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Database: PDB
Entry: 3AEE
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10   3AEE              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 ATPENIN A5                                                           
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 3AEE    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 ATPENIN A5                                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.22 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) : 3.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 27888                          
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) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1436                            
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) : 3.22                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.30                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1808                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.4010                       
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          : 138                                     
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) : 106.19                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.71000                                              
REMARK   3    B22 (A**2) : 0.09000                                              
REMARK   3    B33 (A**2) : -0.79000                                             
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): 0.535         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.456         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 55.552        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8823 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11974 ; 1.110 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 5.477 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;35.032 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;19.184 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;17.217 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1306 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6640 ; 0.004 ; 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 ; 0.248 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8675 ; 0.463 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3413 ; 0.481 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3282 ; 0.839 ; 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   259                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6960 -17.3200  18.0500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1212 T22:   0.2789                                     
REMARK   3      T33:   0.4602 T12:  -0.0551                                     
REMARK   3      T13:   0.0275 T23:   0.0329                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1428 L22:   1.0654                                     
REMARK   3      L33:   3.6172 L12:  -0.4470                                     
REMARK   3      L13:  -0.2137 L23:  -0.4965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0232 S12:  -0.1703 S13:  -0.0205                       
REMARK   3      S21:   0.1066 S22:   0.0118 S23:   0.0322                       
REMARK   3      S31:  -0.4243 S32:   0.1140 S33:   0.0114                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   260        A   349                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.3360   8.8990  24.2460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8785 T22:   0.1208                                     
REMARK   3      T33:   0.7051 T12:  -0.2766                                     
REMARK   3      T13:   0.3355 T23:  -0.1337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4705 L22:   0.4475                                     
REMARK   3      L33:   0.8569 L12:   0.3226                                     
REMARK   3      L13:   0.4612 L23:  -0.4977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2412 S12:  -0.0636 S13:   0.8496                       
REMARK   3      S21:   0.8818 S22:  -0.1680 S23:   0.2911                       
REMARK   3      S31:  -1.1377 S32:   0.1887 S33:  -0.0732                       
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):  -3.1530 -10.6190  11.7850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1369 T22:   0.3235                                     
REMARK   3      T33:   0.5108 T12:  -0.1147                                     
REMARK   3      T13:   0.0719 T23:   0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8936 L22:   1.0910                                     
REMARK   3      L33:   3.7701 L12:  -0.2587                                     
REMARK   3      L13:  -0.1329 L23:  -0.0358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0260 S12:  -0.1287 S13:   0.1768                       
REMARK   3      S21:  -0.2011 S22:   0.0279 S23:  -0.1782                       
REMARK   3      S31:  -0.5426 S32:   0.4969 S33:  -0.0018                       
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    49                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3510 -11.5120  47.6850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2174 T22:   1.0378                                     
REMARK   3      T33:   0.6371 T12:  -0.2135                                     
REMARK   3      T13:  -0.2541 T23:  -0.0760                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9728 L22:   2.7706                                     
REMARK   3      L33:   4.1974 L12:   0.3149                                     
REMARK   3      L13:  -1.0727 L23:   2.1885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0630 S12:  -0.7265 S13:   0.0496                       
REMARK   3      S21:   0.1110 S22:   0.1371 S23:  -0.6818                       
