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Database: PDB
Entry: 3ABV
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HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 22-DEC-09   3ABV              
TITLE     CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE    2 N-BIPHENYL-3-YL-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-SULFUR,  
KEYWDS   2 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 3ABV    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-BIPHENYL-3-YL-2-TRIFLUOROMETHYL-BENZAMIDE       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.63                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 28950                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1474                            
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) : 3.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1659                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
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          : 191                                     
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) : 70.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.33000                                              
REMARK   3    B22 (A**2) : 0.27000                                              
REMARK   3    B33 (A**2) : -0.59000                                             
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): 0.470         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.377         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 45.584        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.921                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.882                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8876 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12035 ; 1.075 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1088 ; 4.961 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   375 ;33.862 ;23.413       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1469 ;18.073 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;15.268 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1305 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6667 ; 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):  5412 ; 0.170 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8677 ; 0.323 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3464 ; 0.429 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3341 ; 0.764 ; 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  : 21                                         
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    85                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5440 -21.2280  18.1640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0190 T22:   0.1702                                     
REMARK   3      T33:   0.4976 T12:  -0.0523                                     
REMARK   3      T13:   0.0267 T23:   0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0704 L22:   1.5091                                     
REMARK   3      L33:   3.6378 L12:  -0.4160                                     
REMARK   3      L13:  -0.5000 L23:  -0.1007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:  -0.1540 S13:  -0.0243                       
REMARK   3      S21:  -0.0880 S22:  -0.0420 S23:  -0.0392                       
REMARK   3      S31:   0.0253 S32:  -0.0019 S33:   0.0133                       
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    86        A   260                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6900 -16.0740  18.0490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0743 T22:   0.1644                                     
REMARK   3      T33:   0.5106 T12:  -0.0953                                     
REMARK   3      T13:   0.0329 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4238 L22:   1.1190                                     
REMARK   3      L33:   3.2375 L12:  -0.4831                                     
REMARK   3      L13:  -0.0728 L23:  -0.4608                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0153 S12:  -0.0558 S13:   0.0622                       
REMARK   3      S21:  -0.0065 S22:  -0.0363 S23:   0.0130                       
REMARK   3      S31:  -0.3417 S32:   0.1180 S33:   0.0210                       
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   261        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3650   9.0820  23.5420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5563 T22:   0.0204                                     
REMARK   3      T33:   0.6471 T12:  -0.1141                                     
REMARK   3      T13:   0.1099 T23:  -0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0902 L22:   4.2308                                     
REMARK   3      L33:   4.1037 L12:   0.6824                                     
