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Database: PDB
Entry: 2WP9
LinkDB: 2WP9
Original site: 2WP9 
HEADER    OXIDOREDUCTASE                          03-AUG-09   2WP9              
TITLE     CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE     
TITLE    2 (SQR) SDHB HIS207THR MUTANT                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT;              
COMPND   3 CHAIN: A, E, I;                                                      
COMPND   4 EC: 1.3.5.1, 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: 1.3.5.1, 1.3.99.1;                                               
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES;                                                       
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT;           
COMPND  16 CHAIN: C, G, K;                                                      
COMPND  17 SYNONYM: SUCCINATE DEHYDROGENASE CYTOCHROME B-556 SUBUNIT, CYTOCHROME
COMPND  18 B-556;                                                               
COMPND  19 EC: 1.3.5.1;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 OTHER_DETAILS: RESIDUES 8-129 MODELLED;                              
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR        
COMPND  24 SUBUNIT;                                                             
COMPND  25 CHAIN: D, H, L;                                                      
COMPND  26 SYNONYM: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN;
COMPND  27 EC: 1.3.5.1;                                                         
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 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    CELL INNER MEMBRANE, TRICARBOXYLIC ACID CYCLE, METAL-BINDING,         
KEYWDS   2 TRANSMEMBRANE, FLAVOPROTEIN, OXIDOREDUCTASE, ELECTRON TRANSPORT      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.RUPRECHT,V.YANKOVSKAYA,E.MAKLASHINA,S.IWATA,G.CECCHINI              
REVDAT   4   30-JAN-19 2WP9    1       JRNL   ATOM                              
REVDAT   3   13-APR-11 2WP9    1       JRNL                                     
REVDAT   2   23-FEB-11 2WP9    1       JRNL                                     
REVDAT   1   25-AUG-10 2WP9    0                                                
JRNL        AUTH   J.RUPRECHT,S.IWATA,R.A.ROTHERY,J.H.WEINER,E.MAKLASHINA,      
JRNL        AUTH 2 G.CECCHINI                                                   
JRNL        TITL   PERTURBATION OF THE QUINONE-BINDING SITE OF COMPLEX II       
JRNL        TITL 2 ALTERS THE ELECTRONIC PROPERTIES OF THE PROXIMAL [3FE-4S]    
JRNL        TITL 3 IRON-SULFUR CLUSTER.                                         
JRNL        REF    J. BIOL. CHEM.                V. 286 12756 2011              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   21310949                                                     
JRNL        DOI    10.1074/JBC.M110.209874                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0067                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 116577                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : SELECTED TO BE IDENTICAL TO     
REMARK   3                                      2WDQ                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6188                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8281                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 419                          
REMARK   3   BIN FREE R VALUE                    : 0.3260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 24507                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 423                                     
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.12000                                              
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : -0.07000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.284         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.211         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.943        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 25533 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 34629 ; 1.357 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3147 ; 5.364 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1107 ;33.177 ;23.388       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4203 ;15.133 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   192 ;19.306 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3837 ; 0.094 ; 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): 15645 ; 0.335 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 25140 ; 0.680 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9888 ; 1.423 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9438 ; 2.143 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 ;  0.06 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    E    (A):   4522 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    I    (A):   4522 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   4522 ;  0.11 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):   4522 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      1    I (A**2):   4522 ;  0.09 ;  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):   1865 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    F    (A):   1865 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    J    (A):   1865 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1865 ;  0.12 ;  0.50           
REMARK   3   TIGHT THERMAL      2    F (A**2):   1865 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      2    J (A**2):   1865 ;  0.10 ;  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     129      1                      
REMARK   3           1     G      8       G     129      1                      
REMARK   3           1     K      8       K     129      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):    947 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    G    (A):    947 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    K    (A):    947 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      3    C (A**2):    947 ;  0.09 ;  0.50           
REMARK   3   TIGHT THERMAL      3    G (A**2):    947 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      3    K (A**2):    947 ;  0.07 ;  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 ;  0.03 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    L    (A):    835 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      4    D (A**2):    835 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      4    H (A**2):    835 ;  0.07 ;  0.50           
REMARK   3   TIGHT THERMAL      4    L (A**2):    835 ;  0.07 ;  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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   588                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6530 -11.1600 -24.2240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4046 T22:  -0.1600                                     
REMARK   3      T33:  -0.1293 T12:   0.0248                                     
REMARK   3      T13:   0.0608 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0346 L22:   1.4604                                     
REMARK   3      L33:   1.5701 L12:  -0.1310                                     
REMARK   3      L13:   0.0744 L23:  -0.2125                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0076 S12:  -0.0965 S13:   0.0057                       
REMARK   3      S21:   0.1917 S22:  -0.0306 S23:   0.2465                       
REMARK   3      S31:  -0.0580 S32:  -0.2144 S33:   0.0383                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0370  -8.5870 -30.5910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4198 T22:  -0.1547                                     
REMARK   3      T33:  -0.1583 T12:  -0.0028                                     
REMARK   3      T13:  -0.0450 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6747 L22:   1.9822                                     
REMARK   3      L33:   1.3931 L12:  -0.1799                                     
REMARK   3      L13:  -0.1973 L23:  -0.5426                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0317 S12:   0.0685 S13:   0.1588                       
REMARK   3      S21:   0.1806 S22:  -0.0213 S23:  -0.2070                       
REMARK   3      S31:  -0.1182 S32:   0.1903 S33:   0.0530                       
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   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.1910  -4.9320 -31.6350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2810 T22:   0.0789                                     
REMARK   3      T33:   0.3356 T12:  -0.0662                                     