REMARK   3      S31:  -0.2735 S32:   1.2246 S33:  -0.2001                       
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    50        B    79                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7160 -12.2810  40.1490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2752 T22:   0.7625                                     
REMARK   3      T33:   0.5304 T12:  -0.3180                                     
REMARK   3      T13:  -0.1324 T23:   0.1071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3049 L22:   2.2086                                     
REMARK   3      L33:   3.0291 L12:   1.3445                                     
REMARK   3      L13:   0.3708 L23:   2.3370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0703 S12:   0.0117 S13:   0.0824                       
REMARK   3      S21:  -0.3600 S22:   0.1734 S23:  -0.1803                       
REMARK   3      S31:  -0.6317 S32:   0.6133 S33:  -0.1030                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    80        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0770 -10.8470  50.1320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1975 T22:   0.5802                                     
REMARK   3      T33:   0.4216 T12:  -0.1267                                     
REMARK   3      T13:  -0.0909 T23:  -0.1731                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5311 L22:   4.4380                                     
REMARK   3      L33:   8.5293 L12:   1.1187                                     
REMARK   3      L13:  -1.3782 L23:   0.0940                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1675 S12:  -1.3041 S13:   0.7942                       
REMARK   3      S21:  -0.0565 S22:  -0.2625 S23:   0.3422                       
REMARK   3      S31:  -0.9673 S32:   0.3931 S33:   0.0951                       
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   107        B   165                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.8020 -22.2620  33.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2016 T22:   0.2971                                     
REMARK   3      T33:   0.5254 T12:  -0.0007                                     
REMARK   3      T13:  -0.0076 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6477 L22:   0.3112                                     
REMARK   3      L33:   4.6877 L12:  -0.3214                                     
REMARK   3      L13:  -1.6765 L23:  -0.4706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1076 S12:  -0.0108 S13:  -0.0224                       
REMARK   3      S21:  -0.1039 S22:   0.0505 S23:   0.1078                       
REMARK   3      S31:   0.1648 S32:  -0.4912 S33:  -0.1581                       
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   166        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3220 -25.1220  45.0470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2714 T22:   0.1819                                     
REMARK   3      T33:   0.5672 T12:  -0.0264                                     
REMARK   3      T13:   0.0895 T23:  -0.0769                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9183 L22:   0.3220                                     
REMARK   3      L33:   5.5690 L12:  -0.2952                                     
REMARK   3      L13:  -1.2731 L23:  -1.0498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1764 S12:   0.1259 S13:   0.0185                       
REMARK   3      S21:  -0.0207 S22:   0.0732 S23:   0.0573                       
REMARK   3      S31:   0.3597 S32:  -0.5112 S33:   0.1033                       
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    65                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1810 -29.4220  58.3240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2926 T22:   0.1709                                     
REMARK   3      T33:   0.4523 T12:   0.0760                                     
REMARK   3      T13:   0.0175 T23:   0.0895                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7894 L22:   1.3386                                     
REMARK   3      L33:   4.9856 L12:   1.1251                                     
REMARK   3      L13:  -1.6394 L23:  -0.8642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0399 S12:  -0.3397 S13:  -0.1121                       
REMARK   3      S21:   0.1528 S22:  -0.2112 S23:   0.0794                       
REMARK   3      S31:  -0.0105 S32:   0.7986 S33:   0.1713                       
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    66        C    89                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.5380 -27.3890  94.3010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7235 T22:   0.4099                                     
REMARK   3      T33:   0.3477 T12:   0.0800                                     
REMARK   3      T13:  -0.0393 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6770 L22:   9.8056                                     
REMARK   3      L33:   8.9614 L12:   2.5096                                     
REMARK   3      L13:  -1.8693 L23:  -1.3813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2198 S12:  -0.3761 S13:   0.3675                       
REMARK   3      S21:   1.6528 S22:   0.1465 S23:   0.3943                       
REMARK   3      S31:  -0.5261 S32:   0.3326 S33:  -0.3663                       
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    90        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.2380 -14.5500  68.4880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6744 T22:   0.0755                                     
REMARK   3      T33:   0.4060 T12:  -0.0184                                     
REMARK   3      T13:   0.1335 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1881 L22:   3.2341                                     
