            
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   : 20323                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1430                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 77.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.220                              
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   (%): 65.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56                     
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       35.58750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      146.84550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.99400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      146.84550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.58750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.99400            
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: 13010 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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      -23.51     65.67                                   
REMARK 500    PRO A  53      -39.19    -39.35                                   
REMARK 500    THR A 121     -167.91   -113.00                                   
REMARK 500    VAL A 150       56.69   -110.45                                   
REMARK 500    ALA A 151       72.55     44.92                                   
REMARK 500    ASP A 152       -4.60     66.85                                   
REMARK 500    PRO A 290      -81.57    -65.89                                   
REMARK 500    VAL A 291       52.07   -104.69                                   
REMARK 500    ALA A 292      -36.95   -141.74                                   
REMARK 500    LYS A 293     -145.25     59.48                                   
REMARK 500    ARG A 313       32.81    -96.73                                   
REMARK 500    HIS A 365      -57.41   -133.36                                   
REMARK 500    ASN A 374     -177.10    -69.38                                   
REMARK 500    CYS A 433      118.28     63.86                                   
REMARK 500    PHE A 459       47.54   -100.06                                   
REMARK 500    ALA A 482     -155.45    -85.19                                   
REMARK 500    ARG A 512       56.43   -118.48                                   
REMARK 500    TRP A 516       75.87     43.58                                   
REMARK 500    LYS A 544       63.71   -112.57                                   
REMARK 500    GLN A 569      -41.53   -164.50                                   
REMARK 500    ILE B  55      -69.01    -91.44                                   
REMARK 500    SER B  64      -84.21   -156.76                                   
REMARK 500    CYS B  73       36.02    -77.37                                   
REMARK 500    LYS B 109      120.67   -174.15                                   
REMARK 500    ASP B 110       92.49     44.65                                   
REMARK 500    LEU B 111        8.16     59.43                                   
REMARK 500    GLU B 126       81.17     58.34                                   
REMARK 500    LEU B 155      -43.70   -137.01                                   
REMARK 500    GLN B 207       26.37    -78.82                                   
REMARK 500    SER C  22     -169.18   -119.42                                   
REMARK 500    HIS C  29      -60.27   -124.45                                   
REMARK 500    LEU C  82       83.47     45.59                                   
REMARK 500    ALA C 142       62.82   -100.45                                   
REMARK 500    ASP D 123     -157.48   -109.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  137.3                                              
REMARK 620 3 FES B 302   S2  121.3  90.4                                        
REMARK 620 N                    1     2                                         
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   86.2                                              
REMARK 620 3 HEM C1305   NB   99.9  88.7                                        
REMARK 620 4 HEM C1305   NC   93.3 177.2  88.7                                  
REMARK 620 5 HEM C1305   ND   84.0  91.3 176.0  91.4                            
REMARK 620 6 HIS D  79   NE2 166.1  87.9  92.4  93.2  83.6                      
REMARK 620 N                    1     2     3     4     5                       
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  111.7                                              
REMARK 620 3 SF4 B 303   S3  116.2 105.6                                        
REMARK 620 4 SF4 B 303   S4  112.3 105.1 105.1                                  
REMARK 620 N                    1     2     3                                   
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  114.2                                              
REMARK 620 3 FES B 302   S2  132.7  90.4                                        
REMARK 620 4 CYS B  70   SG  100.1 115.0 104.9                                  
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 158   SG                                                     
REMARK 620 2 SF4 B 303   S1  106.7                                              
REMARK 620 3 SF4 B 303   S2  124.2 105.0                                        
REMARK 620 4 SF4 B 303   S3  109.0 105.6 104.9                                  
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 161   SG                                                     
REMARK 620 2 SF4 B 303   S2  116.9                                              
REMARK 620 3 SF4 B 303   S3  109.5 105.1                                        
REMARK 620 4 SF4 B 303   S4  114.3 104.9 105.3                                  
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 221   SG                                                     
REMARK 620 2 F3S B 304   S1  136.2                                              
REMARK 620 3 F3S B 304   S2  106.9 105.6                                        
REMARK 620 4 F3S B 304   S3  100.5 101.4 100.7                                  
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  128.1                                              
REMARK 620 3 SF4 B 303   S2  113.2 105.1                                        
REMARK 620 4 SF4 B 303   S4   97.8 105.1 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12J B 1201                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ABV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE4   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE8   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE9   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEB   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEC   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AED   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEE   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEF   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX WITH AN EMPTY QUINONE-BINDING               
REMARK 900 POCKET                                                               
REMARK 900 RELATED ID: 3AEG   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF CHAIN D IS REFERRED IN REF 2 IN A5GZW8, UNIPROT.     
