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Database: PDB
Entry: 2WS3
LinkDB: 2WS3
Original site: 2WS3 
HEADER    OXIDOREDUCTASE                          03-SEP-09   2WS3              
TITLE     CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE     
TITLE    2 (SQR) SDHD TYR83PHE MUTANT                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT;              
COMPND   3 CHAIN: A, E, I;                                                      
COMPND   4 EC: 1.3.99.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: FAD ATOM C8M IS COVALENTLY LINKED TO NE2 OF SDHA      
COMPND   7  HIS45;                                                              
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT;               
COMPND  10 CHAIN: B, F, J;                                                      
COMPND  11 EC: 1.3.99.1;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B-556 SUBUNIT;          
COMPND  15 CHAIN: C, G, K;                                                      
COMPND  16 SYNONYM: CYTOCHROME B-556;                                           
COMPND  17 EC: 1.3.5.1;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 OTHER_DETAILS: RESIDUES 8-128 MODELLED;                              
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR        
COMPND  22  SUBUNIT;                                                            
COMPND  23 CHAIN: D, H, L;                                                      
COMPND  24 EC: 1.3.5.1;                                                         
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MUTATION: YES;                                                       
COMPND  27 OTHER_DETAILS: RESIDUES 11-115 MODELLED                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 562;                                                 
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  19 ORGANISM_TAXID: 562;                                                 
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  27 ORGANISM_TAXID: 562;                                                 
SOURCE  28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  30 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  31 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  32 EXPRESSION_SYSTEM_PLASMID: PFAS                                      
KEYWDS    ELECTRON TRANSPORT, OXIDOREDUCTASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.RUPRECHT,V.YANKOVSKAYA,E.MAKLASHINA,S.IWATA,G.CECCHINI              
REVDAT   3   29-SEP-10 2WS3    1       DBREF                                    
REVDAT   2   22-SEP-10 2WS3    1       DBREF                                    
REVDAT   1   25-AUG-10 2WS3    0                                                
JRNL        AUTH   J.RUPRECHT,V.YANKOVSKAYA,E.MAKLASHINA,S.IWATA,G.CECCHINI     
JRNL        TITL   SUCCINATE DEHYDROGENASE ACTIVITY                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.2                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.77                          
REMARK   3   NUMBER OF REFLECTIONS             : 71105                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : IDENTICAL TO 2WDQ               
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.22039                         
REMARK   3   R VALUE            (WORKING SET) : 0.21870                         
REMARK   3   FREE R VALUE                     : 0.25271                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3797                            
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) : 3.2                          
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.283                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5162                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.300                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 289                          
REMARK   3   BIN FREE R VALUE                    : 0.330                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 24477                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 423                                     
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) : 72.0                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.70                                                
REMARK   3    B22 (A**2) : 1.19                                                 
REMARK   3    B33 (A**2) : 3.51                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0                                                    
REMARK   3    B23 (A**2) : 0                                                    
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): 0.487         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.412         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.792        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 25501 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 34581 ; 1.301 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3144 ; 5.420 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1107 ;33.907 ;23.388       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4200 ;16.248 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   192 ;17.774 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3831 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19230 ; 0.005 ; 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): 15636 ; 0.139 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 25125 ; 0.230 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9865 ; 0.638 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9405 ; 0.869 ; 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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A E I                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     588      1                      
REMARK   3           1     E      1       E     588      1                      
REMARK   3           1     I      1       I     588      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   4522 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   4522 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    I    (A):   4522 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   4522 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):   4522 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      1    I (A**2):   4522 ;  0.07 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B F J                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     238      1                      
REMARK   3           1     F      1       F     238      1                      
REMARK   3           1     J      1       J     238      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1869 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    F    (A):   1869 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    J    (A):   1869 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1869 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      2    F (A**2):   1869 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      2    J (A**2):   1869 ;  0.08 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C G K                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      8       C     128      1                      
REMARK   3           1     G      8       G     128      1                      
REMARK   3           1     K      8       K     128      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):    933 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    G    (A):    933 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    K    (A):    933 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      3    C (A**2):    933 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      3    G (A**2):    933 ;  0.05 ;  0.50           
REMARK   3   TIGHT THERMAL      3    K (A**2):    933 ;  0.06 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : D H L                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D     11       D     115      1                      
REMARK   3           1     H     11       H     115      1                      
REMARK   3           1     L     11       L     115      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    D    (A):    835 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    H    (A):    835 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    L    (A):    835 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      4    D (A**2):    835 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      4    H (A**2):    835 ;  0.06 ;  0.50           
REMARK   3   TIGHT THERMAL      4    L (A**2):    835 ;  0.06 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   588                          
REMARK   3    RESIDUE RANGE :   A   601        A   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2867 -10.8839 -23.6106              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0674 T22:   0.0384                                     
REMARK   3      T33:   0.1940 T12:  -0.0072                                     
REMARK   3      T13:   0.1023 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7033 L22:   1.9944                                     
REMARK   3      L33:   1.8113 L12:  -0.0217                                     
REMARK   3      L13:   0.1770 L23:  -0.1365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0299 S12:   0.0145 S13:   0.2576                       
REMARK   3      S21:   0.3454 S22:  -0.0802 S23:   0.4508                       
REMARK   3      S31:  -0.0047 S32:  -0.2080 S33:   0.0503                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   238                          
REMARK   3    RESIDUE RANGE :   B   302        B   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6688  -8.1688 -29.7650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0598 T22:   0.0762                                     
REMARK   3      T33:   0.1040 T12:  -0.0002                                     
REMARK   3      T13:  -0.0598 T23:   0.0493                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8210 L22:   3.2648                                     
REMARK   3      L33:   1.7589 L12:   0.0613                                     
REMARK   3      L13:   0.1999 L23:  -0.7221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0968 S12:   0.3654 S13:   0.4308                       
REMARK   3      S21:   0.4190 S22:   0.0342 S23:  -0.3362                       
REMARK   3      S31:  -0.0467 S32:   0.2111 S33:   0.0626                       
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 :   C     8        C   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.4974  -4.4443 -30.5164              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1713 T22:   0.2499                                     
REMARK   3      T33:   0.5761 T12:  -0.0183                                     
REMARK   3      T13:  -0.0474 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7929 L22:   1.5258                                     
REMARK   3      L33:   1.4693 L12:  -0.7876                                     
REMARK   3      L13:   0.3362 L23:  -0.1820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0236 S12:  -0.0610 S13:   0.6350                       
REMARK   3      S21:   0.1596 S22:   0.0964 S23:  -0.5230                       
REMARK   3      S31:   0.0296 S32:   0.2758 S33:  -0.0727                       
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 :   D    11        D   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.8484 -16.6032 -37.2742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0795 T22:   0.3070                                     
REMARK   3      T33:   0.5489 T12:   0.0596                                     
REMARK   3      T13:   0.0029 T23:   0.0484                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5287 L22:   2.1208                                     
REMARK   3      L33:   2.4375 L12:  -0.4842                                     
REMARK   3      L13:  -0.3677 L23:  -0.5294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1613 S12:   0.5077 S13:   0.2095                       
REMARK   3      S21:  -0.0489 S22:  -0.1285 S23:  -0.7178                       
REMARK   3      S31:   0.0407 S32:   0.5794 S33:  -0.0328                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   588                          
REMARK   3    RESIDUE RANGE :   E   601        E   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8631 -71.9087 -28.1864              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3590 T22:   0.0428                                     
REMARK   3      T33:   0.2717 T12:   0.0006                                     
REMARK   3      T13:  -0.0886 T23:  -0.0753                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6660 L22:   2.0360                                     
REMARK   3      L33:   1.5426 L12:   0.4347                                     
REMARK   3      L13:   0.2919 L23:   0.2069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1003 S12:   0.0905 S13:  -0.4520                       
REMARK   3      S21:   0.4611 S22:  -0.0059 S23:   0.1437                       
REMARK   3      S31:   0.2657 S32:  -0.0288 S33:  -0.0943                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   238                          
REMARK   3    RESIDUE RANGE :   F   302        F   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.6012 -60.4421 -27.3896              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2941 T22:   0.1253                                     
REMARK   3      T33:   0.2626 T12:   0.1028                                     
REMARK   3      T13:  -0.2333 T23:  -0.1061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7109 L22:   1.9028                                     
REMARK   3      L33:   1.9438 L12:   0.6262                                     
REMARK   3      L13:   0.0060 L23:   0.1834                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1059 S12:   0.2247 S13:  -0.2625                       
REMARK   3      S21:   0.3891 S22:   0.0096 S23:  -0.4336                       
REMARK   3      S31:   0.3159 S32:   0.3368 S33:  -0.1155                       
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 :   G     8        G   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.8194 -52.8861 -29.4649              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3583 T22:   0.4062                                     
REMARK   3      T33:   0.8701 T12:   0.2383                                     
REMARK   3      T13:  -0.3313 T23:  -0.1457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9511 L22:   2.1538                                     
REMARK   3      L33:   1.6316 L12:   1.7228                                     
REMARK   3      L13:  -1.4324 L23:  -0.4768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1475 S12:   0.1301 S13:  -0.8298                       
REMARK   3      S21:  -0.0255 S22:  -0.1279 S23:  -0.9757                       
REMARK   3      S31:   0.3091 S32:   0.3971 S33:  -0.0196                       
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 :   H    11        H   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.3585 -39.9454 -37.4617              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1505 T22:   0.4533                                     
REMARK   3      T33:   0.7239 T12:   0.1474                                     
REMARK   3      T13:  -0.1364 T23:  -0.1371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9402 L22:   2.6576                                     
REMARK   3      L33:   3.3943 L12:   0.4883                                     
REMARK   3      L13:  -0.3236 L23:   0.1938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2058 S12:   0.5610 S13:  -0.2986                       
REMARK   3      S21:  -0.1223 S22:  -0.0330 S23:  -0.9741                       
REMARK   3      S31:   0.0808 S32:   0.5372 S33:  -0.1729                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   588                          
REMARK   3    RESIDUE RANGE :   I   601        I   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3316 -37.4470 -80.4759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7582 T22:   1.5265                                     
REMARK   3      T33:   0.4914 T12:   0.0487                                     
REMARK   3      T13:  -0.2433 T23:  -0.0878                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8886 L22:   2.0358                                     
REMARK   3      L33:   0.8853 L12:  -0.1993                                     
REMARK   3      L13:   0.0631 L23:   0.1587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0306 S12:   1.0057 S13:  -0.0773                       
REMARK   3      S21:  -0.7076 S22:   0.1108 S23:   0.3906                       
REMARK   3      S31:   0.0610 S32:  -0.2038 S33:  -0.1413                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   238                          
REMARK   3    RESIDUE RANGE :   J   302        J   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0370 -36.5463 -75.0261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5491 T22:   1.1139                                     
REMARK   3      T33:   0.2429 T12:   0.0853                                     
REMARK   3      T13:  -0.0402 T23:  -0.1148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6004 L22:   2.3094                                     
REMARK   3      L33:   1.7470 L12:   0.3612                                     
REMARK   3      L13:  -0.1263 L23:  -0.0423                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0141 S12:   1.0614 S13:  -0.2244                       
REMARK   3      S21:  -0.6824 S22:   0.2131 S23:  -0.0410                       
REMARK   3      S31:   0.1689 S32:  -0.0389 S33:  -0.1990                       
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 :   K     8        K   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.2565 -29.5913 -72.7546              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6189 T22:   1.3439                                     
REMARK   3      T33:   0.4297 T12:   0.1114                                     
REMARK   3      T13:   0.2326 T23:  -0.1387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6512 L22:   2.4007                                     
REMARK   3      L33:   1.9598 L12:   1.2428                                     
REMARK   3      L13:  -0.0625 L23:  -0.0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0417 S12:   1.2560 S13:  -0.0547                       
REMARK   3      S21:  -0.5677 S22:   0.1239 S23:  -0.3743                       
REMARK   3      S31:  -0.1269 S32:   0.2329 S33:  -0.0821                       
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 :   L    11        L   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.0119 -28.0028 -57.9783              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2589 T22:   0.9204                                     
REMARK   3      T33:   0.4392 T12:   0.1204                                     
REMARK   3      T13:   0.1570 T23:  -0.0849                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5586 L22:   3.9518                                     
REMARK   3      L33:   2.0701 L12:  -0.0692                                     
REMARK   3      L13:   0.5422 L23:  -0.2065                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0096 S12:   0.8958 S13:  -0.0548                       
REMARK   3      S21:  -0.1220 S22:   0.0607 S23:  -0.8173                       
REMARK   3      S31:  -0.0321 S32:   0.6175 S33:  -0.0704                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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. DENSITY FOR THE N-TERMINUS OF SDH C (RESIDUES 1-7 OF     
REMARK   3  CHAINS C, G, K) AND THE N-TERMINUS OF SDHD (RESIDUES 1-10 OF        
REMARK   3  CHAINS D, H AND L) WAS WEAK AND THESE REGIONS ARE NOT INCLUDED IN   
REMARK   3  THE MODEL. THE SIDE CHAIN OF SDHD TRP113 IS TRUNCATED AT THE        
REMARK   3  CBETA ATOM SINCE DENSITY FOR THE SIDE CHAIN WAS POOR. ATOM RECORD   
REMARK   3  CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD           
REMARK   3  CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.                         