REMARK   3      L33:   7.9116 L12:  -0.2362                                     
REMARK   3      L13:  -2.2400 L23:   0.8311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4664 S12:  -0.0061 S13:   0.1134                       
REMARK   3      S21:   0.6545 S22:  -0.0942 S23:   0.0017                       
REMARK   3      S31:  -0.7813 S32:  -0.2949 S33:  -0.3722                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    35        D    80                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.2320 -29.7950  67.2780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4915 T22:   0.3851                                     
REMARK   3      T33:   0.7294 T12:   0.0437                                     
REMARK   3      T13:   0.3017 T23:  -0.0702                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9703 L22:   3.9776                                     
REMARK   3      L33:   7.6762 L12:   2.4768                                     
REMARK   3      L13:  -2.3406 L23:   1.1536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1519 S12:   0.1436 S13:  -0.3233                       
REMARK   3      S21:  -0.0550 S22:  -0.4838 S23:   0.3172                       
REMARK   3      S31:  -0.2838 S32:  -1.1501 S33:   0.6357                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    81        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3730 -36.2440  61.1160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9249 T22:   0.1350                                     
REMARK   3      T33:   1.1061 T12:   0.0215                                     
REMARK   3      T13:   0.3434 T23:   0.2558                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0062 L22:   0.2138                                     
REMARK   3      L33:  12.3740 L12:  -0.4161                                     
REMARK   3      L13:   9.8327 L23:  -0.7177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3195 S12:  -0.0034 S13:  -0.5394                       
REMARK   3      S21:  -0.2101 S22:  -0.0147 S23:  -0.1161                       
REMARK   3      S31:   0.4947 S32:   0.0993 S33:  -0.3048                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    97        D   122                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.9330 -41.9250  73.8030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8255 T22:   0.3256                                     
REMARK   3      T33:   0.5523 T12:  -0.2679                                     
REMARK   3      T13:   0.2597 T23:   0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2609 L22:   4.3155                                     
REMARK   3      L33:   0.1459 L12:  -1.5816                                     
REMARK   3      L13:  -0.6559 L23:  -0.4517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0096 S12:   1.1538 S13:  -0.5367                       
REMARK   3      S21:  -0.1148 S22:  -0.1500 S23:  -0.1335                       
REMARK   3      S31:   0.1012 S32:  -0.1156 S33:   0.1404                       
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   123        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5960 -27.0720  88.1940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8086 T22:   0.5063                                     
REMARK   3      T33:   0.6081 T12:   0.0717                                     
REMARK   3      T13:   0.1619 T23:  -0.0834                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7765 L22:   0.2365                                     
REMARK   3      L33:   3.6985 L12:   0.5542                                     
REMARK   3      L13:  -2.5487 L23:  -0.7616                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1277 S12:  -0.0339 S13:  -0.1595                       
REMARK   3      S21:   0.0626 S22:  -0.1718 S23:   0.0588                       
REMARK   3      S31:   0.0867 S32:  -0.0667 S33:   0.2995                       
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 3AEE 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 RCSB029148.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-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               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.80000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27959                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
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     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6570                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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   (%): 65.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
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       35.37550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      146.86750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.92050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      146.86750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.37550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.92050            
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: 12770 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THESE COMPLEX FORMS MITOCHONDRIAL RESPIRATORY COMPLEX II.            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     ALA B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     LYS B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     ALA B   250                                                      
REMARK 465     SER B   251                                                      
REMARK 465     ALA B   252                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     ALA D    34                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  62      -61.48   -120.46                                   
