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Database: PDB
Entry: 3AEA
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Original site: 3AEA 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AEA              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 N-(3-DIMETHYLAMINOMETHYL-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 3AEA    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-DIMETHYLAMINOMETHYL-PHENYL)-2-               
JRNL        TITL 3 TRIFLUOROMETHYL-BENZAMIDE                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
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) : 3.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 25081                          
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) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1271                            
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) : 3.39                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.47                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1587                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 97                           
REMARK   3   BIN FREE R VALUE                    : 0.4420                       
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          : 189                                     
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) : 113.73                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.13000                                              
REMARK   3    B22 (A**2) : 0.27000                                              
REMARK   3    B33 (A**2) : -0.40000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.599         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.494         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 62.262        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.913                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.878                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8873 ; 0.005 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12031 ; 0.876 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 4.235 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;33.752 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;15.289 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;11.893 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1305 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6662 ; 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):  5410 ; 0.117 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8674 ; 0.216 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3463 ; 0.184 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3340 ; 0.334 ; 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  : 11                                         
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   256                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2070  17.7680 -17.8950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1724 T22:   0.1213                                     
REMARK   3      T33:   0.4135 T12:   0.0968                                     
REMARK   3      T13:   0.0018 T23:   0.0286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3258 L22:   1.1106                                     
REMARK   3      L33:   4.8738 L12:   0.4450                                     
REMARK   3      L13:   0.5287 L23:  -0.5833                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0217 S12:   0.1495 S13:   0.0392                       
REMARK   3      S21:   0.0429 S22:  -0.0480 S23:  -0.0056                       
REMARK   3      S31:   0.4079 S32:  -0.0204 S33:   0.0697                       
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   257        A   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.8750  -8.5520 -24.6500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1955 T22:   0.3025                                     
REMARK   3      T33:   1.0427 T12:  -0.0523                                     
REMARK   3      T13:  -0.4201 T23:  -0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8317 L22:   0.6231                                     
REMARK   3      L33:   0.2077 L12:  -1.4065                                     
REMARK   3      L13:   0.3163 L23:  -0.2431                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5735 S12:   0.3955 S13:  -0.8476                       
REMARK   3      S21:  -0.7091 S22:  -0.2303 S23:   0.3565                       
REMARK   3      S31:   0.6407 S32:  -0.0322 S33:  -0.3431                       
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   350        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7310  10.7190 -11.7020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2041 T22:   0.2312                                     
REMARK   3      T33:   0.4075 T12:   0.1596                                     
REMARK   3      T13:  -0.0428 T23:   0.0807                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4462 L22:   1.7937                                     
REMARK   3      L33:   4.3648 L12:   0.3929                                     