REMARK   4                                                                      
REMARK   4 2WS3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41026.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71105                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.03                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.10                              
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) : 3.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.61                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2WDQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5                                   
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       59.92500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.65500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       92.35500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.65500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.92500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       92.35500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 15680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.4 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L                            
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 15610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.7 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 15620 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.2 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 ENGINEERED RESIDUE IN CHAIN D, TYR 83 TO PHE                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, TYR 83 TO PHE                         
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, TYR 83 TO PHE                         
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     MET C     1                                                      
REMARK 465     ILE C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     ASN C     4                                                      
REMARK 465     VAL C     5                                                      
REMARK 465     LYS C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     TRP C   129                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     ASN D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     ALA D     7                                                      
REMARK 465     LEU D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     ARG D    10                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ILE G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     ASN G     4                                                      
REMARK 465     VAL G     5                                                      
REMARK 465     LYS G     6                                                      
REMARK 465     LYS G     7                                                      
REMARK 465     TRP G   129                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     ASN H     4                                                      
REMARK 465     ALA H     5                                                      
REMARK 465     SER H     6                                                      
REMARK 465     ALA H     7                                                      
REMARK 465     LEU H     8                                                      
REMARK 465     GLY H     9                                                      
REMARK 465     ARG H    10                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ILE K     2                                                      
REMARK 465     ARG K     3                                                      
REMARK 465     ASN K     4                                                      
REMARK 465     VAL K     5                                                      
REMARK 465     LYS K     6                                                      
REMARK 465     LYS K     7                                                      
REMARK 465     TRP K   129                                                      
REMARK 465     MET L     1                                                      
REMARK 465     VAL L     2                                                      
REMARK 465     SER L     3                                                      
REMARK 465     ASN L     4                                                      
REMARK 465     ALA L     5                                                      
REMARK 465     SER L     6                                                      
REMARK 465     ALA L     7                                                      
REMARK 465     LEU L     8                                                      
REMARK 465     GLY L     9                                                      
REMARK 465     ARG L    10                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TRP D 113    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D 113    CZ3  CH2                                            
REMARK 470     TRP H 113    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 113    CZ3  CH2                                            
REMARK 470     TRP L 113    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP L 113    CZ3  CH2                                            
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   NE2  HIS A    45     C8M  FAD A   601              1.94            
REMARK 500   NE2  HIS E    45     C8M  FAD E   601              2.08            
REMARK 500   OG   SER I   404     O3'  FAD I   601              2.15            
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    GLN A  50      -65.24   -124.20                                   
REMARK 500    ALA A 138     -123.84     45.73                                   
REMARK 500    ALA A 205       34.52   -156.07                                   
REMARK 500    THR A 244       79.22   -117.81                                   
REMARK 500    ALA A 249      -45.35   -133.49                                   
REMARK 500    LYS A 281     -125.61     60.27                                   
REMARK 500    ASP A 304     -167.85   -112.79                                   
REMARK 500    HIS A 354      -58.10   -132.05                                   
REMARK 500    ASN A 398      116.66   -163.39                                   
REMARK 500    SER A 472     -153.74    -72.20                                   
REMARK 500    VAL B  14      -57.00   -126.66                                   
REMARK 500    ARG B  53      147.20   -171.44                                   
REMARK 500    SER B  54      -67.19   -147.04                                   
REMARK 500    ARG B  56       16.82     49.67                                   
REMARK 500    ASP B  63       59.99   -105.77                                   
REMARK 500    ARG B 101      131.24   -171.14                                   
REMARK 500    ASP B 102     -110.33     43.40                                   
REMARK 500    ARG B 131     -116.79   -127.81                                   
REMARK 500    ALA B 153       -5.62     78.48                                   
REMARK 500    GLU B 189       31.93    -87.40                                   
REMARK 500    SER C  51        4.93    -66.39                                   
REMARK 500    SER D  40      -16.03   -141.35                                   
REMARK 500    PRO E  41      -38.71    -38.30                                   
REMARK 500    GLN E  50      -66.20   -121.89                                   
REMARK 500    VAL E  55      131.30   -170.44                                   
REMARK 500    ALA E 138     -126.35     43.79                                   
REMARK 500    LEU E 167      -70.43    -87.26                                   
REMARK 500    ALA E 205       36.70   -146.11                                   
REMARK 500    THR E 244       74.69   -109.27                                   
REMARK 500    ALA E 249      -44.53   -133.01                                   
REMARK 500    LYS E 281     -123.09     66.77                                   
REMARK 500    ALA E 284     -177.85    -69.49                                   
REMARK 500    ASP E 304     -167.19   -114.57                                   
REMARK 500    HIS E 354      -56.56   -134.36                                   
REMARK 500    SER E 472     -153.23    -73.76                                   
REMARK 500    VAL F  14      -58.41   -128.87                                   
REMARK 500    SER F  54      -71.86   -145.85                                   
REMARK 500    ARG F  56       16.11     49.63                                   
REMARK 500    ASP F  63       57.90   -102.46                                   
REMARK 500    ARG F 101      130.76   -170.92                                   
REMARK 500    ASP F 102     -110.19     43.32                                   
REMARK 500    LYS F 118       70.38     56.40                                   
REMARK 500    ARG F 131     -116.12   -128.78                                   
REMARK 500    ALA F 153       -8.85     78.51                                   
REMARK 500    GLU F 189       33.57    -88.79                                   
REMARK 500    ASP G  14      101.59    -56.08                                   
REMARK 500    SER G  51        5.25    -69.83                                   
REMARK 500    SER H  40      -14.51   -141.79                                   
REMARK 500    PRO I  41      -36.77    -37.03                                   
REMARK 500    GLN I  50      -64.72   -122.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      71 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1589  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 390   O                                                      
REMARK 620 2 GLY A 358   O    94.5                                              
REMARK 620 3 MET A 357   O    97.6  65.0                                        
REMARK 620 4 GLU A 388   O    83.1  90.9 155.9                                  
REMARK 620 5 MET A 356   O   172.0  77.5  78.3  97.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E1589  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET E 357   O                                                      
REMARK 620 2 GLY E 358   O    66.5                                              
REMARK 620 3 GLU E 388   O   158.9  93.1                                        
REMARK 620 4 ALA E 390   O    99.0  98.0  88.6                                  
REMARK 620 5 MET E 356   O    78.4  79.8  93.3 177.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA I1589  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET I 356   O                                                      
REMARK 620 2 MET I 357   O    72.4                                              
REMARK 620 3 GLY I 358   O    71.2  59.8                                        
REMARK 620 4 ALA I 390   O   160.2  94.3  89.5                                  
REMARK 620 5 GLU I 388   O    90.5 140.8  81.4  91.0                            
REMARK 620 N                    1     2     3     4                             
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  60   SG                                                     
REMARK 620 2 FES B 302  FE2  145.8                                              
REMARK 620 3 FES B 302   S1  124.4  46.1                                        
REMARK 620 4 FES B 302   S2  125.5  47.5  93.6                                  
REMARK 620 5 CYS B  55   SG  103.6 110.5 101.7 104.8                            
REMARK 620 N                    1     2     3     4                             
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 ASP B  63   OD1                                                    
REMARK 620 2 FES B 302  FE1  119.3                                              
REMARK 620 3 FES B 302   S1  107.9  46.4                                        
REMARK 620 4 FES B 302   S2  112.9  46.2  92.6                                  
REMARK 620 5 CYS B  75   SG  120.7 117.7  99.4 117.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES F 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  55   SG                                                     