REMARK 500    MET A  72      -76.03    -94.13                                   
REMARK 500    ALA A 151     -128.79     41.53                                   
REMARK 500    ARG A 153       64.92   -117.88                                   
REMARK 500    ASP A 170       44.96    -83.22                                   
REMARK 500    LEU A 180      -62.05    -97.05                                   
REMARK 500    ALA A 213       56.68   -140.04                                   
REMARK 500    TYR A 217       46.31   -144.05                                   
REMARK 500    ARG A 219       11.20    -64.77                                   
REMARK 500    MET A 237      -37.32    -37.15                                   
REMARK 500    ARG A 283       85.98    -69.13                                   
REMARK 500    MET A 285       26.36    -78.69                                   
REMARK 500    LYS A 293     -153.64     59.15                                   
REMARK 500    LEU A 295       45.10   -105.61                                   
REMARK 500    HIS A 365      -43.87   -144.37                                   
REMARK 500    ASN A 408      114.03   -165.16                                   
REMARK 500    ASN A 461       67.17   -113.60                                   
REMARK 500    ALA A 481       54.10   -118.07                                   
REMARK 500    ALA A 482     -153.37    -77.67                                   
REMARK 500    ASP A 503      -19.83    -45.39                                   
REMARK 500    TRP A 516       56.52     33.75                                   
REMARK 500    LYS A 544       54.96   -104.11                                   
REMARK 500    GLN A 569      -78.34    -81.86                                   
REMARK 500    GLN A 571      129.33   -175.73                                   
REMARK 500    GLU A 598     -169.97   -116.79                                   
REMARK 500    THR A 606     -157.14    -92.86                                   
REMARK 500    ASN A 608       95.04   -166.38                                   
REMARK 500    TRP B  19      116.21   -162.13                                   
REMARK 500    ILE B  55      -72.11   -105.94                                   
REMARK 500    SER B  64      -84.75   -157.37                                   
REMARK 500    ASP B 110     -124.11     48.03                                   
REMARK 500    GLU B 126       72.88     51.54                                   
REMARK 500    GLU B 134        5.51    -65.74                                   
REMARK 500    CYS B 164      -85.17    -33.23                                   
REMARK 500    THR B 217       59.13     39.25                                   
REMARK 500    HIS C  29      -88.27   -116.09                                   
REMARK 500    LYS C  78       64.48    -68.44                                   
REMARK 500    SER C  79      -65.98    -91.39                                   
REMARK 500    CYS C  81     -165.77     57.77                                   
REMARK 500    PRO C  84      -66.04    -10.69                                   
REMARK 500    THR C  85       48.76    -79.26                                   
REMARK 500    LEU C  86      -41.61   -158.43                                   
REMARK 500    LEU C 117       47.43   -106.10                                   
REMARK 500    LYS D  37       51.50    -92.73                                   
REMARK 500    ASN D  63       76.24   -153.32                                   
REMARK 500    VAL D  92       86.30    -69.40                                   
REMARK 500    ASP D 123     -160.00   -125.81                                   
REMARK 500    LYS D 135       76.41    -69.99                                   
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  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  70   SG                                                     
REMARK 620 2 FES B 302   S1  104.4                                              
REMARK 620 3 FES B 302   S2  121.2  91.0                                        
REMARK 620 4 CYS B  65   SG  104.8 124.8 111.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  117.5                                              
REMARK 620 3 FES B 302   S2  129.1  91.2                                        
REMARK 620 4 CYS B  85   SG  104.0 118.1  96.4                                  
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   90.4                                              
REMARK 620 3 HEM C1305   NB   97.6  88.5                                        
REMARK 620 4 HEM C1305   NC   83.7 173.8  90.9                                  
REMARK 620 5 HEM C1305   ND   80.7  90.1 177.8  90.3                            
REMARK 620 6 HIS D  79   NE2 173.6  96.0  83.2  90.0  98.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 303   S2  106.7                                              
REMARK 620 3 SF4 B 303   S3  132.6 104.3                                        
REMARK 620 4 SF4 B 303   S4  100.5 107.2 103.5                                  
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   84.7                                              
REMARK 620 3 F3S B 304   S3   93.3  97.5                                        
REMARK 620 4 F3S B 304   S4   97.0 161.3 101.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 221   SG                                                     
REMARK 620 2 F3S B 304   S1  108.6                                              
REMARK 620 3 F3S B 304   S3  113.2  97.5                                        
REMARK 620 4 F3S B 304   S4  105.2 131.9  99.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 215   SG                                                     
REMARK 620 2 F3S B 304   S1  102.4                                              