REMARK   3      L13:  -0.1378 L23:  -0.6568                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0747 S12:   0.1024 S13:  -0.2924                       
REMARK   3      S21:   0.1912 S22:  -0.0108 S23:  -0.2066                       
REMARK   3      S31:   0.7071 S32:   0.6399 S33:   0.0854                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     9        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.9990  11.7690 -46.0470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1814 T22:   0.5391                                     
REMARK   3      T33:   0.4039 T12:   0.2158                                     
REMARK   3      T13:   0.1114 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9144 L22:   3.8027                                     
REMARK   3      L33:   4.8256 L12:   0.5574                                     
REMARK   3      L13:   0.5849 L23:   0.2533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1108 S12:   0.6312 S13:  -0.5236                       
REMARK   3      S21:  -0.3833 S22:   0.1051 S23:  -0.4665                       
REMARK   3      S31:   0.5761 S32:   1.1389 S33:   0.0057                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   107        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4080  24.2640 -40.1430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3132 T22:   0.1516                                     
REMARK   3      T33:   0.5143 T12:   0.0603                                     
REMARK   3      T13:  -0.0927 T23:  -0.1268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9938 L22:   0.5432                                     
REMARK   3      L33:   6.4904 L12:   0.5042                                     
REMARK   3      L13:   1.7308 L23:  -1.0194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1174 S12:  -0.1895 S13:   0.0295                       
REMARK   3      S21:  -0.1117 S22:   0.0143 S23:   0.2104                       
REMARK   3      S31:  -0.2424 S32:  -0.6760 S33:   0.1031                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     6        C    65                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.1350  29.7450 -58.4270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3937 T22:   0.1523                                     
REMARK   3      T33:   0.4480 T12:   0.0085                                     
REMARK   3      T13:  -0.0559 T23:   0.0927                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7407 L22:   0.9600                                     
REMARK   3      L33:   3.6037 L12:   0.0514                                     
REMARK   3      L13:   1.1177 L23:  -0.1989                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1047 S12:   0.1455 S13:   0.0041                       
REMARK   3      S21:  -0.1756 S22:  -0.1062 S23:  -0.0597                       
REMARK   3      S31:  -0.2751 S32:   0.6880 S33:   0.2109                       
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    66        C    89                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7800  28.2190 -94.6590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0654 T22:   0.7672                                     
REMARK   3      T33:   0.4614 T12:   0.0539                                     
REMARK   3      T13:  -0.0358 T23:   0.1647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2998 L22:  13.8113                                     
REMARK   3      L33:  11.2638 L12:  -3.3474                                     
REMARK   3      L13:   2.2292 L23:   0.3123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8048 S12:   0.2833 S13:   0.0097                       
REMARK   3      S21:  -2.0002 S22:  -0.5041 S23:  -0.2042                       
REMARK   3      S31:   1.5932 S32:   0.2343 S33:  -0.3007                       
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    90        C   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9610  17.5630 -66.8630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7381 T22:   0.2185                                     
REMARK   3      T33:   0.5418 T12:   0.0339                                     
REMARK   3      T13:  -0.1567 T23:  -0.0650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2129 L22:   2.8195                                     
REMARK   3      L33:   6.4579 L12:  -1.7902                                     
REMARK   3      L13:   5.7131 L23:  -1.3606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5510 S12:   0.3135 S13:  -0.2490                       
REMARK   3      S21:  -0.7752 S22:  -0.2259 S23:   0.3827                       
REMARK   3      S31:   0.5749 S32:   0.3957 S33:  -0.3251                       
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   121        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2160  11.0710 -72.0470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6639 T22:   0.0702                                     
REMARK   3      T33:   0.4662 T12:   0.0534                                     
REMARK   3      T13:  -0.2043 T23:  -0.0821                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5636 L22:   3.2004                                     