REMARK   3      L13:  -1.2574 L23:  -1.0834                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4766 S12:  -0.1408 S13:   0.7476                       
REMARK   3      S21:   0.4196 S22:  -0.1145 S23:   0.0462                       
REMARK   3      S31:  -1.4125 S32:   0.2632 S33:  -0.3620                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   345        A   430                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8210 -12.3160  14.2280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2416 T22:   0.2732                                     
REMARK   3      T33:   0.5779 T12:  -0.0473                                     
REMARK   3      T13:   0.0530 T23:   0.0625                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8751 L22:   1.2328                                     
REMARK   3      L33:   1.5623 L12:   0.1136                                     
REMARK   3      L13:  -0.0700 L23:   0.0354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1346 S12:   0.1796 S13:   0.1321                       
REMARK   3      S21:  -0.1396 S22:  -0.1726 S23:   0.0982                       
REMARK   3      S31:  -0.4727 S32:  -0.0457 S33:   0.0380                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   431        A   511                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5200 -15.1550  20.6680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0639 T22:   0.6720                                     
REMARK   3      T33:   0.5016 T12:  -0.1811                                     
REMARK   3      T13:   0.0622 T23:   0.0904                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8705 L22:   2.9555                                     
REMARK   3      L33:   2.3035 L12:  -0.0939                                     
REMARK   3      L13:  -0.6693 L23:  -0.6443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0188 S12:  -0.3245 S13:   0.0826                       
REMARK   3      S21:  -0.1877 S22:  -0.1449 S23:  -0.4920                       
REMARK   3      S31:  -0.2385 S32:   1.1511 S33:   0.1262                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   512        A   622                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5370  -6.4180   5.0390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3383 T22:   0.2345                                     
REMARK   3      T33:   0.5165 T12:  -0.1660                                     
REMARK   3      T13:   0.0705 T23:   0.0640                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2208 L22:   1.1837                                     
REMARK   3      L33:   3.9893 L12:  -0.6131                                     
REMARK   3      L13:   0.0147 L23:  -0.5839                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1105 S12:   0.1624 S13:   0.4792                       
REMARK   3      S21:  -0.2946 S22:  -0.2162 S23:  -0.3076                       
REMARK   3      S31:  -0.8190 S32:   0.6640 S33:   0.1057                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     9        B    40                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4430 -13.3460  48.9480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3799 T22:   1.3080                                     
REMARK   3      T33:   0.8206 T12:  -0.3032                                     
REMARK   3      T13:  -0.1030 T23:   0.1255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5240 L22:  -3.6165                                     
REMARK   3      L33:   3.9907 L12:   0.0933                                     
REMARK   3      L13:  -0.4932 L23:   3.1973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3715 S12:  -0.7381 S13:  -0.1936                       
REMARK   3      S21:  -0.0088 S22:   0.5177 S23:  -0.3307                       
REMARK   3      S31:  -0.5696 S32:   1.7306 S33:  -0.1462                       
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    41        B    79                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.2330 -11.3260  40.4070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2705 T22:   0.7759                                     
REMARK   3      T33:   0.5803 T12:  -0.2817                                     
REMARK   3      T13:  -0.0297 T23:   0.0836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4720 L22:   4.9470                                     
REMARK   3      L33:   0.1798 L12:  -1.4058                                     
REMARK   3      L13:  -2.6028 L23:   1.2864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0924 S12:  -0.1735 S13:   0.4572                       
REMARK   3      S21:  -0.3851 S22:   0.0816 S23:  -0.2862                       
REMARK   3      S31:  -0.1586 S32:   0.3556 S33:  -0.1739                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    80        B   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8420 -12.7370  49.5110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3853 T22:   0.7656                                     