DBREF  3AE7 A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AE7 B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AE7 C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AE7 D   34   136  UNP    A5GZW8   DHSD_PIG        57    159             
SEQRES   1 A  622  SER SER ALA LYS VAL SER ASP ALA ILE SER THR GLN TYR          
SEQRES   2 A  622  PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY          
SEQRES   3 A  622  ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER          
SEQRES   4 A  622  GLU ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE          
SEQRES   5 A  622  PRO THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE          
SEQRES   6 A  622  ASN ALA ALA LEU GLY ASN MET GLU GLU ASP ASN TRP ARG          
SEQRES   7 A  622  TRP HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU          
SEQRES   8 A  622  GLY ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA          
SEQRES   9 A  622  PRO ALA SER VAL VAL GLU LEU GLU ASN TYR GLY MET PRO          
SEQRES  10 A  622  PHE SER ARG THR GLU ASP GLY LYS ILE TYR GLN ARG ALA          
SEQRES  11 A  622  PHE GLY GLY GLN SER LEU LYS PHE GLY LYS GLY GLY GLN          
SEQRES  12 A  622  ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS          
SEQRES  13 A  622  SER LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR          
SEQRES  14 A  622  ASP THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU          
SEQRES  15 A  622  LEU MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU          
SEQRES  16 A  622  CYS ILE GLU ASP GLY SER ILE HIS ARG ILE ARG ALA ARG          
SEQRES  17 A  622  ASN THR VAL VAL ALA THR GLY GLY TYR GLY ARG THR TYR          
SEQRES  18 A  622  PHE SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY          
SEQRES  19 A  622  THR ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP          
SEQRES  20 A  622  LEU GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY          
SEQRES  21 A  622  ALA GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY          
SEQRES  22 A  622  GLY ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU          
SEQRES  23 A  622  ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP          
SEQRES  24 A  622  VAL VAL SER ARG SER MET THR LEU GLU ILE ARG GLU GLY          
SEQRES  25 A  622  ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN          
SEQRES  26 A  622  LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA VAL ARG LEU          
SEQRES  27 A  622  PRO GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL          
SEQRES  28 A  622  ASP VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL          
SEQRES  29 A  622  HIS TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY          
SEQRES  30 A  622  GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP GLN VAL VAL          
SEQRES  31 A  622  PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA CYS ALA SER          
SEQRES  32 A  622  VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU          
SEQRES  33 A  622  ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU SER ILE          
SEQRES  34 A  622  ALA GLU SER CYS ARG PRO GLY ASP LYS VAL PRO SER ILE          
SEQRES  35 A  622  LYS PRO ASN ALA GLY GLU GLU SER VAL MET ASN LEU ASP          
SEQRES  36 A  622  LYS LEU ARG PHE ALA ASN GLY THR ILE ARG THR SER GLU          
SEQRES  37 A  622  LEU ARG LEU SER MET GLN LYS SER MET GLN SER HIS ALA          
SEQRES  38 A  622  ALA VAL PHE ARG VAL GLY SER VAL LEU GLN GLU GLY CYS          
SEQRES  39 A  622  GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU GLN HIS LEU          
SEQRES  40 A  622  LYS THR PHE ASP ARG GLY MET VAL TRP ASN THR ASP LEU          
SEQRES  41 A  622  VAL GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA          
SEQRES  42 A  622  LEU GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER          
SEQRES  43 A  622  ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS GLU ARG VAL          
SEQRES  44 A  622  ASP GLU TYR ASP TYR SER LYS PRO ILE GLN GLY GLN GLN          
SEQRES  45 A  622  LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS HIS THR LEU          
SEQRES  46 A  622  SER TYR VAL ASP VAL LYS THR GLY LYS VAL SER LEU GLU          
SEQRES  47 A  622  TYR ARG PRO VAL ILE ASP LYS THR LEU ASN GLU ALA ASP          
SEQRES  48 A  622  CYS ALA THR VAL PRO PRO ALA ILE ARG SER TYR                  
SEQRES   1 B  252  ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE LYS LYS          
SEQRES   2 B  252  PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR GLY ASP          
SEQRES   3 B  252  LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU ASN ASN          
SEQRES   4 B  252  CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS          
SEQRES   5 B  252  ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG SER CYS          
SEQRES   6 B  252  ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ASN          
SEQRES   7 B  252  GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE ASP THR          
SEQRES   8 B  252  ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU PRO HIS          
SEQRES   9 B  252  MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU SER ASN          