REMARK   3      L33:  13.9912 L12:   0.4437                                     
REMARK   3      L13:   1.8503 L23:   3.7758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5448 S12:   0.1216 S13:   0.0646                       
REMARK   3      S21:   0.0554 S22:  -0.1557 S23:   0.6239                       
REMARK   3      S31:   0.1992 S32:   0.2137 S33:  -0.3892                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    35        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9310  32.0910 -65.7370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6024 T22:   0.2931                                     
REMARK   3      T33:   0.6663 T12:   0.1422                                     
REMARK   3      T13:  -0.2307 T23:  -0.1270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9500 L22:   3.4982                                     
REMARK   3      L33:   5.1925 L12:  -0.0802                                     
REMARK   3      L13:  -2.6095 L23:  -2.2567                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0121 S12:  -0.0060 S13:   0.1719                       
REMARK   3      S21:   0.0342 S22:   0.1439 S23:   0.1906                       
REMARK   3      S31:  -0.2073 S32:  -0.2176 S33:  -0.1559                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    97        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8470  37.3300 -79.0230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6881 T22:   0.6469                                     
REMARK   3      T33:   0.6146 T12:  -0.0016                                     
REMARK   3      T13:  -0.1553 T23:  -0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3630 L22:   4.9937                                     
REMARK   3      L33:   4.7789 L12:  -1.0236                                     
REMARK   3      L13:   2.0550 L23:  -3.2969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0918 S12:   0.2115 S13:   0.3412                       
REMARK   3      S21:   0.1044 S22:  -0.4912 S23:   0.0807                       
REMARK   3      S31:  -0.0783 S32:  -0.6819 S33:   0.5830                       
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 3AEA 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 RCSB029144.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25146                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3330                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.51                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.180                              
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   (%): 65.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 5% 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       35.75250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.47950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.87550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.47950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.75250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.87550            
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: 12940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 181   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET A  72      -61.72    -94.05                                   
REMARK 500    ALA A 151     -139.60     52.32                                   
REMARK 500    ARG A 153       53.21   -111.17                                   
REMARK 500    ASN A 278     -149.28    -97.57                                   
REMARK 500    ARG A 283       91.34    -69.93                                   
REMARK 500    TYR A 288      -61.65    -93.09                                   
REMARK 500    LYS A 293     -140.52     57.47                                   
REMARK 500    LEU A 295       47.38   -101.68                                   
REMARK 500    LYS A 319       78.15     57.70                                   
REMARK 500    ASP A 320      -39.15   -139.80                                   
REMARK 500    VAL A 322     -140.58   -104.60                                   
REMARK 500    LEU A 334       33.89    -85.38                                   
REMARK 500    ALA A 335      -30.89   -135.52                                   
REMARK 500    HIS A 365      -58.98   -134.07                                   
REMARK 500    CYS A 401       79.95   -153.67                                   
REMARK 500    ALA A 482     -154.38    -77.88                                   
REMARK 500    HIS A 506       33.07    -99.14                                   
REMARK 500    TRP A 516       73.88     41.54                                   
REMARK 500    LYS A 544       68.05   -107.65                                   
REMARK 500    PHE A 555       70.27   -114.66                                   
REMARK 500    GLN A 569      -80.78   -159.29                                   
REMARK 500    GLN A 577       35.88    -95.07                                   
REMARK 500    GLU A 578      -24.29   -140.02                                   
REMARK 500    ASN B  39       51.08   -100.35                                   
REMARK 500    GLU B  54      -55.24   -122.31                                   