REMARK   3      T33:   0.6957 T12:  -0.3098                                     
REMARK   3      T13:   0.0128 T23:  -0.1544                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3120 L22:   2.6573                                     
REMARK   3      L33:   2.6866 L12:  -1.2812                                     
REMARK   3      L13:  -0.4557 L23:  -0.6486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1894 S12:  -0.7343 S13:   0.4982                       
REMARK   3      S21:   0.1710 S22:  -0.2372 S23:   0.0898                       
REMARK   3      S31:  -0.4957 S32:   0.7759 S33:   0.0479                       
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 :   B   110        B   177                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0180 -23.4170  36.1350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1282 T22:   0.0806                                     
REMARK   3      T33:   0.5454 T12:  -0.0415                                     
REMARK   3      T13:   0.0573 T23:  -0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8294 L22:   0.8379                                     
REMARK   3      L33:   4.9304 L12:  -1.0392                                     
REMARK   3      L13:   0.5734 L23:  -0.8425                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2406 S12:   0.1012 S13:  -0.1073                       
REMARK   3      S21:  -0.0150 S22:  -0.1202 S23:   0.1576                       
REMARK   3      S31:   0.2899 S32:  -0.1380 S33:  -0.1205                       
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 :   B   178        B   219                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.5890 -27.3590  42.3590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4354 T22:   0.2981                                     
REMARK   3      T33:   0.7435 T12:  -0.1110                                     
REMARK   3      T13:   0.1707 T23:  -0.0874                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6636 L22:   0.3170                                     
REMARK   3      L33:   7.6114 L12:   0.3978                                     
REMARK   3      L13:  -2.0112 L23:  -0.9796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2508 S12:   0.1398 S13:   0.0953                       
REMARK   3      S21:   0.1590 S22:  -0.0581 S23:   0.3511                       
REMARK   3      S31:   0.9015 S32:  -0.8000 S33:   0.3089                       
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 :   B   220        B   247                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.4910 -21.0750  46.4640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2458 T22:   0.1814                                     
REMARK   3      T33:   0.6539 T12:  -0.0182                                     
REMARK   3      T13:   0.1085 T23:  -0.1186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2667 L22:   3.5618                                     
REMARK   3      L33:   6.8704 L12:  -2.5738                                     
REMARK   3      L13:  -1.5591 L23:  -1.9658                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1773 S12:   0.1444 S13:   0.2083                       
REMARK   3      S21:  -0.0684 S22:  -0.0280 S23:   0.0927                       
REMARK   3      S31:  -0.2290 S32:  -0.7900 S33:  -0.1493                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     6        C    35                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7370 -31.0420  47.1800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5870 T22:   0.5234                                     
REMARK   3      T33:   0.7621 T12:   0.1846                                     
REMARK   3      T13:   0.1245 T23:   0.1820                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5538 L22:  11.0293                                     
REMARK   3      L33:   7.1149 L12:   3.2725                                     
REMARK   3      L13:   3.7357 L23:   6.2856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2996 S12:   0.1366 S13:   0.1173                       
REMARK   3      S21:   1.1356 S22:  -0.6052 S23:  -0.0357                       
REMARK   3      S31:   1.7329 S32:   0.9277 S33:   0.3056                       
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 :   C    36        C    68                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.0820 -29.7310  74.2100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5312 T22:   0.1136                                     
REMARK   3      T33:   0.6094 T12:  -0.0308                                     
REMARK   3      T13:   0.2375 T23:   0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9215 L22:   2.8278                                     
REMARK   3      L33:   0.3790 L12:   1.1892                                     
REMARK   3      L13:   1.0521 L23:   1.5081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:  -0.2590 S13:   0.1013                       