REMARK   3      T13:  -0.0365 T23:   0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1562 L22:   1.0481                                     
REMARK   3      L33:   1.3117 L12:  -0.4326                                     
REMARK   3      L13:   0.9239 L23:   0.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0354 S12:  -0.0688 S13:   0.5547                       
REMARK   3      S21:   0.1164 S22:  -0.0400 S23:  -0.6531                       
REMARK   3      S31:  -0.1363 S32:   0.3918 S33:   0.0046                       
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):  67.1840 -17.6350 -37.9740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3770 T22:   0.1753                                     
REMARK   3      T33:   0.2944 T12:  -0.0198                                     
REMARK   3      T13:   0.0113 T23:  -0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9829 L22:   1.4469                                     
REMARK   3      L33:   3.6007 L12:  -0.7490                                     
REMARK   3      L13:   1.3773 L23:  -0.3471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0821 S12:   0.4285 S13:   0.0255                       
REMARK   3      S21:  -0.0461 S22:   0.0766 S23:  -0.5734                       
REMARK   3      S31:  -0.1844 S32:   0.8326 S33:   0.0056                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   588                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5910 -72.4400 -26.7740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0811 T22:  -0.1592                                     
REMARK   3      T33:  -0.1093 T12:  -0.0572                                     
REMARK   3      T13:  -0.0523 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4615 L22:   1.7127                                     
REMARK   3      L33:   1.5114 L12:   0.3940                                     
REMARK   3      L13:   0.3832 L23:   0.5472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1946 S12:  -0.0835 S13:  -0.1577                       
REMARK   3      S21:   0.4550 S22:  -0.1083 S23:   0.1368                       
REMARK   3      S31:   0.3221 S32:  -0.1095 S33:  -0.0863                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5690 -61.2900 -26.3560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1615 T22:  -0.1078                                     
REMARK   3      T33:  -0.0767 T12:   0.0559                                     
REMARK   3      T13:  -0.1894 T23:  -0.0512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9109 L22:   1.3930                                     
REMARK   3      L33:   1.6627 L12:   0.5420                                     
REMARK   3      L13:   0.1589 L23:   0.0915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1449 S12:   0.0189 S13:  -0.0910                       
REMARK   3      S21:   0.3292 S22:   0.0185 S23:  -0.3149                       
REMARK   3      S31:   0.3146 S32:   0.1975 S33:  -0.1634                       
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   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.1750 -53.9950 -28.6600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1570 T22:   0.2105                                     
REMARK   3      T33:   0.5409 T12:   0.1693                                     
REMARK   3      T13:  -0.2923 T23:  -0.0577                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0477 L22:   1.8495                                     
REMARK   3      L33:   1.6068 L12:   0.7233                                     
REMARK   3      L13:  -0.9936 L23:  -0.4638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2225 S12:  -0.0103 S13:  -0.4709                       
REMARK   3      S21:   0.1944 S22:  -0.1859 S23:  -0.9921                       
REMARK   3      S31:   0.3113 S32:   0.5732 S33:  -0.0366                       
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):  71.4910 -41.2390 -37.1540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3023 T22:   0.2971                                     
REMARK   3      T33:   0.4363 T12:   0.0948                                     
REMARK   3      T13:  -0.1336 T23:  -0.0531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1442 L22:   2.2178                                     
REMARK   3      L33:   4.2933 L12:   0.5042                                     
REMARK   3      L13:  -0.8443 L23:   0.8446                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0647 S12:   0.1667 S13:   0.0168                       
REMARK   3      S21:   0.0928 S22:   0.1997 S23:  -0.9513                       
REMARK   3      S31:   0.0415 S32:   0.8766 S33:  -0.2645                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     1        I   588                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0330 -39.9820 -79.9620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0187 T22:   0.1929                                     
REMARK   3      T33:  -0.1594 T12:   0.0453                                     
REMARK   3      T13:  -0.1412 T23:  -0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9817 L22:   2.0436                                     
REMARK   3      L33:   1.4970 L12:  -0.1110                                     
REMARK   3      L13:   0.3743 L23:   0.1911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0399 S12:   0.3654 S13:  -0.0230                       
REMARK   3      S21:  -0.5864 S22:   0.0278 S23:   0.2649                       
REMARK   3      S31:   0.0536 S32:  -0.2114 S33:  -0.0677                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     1        J   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.7950 -39.1450 -74.7230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0908 T22:   0.1275                                     
REMARK   3      T33:  -0.1986 T12:   0.0931                                     
REMARK   3      T13:   0.1007 T23:  -0.0330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2029 L22:   1.9169                                     
REMARK   3      L33:   1.3567 L12:   0.0115                                     
REMARK   3      L13:   0.1587 L23:   0.3801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0637 S12:   0.3167 S13:  -0.0297                       
REMARK   3      S21:  -0.5145 S22:   0.0574 S23:  -0.2889                       
REMARK   3      S31:   0.0534 S32:   0.2848 S33:  -0.1210                       
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   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.4990 -32.3810 -72.9490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0449 T22:   0.7567                                     
REMARK   3      T33:   0.2001 T12:   0.0856                                     
REMARK   3      T13:   0.3317 T23:  -0.0299                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7601 L22:   2.0588                                     
REMARK   3      L33:   1.4247 L12:   1.2145                                     
REMARK   3      L13:   0.8432 L23:   0.3848                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0403 S12:   0.6508 S13:  -0.0498                       
REMARK   3      S21:  -0.4218 S22:   0.1672 S23:  -0.5163                       
REMARK   3      S31:  -0.1092 S32:   0.7381 S33:  -0.1269                       
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):  69.1010 -30.1340 -58.1620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2548 T22:   0.6216                                     
REMARK   3      T33:   0.2467 T12:   0.0020                                     
REMARK   3      T13:   0.1941 T23:  -0.1227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7876 L22:   3.7472                                     
REMARK   3      L33:   2.4163 L12:   0.2797                                     
REMARK   3      L13:   0.2536 L23:  -0.1177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1120 S12:   0.2602 S13:  -0.0534                       
REMARK   3      S21:  -0.2481 S22:  -0.0082 S23:  -0.9457                       
REMARK   3      S31:  -0.2160 S32:   0.7311 S33:  -0.1038                       
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   : 1.20                                          
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      
REMARK   3  IN 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          
REMARK   3  RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD    
REMARK   3  CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.                         
REMARK   4                                                                      
REMARK   4 2WP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290040636.                                   