REMARK 620 3 F3S B 304   S2  106.0 121.6                                        
REMARK 620 4 F3S B 304   S3  134.8  97.8  96.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 225   SG                                                     
REMARK 620 2 SF4 B 303   S1   96.1                                              
REMARK 620 3 SF4 B 303   S3  109.5 103.6                                        
REMARK 620 4 SF4 B 303   S4  134.0 106.2 103.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AT5 C 1201                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ABV   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE1   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE2   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE3   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE4   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE5   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE6   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE7   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE8   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AE9   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEA   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 3AEB   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR                
REMARK 900 RELATED ID: 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: 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  3AEE A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3AEE B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3AEE C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3AEE D   34   136  UNP    A5GZW8   DHSD_PIG        57    159             
SEQRES   1 A  622  SER SER ALA LYS VAL SER ASP ALA ILE SER THR GLN TYR          
SEQRES   2 A  622  PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY          
SEQRES   3 A  622  ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER          
SEQRES   4 A  622  GLU ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE          
SEQRES   5 A  622  PRO THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE          
SEQRES   6 A  622  ASN ALA ALA LEU GLY ASN MET GLU GLU ASP ASN TRP ARG          
SEQRES   7 A  622  TRP HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU          
SEQRES   8 A  622  GLY ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA          
SEQRES   9 A  622  PRO ALA SER VAL VAL GLU LEU GLU ASN TYR GLY MET PRO          
SEQRES  10 A  622  PHE SER ARG THR GLU ASP GLY LYS ILE TYR GLN ARG ALA          
SEQRES  11 A  622  PHE GLY GLY GLN SER LEU LYS PHE GLY LYS GLY GLY GLN          
SEQRES  12 A  622  ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS          
SEQRES  13 A  622  SER LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR          
SEQRES  14 A  622  ASP THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU          
SEQRES  15 A  622  LEU MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU          
SEQRES  16 A  622  CYS ILE GLU ASP GLY SER ILE HIS ARG ILE ARG ALA ARG          
SEQRES  17 A  622  ASN THR VAL VAL ALA THR GLY GLY TYR GLY ARG THR TYR          
SEQRES  18 A  622  PHE SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY          
SEQRES  19 A  622  THR ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP          
SEQRES  20 A  622  LEU GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY          
SEQRES  21 A  622  ALA GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY          
SEQRES  22 A  622  GLY ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU          
SEQRES  23 A  622  ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP          
SEQRES  24 A  622  VAL VAL SER ARG SER MET THR LEU GLU ILE ARG GLU GLY          
SEQRES  25 A  622  ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN          
SEQRES  26 A  622  LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA VAL ARG LEU          
SEQRES  27 A  622  PRO GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL          
SEQRES  28 A  622  ASP VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL          
SEQRES  29 A  622  HIS TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY          
SEQRES  30 A  622  GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP GLN VAL VAL          
SEQRES  31 A  622  PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA CYS ALA SER          
SEQRES  32 A  622  VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU          
SEQRES  33 A  622  ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU SER ILE          
SEQRES  34 A  622  ALA GLU SER CYS ARG PRO GLY ASP LYS VAL PRO SER ILE          
SEQRES  35 A  622  LYS PRO ASN ALA GLY GLU GLU SER VAL MET ASN LEU ASP          
SEQRES  36 A  622  LYS LEU ARG PHE ALA ASN GLY THR ILE ARG THR SER GLU          
SEQRES  37 A  622  LEU ARG LEU SER MET GLN LYS SER MET GLN SER HIS ALA          
SEQRES  38 A  622  ALA VAL PHE ARG VAL GLY SER VAL LEU GLN GLU GLY CYS          
SEQRES  39 A  622  GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU GLN HIS LEU          
SEQRES  40 A  622  LYS THR PHE ASP ARG GLY MET VAL TRP ASN THR ASP LEU          
SEQRES  41 A  622  VAL GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA          
SEQRES  42 A  622  LEU GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER          
SEQRES  43 A  622  ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS GLU ARG VAL          
SEQRES  44 A  622  ASP GLU TYR ASP TYR SER LYS PRO ILE GLN GLY GLN GLN          
SEQRES  45 A  622  LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS HIS THR LEU          
SEQRES  46 A  622  SER TYR VAL ASP VAL LYS THR GLY LYS VAL SER LEU GLU          
SEQRES  47 A  622  TYR ARG PRO VAL ILE ASP LYS THR LEU ASN GLU ALA ASP          
SEQRES  48 A  622  CYS ALA THR VAL PRO PRO ALA ILE ARG SER TYR                  
SEQRES   1 B  252  ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE LYS LYS          