REMARK 620 2 FES F 302  FE2  111.4                                              
REMARK 620 3 FES F 302   S1   93.9  46.8                                        
REMARK 620 4 FES F 302   S2  117.4  47.2  93.9                                  
REMARK 620 5 CYS F  60   SG  102.3 141.7 115.2 128.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES F 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FES F 302  FE1                                                     
REMARK 620 2 FES F 302   S1   47.5                                              
REMARK 620 3 FES F 302   S2   46.8  94.3                                        
REMARK 620 4 ASP F  63   OD1 122.4 118.4 103.1                                  
REMARK 620 5 CYS F  75   SG  117.5 103.6 114.9 119.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES J 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J  60   SG                                                     
REMARK 620 2 FES J 302  FE2  148.7                                              
REMARK 620 3 FES J 302   S1  125.4  46.4                                        
REMARK 620 4 FES J 302   S2  129.9  46.7  92.9                                  
REMARK 620 5 CYS J  55   SG  100.6 108.9  90.1 111.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES J 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FES J 302  FE1                                                     
REMARK 620 2 FES J 302   S1   46.8                                              
REMARK 620 3 FES J 302   S2   46.5  93.1                                        
REMARK 620 4 CYS J  75   SG  118.5  97.0 117.2                                  
REMARK 620 5 ASP J  63   OD1 115.0 116.9 102.0 126.3                            
REMARK 620 N                    1     2     3     4                             
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 155   SG                                                     
REMARK 620 2 SF4 B 303  FE2  146.3                                              
REMARK 620 3 SF4 B 303  FE3  151.7  60.0                                        
REMARK 620 4 SF4 B 303  FE4  133.0  61.3  59.4                                  
REMARK 620 5 SF4 B 303   S2  109.3 102.8  52.9  54.7                            
REMARK 620 6 SF4 B 303   S3  104.9  54.0 102.1  55.8 108.5                      
REMARK 620 7 SF4 B 303   S4  126.2  53.0  52.4 100.7 102.2 104.9                
REMARK 620 N                    1     2     3     4     5     6                 
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 SF4 B 303   S1                                                     
REMARK 620 2 SF4 B 303  FE1  101.1                                              
REMARK 620 3 SF4 B 303  FE3   52.8  61.3                                        
REMARK 620 4 SF4 B 303  FE4   53.7  57.8  58.7                                  
REMARK 620 5 SF4 B 303   S3  104.6  53.4 102.7  54.1                            
REMARK 620 6 SF4 B 303   S4  104.0  54.1  53.1  98.8 105.3                      
REMARK 620 7 CYS B 216   SG  115.1 141.4 154.5 136.8 102.2 123.8                
REMARK 620 N                    1     2     3     4     5     6                 
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 149   SG                                                     
REMARK 620 2 SF4 B 303   S1  131.8                                              
REMARK 620 3 SF4 B 303  FE1  127.9  99.6                                        
REMARK 620 4 SF4 B 303  FE2  156.4  53.6  58.7                                  
REMARK 620 5 SF4 B 303  FE4  143.4  54.5  57.5  60.2                            
REMARK 620 6 SF4 B 303   S2   97.8 106.1  53.1 101.9  53.9                      
REMARK 620 7 SF4 B 303   S4  110.4 104.2  52.8  52.6  99.5 102.8                
REMARK 620 N                    1     2     3     4     5     6                 
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 SF4 B 303   S1                                                     
REMARK 620 2 CYS B 152   SG  111.2                                              
REMARK 620 3 SF4 B 303  FE1  103.7 143.8                                        
REMARK 620 4 SF4 B 303  FE2   53.9 137.1  60.8                                  
REMARK 620 5 SF4 B 303  FE3   53.9 148.7  63.2  61.1                            
REMARK 620 6 SF4 B 303   S2  106.2 119.6  55.7 103.2  54.7                      
REMARK 620 7 SF4 B 303   S3  104.2 106.4  54.5  53.5 104.1 108.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE3                                                     
REMARK 620 2 SF4 F 303  FE4   62.0                                              
REMARK 620 3 SF4 F 303   S2   54.2  52.5                                        
REMARK 620 4 SF4 F 303  FE2   63.2  60.8 102.5                                  
REMARK 620 5 SF4 F 303   S4   54.5 103.5 106.9  55.6                            
REMARK 620 6 SF4 F 303   S3  105.0  53.6 102.9  54.8 108.1                      
REMARK 620 7 CYS F 155   SG  147.7 147.2 123.7 133.7 107.9 106.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE3                                                     
REMARK 620 2 SF4 F 303   S1   53.7                                              
REMARK 620 3 SF4 F 303  FE4   60.7  53.8                                        
REMARK 620 4 CYS F 216   SG  145.5 105.6 134.0                                  
REMARK 620 5 SF4 F 303   S4   52.4 102.7 103.2 122.3                            
REMARK 620 6 SF4 F 303   S3  101.3 105.8  53.9 111.7 107.2                      
REMARK 620 7 SF4 F 303  FE1   58.5 101.3  61.5 152.6  54.6  54.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303   S1                                                     
REMARK 620 2 SF4 F 303  FE4   52.8                                              
REMARK 620 3 CYS F 149   SG  124.7 137.3                                        
REMARK 620 4 SF4 F 303   S2  102.7  52.4  98.2                                  
REMARK 620 5 SF4 F 303  FE2   52.7  58.9 161.4 100.3                            
REMARK 620 6 SF4 F 303   S4  102.9 102.8 117.3 109.3  53.7                      
REMARK 620 7 SF4 F 303  FE1  100.3  60.7 133.3  56.3  58.3  54.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE3                                                     
REMARK 620 2 SF4 F 303   S1   53.6                                              
REMARK 620 3 CYS F 152   SG  157.9 130.0                                        
REMARK 620 4 SF4 F 303   S2   52.8 103.8 111.8                                  
REMARK 620 5 SF4 F 303  FE2   60.5  53.5 141.4 101.9                            
REMARK 620 6 SF4 F 303   S3  100.7 105.0  98.8 104.7  53.3                      
REMARK 620 7 SF4 F 303  FE1   57.3  98.2 130.9  54.9  57.7  53.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 J 303  FE2                                                     
REMARK 620 2 SF4 J 303  FE3   61.5                                              
REMARK 620 3 SF4 J 303  FE4   59.3  60.9                                        
REMARK 620 4 SF4 J 303   S2  102.5  55.5  53.4                                  
REMARK 620 5 CYS J 155   SG  154.1 139.2 138.4 103.2                            
REMARK 620 6 SF4 J 303   S3   54.1 104.0  54.2 104.0 115.6                      
REMARK 620 7 SF4 J 303   S4   53.1  54.3 100.9 108.3 120.1 104.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 J 303  FE3                                                     
REMARK 620 2 SF4 J 303  FE4   60.2                                              
REMARK 620 3 SF4 J 303   S1   53.4  54.4                                        
REMARK 620 4 SF4 J 303  FE1   58.2  60.7 101.0                                  
REMARK 620 5 SF4 J 303   S3  100.8  54.7 107.5  53.5                            
REMARK 620 6 CYS J 216   SG  144.1 154.8 127.3 130.8 110.6                      
REMARK 620 7 SF4 J 303   S4   53.3 103.3 103.1  54.7 105.4 100.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 J 303  FE2                                                     
REMARK 620 2 SF4 J 303  FE4   58.9                                              
REMARK 620 3 SF4 J 303   S1   53.6  53.9                                        
REMARK 620 4 SF4 J 303   S2  100.9  53.2 104.3                                  
REMARK 620 5 CYS J 149   SG  157.5 133.4 114.4 100.6                            
REMARK 620 6 SF4 J 303  FE1   60.2  60.9 102.9  54.7 140.1                      
REMARK 620 7 SF4 J 303   S4   52.8 101.8 102.8 108.7 124.4  55.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 152   SG                                                     
REMARK 620 2 SF4 J 303  FE2  137.1                                              
REMARK 620 3 SF4 J 303  FE3  160.7  60.9                                        
REMARK 620 4 SF4 J 303   S1  125.8  54.4  53.7                                  
REMARK 620 5 SF4 J 303   S2  115.0 103.7  54.5 105.3                            
REMARK 620 6 SF4 J 303  FE1  132.1  60.1  58.3 100.5  53.9                      
REMARK 620 7 SF4 J 303   S3   97.3  54.2 101.0 107.0 103.6  53.2                
REMARK 620 N                    1     2     3     4     5     6                 
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 159   SG                                                     
REMARK 620 2 F3S B 304   S3  116.2                                              
REMARK 620 3 F3S B 304   S1  105.6  99.8                                        
REMARK 620 4 F3S B 304  FE3  133.5  51.4  49.9                                  
REMARK 620 5 F3S B 304   S2  117.7 101.1 115.4 108.8                            
REMARK 620 N                    1     2     3     4                             
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 F3S B 304   S3                                                     
REMARK 620 2 CYS B 206   SG  122.4                                              
REMARK 620 3 F3S B 304  FE1   50.0 159.5                                        
REMARK 620 4 F3S B 304   S1   99.7 125.0  51.2                                  
REMARK 620 5 F3S B 304   S4  102.9  94.9 105.2 109.5                            
REMARK 620 N                    1     2     3     4                             
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 212   SG                                                     
REMARK 620 2 F3S B 304   S3   99.2                                              
REMARK 620 3 F3S B 304   S2   82.9 105.5                                        
REMARK 620 4 F3S B 304   S4   98.1 108.1 145.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S F 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S F 304  FE3                                                     
REMARK 620 2 F3S F 304   S3   50.2                                              
REMARK 620 3 F3S F 304   S2  109.1  93.7                                        
REMARK 620 4 F3S F 304   S1   49.5  97.8 125.0                                  
REMARK 620 5 CYS F 159   SG  137.3 123.3 113.6 103.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S F 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S F 304  FE4                                                     
REMARK 620 2 F3S F 304   S3   56.4                                              
REMARK 620 3 F3S F 304   S4   54.9  99.6                                        
REMARK 620 4 F3S F 304  FE1   53.1  49.6 106.4                                  
REMARK 620 5 CYS F 206   SG  149.0 122.6  98.9 154.5                            
REMARK 620 6 F3S F 304   S1   88.1  98.3 115.6  50.5 120.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S F 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 212   SG                                                     
REMARK 620 2 F3S F 304  FE3  136.5                                              
REMARK 620 3 F3S F 304   S3   98.5  57.8                                        
REMARK 620 4 F3S F 304   S4  100.4  58.1 103.3                                  
REMARK 620 5 F3S F 304   S2   82.5 131.5  96.1 159.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S J 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S J 304   S2                                                     
REMARK 620 2 CYS J 159   SG  105.8                                              