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 CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122882                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.630                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2WDQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: PHASES INITIALLY DETERMINED BY RIGID-BODY REFINEMENT OF      
REMARK 200  2WDQ AGAINST THE DATA                                               
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 0.1M LI2SO4, 0.1M      
REMARK 280  NACL, 0.009% DDM, 3% 1,6-HEXANEDIOL AND 10% (W/V) PEG4000           
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       59.92650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.38850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.90150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.38850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.92650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.90150            
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: 15530 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.3 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 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: 15560 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.9 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: 15520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.1 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, HIS 207 TO THR                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, HIS 207 TO THR                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN J, HIS 207 TO THR                        
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     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     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     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: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 491   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  50      -64.60   -109.20                                   
REMARK 500    ALA A 138     -129.00     41.08                                   
REMARK 500    ALA A 201       53.26   -145.46                                   
REMARK 500    ALA A 205       36.15   -155.48                                   
REMARK 500    LYS A 281     -123.17     48.55                                   
REMARK 500    LEU A 327       35.42   -141.46                                   
REMARK 500    HIS A 354      -49.72   -131.13                                   
REMARK 500    ASN A 398      116.85   -170.17                                   
REMARK 500    SER A 472     -155.60    -81.14                                   
REMARK 500    SER B  54      -74.50   -159.08                                   
REMARK 500    GLU B  57       17.74   -141.21                                   
REMARK 500    ASP B  63       49.86   -107.10                                   
REMARK 500    PRO B  85      124.98    -37.57                                   
REMARK 500    ASP B 102     -114.03     43.65                                   
REMARK 500    LYS B 118       71.08     57.00                                   
REMARK 500    ARG B 131     -112.92   -138.58                                   
REMARK 500    LEU C  13       33.37   -145.21                                   
REMARK 500    SER D  40      -19.83   -155.02                                   
REMARK 500    GLU D  42      108.90    -28.87                                   
REMARK 500    GLN E  50      -67.70   -106.81                                   
REMARK 500    ALA E 138     -129.65     45.58                                   
REMARK 500    ALA E 201       52.20   -145.22                                   
REMARK 500    ALA E 205       31.97   -155.57                                   
REMARK 500    ALA E 249      -30.61   -138.89                                   
REMARK 500    ALA E 277       80.48   -150.50                                   
REMARK 500    ASN E 279      -74.75    -73.72                                   
REMARK 500    LYS E 281     -118.88     46.97                                   
REMARK 500    LEU E 327       36.43   -140.97                                   
REMARK 500    ASN E 398      118.49   -174.53                                   
REMARK 500    SER E 472     -157.07    -83.74                                   
REMARK 500    SER F  54      -71.45   -152.65                                   
REMARK 500    GLU F  57       18.07   -141.56                                   
REMARK 500    ASP F  63       50.92   -106.78                                   
REMARK 500    PRO F  85      129.17    -35.75                                   
REMARK 500    ASP F 102     -113.10     40.87                                   
REMARK 500    LYS F 118       70.43     58.03                                   
REMARK 500    ARG F 131     -113.39   -143.69                                   
REMARK 500    LEU G  13       34.05   -146.04                                   
REMARK 500    SER H  40      -20.02   -156.59                                   
REMARK 500    GLU H  42      111.48    -26.99                                   
REMARK 500    GLN I  50      -61.22   -109.69                                   
REMARK 500    ALA I 138     -126.13     42.59                                   
REMARK 500    LEU I 167      -61.48    -92.52                                   
REMARK 500    ALA I 201       51.09   -142.34                                   
REMARK 500    ALA I 205       32.90   -153.15                                   
REMARK 500    THR I 244       71.64   -119.62                                   
REMARK 500    ALA I 249      -33.45   -139.96                                   
REMARK 500    ALA I 277       77.08   -150.66                                   
REMARK 500    ASN I 279      -72.28    -79.03                                   
REMARK 500    LYS I 281     -123.16     50.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      65 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 A1590  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 390   O                                                      
REMARK 620 2 GLY A 358   O    97.2                                              
REMARK 620 3 MET A 356   O   171.2  74.1                                        
REMARK 620 4 MET A 357   O   101.5  69.6  75.1                                  
REMARK 620 5 GLU A 388   O    88.7  89.6  91.9 157.6                            
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  55   SG                                                     
REMARK 620 2 FES B 302   S1  106.5                                              
REMARK 620 3 FES B 302   S2  120.7  90.6                                        
REMARK 620 4 CYS B  60   SG  104.4 115.6 118.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  63   OD1                                                    
REMARK 620 2 FES B 302   S1  106.2                                              
REMARK 620 3 FES B 302   S2   93.9  92.3                                        
REMARK 620 4 CYS B  75   SG  131.6 107.8 117.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 149   SG                                                     
REMARK 620 2 SF4 B 303   S2  110.8                                              
REMARK 620 3 SF4 B 303   S3  129.2 103.0                                        
REMARK 620 4 SF4 B 303   S4   99.4 104.2 107.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 152   SG                                                     
REMARK 620 2 SF4 B 303   S1   99.0                                              
REMARK 620 3 SF4 B 303   S3  120.8 102.4                                        
REMARK 620 4 SF4 B 303   S4  120.8 102.2 107.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 155   SG                                                     
REMARK 620 2 SF4 B 303   S1  109.8                                              