SEQRES  10 B  252  PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS          
SEQRES  11 B  252  LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN TYR LEU          
SEQRES  12 B  252  GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY LEU TYR          
SEQRES  13 B  252  GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO          
SEQRES  14 B  252  SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA          
SEQRES  15 B  252  VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG          
SEQRES  16 B  252  ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU GLN ASP          
SEQRES  17 B  252  PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS          
SEQRES  18 B  252  THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA          
SEQRES  19 B  252  ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU          
SEQRES  20 B  252  LYS LYS ALA SER ALA                                          
SEQRES   1 C  140  LEU GLY THR THR ALA LYS GLU GLU MET GLU ARG PHE TRP          
SEQRES   2 C  140  ASN LYS ASN LEU GLY SER ASN ARG PRO LEU SER PRO HIS          
SEQRES   3 C  140  ILE THR ILE TYR ARG TRP SER LEU PRO MET ALA MET SER          
SEQRES   4 C  140  ILE CYS HIS ARG GLY THR GLY ILE ALA LEU SER ALA GLY          
SEQRES   5 C  140  VAL SER LEU PHE GLY LEU SER ALA LEU LEU LEU PRO GLY          
SEQRES   6 C  140  ASN PHE GLU SER HIS LEU GLU LEU VAL LYS SER LEU CYS          
SEQRES   7 C  140  LEU GLY PRO THR LEU ILE TYR THR ALA LYS PHE GLY ILE          
SEQRES   8 C  140  VAL PHE PRO LEU MET TYR HIS THR TRP ASN GLY ILE ARG          
SEQRES   9 C  140  HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU THR ILE PRO          
SEQRES  10 C  140  GLN LEU THR GLN SER GLY VAL VAL VAL LEU ILE LEU THR          
SEQRES  11 C  140  VAL LEU SER SER VAL GLY LEU ALA ALA MET                      
SEQRES   1 D  103  ALA SER SER LYS ALA ALA SER LEU HIS TRP THR GLY GLU          
SEQRES   2 D  103  ARG VAL VAL SER VAL LEU LEU LEU GLY LEU LEU PRO ALA          
SEQRES   3 D  103  ALA TYR LEU ASN PRO CYS SER ALA MET ASP TYR SER LEU          
SEQRES   4 D  103  ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY ILE GLY          
SEQRES   5 D  103  GLN VAL VAL THR ASP TYR VAL ARG GLY ASP ALA LEU GLN          
SEQRES   6 D  103  LYS ALA ALA LYS ALA GLY LEU LEU ALA LEU SER ALA PHE          
SEQRES   7 D  103  THR PHE ALA GLY LEU CYS TYR PHE ASN TYR HIS ASP VAL          
SEQRES   8 D  103  GLY ILE CYS LYS ALA VAL ALA MET LEU TRP LYS LEU              
HET    FAD  A 700      53                                                       
HET    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    HEM  C1305      43                                                       
HET    12J  B1201      20                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     12J 2-IODO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE                     
HETSYN     HEM HEME                                                             
HETSYN     12J 2-IODO-N-(3-ISOPROPOXYPHENYL)BENZAMIDE                           
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  FES    FE2 S2                                                       
FORMUL   7  SF4    FE4 S4                                                       
FORMUL   8  F3S    FE3 S4                                                       
FORMUL   9  HEM    C34 H32 FE N4 O4                                             
FORMUL  10  12J    C16 H16 I N O2                                               
HELIX    1   1 GLY A   28  GLY A   42  1                                  15    
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  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 GLY A  232  ALA A  241  1                                  10    
HELIX    9   9 PHE A  284  ALA A  289  1                                   6    
HELIX   10  10 ALA A  292  ALA A  296  5                                   5    
HELIX   11  11 SER A  297  GLY A  312  1                                  16    
HELIX   12  12 PRO A  330  LEU A  338  1                                   9    
HELIX   13  13 LEU A  338  PHE A  348  1                                  11    
HELIX   14  14 ASN A  413  SER A  432  1                                  20    
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  ILE B  125  1                                  11    
HELIX   21  21 SER B  145  LYS B  151  1                                   7    
HELIX   22  22 CYS B  168  ASN B  174  1                                   7    
HELIX   23  23 GLY B  180  TRP B  190  1                                  11    
HELIX   24  24 PHE B  198  ALA B  204  1                                   7    
HELIX   25  25 LYS B  205  GLN B  207  5                                   3    
HELIX   26  26 ASN B  230  THR B  244  1                                  15    
HELIX   27  27 THR C    7  LEU C   20  1                                  14    
HELIX   28  28 SER C   36  LEU C   66  1                                  31    
HELIX   29  29 ASN C   69  LYS C   78  1                                  10    