REMARK 620 3 F3S J 304  FE4   55.1 158.0                                        
REMARK 620 4 F3S J 304   S3   94.3 121.3  56.8                                  
REMARK 620 5 F3S J 304  FE3  107.4 146.1  52.5  49.4                            
REMARK 620 6 F3S J 304   S1  115.8 120.1  80.8  97.2  48.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S J 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S J 304  FE1                                                     
REMARK 620 2 F3S J 304  FE4   54.2                                              
REMARK 620 3 F3S J 304   S3   47.4  56.9                                        
REMARK 620 4 CYS J 206   SG  142.9 152.5 114.6                                  
REMARK 620 5 F3S J 304   S4  110.0  56.1  97.2 103.9                            
REMARK 620 6 F3S J 304   S1   49.1  82.5  96.0 125.0 116.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S J 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S J 304   S2                                                     
REMARK 620 2 F3S J 304  FE1   56.3                                              
REMARK 620 3 F3S J 304   S3   93.6  54.6                                        
REMARK 620 4 CYS J 212   SG   98.1 133.8  95.2                                  
REMARK 620 5 F3S J 304  FE3  129.3  73.3  57.4 122.8                            
REMARK 620 6 F3S J 304   S4  167.5 130.6  98.7  83.1  57.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C1130  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM C1130   ND                                                     
REMARK 620 2 HIS D  71   NE2  91.3                                              
REMARK 620 3 HEM C1130   NC   91.2  91.8                                        
REMARK 620 4 HIS C  84   NE2  89.1 177.7  86.0                                  
REMARK 620 5 HEM C1130   NA   91.8  84.8 175.5  97.4                            
REMARK 620 6 HEM C1130   NB  176.0  92.4  90.4  87.3  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G1130  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  71   NE2                                                    
REMARK 620 2 HEM G1130   NC   96.3                                              
REMARK 620 3 HIS G  84   NE2 172.5  88.6                                        
REMARK 620 4 HEM G1130   NA   86.7 174.7  87.9                                  
REMARK 620 5 HEM G1130   NB   86.2  88.4  88.2  87.5                            
REMARK 620 6 HEM G1130   ND  100.7  94.2  84.6  89.5 172.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K1130  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  84   NE2                                                    
REMARK 620 2 HIS L  71   NE2 171.7                                              
REMARK 620 3 HEM K1130   NA   92.5  95.8                                        
REMARK 620 4 HEM K1130   NB   83.7  95.6  87.5                                  
REMARK 620 5 HEM K1130   NC   80.1  91.6 171.0  86.8                            
REMARK 620 6 HEM K1130   ND   85.3  95.6  91.0 168.8  93.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
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 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES F 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S F 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES J 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 J 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S J 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1589                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E1589                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA I1589                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE C1129                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE G1129                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE K1129                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO A1590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO E1590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO I1590                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WP9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE                  
REMARK 900 OXIDOREDUCTASE (SQR) SDHB HIS207THR MUTANT                           
REMARK 900 RELATED ID: 2WDQ   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH                 
REMARK 900 CARBOXIN BOUND                                                       
REMARK 900 RELATED ID: 2WDR   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH                 
REMARK 900 PENTACHLOROPHENOL BOUND                                              
REMARK 900 RELATED ID: 1NEK   RELATED DB: PDB                                   
REMARK 900 SUCCINATE DEHYDOGENASE FROM E.COLI                                   
REMARK 900 RELATED ID: 1NEN   RELATED DB: PDB                                   
REMARK 900 MOLECULAR ARCHITECTURE OF SUCCINATE DEHYDROGENASE                    
REMARK 900 (COMPLEXII) PREVENTS REACTIVE OXYGEN SPECIES GENERATION              
REMARK 900 RELATED ID: 2WU2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE                  
REMARK 900 OXIDOREDUCTASE (SQR) SDHC HIS84MET MUTANT                            
REMARK 900 RELATED ID: 2ACZ   RELATED DB: PDB                                   
REMARK 900 COMPLEX II (SUCCINATE DEHYDROGENASE) FROM E. COLI                    
REMARK 900 WITHATPENIN A5 INHIBITOR CO-CRYSTALLIZED AT THE                      
REMARK 900 UBIQUINONEBINDING SITE                                               
REMARK 900 RELATED ID: 2WU5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE                  
REMARK 900 OXIDOREDUCTASE (SQR) SDHD HIS71MET MUTANT                            
REMARK 900 RELATED ID: 2WDV   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH AN              
REMARK 900 EMPTY QUINONE-BINDING POCKET                                         
DBREF  2WS3 A    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WS3 B    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WS3 C    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WS3 D    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WS3 E    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WS3 F    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WS3 G    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WS3 H    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WS3 I    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WS3 J    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WS3 K    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WS3 L    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
SEQADV 2WS3 PHE D   83  UNP  P0AC44    TYR    83 ENGINEERED MUTATION            
SEQADV 2WS3 PHE H   83  UNP  P0AC44    TYR    83 ENGINEERED MUTATION            
SEQADV 2WS3 PHE L   83  UNP  P0AC44    TYR    83 ENGINEERED MUTATION            
SEQRES   1 A  588  MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE          
SEQRES   2 A  588  GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE          
SEQRES   3 A  588  SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL          
SEQRES   4 A  588  PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY          
SEQRES   5 A  588  ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP          
SEQRES   6 A  588  GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR          
SEQRES   7 A  588  ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR          
SEQRES   8 A  588  GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU          
SEQRES   9 A  588  PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG          
SEQRES  10 A  588  PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN          
SEQRES  11 A  588  ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS          
SEQRES  12 A  588  ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN          
SEQRES  13 A  588  HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU          
SEQRES  14 A  588  VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA          
SEQRES  15 A  588  LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA          
SEQRES  16 A  588  ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE          
SEQRES  17 A  588  TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP          
SEQRES  18 A  588  GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN          
SEQRES  19 A  588  ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA          
SEQRES  20 A  588  GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU          
SEQRES  21 A  588  GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET          
SEQRES  22 A  588  GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG          
SEQRES  23 A  588  ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU          
SEQRES  24 A  588  GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS          
SEQRES  25 A  588  LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER          
SEQRES  26 A  588  ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA          
SEQRES  27 A  588  HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO          
SEQRES  28 A  588  THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL          
SEQRES  29 A  588  THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP          
SEQRES  30 A  588  VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA          
SEQRES  31 A  588  CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN          
SEQRES  32 A  588  SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY          
SEQRES  33 A  588  LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU          
SEQRES  34 A  588  ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP          
SEQRES  35 A  588  ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP          
SEQRES  36 A  588  PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN          
SEQRES  37 A  588  HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA          
SEQRES  38 A  588  LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU          
SEQRES  39 A  588  LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN          
SEQRES  40 A  588  THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET          
SEQRES  41 A  588  GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG          
SEQRES  42 A  588  THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO          
SEQRES  43 A  588  ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR          
SEQRES  44 A  588  LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN          
SEQRES  45 A  588  MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE          
SEQRES  46 A  588  ARG THR TYR                                                  
SEQRES   1 B  238  MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP          
SEQRES   2 B  238  VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU          
SEQRES   3 B  238  ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU          
SEQRES   4 B  238  ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG          
SEQRES   5 B  238  ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU          
SEQRES   6 B  238  ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO          
SEQRES   7 B  238  ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE          
SEQRES   8 B  238  ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL          
SEQRES   9 B  238  VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE          
SEQRES  10 B  238  LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA          
SEQRES  11 B  238  ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU          
SEQRES  12 B  238  ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER          
SEQRES  13 B  238  THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE          
SEQRES  14 B  238  ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU          
SEQRES  15 B  238  ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP          
SEQRES  16 B  238  GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER          
SEQRES  17 B  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 B  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 B  238  GLN ARG ASN ALA                                              