REMARK 620 3 SF4 B 303   S2  125.4 106.4                                        
REMARK 620 4 SF4 B 303   S4  107.0 103.1 102.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 159   SG                                                     
REMARK 620 2 F3S B 304   S1  105.7                                              
REMARK 620 3 F3S B 304   S2  119.9 120.6                                        
REMARK 620 4 F3S B 304   S3  112.2  93.6 101.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 206   SG                                                     
REMARK 620 2 F3S B 304   S1  121.5                                              
REMARK 620 3 F3S B 304   S3  115.3  93.4                                        
REMARK 620 4 F3S B 304   S4  106.8 117.1 100.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 212   SG                                                     
REMARK 620 2 F3S B 304   S2   89.2                                              
REMARK 620 3 F3S B 304   S3  106.7 108.9                                        
REMARK 620 4 F3S B 304   S4   92.9 139.4 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 216   SG                                                     
REMARK 620 2 SF4 B 303   S1  113.0                                              
REMARK 620 3 SF4 B 303   S2  117.2 107.9                                        
REMARK 620 4 SF4 B 303   S3  110.5 104.0 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C1129  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  84   NE2                                                    
REMARK 620 2 HEM C1129   NA   88.3                                              
REMARK 620 3 HEM C1129   NB   90.6  87.6                                        
REMARK 620 4 HEM C1129   NC   91.3 175.8  88.2                                  
REMARK 620 5 HEM C1129   ND   85.2  87.9 174.0  96.2                            
REMARK 620 6 HIS D  71   NE2 171.7  87.4  82.1  92.5 101.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E1590  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET E 356   O                                                      
REMARK 620 2 MET E 357   O    82.3                                              
REMARK 620 3 GLY E 358   O    82.2  73.7                                        
REMARK 620 4 GLU E 388   O    90.0 163.9  91.3                                  
REMARK 620 5 ALA E 390   O   174.3 101.8  95.0  85.1                            
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   S1  102.6                                              
REMARK 620 3 FES F 302   S2  112.0  94.3                                        
REMARK 620 4 CYS F  60   SG  108.0 114.6 123.1                                  
REMARK 620 N                    1     2     3                                   
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 ASP F  63   OD1                                                    
REMARK 620 2 FES F 302   S1  111.2                                              
REMARK 620 3 FES F 302   S2   96.4  96.0                                        
REMARK 620 4 CYS F  75   SG  122.3 112.1 115.0                                  
REMARK 620 N                    1     2     3                                   
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 CYS F 149   SG                                                     
REMARK 620 2 SF4 F 303   S1  114.9                                              
REMARK 620 3 SF4 F 303   S2  123.8 106.0                                        
REMARK 620 4 SF4 F 303   S4  102.5 100.8 106.0                                  
REMARK 620 N                    1     2     3                                   
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 CYS F 152   SG                                                     
REMARK 620 2 SF4 F 303   S1  120.9                                              
REMARK 620 3 SF4 F 303   S3  103.1 106.5                                        
REMARK 620 4 SF4 F 303   S4  116.9 101.7 106.7                                  
REMARK 620 N                    1     2     3                                   
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 CYS F 155   SG                                                     
REMARK 620 2 SF4 F 303   S2  111.7                                              
REMARK 620 3 SF4 F 303   S3  117.6 108.1                                        
REMARK 620 4 SF4 F 303   S4  106.9 105.6 106.1                                  
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 CYS F 159   SG                                                     
REMARK 620 2 F3S F 304   S1  114.2                                              
REMARK 620 3 F3S F 304   S2  104.1 133.4                                        
REMARK 620 4 F3S F 304   S3  111.2  94.6  95.4                                  
REMARK 620 N                    1     2     3                                   
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 CYS F 206   SG                                                     
REMARK 620 2 F3S F 304   S1  111.6                                              
REMARK 620 3 F3S F 304   S3  116.4  96.4                                        
REMARK 620 4 F3S F 304   S4  108.4 124.9  98.2                                  
REMARK 620 N                    1     2     3                                   
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   S2   88.6                                              
REMARK 620 3 F3S F 304   S3  103.7 101.3                                        
REMARK 620 4 F3S F 304   S4   93.7 154.1 103.2                                  
REMARK 620 N                    1     2     3                                   
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 CYS F 216   SG                                                     
REMARK 620 2 SF4 F 303   S1  112.8                                              
REMARK 620 3 SF4 F 303   S2  119.2 102.9                                        
REMARK 620 4 SF4 F 303   S3  105.9 106.3 109.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G1129  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  84   NE2                                                    
REMARK 620 2 HEM G1129   NA   83.2                                              
REMARK 620 3 HEM G1129   NB   92.0  88.3                                        
REMARK 620 4 HEM G1129   NC   93.9 175.8  88.8                                  
REMARK 620 5 HEM G1129   ND   80.9  90.4 172.9  92.1                            
REMARK 620 6 HIS H  71   NE2 176.3  96.5  84.3  86.2 102.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA I1590  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA I 390   O                                                      
REMARK 620 2 GLU I 388   O    82.5                                              
REMARK 620 3 GLY I 358   O    84.4  84.2                                        
REMARK 620 4 MET I 357   O    98.9 148.0  64.3                                  
REMARK 620 5 MET I 356   O   155.1  89.7  71.3  75.6                            
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  55   SG                                                     
REMARK 620 2 FES J 302   S1  100.9                                              
REMARK 620 3 FES J 302   S2  120.8  94.3                                        
REMARK 620 4 CYS J  60   SG  111.7 118.0 110.2                                  
REMARK 620 N                    1     2     3                                   
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 ASP J  63   OD1                                                    
REMARK 620 2 FES J 302   S1  121.3                                              
REMARK 620 3 FES J 302   S2   89.2  95.5                                        
REMARK 620 4 CYS J  75   SG  127.9 100.4 118.3                                  