REMARK 500    SER B  57       44.22    -91.09                                   
REMARK 500    LEU B  59       98.17    -58.07                                   
REMARK 500    SER B  64      -83.11   -151.55                                   
REMARK 500    ARG B  66       26.65     43.59                                   
REMARK 500    CYS B  70      -45.29   -138.61                                   
REMARK 500    CYS B  73       23.72    -79.44                                   
REMARK 500    ASP B 110     -133.22     51.42                                   
REMARK 500    LEU B 111       30.71    -81.38                                   
REMARK 500    GLU B 126       76.94     60.80                                   
REMARK 500    ASN C  23       31.99    -84.32                                   
REMARK 500    HIS C  29      -65.83   -135.77                                   
REMARK 500    ASP D 123     -169.14   -115.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EPH D 1306                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  136.0                                              
REMARK 620 3 FES B 302   S2  117.6  91.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 161   SG                                                     
REMARK 620 2 SF4 B 303   S1  119.4                                              
REMARK 620 3 SF4 B 303   S3  109.6 103.7                                        
REMARK 620 4 SF4 B 303   S4  112.1 105.7 105.1                                  
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  65   SG                                                     
REMARK 620 2 FES B 302   S1  115.5                                              
REMARK 620 3 FES B 302   S2  131.4  91.1                                        
REMARK 620 4 CYS B  70   SG  107.0 106.9 102.4                                  
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  110.3                                              
REMARK 620 3 F3S B 304   S3  136.4  99.6                                        
REMARK 620 4 F3S B 304   S4  107.3 100.3  97.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 164   SG                                                     
REMARK 620 2 SF4 B 303   S2  118.4                                              
REMARK 620 3 SF4 B 303   S3  102.6 106.2                                        
REMARK 620 4 SF4 B 303   S4  118.8 104.6 104.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C1305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 101   NE2                                                    
REMARK 620 2 HEM C1305   NA   91.4                                              
REMARK 620 3 HEM C1305   NB  100.0  88.8                                        
REMARK 620 4 HEM C1305   NC   86.2 176.7  89.5                                  
REMARK 620 5 HEM C1305   ND   83.1  92.6 176.6  89.3                            
REMARK 620 6 HIS D  79   NE2 170.8  97.4  82.8  85.2  93.9                      
REMARK 620 N                    1     2     3     4     5                       
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  131.5                                              
REMARK 620 3 SF4 B 303   S2  107.2 104.8                                        
REMARK 620 4 SF4 B 303   S4  100.3 105.8 104.5                                  
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   95.2                                              
REMARK 620 3 F3S B 304   S2  122.6 101.0                                        
REMARK 620 4 F3S B 304   S3  135.6  87.5 100.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 225   SG                                                     
REMARK 620 2 SF4 B 303   S1  104.8                                              
REMARK 620 3 SF4 B 303   S2  134.4 104.8                                        
REMARK 620 4 SF4 B 303   S3   99.2 103.8 106.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLI A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F9A D 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: 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  3AEA A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AEA B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AEA C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AEA D   34   136  UNP    A5GZW8   DHSD_PIG        57    159             
SEQRES   1 A  622  SER SER ALA LYS VAL SER ASP ALA ILE SER THR GLN TYR          
SEQRES   2 A  622  PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY          
SEQRES   3 A  622  ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER          
SEQRES   4 A  622  GLU ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE          
SEQRES   5 A  622  PRO THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE          
SEQRES   6 A  622  ASN ALA ALA LEU GLY ASN MET GLU GLU ASP ASN TRP ARG          
SEQRES   7 A  622  TRP HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU          
SEQRES   8 A  622  GLY ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA          
SEQRES   9 A  622  PRO ALA SER VAL VAL GLU LEU GLU ASN TYR GLY MET PRO          
SEQRES  10 A  622  PHE SER ARG THR GLU ASP GLY LYS ILE TYR GLN ARG ALA          