REMARK   3      S21:   0.4628 S22:  -0.0432 S23:   0.2152                       
REMARK   3      S31:   0.0590 S32:   0.0773 S33:   0.0678                       
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 :   C    69        C    88                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.9620 -27.1000  95.0390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8938 T22:   0.7193                                     
REMARK   3      T33:   0.8394 T12:   0.0397                                     
REMARK   3      T13:  -0.0758 T23:   0.0778                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5237 L22:   9.0224                                     
REMARK   3      L33:  15.6553 L12:   4.9128                                     
REMARK   3      L13:  -4.2238 L23:   1.1517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2298 S12:  -0.8630 S13:  -0.1233                       
REMARK   3      S21:   0.4430 S22:  -0.6565 S23:  -0.0394                       
REMARK   3      S31:  -0.6344 S32:   0.6799 S33:   0.4267                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    89        C   120                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.6510 -17.6750  67.3200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4887 T22:   0.1459                                     
REMARK   3      T33:   0.6718 T12:   0.0063                                     
REMARK   3      T13:   0.1091 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7315 L22:   3.7389                                     
REMARK   3      L33:  11.9715 L12:   1.4759                                     
REMARK   3      L13:  -4.3176 L23:  -3.4515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3558 S12:  -0.1895 S13:   0.0704                       
REMARK   3      S21:   0.4229 S22:  -0.3132 S23:  -0.1555                       
REMARK   3      S31:  -1.2209 S32:   0.8565 S33:  -0.0427                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   121        C   143                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.4360 -11.1040  71.9360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7496 T22:   0.0907                                     
REMARK   3      T33:   0.5257 T12:  -0.1171                                     
REMARK   3      T13:   0.2478 T23:  -0.0635                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8105 L22:   7.9168                                     
REMARK   3      L33:   0.3666 L12:  -1.7634                                     
REMARK   3      L13:   3.1900 L23:   4.0700                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0362 S12:   0.0583 S13:  -0.0511                       
REMARK   3      S21:   0.0431 S22:   0.0970 S23:   0.1801                       
REMARK   3      S31:  -0.3013 S32:   0.0140 S33:  -0.0608                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    35        D    72                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.4800 -29.6870  66.8690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6199 T22:   0.4155                                     
REMARK   3      T33:   0.9675 T12:  -0.0408                                     
REMARK   3      T13:   0.3443 T23:  -0.0340                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9931 L22:   3.7563                                     
REMARK   3      L33:   7.7486 L12:   2.1472                                     
REMARK   3      L13:   2.1099 L23:  -1.4748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4251 S12:   0.0671 S13:  -0.2024                       
REMARK   3      S21:  -0.0493 S22:   0.1908 S23:   0.0370                       
REMARK   3      S31:  -0.1577 S32:  -0.6470 S33:   0.2343                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    73        D    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.9360 -36.0180  63.7410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4626 T22:   0.1674                                     
REMARK   3      T33:   0.7244 T12:  -0.0495                                     
REMARK   3      T13:   0.1353 T23:   0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4284 L22:   0.5457                                     
REMARK   3      L33:  10.6262 L12:   2.1526                                     
REMARK   3      L13:  -2.6854 L23:  -2.6935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2390 S12:  -0.3749 S13:  -0.7702                       
REMARK   3      S21:  -0.1668 S22:  -0.2356 S23:  -0.1506                       
REMARK   3      S31:   0.6643 S32:   0.9991 S33:   0.4746                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    97        D   124                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.1060 -42.2220  74.9370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5117 T22:   0.2955                                     
REMARK   3      T33:   0.7380 T12:  -0.0553                                     