REMARK 620 N                    1     2     3                                   
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 CYS J 149   SG                                                     
REMARK 620 2 SF4 J 303   S1  118.3                                              
REMARK 620 3 SF4 J 303   S2   95.2 101.6                                        
REMARK 620 4 SF4 J 303   S4  125.1 104.2 109.1                                  
REMARK 620 N                    1     2     3                                   
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   S1  123.4                                              
REMARK 620 3 SF4 J 303   S2  113.9 102.6                                        
REMARK 620 4 SF4 J 303   S3  103.9 105.0 106.9                                  
REMARK 620 N                    1     2     3                                   
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 CYS J 155   SG                                                     
REMARK 620 2 SF4 J 303   S2  114.9                                              
REMARK 620 3 SF4 J 303   S3  110.3 104.7                                        
REMARK 620 4 SF4 J 303   S4  111.8 108.4 106.2                                  
REMARK 620 N                    1     2     3                                   
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 CYS J 159   SG                                                     
REMARK 620 2 F3S J 304   S1  109.7                                              
REMARK 620 3 F3S J 304   S2  111.3 121.9                                        
REMARK 620 4 F3S J 304   S3  124.8  96.7  92.0                                  
REMARK 620 N                    1     2     3                                   
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 CYS J 206   SG                                                     
REMARK 620 2 F3S J 304   S2  113.6                                              
REMARK 620 3 F3S J 304   S3  110.5  90.9                                        
REMARK 620 4 F3S J 304   S4  108.7 127.9 101.6                                  
REMARK 620 N                    1     2     3                                   
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 CYS J 212   SG                                                     
REMARK 620 2 F3S J 304   S1   86.0                                              
REMARK 620 3 F3S J 304   S3   92.4  98.1                                        
REMARK 620 4 F3S J 304   S4   99.3 157.2 103.8                                  
REMARK 620 N                    1     2     3                                   
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 CYS J 216   SG                                                     
REMARK 620 2 SF4 J 303   S1  111.8                                              
REMARK 620 3 SF4 J 303   S3  115.8 106.2                                        
REMARK 620 4 SF4 J 303   S4  112.6 103.8 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K1129  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  84   NE2                                                    
REMARK 620 2 HEM K1129   NA   84.6                                              
REMARK 620 3 HEM K1129   NB   93.0  89.1                                        
REMARK 620 4 HEM K1129   NC   90.7 175.1  89.6                                  
REMARK 620 5 HEM K1129   ND   80.9  87.9 173.4  92.9                            
REMARK 620 6 HIS L  71   NE2 178.7  96.7  87.0  88.0  99.2                      
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 TEO A 1589                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE C 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO E 1589                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 1590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES F 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S F 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE G 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO I 1589                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA I 1590                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES J 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 J 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S J 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE K 1130                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WDQ   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH 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: 1NEN   RELATED DB: PDB                                   
REMARK 900 MOLECULAR ARCHITECTURE OF SUCCINATE DEHYDROGENASE (COMPLEXII)        
REMARK 900 PREVENTS REACTIVE OXYGEN SPECIES GENERATION                          
REMARK 900 RELATED ID: 1NEK   RELATED DB: PDB                                   
REMARK 900 SUCCINATE DEHYDOGENASE FROM E.COLI                                   
REMARK 900 RELATED ID: 2WU2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE   
REMARK 900 (SQR) SDHC HIS84MET MUTANT                                           
REMARK 900 RELATED ID: 2ACZ   RELATED DB: PDB                                   
REMARK 900 COMPLEX II (SUCCINATE DEHYDROGENASE) FROM E. COLI WITHATPENIN A5     
REMARK 900 INHIBITOR CO-CRYSTALLIZED AT THE UBIQUINONEBINDING SITE              
REMARK 900 RELATED ID: 2WU5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE   
REMARK 900 (SQR) SDHD HIS71MET MUTANT                                           
REMARK 900 RELATED ID: 2WDV   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH AN EMPTY        
REMARK 900 QUINONE-BINDING POCKET                                               
DBREF  2WP9 A    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WP9 B    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WP9 C    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WP9 D    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WP9 E    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WP9 F    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WP9 G    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WP9 H    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WP9 I    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WP9 J    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WP9 K    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WP9 L    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
SEQADV 2WP9 THR B  207  UNP  P07014    HIS   207 ENGINEERED MUTATION            
SEQADV 2WP9 THR F  207  UNP  P07014    HIS   207 ENGINEERED MUTATION            
SEQADV 2WP9 THR J  207  UNP  P07014    HIS   207 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 THR 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 TYR 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 THR 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 TYR 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 THR 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 TYR 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    TEO  A1589       9                                                       
HET     NA  A1590       1                                                       
HET    FES  B 302       4                                                       
HET    SF4  B 303       8                                                       
HET    F3S  B 304       7                                                       
HET    HEM  C1129      43                                                       
HET    CBE  C1130      16                                                       
HET    FAD  E 601      53                                                       
HET    TEO  E1589       9                                                       
HET     NA  E1590       1                                                       
HET    FES  F 302       4                                                       
HET    SF4  F 303       8                                                       