SEQRES  11 A  622  PHE GLY GLY GLN SER LEU LYS PHE GLY LYS GLY GLY GLN          
SEQRES  12 A  622  ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS          
SEQRES  13 A  622  SER LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR          
SEQRES  14 A  622  ASP THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU          
SEQRES  15 A  622  LEU MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU          
SEQRES  16 A  622  CYS ILE GLU ASP GLY SER ILE HIS ARG ILE ARG ALA ARG          
SEQRES  17 A  622  ASN THR VAL VAL ALA THR GLY GLY TYR GLY ARG THR TYR          
SEQRES  18 A  622  PHE SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY          
SEQRES  19 A  622  THR ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP          
SEQRES  20 A  622  LEU GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY          
SEQRES  21 A  622  ALA GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY          
SEQRES  22 A  622  GLY ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU          
SEQRES  23 A  622  ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP          
SEQRES  24 A  622  VAL VAL SER ARG SER MET THR LEU GLU ILE ARG GLU GLY          
SEQRES  25 A  622  ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN          
SEQRES  26 A  622  LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA VAL ARG LEU          
SEQRES  27 A  622  PRO GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL          
SEQRES  28 A  622  ASP VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL          
SEQRES  29 A  622  HIS TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY          
SEQRES  30 A  622  GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP GLN VAL VAL          
SEQRES  31 A  622  PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA CYS ALA SER          
SEQRES  32 A  622  VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU          
SEQRES  33 A  622  ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU SER ILE          
SEQRES  34 A  622  ALA GLU SER CYS ARG PRO GLY ASP LYS VAL PRO SER ILE          
SEQRES  35 A  622  LYS PRO ASN ALA GLY GLU GLU SER VAL MET ASN LEU ASP          
SEQRES  36 A  622  LYS LEU ARG PHE ALA ASN GLY THR ILE ARG THR SER GLU          
SEQRES  37 A  622  LEU ARG LEU SER MET GLN LYS SER MET GLN SER HIS ALA          
SEQRES  38 A  622  ALA VAL PHE ARG VAL GLY SER VAL LEU GLN GLU GLY CYS          
SEQRES  39 A  622  GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU GLN HIS LEU          
SEQRES  40 A  622  LYS THR PHE ASP ARG GLY MET VAL TRP ASN THR ASP LEU          
SEQRES  41 A  622  VAL GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA          
SEQRES  42 A  622  LEU GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER          
SEQRES  43 A  622  ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS GLU ARG VAL          
SEQRES  44 A  622  ASP GLU TYR ASP TYR SER LYS PRO ILE GLN GLY GLN GLN          
SEQRES  45 A  622  LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS HIS THR LEU          
SEQRES  46 A  622  SER TYR VAL ASP VAL LYS THR GLY LYS VAL SER LEU GLU          
SEQRES  47 A  622  TYR ARG PRO VAL ILE ASP LYS THR LEU ASN GLU ALA ASP          
SEQRES  48 A  622  CYS ALA THR VAL PRO PRO ALA ILE ARG SER TYR                  
SEQRES   1 B  252  ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE LYS LYS          
SEQRES   2 B  252  PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR GLY ASP          
SEQRES   3 B  252  LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU ASN ASN          
SEQRES   4 B  252  CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS          
SEQRES   5 B  252  ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG SER CYS          
SEQRES   6 B  252  ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ASN          
SEQRES   7 B  252  GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE ASP THR          
SEQRES   8 B  252  ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU PRO HIS          
SEQRES   9 B  252  MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU SER ASN          
SEQRES  10 B  252  PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS          
SEQRES  11 B  252  LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN TYR LEU          
SEQRES  12 B  252  GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY LEU TYR          
SEQRES  13 B  252  GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO          
SEQRES  14 B  252  SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA          
SEQRES  15 B  252  VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG          
SEQRES  16 B  252  ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU GLN ASP          
SEQRES  17 B  252  PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS          
SEQRES  18 B  252  THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA          
SEQRES  19 B  252  ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU          
SEQRES  20 B  252  LYS LYS ALA SER ALA                                          
SEQRES   1 C  140  LEU GLY THR THR ALA LYS GLU GLU MET GLU ARG PHE TRP          
SEQRES   2 C  140  ASN LYS ASN LEU GLY SER ASN ARG PRO LEU SER PRO HIS          