SEQRES   2 B  252  PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR GLY ASP          
SEQRES   3 B  252  LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU ASN ASN          
SEQRES   4 B  252  CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS          
SEQRES   5 B  252  ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG SER CYS          
SEQRES   6 B  252  ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ASN          
SEQRES   7 B  252  GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE ASP THR          
SEQRES   8 B  252  ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU PRO HIS          
SEQRES   9 B  252  MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU SER ASN          
SEQRES  10 B  252  PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS          
SEQRES  11 B  252  LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN TYR LEU          
SEQRES  12 B  252  GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY LEU TYR          
SEQRES  13 B  252  GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO          
SEQRES  14 B  252  SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA          
SEQRES  15 B  252  VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG          
SEQRES  16 B  252  ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU GLN ASP          
SEQRES  17 B  252  PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS          
SEQRES  18 B  252  THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA          
SEQRES  19 B  252  ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU          
SEQRES  20 B  252  LYS LYS ALA SER ALA                                          
SEQRES   1 C  140  LEU GLY THR THR ALA LYS GLU GLU MET GLU ARG PHE TRP          
SEQRES   2 C  140  ASN LYS ASN LEU GLY SER ASN ARG PRO LEU SER PRO HIS          
SEQRES   3 C  140  ILE THR ILE TYR ARG TRP SER LEU PRO MET ALA MET SER          
SEQRES   4 C  140  ILE CYS HIS ARG GLY THR GLY ILE ALA LEU SER ALA GLY          
SEQRES   5 C  140  VAL SER LEU PHE GLY LEU SER ALA LEU LEU LEU PRO GLY          
SEQRES   6 C  140  ASN PHE GLU SER HIS LEU GLU LEU VAL LYS SER LEU CYS          
SEQRES   7 C  140  LEU GLY PRO THR LEU ILE TYR THR ALA LYS PHE GLY ILE          
SEQRES   8 C  140  VAL PHE PRO LEU MET TYR HIS THR TRP ASN GLY ILE ARG          
SEQRES   9 C  140  HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU THR ILE PRO          
SEQRES  10 C  140  GLN LEU THR GLN SER GLY VAL VAL VAL LEU ILE LEU THR          
SEQRES  11 C  140  VAL LEU SER SER VAL GLY LEU ALA ALA MET                      
SEQRES   1 D  103  ALA SER SER LYS ALA ALA SER LEU HIS TRP THR GLY GLU          
SEQRES   2 D  103  ARG VAL VAL SER VAL LEU LEU LEU GLY LEU LEU PRO ALA          
SEQRES   3 D  103  ALA TYR LEU ASN PRO CYS SER ALA MET ASP TYR SER LEU          
SEQRES   4 D  103  ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY ILE GLY          
SEQRES   5 D  103  GLN VAL VAL THR ASP TYR VAL ARG GLY ASP ALA LEU GLN          
SEQRES   6 D  103  LYS ALA ALA LYS ALA GLY LEU LEU ALA LEU SER ALA PHE          
SEQRES   7 D  103  THR PHE ALA GLY LEU CYS TYR PHE ASN TYR HIS ASP VAL          
SEQRES   8 D  103  GLY ILE CYS LYS ALA VAL ALA MET LEU TRP LYS LEU              
HET    FAD  A 700      53                                                       
HET    FES  B 302       4                                                       
HET    F3S  B 304       7                                                       
HET    SF4  B 303       8                                                       
HET    HEM  C1305      43                                                       
HET    AT5  C1201      23                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     AT5 3-[(2S,4S,5R)-5,6-DICHLORO-2,4-DIMETHYL-1-OXOHEXYL]-4-           
HETNAM   2 AT5  HYDROXY-5,6-DIMETHOXY-2(1H)-PYRIDINONE                          
HETSYN     HEM HEME                                                             
HETSYN     AT5 ATPENIN A5; AA5                                                  
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  FES    FE2 S2                                                       
FORMUL   7  F3S    FE3 S4                                                       
FORMUL   8  SF4    FE4 S4                                                       
FORMUL   9  HEM    C34 H32 FE N4 O4                                             
FORMUL  10  AT5    C15 H21 CL2 N O5                                             
HELIX    1   1 GLY A   28  ALA A   41  1                                  14    
HELIX    2   2 PHE A   52  ALA A   61  5                                  10    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  GLY A  115  1                                  23    
HELIX    5   5 ARG A  153  LEU A  167  1                                  15    
HELIX    6   6 TYR A  217  TYR A  221  5                                   5    
HELIX    7   7 GLY A  232  ARG A  240  1                                   9    
HELIX    8   8 THR A  266  ARG A  270  5                                   5    
HELIX    9   9 ARG A  283  ARG A  287  5                                   5    
HELIX   10  10 ASP A  299  GLU A  311  1                                  13    
HELIX   11  11 PRO A  330  LEU A  338  1                                   9    
HELIX   12  12 LEU A  338  ALA A  349  1                                  12    
HELIX   13  13 ASP A  352  LYS A  355  5                                   4    
HELIX   14  14 ASN A  413  GLU A  431  1                                  19    
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 PRO A  575  HIS A  579  5                                   5    
HELIX   20  20 MET B   43  ILE B   55  1                                  13    
HELIX   21  21 LEU B  115  SER B  124  1                                  10    