HET    F3S  F 304       7                                                       
HET    HEM  G1129      43                                                       
HET    CBE  G1130      16                                                       
HET    FAD  I 601      53                                                       
HET    TEO  I1589       9                                                       
HET     NA  I1590       1                                                       
HET    FES  J 302       4                                                       
HET    SF4  J 303       8                                                       
HET    F3S  J 304       7                                                       
HET    HEM  K1129      43                                                       
HET    CBE  K1130      16                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     TEO MALATE LIKE INTERMEDIATE                                         
HETNAM      NA SODIUM ION                                                       
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CBE 2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-                   
HETNAM   2 CBE  CARBOXAMIDE                                                     
HETSYN     HEM HEME                                                             
HETSYN     CBE 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-CARBOXANILID;                
HETSYN   2 CBE  CARBOXIN; CBX                                                   
FORMUL  13  FAD    3(C27 H33 N9 O15 P2)                                         
FORMUL  14  TEO    3(C4 H4 O5 2-)                                               
FORMUL  15   NA    3(NA 1+)                                                     
FORMUL  16  FES    3(FE2 S2)                                                    
FORMUL  17  SF4    3(FE4 S4)                                                    
FORMUL  18  F3S    3(FE3 S4)                                                    
FORMUL  19  HEM    3(C34 H32 FE N4 O4)                                          
FORMUL  20  CBE    3(C12 H13 N O2 S)                                            
FORMUL  37  HOH   *128(H2 O)                                                    
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  MET A  102  1                                  22    
HELIX    6   6 ARG A  140  HIS A  157  1                                  18    
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  GLY A  427  1                                  26    
HELIX   17  17 SER A  433  LEU A  441  1                                   9    
HELIX   18  18 LEU A  441  ASN A  450  1                                  10    
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 ILE B   79  LEU B   82  5                                   4    
HELIX   25  25 MET B  107  ILE B  117  1                                  11    
HELIX   26  26 MET B  136  LYS B  142  1                                   7    
HELIX   27  27 CYS B  155  SER B  158  5                                   4    
HELIX   28  28 CYS B  159  ASN B  165  1                                   7    
HELIX   29  29 GLY B  171  ILE B  183  1                                  13    
HELIX   30  30 GLU B  189  GLY B  196  1                                   8    
HELIX   31  31 MET B  210  CYS B  216  1                                   7    
HELIX   32  32 ASN B  221  ALA B  238  1                                  18    
HELIX   33  33 ASP C   14  ILE C   18  5                                   5    
HELIX   34  34 PRO C   21  SER C   54  1                                  34    
HELIX   35  35 SER C   54  SER C   67  1                                  14    
HELIX   36  36 SER C   67  PHE C   96  1                                  30    
HELIX   37  37 THR C  102  TRP C  129  1                                  28    
HELIX   38  38 ASN D   11  ALA D   38  1                                  28    
HELIX   39  39 THR D   44  SER D   54  1                                  11    
HELIX   40  40 SER D   54  VAL D   84  1                                  31    
HELIX   41  41 PRO D   86  TRP D  113  1                                  28    
HELIX   42  42 GLY E   16  SER E   29  1                                  14    
HELIX   43  43 PHE E   40  SER E   44  5                                   5    
HELIX   44  44 SER E   44  ALA E   49  5                                   6    
HELIX   45  45 ASN E   64  SER E   76  1                                  13    
HELIX   46  46 ASP E   81  MET E  102  1                                  22    
HELIX   47  47 ARG E  140  ASN E  156  1                                  17    
HELIX   48  48 ALA E  205  TYR E  209  5                                   5    
HELIX   49  49 GLY E  220  ALA E  229  1                                  10    
HELIX   50  50 GLU E  255  GLU E  260  1                                   6    
HELIX   51  51 PHE E  272  ALA E  277  1                                   6    
HELIX   52  52 ALA E  280  ALA E  284  5                                   5    
HELIX   53  53 GLY E  285  GLU E  299  1                                  15    
HELIX   54  54 LEU E  315  LEU E  318  5                                   4    
HELIX   55  55 GLY E  319  LEU E  327  1                                   9    
HELIX   56  56 LEU E  327  HIS E  339  1                                  13    
HELIX   57  57 GLY E  402  GLY E  427  1                                  26    
HELIX   58  58 SER E  433  SER E  440  1                                   8    
HELIX   59  59 LEU E  441  ASN E  450  1                                  10    
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 CYS F   75  THR F   77  5                                   3    
HELIX   65  65 ILE F   79  LEU F   82  5                                   4    
HELIX   66  66 MET F  107  ILE F  117  1                                  11    
HELIX   67  67 MET F  136  LYS F  142  1                                   7    
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 ASN F  211  CYS F  216  1                                   6    
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   53  1                                  33    
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  TRP G  129  1                                  28    
HELIX   79  79 ASN H   11  ALA H   38  1                                  28    
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  GLY I  427  1                                  26    
HELIX   99  99 SER I  433  SER I  440  1                                   8    
HELIX  100 100 LEU I  441  ASN I  450  1                                  10    
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 ILE J   79  LEU J   82  5                                   4    
HELIX  106 106 MET J  107  ILE J  117  1                                  11    
HELIX  107 107 MET J  136  LYS J  142  1                                   7    
HELIX  108 108 CYS J  155  SER J  158  5                                   4    
HELIX  109 109 CYS J  159  ASN J  165  1                                   7    
HELIX  110 110 GLY J  171  ILE J  183  1                                  13    
HELIX  111 111 GLU J  189  GLY J  196  1                                   8    
HELIX  112 112 MET J  210  CYS J  216  1                                   7    
HELIX  113 113 ASN J  221  ALA J  238  1                                  18    
HELIX  114 114 ASP K   14  ILE K   18  5                                   5    
HELIX  115 115 PRO K   21  SER K   53  1                                  33    
HELIX  116 116 SER K   54  SER K   67  1                                  14    
HELIX  117 117 SER K   67  PHE K   96  1                                  30    
HELIX  118 118 THR K  102  TRP K  129  1                                  28    
HELIX  119 119 ASN L   11  ALA L   38  1                                  28    
HELIX  120 120 THR L   44  SER L   54  1                                  11    