HELIX   30  30 SER C   79  CYS C   81  5                                   3    
HELIX   31  31 GLY C   83  GLY C  114  1                                  32    
HELIX   32  32 THR C  118  ALA C  142  1                                  25    
HELIX   33  33 ALA D   38  ASN D   63  1                                  26    
HELIX   34  34 CYS D   65  VAL D   92  1                                  28    
HELIX   35  35 GLY D   94  HIS D  122  1                                  29    
HELIX   36  36 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  SER A 172           
SHEET    3   A 6 VAL A  15  VAL A  25  1  N  VAL A  24   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  SER A 172           
SHEET    3   B 6 VAL A  15  VAL A  25  1  N  VAL A  24   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 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  VAL A 588 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 VAL A 595  PRO A 601 -1  O  ARG A 600   N  HIS A 583           
SHEET    1   E 2 VAL A 251  HIS A 254  0                                        
SHEET    2   E 2 THR A 363  ASN A 367 -1  O  TYR A 366   N  GLN A 252           
SHEET    1   F 3 ILE A 275  ILE A 277  0                                        
SHEET    2   F 3 VAL A 322  GLN A 325 -1  O  GLN A 325   N  ILE A 275           
SHEET    3   F 3 ILE A 358  VAL A 360 -1  O  VAL A 360   N  VAL A 322           
SHEET    1   G 2 ILE A 371  PRO A 372  0                                        
SHEET    2   G 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   H 2 ILE A 464  ARG A 465  0                                        
SHEET    2   H 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   I 3 PHE A 484  ARG A 485  0                                        
SHEET    2   I 3 HIS A 550  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    3   I 3 SER A 546  ARG A 547 -1  N  ARG A 547   O  HIS A 550           
SHEET    1   J 5 HIS B  29  ASP B  36  0                                        
SHEET    2   J 5 ILE B  11  ARG B  18 -1  N  ILE B  16   O  GLN B  31           
SHEET    3   J 5 SER B  97  TYR B 100  1  O  ILE B  99   N  ALA B  15           
SHEET    4   J 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   J 5 ASN B  81  LEU B  83 -1  O  THR B  82   N  MET B  75           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  2.08  
LINK         SG  CYS B  73                FE1  FES B 302     1555   1555  1.94  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.16  
LINK         SG  CYS B 164                FE2  SF4 B 303     1555   1555  2.22  
LINK         SG  CYS B  65                FE2  FES B 302     1555   1555  2.22  
LINK         SG  CYS B 158                FE4  SF4 B 303     1555   1555  2.26  
LINK         SG  CYS B  70                FE2  FES B 302     1555   1555  2.32  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.35  
LINK         SG  CYS B 161                FE1  SF4 B 303     1555   1555  2.42  
LINK         SG  CYS B 221                FE1  F3S B 304     1555   1555  2.47  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.67  
SITE     1 AC1 30 GLY A  26  ALA A  27  GLY A  28  VAL A  48                    
SITE     2 AC1 30 THR A  49  LYS A  50  LEU A  51  SER A  56                    
SITE     3 AC1 30 HIS A  57  THR A  58  ALA A  60  ALA A  61                    
SITE     4 AC1 30 GLN A  62  GLY A  63  GLY A  64  TYR A 177                    
SITE     5 AC1 30 PHE A 178  ALA A 179  ALA A 213  THR A 214                    
SITE     6 AC1 30 GLY A 215  THR A 225  SER A 226  ASP A 233                    
SITE     7 AC1 30 TYR A 366  GLU A 398  ARG A 409  SER A 414                    
SITE     8 AC1 30 LEU A 415  LEU A 418                                          
SITE     1 AC2  8 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC2  8 CYS B  70  GLY B  71  CYS B  73  CYS B  85                    
SITE     1 AC3  9 CYS B 158  ILE B 159  LEU B 160  CYS B 161                    
SITE     2 AC3  9 ALA B 162  CYS B 164  ALA B 182  CYS B 225                    
SITE     3 AC3  9 PRO B 226                                                     
SITE     1 AC4  9 CYS B 168  SER B 170  TYR B 178  PRO B 181                    
SITE     2 AC4  9 CYS B 215  THR B 217  ILE B 218  MET B 219                    
SITE     3 AC4  9 CYS B 221                                                     
SITE     1 AC5 13 HIS C  45  ARG C  46  GLY C  49  SER C  53                    
SITE     2 AC5 13 HIS C 101  HIS C 108  ARG D  47  SER D  50                    
SITE     3 AC5 13 LEU D  53  LEU D  54  LEU D  57  HIS D  79                    
SITE     4 AC5 13 GLY D  83                                                     
SITE     1 AC6 10 PRO B 169  TRP B 173  HIS B 216  ILE B 218                    
SITE     2 AC6 10 ILE C  30  TRP C  35  SER C  42  ARG C  46                    
SITE     3 AC6 10 ASP D  90  TYR D  91                                          
CRYST1   71.175   83.988  293.691  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      0.014050  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003405        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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