REMARK   3      T13:   0.0685 T23:   0.0706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1829 L22:   9.5504                                     
REMARK   3      L33:   6.9223 L12:  -2.8345                                     
REMARK   3      L13:  -3.5320 L23:   2.0403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0254 S12:  -0.2503 S13:  -0.0849                       
REMARK   3      S21:  -0.3846 S22:  -0.1257 S23:  -0.2956                       
REMARK   3      S31:   0.4792 S32:  -0.1249 S33:   0.1003                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   125        D   136                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5320 -26.4320  88.3340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9819 T22:   1.1743                                     
REMARK   3      T33:   1.0453 T12:   0.0213                                     
REMARK   3      T13:   0.1634 T23:  -0.2006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3316 L22:  -9.4143                                     
REMARK   3      L33:  -2.3987 L12:  -6.9381                                     
REMARK   3      L13:  -2.7026 L23:   6.0939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3578 S12:  -0.9051 S13:  -0.1222                       
REMARK   3      S21:   0.2862 S22:  -0.7687 S23:   1.0342                       
REMARK   3      S31:  -1.7040 S32:  -0.4777 S33:   0.4109                       
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 3ABV COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB029061.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
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) : 1.0000                             
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   : 29008                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.3330                            
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.220                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ZOY                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 7% 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 7.4, 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       35.85100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      147.21600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.08500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      147.21600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.85100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.08500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42210 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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   SG   CYS B   215     S1   F3S B   304              1.92            
REMARK 500   SG   CYS B   168     S4   F3S B   304              2.19            
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    THR A  11      -12.20     76.18                                   
REMARK 500    GLN A  62      -51.07   -136.94                                   
REMARK 500    THR A 121     -163.74   -111.31                                   
REMARK 500    ALA A 151     -133.57     50.26                                   
REMARK 500    ASP A 170       33.01    -85.52                                   
REMARK 500    ASP A 199       10.83   -146.89                                   
REMARK 500    THR A 256       72.06   -111.87                                   
REMARK 500    ARG A 283       85.63    -66.28                                   
REMARK 500    LYS A 293     -135.23     53.57                                   
REMARK 500    PRO A 317        0.03    -65.20                                   
REMARK 500    HIS A 365      -51.39   -148.53                                   
REMARK 500    CYS A 401       86.76   -154.15                                   
REMARK 500    ALA A 482     -151.17   -100.13                                   
REMARK 500    TRP A 516       63.15     36.55                                   
REMARK 500    LYS A 544       58.55   -100.61                                   
REMARK 500    PHE A 555       78.37   -119.66                                   
REMARK 500    GLN A 569      -98.08    -19.68                                   
REMARK 500    ASN A 608      105.09   -164.42                                   
REMARK 500    SER B  64      -70.75   -146.59                                   
REMARK 500    ARG B  66       27.48     43.75                                   
REMARK 500    LYS B 109      124.16   -171.57                                   
REMARK 500    ASP B 110     -126.90     57.65                                   
REMARK 500    GLU B 126       72.68     58.16                                   
REMARK 500    LYS B 139      -30.23   -134.49                                   
REMARK 500    TYR B 213       24.36    -79.14                                   
REMARK 500    MET B 219        6.86     56.51                                   
REMARK 500    HIS C  29      -81.26   -129.59                                   