HELIX  121 121 SER L   54  VAL L   84  1                                  31    
HELIX  122 122 PRO L   86  TRP L  113  1                                  28    
SHEET    1  AA 6 THR A 159  SER A 162  0                                        
SHEET    2  AA 6 CYS A  33  SER A  37  1  O  CYS A  33   N  THR A 159           
SHEET    3  AA 6 VAL A   5  ILE A  13  1  O  ALA A  10   N  ALA A  34           
SHEET    4  AA 6 VAL A 190  LEU A 200  1  O  TYR A 192   N  ARG A   6           
SHEET    5  AA 6 ASP A 377  ALA A 385 -1  O  GLY A 382   N  THR A 198           
SHEET    6  AA 6 GLN A 367  VAL A 371  1  O  ALA A 368   N  VAL A 380           
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 VAL A   5  ILE A  13  1  O  ALA A  10   N  ALA A  34           
SHEET    4  AB 6 VAL A 190  LEU A 200  1  O  TYR A 192   N  ARG A   6           
SHEET    5  AB 6 VAL A 177  CYS A 184 -1  O  VAL A 178   N  ALA A 195           
SHEET    6  AB 6 TRP A 164  LYS A 171 -1  O  TYR A 165   N  LEU A 183           
SHEET    1  AC 3 ILE A  53  THR A  54  0                                        
SHEET    2  AC 3 THR A 134  ALA A 135 -1  O  ALA A 135   N  ILE A  53           
SHEET    3  AC 3 GLN A 116  ARG A 117 -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 6 THR E 159  SER E 162  0                                        
SHEET    2  EA 6 CYS E  33  SER E  37  1  O  CYS E  33   N  THR E 159           
SHEET    3  EA 6 VAL E   5  ILE E  13  1  O  ALA E  10   N  ALA E  34           
SHEET    4  EA 6 VAL E 190  LEU E 200  1  O  TYR E 192   N  ARG E   6           
SHEET    5  EA 6 ASP E 377  ALA E 385 -1  O  GLY E 382   N  THR E 198           
SHEET    6  EA 6 GLN E 367  VAL E 371  1  O  ALA E 368   N  VAL E 380           
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 VAL E   5  ILE E  13  1  O  ALA E  10   N  ALA E  34           
SHEET    4  EB 6 VAL E 190  LEU E 200  1  O  TYR E 192   N  ARG E   6           
SHEET    5  EB 6 VAL E 177  CYS E 184 -1  O  VAL E 178   N  ALA E 195           
SHEET    6  EB 6 TRP E 164  LYS E 171 -1  O  TYR E 165   N  LEU E 183           
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 THR I 134  ALA I 135 -1  O  ALA I 135   N  ILE I  53           
SHEET    3  IC 3 GLN I 116  ARG I 117 -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         NE2 HIS A  45                 C8M FAD A 601     1555   1555  1.50  
LINK        NA    NA A1590                 O   ALA A 390     1555   1555  2.33  
LINK        NA    NA A1590                 O   GLY A 358     1555   1555  2.49  
LINK        NA    NA A1590                 O   MET A 356     1555   1555  2.66  
LINK        NA    NA A1590                 O   MET A 357     1555   1555  3.08  
LINK        NA    NA A1590                 O   GLU A 388     1555   1555  2.52  
LINK         SG  CYS B  55                FE1  FES B 302     1555   1555  2.25  
LINK         SG  CYS B  60                FE1  FES B 302     1555   1555  2.23  
LINK         OD1 ASP B  63                FE2  FES B 302     1555   1555  1.83  
LINK         SG  CYS B  75                FE2  FES B 302     1555   1555  2.23  
LINK         SG  CYS B 149                FE1  SF4 B 303     1555   1555  2.29  
LINK         SG  CYS B 152                FE2  SF4 B 303     1555   1555  2.29  
LINK         SG  CYS B 155                FE3  SF4 B 303     1555   1555  2.29  
LINK         SG  CYS B 159                FE1  F3S B 304     1555   1555  2.31  
LINK         SG  CYS B 206                FE3  F3S B 304     1555   1555  2.25  
LINK         SG  CYS B 212                FE4  F3S B 304     1555   1555  2.27  
LINK         SG  CYS B 216                FE4  SF4 B 303     1555   1555  2.30  
LINK         NE2 HIS C  84                FE   HEM C1129     1555   1555  1.93  
LINK         NE2 HIS D  71                FE   HEM C1129     1555   1555  2.04  
LINK         NE2 HIS E  45                 C8M FAD E 601     1555   1555  1.51  
LINK        NA    NA E1590                 O   MET E 356     1555   1555  2.50  
LINK        NA    NA E1590                 O   MET E 357     1555   1555  2.73  
LINK        NA    NA E1590                 O   GLY E 358     1555   1555  2.29  
LINK        NA    NA E1590                 O   GLU E 388     1555   1555  2.60  
LINK        NA    NA E1590                 O   ALA E 390     1555   1555  2.53  
LINK         SG  CYS F  55                FE1  FES F 302     1555   1555  2.32  
LINK         SG  CYS F  60                FE1  FES F 302     1555   1555  2.32  
LINK         OD1 ASP F  63                FE2  FES F 302     1555   1555  1.83  
LINK         SG  CYS F  75                FE2  FES F 302     1555   1555  2.28  
LINK         SG  CYS F 149                FE3  SF4 F 303     1555   1555  2.33  
LINK         SG  CYS F 152                FE2  SF4 F 303     1555   1555  2.33  
LINK         SG  CYS F 155                FE1  SF4 F 303     1555   1555  2.29  
LINK         SG  CYS F 159                FE1  F3S F 304     1555   1555  2.29  
LINK         SG  CYS F 206                FE3  F3S F 304     1555   1555  2.27  
LINK         SG  CYS F 212                FE4  F3S F 304     1555   1555  2.33  
LINK         SG  CYS F 216                FE4  SF4 F 303     1555   1555  2.31  
LINK         NE2 HIS G  84                FE   HEM G1129     1555   1555  1.94  
LINK         NE2 HIS H  71                FE   HEM G1129     1555   1555  1.97  
LINK         NE2 HIS I  45                 C8M FAD I 601     1555   1555  1.49  
LINK        NA    NA I1590                 O   ALA I 390     1555   1555  2.46  
LINK        NA    NA I1590                 O   GLU I 388     1555   1555  2.54  
LINK        NA    NA I1590                 O   GLY I 358     1555   1555  2.69  
LINK        NA    NA I1590                 O   MET I 357     1555   1555  2.99  
LINK        NA    NA I1590                 O   MET I 356     1555   1555  2.57  
LINK         SG  CYS J  55                FE1  FES J 302     1555   1555  2.31  
LINK         SG  CYS J  60                FE1  FES J 302     1555   1555  2.29  
LINK         OD1 ASP J  63                FE2  FES J 302     1555   1555  1.81  
LINK         SG  CYS J  75                FE2  FES J 302     1555   1555  2.30  
LINK         SG  CYS J 149                FE3  SF4 J 303     1555   1555  2.35  
LINK         SG  CYS J 152                FE4  SF4 J 303     1555   1555  2.31  
LINK         SG  CYS J 155                FE1  SF4 J 303     1555   1555  2.31  
LINK         SG  CYS J 159                FE1  F3S J 304     1555   1555  2.31  
LINK         SG  CYS J 206                FE4  F3S J 304     1555   1555  2.28  
LINK         SG  CYS J 212                FE3  F3S J 304     1555   1555  2.32  
LINK         SG  CYS J 216                FE2  SF4 J 303     1555   1555  2.27  
LINK         NE2 HIS K  84                FE   HEM K1129     1555   1555  1.98  
LINK         NE2 HIS L  71                FE   HEM K1129     1555   1555  1.99  
CISPEP   1 VAL A  392    SER A  393          0        -2.76                     
CISPEP   2 VAL E  392    SER E  393          0        -1.14                     
CISPEP   3 VAL I  392    SER I  393          0        -1.13                     
SITE     1 AC1 40 GLY A  14  ALA A  15  GLY A  16  GLY A  17                    
SITE     2 AC1 40 ALA A  18  SER A  37  LYS A  38  VAL A  39                    
SITE     3 AC1 40 SER A  44  HIS A  45  THR A  46  SER A  48                    
SITE     4 AC1 40 ALA A  49  GLN A  50  GLY A  51  GLY A  52                    
SITE     5 AC1 40 TRP A 164  TYR A 165  ALA A 166  ALA A 201                    
SITE     6 AC1 40 THR A 202  GLY A 203  THR A 213  ASN A 214                    
SITE     7 AC1 40 ASP A 221  LEU A 252  HIS A 354  TYR A 355                    
SITE     8 AC1 40 GLY A 387  GLU A 388  ARG A 399  GLY A 402                    
SITE     9 AC1 40 ASN A 403  SER A 404  LEU A 405  LEU A 408                    
SITE    10 AC1 40 TEO A1589  HOH A2024  HOH A2052  HOH A2053                    