SEQRES   3 C  140  ILE THR ILE TYR ARG TRP SER LEU PRO MET ALA MET SER          
SEQRES   4 C  140  ILE CYS HIS ARG GLY THR GLY ILE ALA LEU SER ALA GLY          
SEQRES   5 C  140  VAL SER LEU PHE GLY LEU SER ALA LEU LEU LEU PRO GLY          
SEQRES   6 C  140  ASN PHE GLU SER HIS LEU GLU LEU VAL LYS SER LEU CYS          
SEQRES   7 C  140  LEU GLY PRO THR LEU ILE TYR THR ALA LYS PHE GLY ILE          
SEQRES   8 C  140  VAL PHE PRO LEU MET TYR HIS THR TRP ASN GLY ILE ARG          
SEQRES   9 C  140  HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU THR ILE PRO          
SEQRES  10 C  140  GLN LEU THR GLN SER GLY VAL VAL VAL LEU ILE LEU THR          
SEQRES  11 C  140  VAL LEU SER SER VAL GLY LEU ALA ALA MET                      
SEQRES   1 D  103  ALA SER SER LYS ALA ALA SER LEU HIS TRP THR GLY GLU          
SEQRES   2 D  103  ARG VAL VAL SER VAL LEU LEU LEU GLY LEU LEU PRO ALA          
SEQRES   3 D  103  ALA TYR LEU ASN PRO CYS SER ALA MET ASP TYR SER LEU          
SEQRES   4 D  103  ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY ILE GLY          
SEQRES   5 D  103  GLN VAL VAL THR ASP TYR VAL ARG GLY ASP ALA LEU GLN          
SEQRES   6 D  103  LYS ALA ALA LYS ALA GLY LEU LEU ALA LEU SER ALA PHE          
SEQRES   7 D  103  THR PHE ALA GLY LEU CYS TYR PHE ASN TYR HIS ASP VAL          
SEQRES   8 D  103  GLY ILE CYS LYS ALA VAL ALA MET LEU TRP LYS LEU              
HET    FAD  A 700      53                                                       
HET    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    MLI  A 701       7                                                       
HET    HEM  C1305      43                                                       
HET    F9A  D1201      23                                                       
HET    EPH  D1306      44                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     MLI MALONATE ION                                                     
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     F9A N-{3-[(DIMETHYLAMINO)METHYL]PHENYL}-2-                           
HETNAM   2 F9A  (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  SF4    FE4 S4                                                       
FORMUL   8  F3S    FE3 S4                                                       
FORMUL   9  MLI    C3 H2 O4 2-                                                  
FORMUL  10  HEM    C34 H32 FE N4 O4                                             
FORMUL  11  F9A    C17 H17 F3 N2 O                                              
FORMUL  12  EPH    C39 H68 N O8 P                                               
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  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  ARG A  240  1                                   9    
HELIX    9   9 GLU A  267  GLY A  273  1                                   7    
HELIX   10  10 PHE A  284  ALA A  289  1                                   6    
HELIX   11  11 SER A  297  GLU A  311  1                                  15    
HELIX   12  12 GLU A  332  ARG A  337  1                                   6    
HELIX   13  13 PRO A  339  PHE A  348  1                                  10    
HELIX   14  14 ASN A  413  CYS A  433  1                                  21    
HELIX   15  15 GLY A  447  PHE A  459  1                                  13    
HELIX   16  16 THR A  466  ALA A  481  1                                  16    
HELIX   17  17 VAL A  486  ASP A  503  1                                  18    
HELIX   18  18 ASN A  517  ARG A  543  1                                  27    
HELIX   19  19 MET B   43  GLU B   54  1                                  12    
HELIX   20  20 LEU B  115  ILE B  125  1                                  11    
HELIX   21  21 SER B  145  LYS B  151  1                                   7    
HELIX   22  22 CYS B  164  SER B  167  5                                   4    
HELIX   23  23 CYS B  168  ASN B  174  1                                   7    
HELIX   24  24 GLY B  180  TRP B  190  1                                  11    
HELIX   25  25 PHE B  198  LYS B  205  1                                   8    
HELIX   26  26 MET B  219  CYS B  225  1                                   7    
HELIX   27  27 ASN B  230  TYR B  245  1                                  16    
HELIX   28  28 THR C    7  GLY C   21  1                                  15    
HELIX   29  29 SER C   36  LEU C   66  1                                  31    
HELIX   30  30 ASN C   69  LYS C   78  1                                  10    
HELIX   31  31 THR C   85  LEU C  113  1                                  29    
HELIX   32  32 THR C  118  ALA C  142  1                                  25    
HELIX   33  33 LYS D   37  ASN D   63  1                                  27    
HELIX   34  34 CYS D   65  VAL D   92  1                                  28    
HELIX   35  35 GLY D   94  ASP D  123  1                                  30    
HELIX   36  36 GLY D  125  LYS D  135  1                                  11    
SHEET    1   A 4 HIS A  18  GLU A  19  0                                        
SHEET    2   A 4 ILE A 202  ARG A 206  1  O  ARG A 206   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  PHE A 174           