SEQRES   1 C  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 C  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 C  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 C  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 C  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 C  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 C  129  THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS          
SEQRES   8 C  129  MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU          
SEQRES   9 C  129  ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR          
SEQRES  10 C  129  VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP              
SEQRES   1 D  115  MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL          
SEQRES   2 D  115  HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU          
SEQRES   3 D  115  THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR          
SEQRES   4 D  115  SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE          
SEQRES   5 D  115  ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU          
SEQRES   6 D  115  PHE SER ILE LEU ILE HIS ALA TRP ILE GLY MET TRP GLN          
SEQRES   7 D  115  VAL LEU THR ASP PHE VAL LYS PRO LEU ALA LEU ARG LEU          
SEQRES   8 D  115  MET LEU GLN LEU VAL ILE VAL VAL ALA LEU VAL VAL TYR          
SEQRES   9 D  115  VAL ILE TYR GLY PHE VAL VAL VAL TRP GLY VAL                  
SEQRES   1 E  588  MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE          
SEQRES   2 E  588  GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE          
SEQRES   3 E  588  SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL          
SEQRES   4 E  588  PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY          
SEQRES   5 E  588  ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP          
SEQRES   6 E  588  GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR          
SEQRES   7 E  588  ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR          
SEQRES   8 E  588  GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU          
SEQRES   9 E  588  PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG          
SEQRES  10 E  588  PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN          
SEQRES  11 E  588  ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS          
SEQRES  12 E  588  ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN          
SEQRES  13 E  588  HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU          
SEQRES  14 E  588  VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA          
SEQRES  15 E  588  LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA          
SEQRES  16 E  588  ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE          
SEQRES  17 E  588  TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP          
SEQRES  18 E  588  GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN          
SEQRES  19 E  588  ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA          
SEQRES  20 E  588  GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU          
SEQRES  21 E  588  GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET          
SEQRES  22 E  588  GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG          
SEQRES  23 E  588  ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU          
SEQRES  24 E  588  GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS          
SEQRES  25 E  588  LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER          
SEQRES  26 E  588  ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA          
SEQRES  27 E  588  HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO          
SEQRES  28 E  588  THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL          
SEQRES  29 E  588  THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP          
SEQRES  30 E  588  VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA          
SEQRES  31 E  588  CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN          
SEQRES  32 E  588  SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY          
SEQRES  33 E  588  LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU          
SEQRES  34 E  588  ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP          
SEQRES  35 E  588  ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP          
SEQRES  36 E  588  PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN          
SEQRES  37 E  588  HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA          
SEQRES  38 E  588  LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU          
SEQRES  39 E  588  LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN          
SEQRES  40 E  588  THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET          
SEQRES  41 E  588  GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG          
SEQRES  42 E  588  THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO          
SEQRES  43 E  588  ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR          
SEQRES  44 E  588  LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN          
SEQRES  45 E  588  MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE          
SEQRES  46 E  588  ARG THR TYR                                                  
SEQRES   1 F  238  MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP          
SEQRES   2 F  238  VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU          
SEQRES   3 F  238  ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU          
SEQRES   4 F  238  ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG          
SEQRES   5 F  238  ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU          
SEQRES   6 F  238  ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO          
SEQRES   7 F  238  ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE          
SEQRES   8 F  238  ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL          
SEQRES   9 F  238  VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE          
SEQRES  10 F  238  LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA          
SEQRES  11 F  238  ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU          
SEQRES  12 F  238  ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER          
SEQRES  13 F  238  THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE          
SEQRES  14 F  238  ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU          
SEQRES  15 F  238  ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP          
SEQRES  16 F  238  GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER          
SEQRES  17 F  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 F  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 F  238  GLN ARG ASN ALA                                              
SEQRES   1 G  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 G  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 G  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 G  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 G  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 G  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 G  129  THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS          
SEQRES   8 G  129  MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU          
SEQRES   9 G  129  ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR          
SEQRES  10 G  129  VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP              
SEQRES   1 H  115  MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL          
SEQRES   2 H  115  HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU          
SEQRES   3 H  115  THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR          
SEQRES   4 H  115  SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE          
SEQRES   5 H  115  ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU          
SEQRES   6 H  115  PHE SER ILE LEU ILE HIS ALA TRP ILE GLY MET TRP GLN          
SEQRES   7 H  115  VAL LEU THR ASP PHE VAL LYS PRO LEU ALA LEU ARG LEU          
SEQRES   8 H  115  MET LEU GLN LEU VAL ILE VAL VAL ALA LEU VAL VAL TYR          
SEQRES   9 H  115  VAL ILE TYR GLY PHE VAL VAL VAL TRP GLY VAL                  
SEQRES   1 I  588  MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE          
SEQRES   2 I  588  GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE          
SEQRES   3 I  588  SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL          
SEQRES   4 I  588  PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY          
SEQRES   5 I  588  ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP          
SEQRES   6 I  588  GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR          
SEQRES   7 I  588  ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR          
SEQRES   8 I  588  GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU          
SEQRES   9 I  588  PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG          
SEQRES  10 I  588  PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN          
SEQRES  11 I  588  ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS          
SEQRES  12 I  588  ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN          
SEQRES  13 I  588  HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU          
SEQRES  14 I  588  VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA          
SEQRES  15 I  588  LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA          
SEQRES  16 I  588  ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE          
SEQRES  17 I  588  TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP          
SEQRES  18 I  588  GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN          
SEQRES  19 I  588  ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA          
SEQRES  20 I  588  GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU          
SEQRES  21 I  588  GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET          
SEQRES  22 I  588  GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG          
SEQRES  23 I  588  ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU          
SEQRES  24 I  588  GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS          
SEQRES  25 I  588  LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER          
SEQRES  26 I  588  ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA          
SEQRES  27 I  588  HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO          
SEQRES  28 I  588  THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL          
SEQRES  29 I  588  THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP          
SEQRES  30 I  588  VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA          
SEQRES  31 I  588  CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN          
SEQRES  32 I  588  SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY          
SEQRES  33 I  588  LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU          
SEQRES  34 I  588  ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP          
SEQRES  35 I  588  ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP          
SEQRES  36 I  588  PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN          
SEQRES  37 I  588  HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA          
SEQRES  38 I  588  LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU          
SEQRES  39 I  588  LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN          
SEQRES  40 I  588  THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET          
SEQRES  41 I  588  GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG          
SEQRES  42 I  588  THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO          
SEQRES  43 I  588  ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR          
SEQRES  44 I  588  LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN          
SEQRES  45 I  588  MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE          
SEQRES  46 I  588  ARG THR TYR                                                  
SEQRES   1 J  238  MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP          