REMARK 500    LEU C 117       51.87   -105.20                                   
REMARK 500    LYS D  37       63.02   -118.57                                   
REMARK 500    ASP D  95      -86.81    -67.90                                   
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                             F3S B 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 215   SG                                                     
REMARK 620 2 F3S B 304   S1   52.8                                              
REMARK 620 3 F3S B 304   S3  155.4 102.6                                        
REMARK 620 4 F3S B 304   S4  108.5 161.3  96.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  65   SG                                                     
REMARK 620 2 FES B 302   S1  110.4                                              
REMARK 620 3 FES B 302   S2  141.6  91.0                                        
REMARK 620 4 CYS B  70   SG  104.1 104.6 100.6                                  
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   81.6                                              
REMARK 620 3 HEM C1305   NB   91.5  88.6                                        
REMARK 620 4 HEM C1305   NC   99.9 177.8  89.7                                  
REMARK 620 5 HEM C1305   ND   87.5  90.4 178.7  91.3                            
REMARK 620 6 HIS D  79   NE2 169.4  89.3  93.7  89.3  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 161   SG                                                     
REMARK 620 2 SF4 B 303   S1  103.1                                              
REMARK 620 3 SF4 B 303   S3  128.4 105.8                                        
REMARK 620 4 SF4 B 303   S4  108.0 103.2 105.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 164   SG                                                     
REMARK 620 2 SF4 B 303   S1   90.8                                              
REMARK 620 3 SF4 B 303   S2  129.8 106.9                                        
REMARK 620 4 SF4 B 303   S3  116.1 105.4 104.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  73   SG                                                     
REMARK 620 2 FES B 302   S1  132.6                                              
REMARK 620 3 FES B 302   S2  109.6  91.0                                        
REMARK 620 4 CYS B  85   SG  105.9 100.2 118.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 221   SG                                                     
REMARK 620 2 F3S B 304   S1  163.6                                              
REMARK 620 3 F3S B 304   S2  108.3  75.7                                        
REMARK 620 4 F3S B 304   S3   90.8 104.4 100.0                                  
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  130.6                                              
REMARK 620 3 F3S B 304   S3  127.1 100.8                                        
REMARK 620 4 F3S B 304   S4   56.7 111.9  96.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 158   SG                                                     
REMARK 620 2 SF4 B 303   S2  112.0                                              
REMARK 620 3 SF4 B 303   S3   93.6 104.1                                        
REMARK 620 4 SF4 B 303   S4  132.4 104.5 106.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 225   SG                                                     
REMARK 620 2 SF4 B 303   S1  112.2                                              
REMARK 620 3 SF4 B 303   S2  118.2 107.1                                        
REMARK 620 4 SF4 B 303   S4  110.3 103.3 104.6                                  
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 MLI A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F6A B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 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  3ABV A    1   622  UNP    Q0QF01   DHSA_PIG        43    664             
DBREF  3ABV B    1   252  UNP    Q007T0   DHSB_PIG        29    280             
DBREF  3ABV C    4   143  UNP    D0VWV4   C560_PIG        30    169             
DBREF  3ABV 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    MLI  A 701       7                                                       
HET    FES  B 302       4                                                       
HET    HEM  C1305      43                                                       
HET    SF4  B 303       8                                                       
HET    F6A  B1201      25                                                       
HET    EPH  D1306      44                                                       
HET    F3S  B 304       7                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     MLI MALONATE ION                                                     
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F6A N-BIPHENYL-3-YL-2-(TRIFLUOROMETHYL)BENZAMIDE                     
HETNAM     EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-                