SHEET    3   B 6 ALA A  22  VAL A  25  1  N  ALA A  22   O  ALA A  46           
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  VAL A 379   O  VAL A 390           
SHEET    1   C 3 ILE A  65  ASN A  66  0                                        
SHEET    2   C 3 GLN A 143  CYS A 148 -1  O  CYS A 148   N  ILE A  65           
SHEET    3   C 3 GLN A 128  SER A 135 -1  N  ARG A 129   O  CYS A 147           
SHEET    1   D 3 CYS A 245  GLN A 246  0                                        
SHEET    2   D 3 LYS A 582  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 2 ILE A 275  LEU A 276  0                                        
SHEET    2   F 2 LEU A 324  GLN A 325 -1  O  GLN A 325   N  ILE A 275           
SHEET    1   G 2 ILE A 371  PRO A 372  0                                        
SHEET    2   G 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   H 2 ILE A 464  ARG A 465  0                                        
SHEET    2   H 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   I 2 PHE A 484  ARG A 485  0                                        
SHEET    2   I 2 ALA A 551  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    1   J 5 HIS B  29  ASP B  36  0                                        
SHEET    2   J 5 ILE B  11  ARG B  18 -1  N  ARG B  18   O  HIS B  29           
SHEET    3   J 5 SER B  97  TYR B 100  1  O  SER B  97   N  ALA B  15           
SHEET    4   J 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   J 5 ASN B  81  LEU B  83 -1  O  THR B  82   N  MET B  75           
SHEET    1   K 2 VAL B 107  LYS B 109  0                                        
SHEET    2   K 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  ILE B 108           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  2.12  
LINK         SG  CYS B  73                FE2  FES B 302     1555   1555  1.95  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.11  
LINK         SG  CYS B  65                FE1  FES B 302     1555   1555  2.12  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.13  
LINK         SG  CYS B 164                FE1  SF4 B 303     1555   1555  2.14  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.16  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.18  
LINK         SG  CYS B  70                FE1  FES B 302     1555   1555  2.40  
LINK         SG  CYS B 158                FE3  SF4 B 303     1555   1555  2.43  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.49  
LINK         SG  CYS B 225                FE4  SF4 B 303     1555   1555  2.51  
SITE     1 AC1 36 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 36 ALA A  30  VAL A  48  THR A  49  LYS A  50                    
SITE     3 AC1 36 LEU A  51  SER A  56  HIS A  57  THR A  58                    
SITE     4 AC1 36 ALA A  60  ALA A  61  GLN A  62  GLY A  63                    
SITE     5 AC1 36 GLY A  64  TYR A 177  PHE A 178  ALA A 179                    
SITE     6 AC1 36 ALA A 213  GLY A 215  THR A 225  SER A 226                    
SITE     7 AC1 36 ASP A 233  LEU A 264  HIS A 365  TYR A 366                    
SITE     8 AC1 36 GLU A 398  ARG A 409  ALA A 412  ASN A 413                    
SITE     9 AC1 36 SER A 414  LEU A 415  LEU A 418  MLI A 701                    
SITE     1 AC2  8 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC2  8 CYS B  70  GLY B  71  CYS B  73  CYS B  85                    
SITE     1 AC3  9 CYS B 158  LEU B 160  CYS B 161  ALA B 162                    
SITE     2 AC3  9 CYS B 164  ALA B 182  CYS B 225  PRO B 226                    
SITE     3 AC3  9 PRO B 231                                                     
SITE     1 AC4 10 CYS B 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC4 10 THR B 217  ILE B 218  MET B 219  ASN B 220                    
SITE     3 AC4 10 CYS B 221  ILE B 235                                          
SITE     1 AC5 12 GLN A  62  GLY A  63  PHE A 131  HIS A 254                    
SITE     2 AC5 12 LEU A 264  THR A 266  GLU A 267  ARG A 298                    
SITE     3 AC5 12 HIS A 365  ARG A 409  ALA A 412  FAD A 700                    
SITE     1 AC6 17 HIS B 216  HIS C  45  ARG C  46  GLY C  49                    
SITE     2 AC6 17 LEU C  52  SER C  53  HIS C 101  THR C 102                    
SITE     3 AC6 17 HIS C 108  ARG D  47  SER D  50  LEU D  53                    
SITE     4 AC6 17 LEU D  54  LEU D  57  HIS D  79  GLY D  83                    
SITE     5 AC6 17 ILE D  84                                                     
SITE     1 AC7  9 PRO B 169  SER B 170  TRP B 173  HIS B 216                    
SITE     2 AC7  9 TRP C  35  SER C  42  ILE C  43  ARG C  46                    
SITE     3 AC7  9 TYR D  91                                                     
SITE     1 AC8  6 MET C 143  ALA D  60  TYR D  61  LYS D  99                    
SITE     2 AC8  6 CYS D 127  TRP D 134                                          
CRYST1   71.505   83.751  294.959  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      0.013985  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011940  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003390        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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