HELIX   22  22 ASP B  133  GLU B  137  5                                   5    
HELIX   23  23 SER B  145  LYS B  151  1                                   7    
HELIX   24  24 CYS B  168  GLY B  175  1                                   8    
HELIX   25  25 GLY B  180  ILE B  192  1                                  13    
HELIX   26  26 GLU B  200  LYS B  205  1                                   6    
HELIX   27  27 MET B  219  CYS B  225  1                                   7    
HELIX   28  28 ASN B  230  TYR B  245  1                                  16    
HELIX   29  29 THR C    7  LEU C   20  1                                  14    
HELIX   30  30 SER C   36  LEU C   61  1                                  26    
HELIX   31  31 LEU C   61  LEU C   66  1                                   6    
HELIX   32  32 PHE C   70  LYS C   78  1                                   9    
HELIX   33  33 TYR C   88  LEU C  113  1                                  26    
HELIX   34  34 THR C  118  ALA C  142  1                                  25    
HELIX   35  35 LYS D   37  GLY D   55  1                                  19    
HELIX   36  36 GLY D   55  ASN D   63  1                                   9    
HELIX   37  37 CYS D   65  VAL D   92  1                                  28    
HELIX   38  38 ASP D   95  ASP D  123  1                                  29    
HELIX   39  39 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 HIS A  18  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  25           
SHEET    5   A 6 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    6   A 6 TYR A 177  GLU A 185 -1  N  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 HIS A  18  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  25           
SHEET    5   B 6 GLN A 386  ALA A 395  1  O  TYR A 394   N  VAL A 212           
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  SER A 586 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 LEU A 597  PRO A 601 -1  O  ARG A 600   N  HIS A 583           
SHEET    1   E 2 VAL A 251  HIS A 254  0                                        
SHEET    2   E 2 THR A 363  ASN A 367 -1  O  HIS A 365   N  GLN A 252           
SHEET    1   F 3 ILE A 275  ILE A 277  0                                        
SHEET    2   F 3 VAL A 322  GLN A 325 -1  O  GLN A 325   N  ILE A 275           
SHEET    3   F 3 PRO A 357  VAL A 360 -1  O  ILE A 358   N  LEU A 324           
SHEET    1   G 2 ILE A 371  PRO A 372  0                                        
SHEET    2   G 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   H 2 ILE A 464  ARG A 465  0                                        
SHEET    2   H 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   I 2 PHE A 484  ARG A 485  0                                        
SHEET    2   I 2 ALA A 551  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    1   J 5 HIS B  29  ASP B  36  0                                        
SHEET    2   J 5 ILE B  11  ARG B  18 -1  N  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           
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  1.96  
LINK         SG  CYS B  70                FE2  FES B 302     1555   1555  1.95  
LINK         SG  CYS B  73                FE1  FES B 302     1555   1555  1.97  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.14  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.19  
LINK         SG  CYS B  65                FE2  FES B 302     1555   1555  2.35  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.38  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.40  
LINK         SG  CYS B 221                FE3  F3S B 304     1555   1555  2.41  
LINK         SG  CYS B 215                FE1  F3S B 304     1555   1555  2.44  
LINK         SG  CYS B  85                FE1  FES B 302     1555   1555  2.46  
LINK         SG  CYS B 225                FE2  SF4 B 303     1555   1555  2.66  
SITE     1 AC1 33 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 33 ALA A  30  THR A  49  LYS A  50  LEU A  51                    
SITE     3 AC1 33 SER A  56  HIS A  57  THR A  58  ALA A  61                    
SITE     4 AC1 33 GLN A  62  GLY A  63  GLY A  64  TYR A 177                    
SITE     5 AC1 33 PHE A 178  ALA A 179  THR A 214  GLY A 215                    
SITE     6 AC1 33 THR A 225  SER A 226  ASP A 233  LEU A 264                    
SITE     7 AC1 33 HIS A 365  TYR A 366  GLU A 398  ARG A 409                    
SITE     8 AC1 33 ALA A 412  ASN A 413  SER A 414  LEU A 415                    
SITE     9 AC1 33 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 168  TYR B 178  PRO B 181  CYS B 215                    
SITE     2 AC3  9 HIS B 216  THR B 217  MET B 219  ASN B 220                    
SITE     3 AC3  9 CYS B 221                                                     
SITE     1 AC4  8 CYS B 158  ILE B 159  LEU B 160  CYS B 161                    
SITE     2 AC4  8 ALA B 162  CYS B 164  CYS B 225  PRO B 226                    
SITE     1 AC5 13 HIS C  45  ARG C  46  GLY C  49  LEU C  52                    
SITE     2 AC5 13 SER C  53  HIS C 101  HIS C 108  SER D  50                    
SITE     3 AC5 13 LEU D  53  LEU D  54  HIS D  79  GLY D  83                    
SITE     4 AC5 13 VAL D  87                                                     
SITE     1 AC6 11 SER B 170  TRP B 172  TRP B 173  HIS B 216                    
SITE     2 AC6 11 ILE B 218  ILE C  30  MET C  39  SER C  42                    
SITE     3 AC6 11 ILE C  43  ARG C  46  TYR D  91                               
CRYST1   70.751   83.841  293.735  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      0.014134  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011927  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003404        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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