SEQRES   2 J  238  VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU          
SEQRES   3 J  238  ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU          
SEQRES   4 J  238  ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG          
SEQRES   5 J  238  ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU          
SEQRES   6 J  238  ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO          
SEQRES   7 J  238  ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE          
SEQRES   8 J  238  ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL          
SEQRES   9 J  238  VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE          
SEQRES  10 J  238  LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA          
SEQRES  11 J  238  ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU          
SEQRES  12 J  238  ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER          
SEQRES  13 J  238  THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE          
SEQRES  14 J  238  ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU          
SEQRES  15 J  238  ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP          
SEQRES  16 J  238  GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER          
SEQRES  17 J  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 J  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 J  238  GLN ARG ASN ALA                                              
SEQRES   1 K  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 K  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 K  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 K  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 K  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 K  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 K  129  THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS          
SEQRES   8 K  129  MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU          
SEQRES   9 K  129  ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR          
SEQRES  10 K  129  VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP              
SEQRES   1 L  115  MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL          
SEQRES   2 L  115  HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU          
SEQRES   3 L  115  THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR          
SEQRES   4 L  115  SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE          
SEQRES   5 L  115  ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU          
SEQRES   6 L  115  PHE SER ILE LEU ILE HIS ALA TRP ILE GLY MET TRP GLN          
SEQRES   7 L  115  VAL LEU THR ASP PHE VAL LYS PRO LEU ALA LEU ARG LEU          
SEQRES   8 L  115  MET LEU GLN LEU VAL ILE VAL VAL ALA LEU VAL VAL TYR          
SEQRES   9 L  115  VAL ILE TYR GLY PHE VAL VAL VAL TRP GLY VAL                  
HET    FAD  A 601      53                                                       
HET     NA  A1589       1                                                       
HET    TEO  A1590       9                                                       
HET    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    CBE  C1129      16                                                       
HET    HEM  C1130      43                                                       
HET    FAD  E 601      53                                                       
HET     NA  E1589       1                                                       
HET    TEO  E1590       9                                                       
HET    FES  F 302       4                                                       
HET    SF4  F 303       8                                                       
HET    F3S  F 304       7                                                       
HET    CBE  G1129      16                                                       
HET    HEM  G1130      43                                                       
HET    FAD  I 601      53                                                       
HET     NA  I1589       1                                                       
HET    TEO  I1590       9                                                       
HET    FES  J 302       4                                                       
HET    SF4  J 303       8                                                       
HET    F3S  J 304       7                                                       
HET    CBE  K1129      16                                                       
HET    HEM  K1130      43                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     TEO MALATE LIKE INTERMEDIATE                                         
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     CBE 2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE        
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     CBE 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-CARBOXANILID                 
HETSYN     HEM HEME                                                             
FORMUL  13  FAD    3(C27 H33 N9 O15 P2)                                         
FORMUL  14   NA    3(NA 1+)                                                     
FORMUL  15  TEO    3(C4 H4 O5 2-)                                               
FORMUL  16  FES    3(FE2 S2)                                                    
FORMUL  17  SF4    3(FE4 S4)                                                    
FORMUL  18  F3S    3(FE3 S4)                                                    
FORMUL  19  CBE    3(C12 H13 N O2 S)                                            
FORMUL  20  HEM    3(C34 H32 FE N4 O4)                                          
HELIX    1   1 GLY A   16  SER A   29  1                                  14    
HELIX    2   2 PHE A   40  SER A   44  5                                   5    
HELIX    3   3 SER A   44  ALA A   49  5                                   6    
HELIX    4   4 ASN A   64  SER A   76  1                                  13    
HELIX    5   5 ASP A   81  GLY A  103  1                                  23    
HELIX    6   6 ARG A  140  ASN A  156  1                                  17    
HELIX    7   7 ALA A  205  TYR A  209  5                                   5    
HELIX    8   8 GLY A  220  ALA A  229  1                                  10    
HELIX    9   9 GLU A  255  GLU A  260  1                                   6    
HELIX   10  10 PHE A  272  ALA A  277  1                                   6    
HELIX   11  11 ALA A  280  ALA A  284  5                                   5    
HELIX   12  12 GLY A  285  GLU A  299  1                                  15    
HELIX   13  13 LEU A  315  LEU A  318  5                                   4    
HELIX   14  14 GLY A  319  LEU A  327  1                                   9    
HELIX   15  15 LEU A  327  ALA A  338  1                                  12    
HELIX   16  16 GLY A  402  HIS A  418  1                                  17    
HELIX   17  17 HIS A  418  GLY A  427  1                                  10    
HELIX   18  18 SER A  433  ASN A  450  1                                  18    
HELIX   19  19 ASP A  455  PHE A  471  1                                  17    
HELIX   20  20 GLU A  476  LYS A  495  1                                  20    
HELIX   21  21 ASN A  507  ARG A  533  1                                  27    
HELIX   22  22 MET B   34  ASP B   46  1                                  13    
HELIX   23  23 CYS B   75  THR B   77  5                                   3    
HELIX   24  24 PRO B   78  ASN B   83  1                                   6    
HELIX   25  25 MET B  107  ILE B  117  1                                  11    
HELIX   26  26 MET B  136  GLU B  141  1                                   6    
HELIX   27  27 LYS B  142  ASP B  144  5                                   3    
HELIX   28  28 CYS B  155  SER B  158  5                                   4    
HELIX   29  29 CYS B  159  ASN B  165  1                                   7    
HELIX   30  30 GLY B  171  ILE B  183  1                                  13    
HELIX   31  31 GLU B  189  GLY B  196  1                                   8    
HELIX   32  32 MET B  210  CYS B  216  1                                   7    
HELIX   33  33 ASN B  221  ALA B  238  1                                  18    
HELIX   34  34 ASP C   14  ILE C   18  5                                   5    
HELIX   35  35 PRO C   21  SER C   54  1                                  34    
HELIX   36  36 SER C   54  SER C   67  1                                  14    
HELIX   37  37 SER C   67  PHE C   96  1                                  30    
HELIX   38  38 THR C  102  VAL C  128  1                                  27    
HELIX   39  39 ASN D   11  ALA D   38  1                                  28    
HELIX   40  40 THR D   44  SER D   54  1                                  11    
HELIX   41  41 SER D   54  VAL D   84  1                                  31    
HELIX   42  42 PRO D   86  GLY D  114  1                                  29    
HELIX   43  43 GLY E   16  SER E   29  1                                  14    
HELIX   44  44 PHE E   40  SER E   44  5                                   5    
HELIX   45  45 SER E   44  ALA E   49  5                                   6    
HELIX   46  46 ASN E   64  SER E   76  1                                  13    
HELIX   47  47 ASP E   81  MET E  102  1                                  22    
HELIX   48  48 ARG E  140  ASN E  156  1                                  17    
HELIX   49  49 ALA E  205  TYR E  209  5                                   5    
HELIX   50  50 GLY E  220  ALA E  229  1                                  10    
HELIX   51  51 GLU E  255  GLU E  260  1                                   6    
HELIX   52  52 PHE E  272  ALA E  277  1                                   6    
HELIX   53  53 ALA E  280  ALA E  284  5                                   5    
HELIX   54  54 GLY E  285  GLU E  299  1                                  15    
HELIX   55  55 LEU E  315  LEU E  318  5                                   4    
HELIX   56  56 GLY E  319  LEU E  327  1                                   9    
HELIX   57  57 LEU E  327  HIS E  339  1                                  13    
HELIX   58  58 GLY E  402  GLY E  427  1                                  26    
HELIX   59  59 SER E  433  ASN E  450  1                                  18    
HELIX   60  60 ASP E  455  PHE E  471  1                                  17    
HELIX   61  61 GLU E  476  LYS E  495  1                                  20    
HELIX   62  62 ASN E  507  ARG E  533  1                                  27    
HELIX   63  63 MET F   34  ASP F   46  1                                  13    
HELIX   64  64 PRO F   78  ASN F   83  1                                   6    
HELIX   65  65 MET F  107  ILE F  117  1                                  11    
HELIX   66  66 MET F  136  GLU F  141  1                                   6    
HELIX   67  67 LYS F  142  ASP F  144  5                                   3    
HELIX   68  68 CYS F  155  SER F  158  5                                   4    
HELIX   69  69 CYS F  159  ASN F  165  1                                   7    
HELIX   70  70 GLY F  171  ILE F  183  1                                  13    
HELIX   71  71 GLU F  189  GLY F  196  1                                   8    
HELIX   72  72 MET F  210  CYS F  216  1                                   7    
HELIX   73  73 ASN F  221  ALA F  238  1                                  18    
HELIX   74  74 ASP G   14  ILE G   18  5                                   5    
HELIX   75  75 PRO G   21  SER G   54  1                                  34    
HELIX   76  76 SER G   54  SER G   67  1                                  14    
HELIX   77  77 SER G   67  PHE G   96  1                                  30    
HELIX   78  78 THR G  102  VAL G  128  1                                  27    
HELIX   79  79 ASN H   11  THR H   39  1                                  29    
HELIX   80  80 THR H   44  SER H   54  1                                  11    
HELIX   81  81 SER H   54  VAL H   84  1                                  31    
HELIX   82  82 PRO H   86  GLY H  114  1                                  29    