HETNAM   2 EPH  PHOSPHATIDYLETHANOLAMINE                                        
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETSYN     HEM HEME                                                             
FORMUL   5  FAD    C27 H33 N9 O15 P2                                            
FORMUL   6  MLI    C3 H2 O4 2-                                                  
FORMUL   7  FES    FE2 S2                                                       
FORMUL   8  HEM    C34 H32 FE N4 O4                                             
FORMUL   9  SF4    FE4 S4                                                       
FORMUL  10  F6A    C20 H14 F3 N O                                               
FORMUL  11  EPH    C39 H68 N O8 P                                               
FORMUL  12  F3S    FE3 S4                                                       
HELIX    1   1 GLY A   28  ALA A   41  1                                  14    
HELIX    2   2 PHE A   52  ALA A   61  5                                  10    
HELIX    3   3 ASN A   76  SER A   88  1                                  13    
HELIX    4   4 ASP A   93  GLY A  115  1                                  23    
HELIX    5   5 LYS A  137  LYS A  140  5                                   4    
HELIX    6   6 ARG A  153  LEU A  167  1                                  15    
HELIX    7   7 TYR A  217  TYR A  221  5                                   5    
HELIX    8   8 GLY A  232  ALA A  241  1                                  10    
HELIX    9   9 GLU A  267  GLU A  272  1                                   6    
HELIX   10  10 PHE A  284  ALA A  289  1                                   6    
HELIX   11  11 ALA A  292  ALA A  296  5                                   5    
HELIX   12  12 SER A  297  GLU A  311  1                                  15    
HELIX   13  13 PRO A  330  LEU A  338  1                                   9    
HELIX   14  14 LEU A  338  GLY A  350  1                                  13    
HELIX   15  15 ASN A  413  GLU A  431  1                                  19    
HELIX   16  16 GLY A  447  PHE A  459  1                                  13    
HELIX   17  17 THR A  466  ALA A  481  1                                  16    
HELIX   18  18 VAL A  486  ASP A  503  1                                  18    
HELIX   19  19 ASN A  517  ARG A  543  1                                  27    
HELIX   20  20 PRO A  575  HIS A  579  5                                   5    
HELIX   21  21 ASN B   38  CYS B   40  5                                   3    
HELIX   22  22 MET B   43  ILE B   55  1                                  13    
HELIX   23  23 LEU B  115  SER B  124  1                                  10    
HELIX   24  24 SER B  145  LYS B  151  1                                   7    
HELIX   25  25 ALA B  162  SER B  167  1                                   6    
HELIX   26  26 CYS B  168  ASN B  174  1                                   7    
HELIX   27  27 LEU B  179  ILE B  192  1                                  14    
HELIX   28  28 PHE B  198  LYS B  205  1                                   8    
HELIX   29  29 MET B  219  CYS B  225  1                                   7    
HELIX   30  30 ASN B  230  TYR B  245  1                                  16    
HELIX   31  31 THR C    7  GLY C   21  1                                  15    
HELIX   32  32 SER C   36  LEU C   66  1                                  31    
HELIX   33  33 ASN C   69  LEU C   80  1                                  12    
HELIX   34  34 GLY C   83  LEU C  113  1                                  31    
HELIX   35  35 THR C  118  ALA C  142  1                                  25    
HELIX   36  36 LYS D   37  ASN D   63  1                                  27    
HELIX   37  37 CYS D   65  VAL D   92  1                                  28    
HELIX   38  38 GLY D   94  ASP D  123  1                                  30    
HELIX   39  39 VAL D  124  LYS D  135  1                                  12    
SHEET    1   A 4 VAL A  15  GLU A  19  0                                        
SHEET    2   A 4 ILE A 202  ARG A 206  1  O  ARG A 204   N  HIS A  18           
SHEET    3   A 4 GLU A 188  CYS A 196 -1  N  ALA A 194   O  HIS A 203           
SHEET    4   A 4 TYR A 177  GLU A 185 -1  N  LEU A 183   O  ARG A 190           
SHEET    1   B 6 SER A 172  VAL A 175  0                                        
SHEET    2   B 6 THR A  45  THR A  49  1  N  CYS A  47   O  SER A 172           
SHEET    3   B 6 ALA A  22  VAL A  25  1  N  VAL A  24   O  VAL A  48           
SHEET    4   B 6 ASN A 209  VAL A 212  1  O  VAL A 211   N  VAL A  23           
SHEET    5   B 6 GLN A 386  ALA A 395  1  O  TYR A 394   N  THR A 210           
SHEET    6   B 6 GLN A 378  VAL A 383 -1  N  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  ASP A 589 -1  O  SER A 586   N  CYS A 245           
SHEET    3   D 3 LYS A 594  PRO A 601 -1  O  GLU A 598   N  LEU A 585           
SHEET    1   E 4 VAL A 251  ILE A 258  0                                        