HELIX   83  83 GLY I   16  SER I   29  1                                  14    
HELIX   84  84 PHE I   40  SER I   44  5                                   5    
HELIX   85  85 SER I   44  ALA I   49  5                                   6    
HELIX   86  86 ASN I   64  SER I   76  1                                  13    
HELIX   87  87 ASP I   81  MET I  102  1                                  22    
HELIX   88  88 ARG I  140  ASN I  156  1                                  17    
HELIX   89  89 ALA I  205  TYR I  209  5                                   5    
HELIX   90  90 GLY I  220  ALA I  229  1                                  10    
HELIX   91  91 GLU I  255  GLU I  260  1                                   6    
HELIX   92  92 PHE I  272  ALA I  277  1                                   6    
HELIX   93  93 ALA I  280  ALA I  284  5                                   5    
HELIX   94  94 GLY I  285  GLU I  299  1                                  15    
HELIX   95  95 LEU I  315  LEU I  318  5                                   4    
HELIX   96  96 GLY I  319  LEU I  327  1                                   9    
HELIX   97  97 LEU I  327  ALA I  338  1                                  12    
HELIX   98  98 GLY I  402  HIS I  418  1                                  17    
HELIX   99  99 HIS I  418  GLY I  427  1                                  10    
HELIX  100 100 SER I  433  ASN I  450  1                                  18    
HELIX  101 101 ASP I  455  PHE I  471  1                                  17    
HELIX  102 102 GLU I  476  LYS I  495  1                                  20    
HELIX  103 103 ASN I  507  ARG I  533  1                                  27    
HELIX  104 104 MET J   34  ASP J   46  1                                  13    
HELIX  105 105 CYS J   75  THR J   77  5                                   3    
HELIX  106 106 PRO J   78  ASN J   83  1                                   6    
HELIX  107 107 MET J  107  ILE J  117  1                                  11    
HELIX  108 108 MET J  136  LYS J  142  1                                   7    
HELIX  109 109 CYS J  155  SER J  158  5                                   4    
HELIX  110 110 CYS J  159  ASN J  165  1                                   7    
HELIX  111 111 GLY J  171  ILE J  183  1                                  13    
HELIX  112 112 GLU J  189  GLY J  196  1                                   8    
HELIX  113 113 MET J  210  CYS J  216  1                                   7    
HELIX  114 114 ASN J  221  ALA J  238  1                                  18    
HELIX  115 115 ASP K   14  ILE K   18  5                                   5    
HELIX  116 116 PRO K   21  SER K   54  1                                  34    
HELIX  117 117 SER K   54  SER K   67  1                                  14    
HELIX  118 118 SER K   67  PHE K   96  1                                  30    
HELIX  119 119 THR K  102  VAL K  128  1                                  27    
HELIX  120 120 ASN L   11  THR L   39  1                                  29    
HELIX  121 121 THR L   44  SER L   54  1                                  11    
HELIX  122 122 SER L   54  VAL L   84  1                                  31    
HELIX  123 123 PRO L   86  GLY L  114  1                                  29    
SHEET    1  AA 4 VAL A   5  GLU A   7  0                                        
SHEET    2  AA 4 VAL A 190  LYS A 194  1  O  TYR A 192   N  ARG A   6           
SHEET    3  AA 4 VAL A 177  CYS A 184 -1  O  CYS A 180   N  PHE A 193           
SHEET    4  AA 4 TRP A 164  LYS A 171 -1  O  TYR A 165   N  LEU A 183           
SHEET    1  AB 6 THR A 159  SER A 162  0                                        
SHEET    2  AB 6 CYS A  33  SER A  37  1  O  CYS A  33   N  THR A 159           
SHEET    3  AB 6 ALA A  10  ILE A  13  1  O  ALA A  10   N  ALA A  34           
SHEET    4  AB 6 ALA A 197  LEU A 200  1  O  ALA A 197   N  VAL A  11           
SHEET    5  AB 6 ASP A 377  ALA A 385  1  O  GLY A 382   N  THR A 198           
SHEET    6  AB 6 GLN A 367  VAL A 371 -1  O  ALA A 368   N  VAL A 380           
SHEET    1  AC 3 ILE A  53  THR A  54  0                                        
SHEET    2  AC 3 GLN A 130  ALA A 135 -1  O  ALA A 135   N  ILE A  53           
SHEET    3  AC 3 GLN A 116  SER A 123 -1  O  ARG A 117   N  THR A 134           
SHEET    1  AD 3 VAL A 233  GLN A 234  0                                        
SHEET    2  AD 3 CYS A 555  LEU A 560 -1  O  TYR A 559   N  VAL A 233           
SHEET    3  AD 3 SER A 565  SER A 570 -1  O  SER A 565   N  LEU A 560           
SHEET    1  AE 4 TRP A 239  ILE A 246  0                                        
SHEET    2  AE 4 ILE A 347  MET A 356 -1  O  ILE A 350   N  GLY A 245           
SHEET    3  AE 4 ALA A 311  LYS A 314 -1  O  ALA A 311   N  VAL A 349           
SHEET    4  AE 4 TYR A 263  LEU A 265 -1  O  TYR A 263   N  LYS A 314           
SHEET    1  AF 2 ILE A 360  PRO A 361  0                                        
SHEET    2  AF 2 ALA A 390  CYS A 391  1  N  CYS A 391   O  ILE A 360           
SHEET    1  BA 5 ARG B  19  GLU B  26  0                                        
SHEET    2  BA 5 ARG B   2  ARG B   9 -1  O  LEU B   3   N  LEU B  25           
SHEET    3  BA 5 ILE B  89  ARG B  92  1  O  ILE B  89   N  SER B   6           
SHEET    4  BA 5 GLY B  64  MET B  67 -1  O  ASN B  66   N  ARG B  92           
SHEET    5  BA 5 LYS B  70  LEU B  73 -1  O  LYS B  70   N  MET B  67           
SHEET    1  BB 2 VAL B  99  ARG B 101  0                                        
SHEET    2  BB 2 VAL B 104  VAL B 105 -1  O  VAL B 104   N  ILE B 100           
SHEET    1  EA 4 VAL E   5  GLU E   7  0                                        
SHEET    2  EA 4 VAL E 190  LYS E 194  1  O  TYR E 192   N  ARG E   6           
SHEET    3  EA 4 VAL E 177  CYS E 184 -1  O  CYS E 180   N  PHE E 193           
SHEET    4  EA 4 TRP E 164  LYS E 171 -1  O  TYR E 165   N  LEU E 183           
SHEET    1  EB 6 THR E 159  SER E 162  0                                        
SHEET    2  EB 6 CYS E  33  SER E  37  1  O  CYS E  33   N  THR E 159           
SHEET    3  EB 6 ALA E  10  ILE E  13  1  O  ALA E  10   N  ALA E  34           
SHEET    4  EB 6 ALA E 197  LEU E 200  1  O  ALA E 197   N  VAL E  11           
SHEET    5  EB 6 ASP E 377  ALA E 385  1  O  GLY E 382   N  THR E 198           
SHEET    6  EB 6 GLN E 367  VAL E 371 -1  O  ALA E 368   N  VAL E 380           
SHEET    1  EC 3 ILE E  53  THR E  54  0                                        
SHEET    2  EC 3 THR E 134  ALA E 135 -1  O  ALA E 135   N  ILE E  53           
SHEET    3  EC 3 GLN E 116  ARG E 117 -1  O  ARG E 117   N  THR E 134           
SHEET    1  ED 3 VAL E 233  GLN E 234  0                                        
SHEET    2  ED 3 CYS E 555  LEU E 560 -1  O  TYR E 559   N  VAL E 233           
SHEET    3  ED 3 SER E 565  SER E 570 -1  O  SER E 565   N  LEU E 560           
SHEET    1  EE 4 TRP E 239  ILE E 246  0                                        
SHEET    2  EE 4 ILE E 347  MET E 356 -1  O  ILE E 350   N  GLY E 245           
SHEET    3  EE 4 ALA E 311  LYS E 314 -1  O  ALA E 311   N  VAL E 349           
SHEET    4  EE 4 TYR E 263  LEU E 265 -1  O  TYR E 263   N  LYS E 314           
SHEET    1  EF 2 ILE E 360  PRO E 361  0                                        
SHEET    2  EF 2 ALA E 390  CYS E 391  1  N  CYS E 391   O  ILE E 360           
SHEET    1  FA 5 ARG F  19  GLU F  26  0                                        
SHEET    2  FA 5 ARG F   2  ARG F   9 -1  O  LEU F   3   N  LEU F  25           
SHEET    3  FA 5 ILE F  89  ARG F  92  1  O  ILE F  89   N  SER F   6           
SHEET    4  FA 5 GLY F  64  MET F  67 -1  O  ASN F  66   N  ARG F  92           
SHEET    5  FA 5 LYS F  70  LEU F  73 -1  O  LYS F  70   N  MET F  67           
SHEET    1  FB 2 VAL F  99  ARG F 101  0                                        
SHEET    2  FB 2 VAL F 104  VAL F 105 -1  O  VAL F 104   N  ILE F 100           
SHEET    1  IA 6 THR I 159  SER I 162  0                                        
SHEET    2  IA 6 CYS I  33  SER I  37  1  O  CYS I  33   N  THR I 159           
SHEET    3  IA 6 VAL I   5  ILE I  13  1  O  ALA I  10   N  ALA I  34           
SHEET    4  IA 6 VAL I 190  LEU I 200  1  O  TYR I 192   N  ARG I   6           
SHEET    5  IA 6 ASP I 377  ALA I 385 -1  O  GLY I 382   N  THR I 198           
SHEET    6  IA 6 GLN I 367  VAL I 371  1  O  ALA I 368   N  VAL I 380           
SHEET    1  IB 6 THR I 159  SER I 162  0                                        
SHEET    2  IB 6 CYS I  33  SER I  37  1  O  CYS I  33   N  THR I 159           
SHEET    3  IB 6 VAL I   5  ILE I  13  1  O  ALA I  10   N  ALA I  34           
SHEET    4  IB 6 VAL I 190  LEU I 200  1  O  TYR I 192   N  ARG I   6           
SHEET    5  IB 6 VAL I 177  CYS I 184 -1  O  VAL I 178   N  ALA I 195           
SHEET    6  IB 6 TRP I 164  LYS I 171 -1  O  TYR I 165   N  LEU I 183           
SHEET    1  IC 3 ILE I  53  THR I  54  0                                        
SHEET    2  IC 3 GLN I 130  ALA I 135 -1  O  ALA I 135   N  ILE I  53           
SHEET    3  IC 3 GLN I 116  SER I 123 -1  O  ARG I 117   N  THR I 134           
SHEET    1  ID 3 VAL I 233  GLN I 234  0                                        
SHEET    2  ID 3 CYS I 555  LEU I 560 -1  O  TYR I 559   N  VAL I 233           
SHEET    3  ID 3 SER I 565  SER I 570 -1  O  SER I 565   N  LEU I 560           
SHEET    1  IE 4 TRP I 239  ILE I 246  0                                        
SHEET    2  IE 4 ILE I 347  MET I 356 -1  O  ILE I 350   N  GLY I 245           
SHEET    3  IE 4 ALA I 311  LYS I 314 -1  O  ALA I 311   N  VAL I 349           
SHEET    4  IE 4 TYR I 263  LEU I 265 -1  O  TYR I 263   N  LYS I 314           
SHEET    1  IF 2 ILE I 360  PRO I 361  0                                        
SHEET    2  IF 2 ALA I 390  CYS I 391  1  N  CYS I 391   O  ILE I 360           
SHEET    1  JA 5 ARG J  19  GLU J  26  0                                        
SHEET    2  JA 5 ARG J   2  ARG J   9 -1  O  LEU J   3   N  LEU J  25           
SHEET    3  JA 5 ILE J  89  ARG J  92  1  O  ILE J  89   N  SER J   6           
SHEET    4  JA 5 GLY J  64  MET J  67 -1  O  ASN J  66   N  ARG J  92           
SHEET    5  JA 5 LYS J  70  LEU J  73 -1  O  LYS J  70   N  MET J  67           
SHEET    1  JB 2 VAL J  99  ARG J 101  0                                        
SHEET    2  JB 2 VAL J 104  VAL J 105 -1  O  VAL J 104   N  ILE J 100           
LINK        NA    NA A1589                 O   ALA A 390     1555   1555  2.60  
LINK        NA    NA A1589                 O   GLY A 358     1555   1555  2.51  
LINK        NA    NA A1589                 O   MET A 357     1555   1555  2.92  
LINK        NA    NA A1589                 O   GLU A 388     1555   1555  2.32  
LINK        NA    NA A1589                 O   MET A 356     1555   1555  2.65  
LINK         SG  CYS B  55                FE1  FES B 302     1555   1555  2.32  
LINK         SG  CYS B  60                FE1  FES B 302     1555   1555  2.24  
LINK         OD1 ASP B  63                FE2  FES B 302     1555   1555  1.82  
LINK         SG  CYS B  75                FE2  FES B 302     1555   1555  2.29  
LINK         SG  CYS B 149                FE3  SF4 B 303     1555   1555  2.27  
LINK         SG  CYS B 152                FE4  SF4 B 303     1555   1555  2.33  
LINK         SG  CYS B 155                FE1  SF4 B 303     1555   1555  2.30  
LINK         SG  CYS B 159                FE1  F3S B 304     1555   1555  2.28  
LINK         SG  CYS B 206                FE3  F3S B 304     1555   1555  2.29  
LINK         SG  CYS B 212                FE4  F3S B 304     1555   1555  2.32  
LINK         SG  CYS B 216                FE2  SF4 B 303     1555   1555  2.26  
LINK         NE2 HIS C  84                FE   HEM C1130     1555   1555  1.93  
LINK         NE2 HIS D  71                FE   HEM C1130     1555   1555  1.95  
LINK        NA    NA E1589                 O   ALA E 390     1555   1555  2.60  
LINK        NA    NA E1589                 O   MET E 357     1555   1555  2.96  
LINK        NA    NA E1589                 O   GLU E 388     1555   1555  2.36  
LINK        NA    NA E1589                 O   GLY E 358     1555   1555  2.39  
LINK        NA    NA E1589                 O   MET E 356     1555   1555  2.66  
LINK         SG  CYS F  55                FE1  FES F 302     1555   1555  2.30  
LINK         SG  CYS F  60                FE1  FES F 302     1555   1555  2.28  
LINK         OD1 ASP F  63                FE2  FES F 302     1555   1555  1.82  
LINK         SG  CYS F  75                FE2  FES F 302     1555   1555  2.25  
LINK         SG  CYS F 149                FE3  SF4 F 303     1555   1555  2.30  
LINK         SG  CYS F 152                FE4  SF4 F 303     1555   1555  2.28  
LINK         SG  CYS F 155                FE1  SF4 F 303     1555   1555  2.31  
LINK         SG  CYS F 159                FE1  F3S F 304     1555   1555  2.27  
LINK         SG  CYS F 206                FE3  F3S F 304     1555   1555  2.26  
LINK         SG  CYS F 212                FE4  F3S F 304     1555   1555  2.32  
LINK         SG  CYS F 216                FE2  SF4 F 303     1555   1555  2.27  
LINK         NE2 HIS G  84                FE   HEM G1130     1555   1555  1.93  
LINK         NE2 HIS H  71                FE   HEM G1130     1555   1555  1.93  
LINK        NA    NA I1589                 O   MET I 356     1555   1555  2.81  
LINK        NA    NA I1589                 O   MET I 357     1555   1555  3.17  
LINK        NA    NA I1589                 O   GLY I 358     1555   1555  2.82  
LINK        NA    NA I1589                 O   GLU I 388     1555   1555  2.31  
LINK        NA    NA I1589                 O   ALA I 390     1555   1555  2.51  
LINK         SG  CYS J  55                FE1  FES J 302     1555   1555  2.50  
LINK         SG  CYS J  60                FE1  FES J 302     1555   1555  2.29  
LINK         OD1 ASP J  63                FE2  FES J 302     1555   1555  1.82  
LINK         SG  CYS J  75                FE2  FES J 302     1555   1555  2.28  
LINK         SG  CYS J 149                FE3  SF4 J 303     1555   1555  2.34  
LINK         SG  CYS J 152                FE4  SF4 J 303     1555   1555  2.29  
LINK         SG  CYS J 155                FE1  SF4 J 303     1555   1555  2.30  
LINK         SG  CYS J 159                FE1  F3S J 304     1555   1555  2.29  
LINK         SG  CYS J 206                FE3  F3S J 304     1555   1555  2.32  
LINK         SG  CYS J 212                FE4  F3S J 304     1555   1555  2.60  
LINK         SG  CYS J 216                FE2  SF4 J 303     1555   1555  2.29  
LINK         NE2 HIS K  84                FE   HEM K1130     1555   1555  1.98  
LINK         NE2 HIS L  71                FE   HEM K1130     1555   1555  1.95  
CISPEP   1 VAL A  392    SER A  393          0         9.17                     
CISPEP   2 VAL E  392    SER E  393          0         7.23                     
CISPEP   3 VAL I  392    SER I  393          0         7.44                     
SITE     1 AC1 35 GLY A  14  ALA A  15  GLY A  16  GLY A  17                    
SITE     2 AC1 35 ALA A  18  SER A  37  LYS A  38  VAL A  39                    
SITE     3 AC1 35 SER A  44  HIS A  45  THR A  46  SER A  48                    
SITE     4 AC1 35 ALA A  49  GLN A  50  GLY A  51  GLY A  52                    
SITE     5 AC1 35 TRP A 164  ALA A 166  ALA A 201  THR A 202                    
SITE     6 AC1 35 GLY A 203  THR A 213  ASP A 221  LEU A 252                    
SITE     7 AC1 35 HIS A 354  TYR A 355  GLY A 387  GLU A 388                    
SITE     8 AC1 35 ARG A 399  GLY A 402  ASN A 403  SER A 404                    
SITE     9 AC1 35 LEU A 405  LEU A 408  TEO A1590                               
SITE     1 AC2  8 SER B  54  CYS B  55  ARG B  56  GLY B  58                    
SITE     2 AC2  8 CYS B  60  GLY B  61  ASP B  63  CYS B  75                    
SITE     1 AC3  8 CYS B 149  ILE B 150  CYS B 152  ALA B 153                    
SITE     2 AC3  8 CYS B 155  ALA B 173  CYS B 216  PRO B 217                    
SITE     1 AC4  9 CYS B 159  CYS B 206  HIS B 207  SER B 208                    
SITE     2 AC4  9 ILE B 209  MET B 210  ASN B 211  CYS B 212                    
SITE     3 AC4  9 THR B 223                                                     
SITE     1 AC5 37 GLY E  14  ALA E  15  GLY E  16  GLY E  17                    
SITE     2 AC5 37 ALA E  18  SER E  37  LYS E  38  VAL E  39                    
SITE     3 AC5 37 SER E  44  HIS E  45  THR E  46  SER E  48                    
SITE     4 AC5 37 ALA E  49  GLN E  50  GLY E  51  GLY E  52                    
SITE     5 AC5 37 TRP E 164  TYR E 165  ALA E 166  ALA E 201                    
SITE     6 AC5 37 THR E 202  GLY E 203  THR E 213  ASN E 214                    
SITE     7 AC5 37 ASP E 221  LEU E 252  HIS E 354  TYR E 355                    
SITE     8 AC5 37 GLY E 387  GLU E 388  ARG E 399  GLY E 402                    
SITE     9 AC5 37 ASN E 403  SER E 404  LEU E 405  LEU E 408                    
SITE    10 AC5 37 TEO E1590                                                     
SITE     1 AC6  9 SER F  54  CYS F  55  ARG F  56  GLY F  58                    
SITE     2 AC6  9 VAL F  59  CYS F  60  GLY F  61  ASP F  63                    
SITE     3 AC6  9 CYS F  75                                                     
SITE     1 AC7  7 CYS F 149  ILE F 150  CYS F 152  ALA F 153                    
SITE     2 AC7  7 CYS F 155  CYS F 216  PRO F 217                               
SITE     1 AC8  9 CYS F 159  CYS F 206  HIS F 207  SER F 208                    
SITE     2 AC8  9 ILE F 209  MET F 210  ASN F 211  CYS F 212                    
SITE     3 AC8  9 THR F 223                                                     
SITE     1 AC9 37 ILE I  13  GLY I  14  ALA I  15  GLY I  16                    
SITE     2 AC9 37 GLY I  17  ALA I  18  SER I  37  LYS I  38                    
SITE     3 AC9 37 VAL I  39  SER I  44  HIS I  45  THR I  46                    
SITE     4 AC9 37 SER I  48  ALA I  49  GLN I  50  GLY I  51                    
SITE     5 AC9 37 GLY I  52  TRP I 164  TYR I 165  ALA I 166                    
SITE     6 AC9 37 ALA I 201  THR I 202  GLY I 203  THR I 213                    
SITE     7 AC9 37 ASP I 221  LEU I 252  HIS I 354  TYR I 355                    
SITE     8 AC9 37 GLY I 387  GLU I 388  ARG I 399  GLY I 402                    
SITE     9 AC9 37 ASN I 403  SER I 404  LEU I 405  LEU I 408                    
SITE    10 AC9 37 TEO I1590                                                     
SITE     1 BC1  9 SER J  54  CYS J  55  ARG J  56  GLY J  58                    
SITE     2 BC1  9 VAL J  59  CYS J  60  GLY J  61  ASP J  63                    
SITE     3 BC1  9 CYS J  75                                                     
SITE     1 BC2  9 CYS J 149  ILE J 150  CYS J 152  ALA J 153                    
SITE     2 BC2  9 CYS J 154  CYS J 155  CYS J 216  PRO J 217                    
SITE     3 BC2  9 LEU J 220                                                     
SITE     1 BC3  8 CYS J 159  CYS J 206  HIS J 207  SER J 208                    
SITE     2 BC3  8 ILE J 209  MET J 210  CYS J 212  THR J 223                    
SITE     1 BC4  5 MET A 356  MET A 357  GLY A 358  GLU A 388                    
SITE     2 BC4  5 ALA A 390                                                     
SITE     1 BC5  5 MET E 356  MET E 357  GLY E 358  GLU E 388                    
SITE     2 BC5  5 ALA E 390                                                     
SITE     1 BC6  6 TYR I 355  MET I 356  MET I 357  GLY I 358                    
SITE     2 BC6  6 GLU I 388  ALA I 390                                          
SITE     1 BC7  9 SER B 161  TRP B 164  HIS B 207  PHE C  20                    
SITE     2 BC7  9 SER C  27  ILE C  28  ARG C  31  HEM C1130                    
SITE     3 BC7  9 ASP D  82                                                     
SITE     1 BC8 10 PRO F 160  SER F 161  TRP F 164  HIS F 207                    
SITE     2 BC8 10 PHE G  20  SER G  27  ILE G  28  ARG G  31                    
SITE     3 BC8 10 HEM G1130  ASP H  82                                          
SITE     1 BC9 10 PRO J 160  SER J 161  TRP J 164  HIS J 207                    
SITE     2 BC9 10 ILE J 209  SER K  27  ILE K  28  ARG K  31                    
SITE     3 BC9 10 HEM K1130  ASP L  82                                          
SITE     1 CC1 17 HIS B 207  HIS C  30  ARG C  31  GLY C  34                    
SITE     2 CC1 17 THR C  37  PHE C  38  HIS C  84  VAL C  85                    
SITE     3 CC1 17 GLY C  88  HIS C  91  CBE C1129  ALA D  23                    
SITE     4 CC1 17 THR D  27  HIS D  71  ALA D  72  GLY D  75                    
SITE     5 CC1 17 GLN D  78                                                     
SITE     1 CC2 11 GLN A  50  GLY A  51  HIS A 242  THR A 254                    
SITE     2 CC2 11 GLU A 255  ARG A 286  HIS A 354  ARG A 399                    
SITE     3 CC2 11 GLY A 401  GLY A 402  FAD A 601                               
SITE     1 CC3 18 HIS F 207  HIS G  30  ARG G  31  THR G  37                    
SITE     2 CC3 18 PHE G  38  HIS G  84  VAL G  85  GLY G  88                    
SITE     3 CC3 18 HIS G  91  CBE G1129  ARG H  20  ALA H  23                    
SITE     4 CC3 18 LEU H  26  THR H  27  HIS H  71  GLY H  75                    
SITE     5 CC3 18 GLN H  78  VAL H  79                                          
SITE     1 CC4 11 GLN E  50  GLY E  51  HIS E 242  THR E 254                    
SITE     2 CC4 11 GLU E 255  ARG E 286  HIS E 354  ARG E 399                    
SITE     3 CC4 11 GLY E 401  GLY E 402  FAD E 601                               
SITE     1 CC5 16 HIS J 207  HIS K  30  ARG K  31  GLY K  34                    
SITE     2 CC5 16 HIS K  84  GLY K  88  ILE K  89  HIS K  91                    
SITE     3 CC5 16 CBE K1129  ARG L  20  ALA L  23  THR L  27                    
SITE     4 CC5 16 HIS L  71  GLY L  75  MET L  76  VAL L  79                    
SITE     1 CC6 12 GLN I  50  GLY I  51  HIS I 242  LEU I 252                    
SITE     2 CC6 12 THR I 254  GLU I 255  ARG I 286  HIS I 354                    
SITE     3 CC6 12 ARG I 399  GLY I 401  GLY I 402  FAD I 601                    
CRYST1  119.850  184.710  203.310  90.00  90.00  90.00 P 21 21 21   12          
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      0.008344  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005414  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004919        0.00000                         
MTRIX1   1  0.944920  0.286190  0.158790       18.50396    1                    
MTRIX2   1  0.280930 -0.460290 -0.842150      -97.15851    1                    
MTRIX3   1 -0.167930  0.840380 -0.515330      -30.96337    1                    
MTRIX1   2  0.947030  0.281600 -0.154360        4.53321    1                    
MTRIX2   2  0.271360 -0.444710  0.853580      -22.49522    1                    
MTRIX3   2  0.171720 -0.850260 -0.497570     -101.68967    1                    
MTRIX1   3  0.948050  0.280950  0.149250       18.16462    1                    
MTRIX2   3  0.269630 -0.460630 -0.845650      -97.08932    1                    
MTRIX3   3 -0.168830  0.841960 -0.512450      -30.90920    1                    
MTRIX1   4  0.944650  0.281700 -0.168170        4.26520    1                    
MTRIX2   4  0.284180 -0.446440  0.848490      -23.09317    1                    
MTRIX3   4  0.163940 -0.849320 -0.501780     -101.58215    1                    
MTRIX1   5  0.947330  0.284720  0.146660       18.24940    1                    
MTRIX2   5  0.268410 -0.455980 -0.848550      -97.04973    1                    
MTRIX3   5 -0.174720  0.843220 -0.508380      -30.63527    1                    
MTRIX1   6  0.942310  0.283180 -0.178510        4.07432    1                    
MTRIX2   6  0.294860 -0.449710  0.843100      -23.69032    1                    
MTRIX3   6  0.158470 -0.847100 -0.507260     -101.56531    1                    
MTRIX1   7  0.946190  0.286880  0.149750       18.46492    1                    
MTRIX2   7  0.271140 -0.450210 -0.850760      -97.26530    1                    
MTRIX3   7 -0.176650  0.845580 -0.503770      -30.37287    1                    
MTRIX1   8  0.944100  0.276930 -0.178820        3.82943    1                    
MTRIX2   8  0.290680 -0.443530  0.847810      -23.20065    1                    
MTRIX3   8  0.155480 -0.852400 -0.499240     -101.13769    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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