SHEET    2   E 4 ILE A 358  ASN A 367 -1  O  LEU A 361   N  GLY A 257           
SHEET    3   E 4 VAL A 322  GLN A 325 -1  N  VAL A 322   O  VAL A 360           
SHEET    4   E 4 ILE A 275  ILE A 277 -1  N  ILE A 275   O  GLN A 325           
SHEET    1   F 2 ILE A 371  PRO A 372  0                                        
SHEET    2   F 2 ALA A 400  CYS A 401  1  O  CYS A 401   N  ILE A 371           
SHEET    1   G 2 ILE A 464  ARG A 465  0                                        
SHEET    2   G 2 LEU A 507  LYS A 508  1  O  LYS A 508   N  ILE A 464           
SHEET    1   H 2 PHE A 484  ARG A 485  0                                        
SHEET    2   H 2 ALA A 551  ARG A 552  1  O  ALA A 551   N  ARG A 485           
SHEET    1   I 5 HIS B  29  ASP B  36  0                                        
SHEET    2   I 5 ILE B  11  ARG B  18 -1  N  ILE B  16   O  GLN B  31           
SHEET    3   I 5 SER B  97  TYR B 100  1  O  ILE B  99   N  ALA B  15           
SHEET    4   I 5 ALA B  74  ILE B  77 -1  N  ASN B  76   O  TYR B 100           
SHEET    5   I 5 GLY B  80  LEU B  83 -1  O  THR B  82   N  MET B  75           
SHEET    1   J 2 VAL B 107  LYS B 109  0                                        
SHEET    2   J 2 VAL B 112  PRO B 113 -1  O  VAL B 112   N  ILE B 108           
LINK         NE2 HIS A  57                 C8M FAD A 700     1555   1555  1.99  
LINK         SG  CYS B 215                FE3  F3S B 304     1555   1555  2.09  
LINK         SG  CYS B  65                FE2  FES B 302     1555   1555  2.15  
LINK         NE2 HIS C 101                FE   HEM C1305     1555   1555  2.18  
LINK         SG  CYS B 161                FE2  SF4 B 303     1555   1555  2.21  
LINK         SG  CYS B 164                FE4  SF4 B 303     1555   1555  2.26  
LINK         NE2 HIS D  79                FE   HEM C1305     1555   1555  2.30  
LINK         SG  CYS B  73                FE1  FES B 302     1555   1555  2.32  
LINK         SG  CYS B 221                FE1  F3S B 304     1555   1555  2.37  
LINK         SG  CYS B 168                FE4  F3S B 304     1555   1555  2.39  
LINK         SG  CYS B  85                FE1  FES B 302     1555   1555  2.42  
LINK         SG  CYS B 158                FE1  SF4 B 303     1555   1555  2.42  
LINK         SG  CYS B  70                FE2  FES B 302     1555   1555  2.43  
LINK         SG  CYS B 225                FE3  SF4 B 303     1555   1555  2.57  
SITE     1 AC1 35 GLY A  26  ALA A  27  GLY A  28  GLY A  29                    
SITE     2 AC1 35 ALA A  30  THR A  49  LYS A  50  LEU A  51                    
SITE     3 AC1 35 SER A  56  HIS A  57  THR A  58  ALA A  60                    
SITE     4 AC1 35 ALA A  61  GLN A  62  GLY A  63  GLY A  64                    
SITE     5 AC1 35 TYR A 177  PHE A 178  ALA A 179  ALA A 213                    
SITE     6 AC1 35 THR A 214  GLY A 215  THR A 225  ASP A 233                    
SITE     7 AC1 35 LEU A 264  HIS A 365  TYR A 366  GLU A 398                    
SITE     8 AC1 35 ARG A 409  ALA A 412  ASN A 413  SER A 414                    
SITE     9 AC1 35 LEU A 415  LEU A 418  MLI A 701                               
SITE     1 AC2 12 GLN A  62  GLY A  63  PHE A 131  HIS A 254                    
SITE     2 AC2 12 LEU A 264  THR A 266  GLU A 267  ARG A 298                    
SITE     3 AC2 12 HIS A 365  ARG A 409  ALA A 412  FAD A 700                    
SITE     1 AC3  8 SER B  64  CYS B  65  ARG B  66  GLY B  68                    
SITE     2 AC3  8 CYS B  70  GLY B  71  CYS B  73  CYS B  85                    
SITE     1 AC4 15 HIS C  45  ARG C  46  GLY C  49  LEU C  52                    
SITE     2 AC4 15 SER C  53  HIS C 101  THR C 102  GLY C 105                    
SITE     3 AC4 15 ILE C 106  HIS C 108  ARG D  47  SER D  50                    
SITE     4 AC4 15 LEU D  76  HIS D  79  GLY D  83                               
SITE     1 AC5  9 CYS B 158  ILE B 159  LEU B 160  CYS B 161                    
SITE     2 AC5  9 ALA B 162  CYS B 163  CYS B 164  CYS B 225                    
SITE     3 AC5  9 PRO B 226                                                     
SITE     1 AC6 11 PRO B 169  SER B 170  TRP B 172  TRP B 173                    
SITE     2 AC6 11 HIS B 216  TRP C  35  MET C  39  SER C  42                    
SITE     3 AC6 11 ARG C  46  ASP D  90  TYR D  91                               
SITE     1 AC7  3 TYR D  61  LEU D 133  TRP D 134                               
SITE     1 AC8 10 CYS B 168  SER B 170  TYR B 178  CYS B 215                    
SITE     2 AC8 10 THR B 217  ILE B 218  MET B 219  ASN B 220                    
SITE     3 AC8 10 CYS B 221  ILE B 235                                          
CRYST1   71.702   84.170  294.432  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      0.013947  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011881  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003396        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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