SITE     1 AC2 12 GLY A  51  PHE A 119  HIS A 242  LEU A 252                    
SITE     2 AC2 12 THR A 254  GLU A 255  ARG A 286  HIS A 354                    
SITE     3 AC2 12 ARG A 399  GLY A 401  GLY A 402  FAD A 601                    
SITE     1 AC3  5 MET A 356  MET A 357  GLY A 358  GLU A 388                    
SITE     2 AC3  5 ALA A 390                                                     
SITE     1 AC4  9 SER B  54  CYS B  55  ARG B  56  GLY B  58                    
SITE     2 AC4  9 VAL B  59  CYS B  60  GLY B  61  ASP B  63                    
SITE     3 AC4  9 CYS B  75                                                     
SITE     1 AC5  7 CYS B 149  ILE B 150  CYS B 152  ALA B 153                    
SITE     2 AC5  7 CYS B 155  CYS B 216  PRO B 217                               
SITE     1 AC6  8 CYS B 159  CYS B 206  THR B 207  SER B 208                    
SITE     2 AC6  8 MET B 210  ASN B 211  CYS B 212  THR B 223                    
SITE     1 AC7 20 THR B 207  HIS C  30  ARG C  31  GLY C  34                    
SITE     2 AC7 20 THR C  37  PHE C  38  HIS C  84  VAL C  85                    
SITE     3 AC7 20 GLY C  88  ILE C  89  HIS C  91  CBE C1130                    
SITE     4 AC7 20 ARG D  20  ALA D  23  LEU D  26  THR D  27                    
SITE     5 AC7 20 ILE D  68  HIS D  71  GLY D  75  GLN D  78                    
SITE     1 AC8  9 PRO B 160  SER B 161  TRP B 164  THR B 207                    
SITE     2 AC8  9 SER C  27  ARG C  31  HEM C1129  ASP D  82                    
SITE     3 AC8  9 TYR D  83                                                     
SITE     1 AC9 37 GLY E  14  ALA E  15  GLY E  16  GLY E  17                    
SITE     2 AC9 37 ALA E  18  SER E  37  LYS E  38  VAL E  39                    
SITE     3 AC9 37 SER E  44  HIS E  45  THR E  46  SER E  48                    
SITE     4 AC9 37 ALA E  49  GLN E  50  GLY E  51  GLY E  52                    
SITE     5 AC9 37 TRP E 164  TYR E 165  ALA E 166  ALA E 201                    
SITE     6 AC9 37 THR E 202  GLY E 203  THR E 213  ASN E 214                    
SITE     7 AC9 37 ASP E 221  LEU E 252  HIS E 354  TYR E 355                    
SITE     8 AC9 37 GLU E 388  ARG E 399  GLY E 402  ASN E 403                    
SITE     9 AC9 37 SER E 404  LEU E 405  LEU E 408  TEO E1589                    
SITE    10 AC9 37 HOH E2023                                                     
SITE     1 BC1 11 GLY E  51  PHE E 119  HIS E 242  THR E 254                    
SITE     2 BC1 11 GLU E 255  ARG E 286  HIS E 354  ARG E 399                    
SITE     3 BC1 11 GLY E 401  GLY E 402  FAD E 601                               
SITE     1 BC2  5 MET E 356  MET E 357  GLY E 358  GLU E 388                    
SITE     2 BC2  5 ALA E 390                                                     
SITE     1 BC3  8 SER F  54  CYS F  55  ARG F  56  GLY F  58                    
SITE     2 BC3  8 CYS F  60  GLY F  61  ASP F  63  CYS F  75                    
SITE     1 BC4  7 CYS F 149  ILE F 150  CYS F 152  ALA F 153                    
SITE     2 BC4  7 CYS F 155  CYS F 216  PRO F 217                               
SITE     1 BC5  7 CYS F 159  CYS F 206  THR F 207  MET F 210                    
SITE     2 BC5  7 ASN F 211  CYS F 212  THR F 223                               
SITE     1 BC6 17 HIS G  30  ARG G  31  GLY G  34  THR G  37                    
SITE     2 BC6 17 PHE G  38  HIS G  84  VAL G  85  GLY G  88                    
SITE     3 BC6 17 ILE G  89  CBE G1130  VAL H  19  ARG H  20                    
SITE     4 BC6 17 THR H  27  HIS H  71  GLY H  75  GLN H  78                    
SITE     5 BC6 17 VAL H  79                                                     
SITE     1 BC7  9 TRP F 164  THR F 207  PHE G  20  SER G  27                    
SITE     2 BC7  9 ILE G  28  ARG G  31  HEM G1129  ASP H  82                    
SITE     3 BC7  9 TYR H  83                                                     
SITE     1 BC8 38 GLY I  14  ALA I  15  GLY I  16  GLY I  17                    
SITE     2 BC8 38 ALA I  18  SER I  37  LYS I  38  VAL I  39                    
SITE     3 BC8 38 SER I  44  HIS I  45  THR I  46  SER I  48                    
SITE     4 BC8 38 ALA I  49  GLN I  50  GLY I  51  GLY I  52                    
SITE     5 BC8 38 TRP I 164  TYR I 165  ALA I 166  ALA I 201                    
SITE     6 BC8 38 THR I 202  GLY I 203  THR I 213  ASN I 214                    
SITE     7 BC8 38 ASP I 221  LEU I 252  HIS I 354  TYR I 355                    
SITE     8 BC8 38 GLU I 388  ARG I 399  GLY I 402  ASN I 403                    
SITE     9 BC8 38 SER I 404  LEU I 405  LEU I 408  TEO I1589                    
SITE    10 BC8 38 HOH I2009  HOH I2013                                          
SITE     1 BC9 11 GLY I  51  PHE I 119  HIS I 242  THR I 254                    
SITE     2 BC9 11 GLU I 255  ARG I 286  HIS I 354  ARG I 399                    
SITE     3 BC9 11 GLY I 401  GLY I 402  FAD I 601                               
SITE     1 CC1  6 TYR I 355  MET I 356  MET I 357  GLY I 358                    
SITE     2 CC1  6 GLU I 388  ALA I 390                                          
SITE     1 CC2  9 SER J  54  CYS J  55  ARG J  56  GLY J  58                    
SITE     2 CC2  9 VAL J  59  CYS J  60  GLY J  61  ASP J  63                    
SITE     3 CC2  9 CYS J  75                                                     
SITE     1 CC3  8 CYS J 149  ILE J 150  CYS J 152  ALA J 153                    
SITE     2 CC3  8 CYS J 154  CYS J 155  CYS J 216  PRO J 217                    
SITE     1 CC4  8 CYS J 159  CYS J 206  THR J 207  SER J 208                    
SITE     2 CC4  8 MET J 210  ASN J 211  CYS J 212  THR J 223                    
SITE     1 CC5 19 HIS K  30  ARG K  31  GLY K  34  PHE K  38                    
SITE     2 CC5 19 HIS K  84  VAL K  85  GLY K  88  CBE K1130                    
SITE     3 CC5 19 ARG L  20  ALA L  23  LEU L  26  THR L  27                    
SITE     4 CC5 19 ILE L  68  HIS L  71  ALA L  72  GLY L  75                    
SITE     5 CC5 19 MET L  76  GLN L  78  VAL L  79                               
SITE     1 CC6  9 TRP J 164  THR J 207  PHE K  20  SER K  27                    
SITE     2 CC6  9 ILE K  28  ARG K  31  HEM K1129  ASP L  82                    
SITE     3 CC6  9 TYR L  83                                                     
CRYST1  119.853  183.803  202.777  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  0.005441  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004932        0.00000                         
MTRIX1   1  0.949220  0.286670  0.129620       17.36060    1                    
MTRIX2   1  0.256880 -0.468330 -0.845390      -98.56210    1                    
MTRIX3   1 -0.181640  0.835760 -0.518180      -29.69555    1                    
MTRIX1   2  0.950380  0.268940 -0.156390        3.68480    1                    
MTRIX2   2  0.269320 -0.459600  0.846310      -25.04748    1                    
MTRIX3   2  0.155730 -0.846430 -0.509220     -101.99783    1                    
MTRIX1   3  0.951360  0.282080  0.123840       17.14904    1                    
MTRIX2   3  0.249870 -0.471390 -0.845790      -98.45415    1                    
MTRIX3   3 -0.180200  0.835600 -0.518940      -29.81741    1                    
MTRIX1   4  0.950090  0.260140 -0.172210        3.17224    1                    
MTRIX2   4  0.278820 -0.460370  0.842810      -25.39694    1                    
MTRIX3   4  0.139970 -0.848760 -0.509920     -101.67189    1                    
MTRIX1   5  0.950750  0.283670  0.124940       17.34645    1                    
MTRIX2   5  0.250140 -0.464130 -0.849710      -98.44913    1                    
MTRIX3   5 -0.183050  0.839110 -0.512230      -29.51782    1                    
MTRIX1   6  0.948620  0.257260 -0.184240        2.89664    1                    
MTRIX2   6  0.288140 -0.461610  0.838990      -25.73201    1                    
MTRIX3   6  0.130790 -0.848960 -0.512010     -101.30891    1                    
MTRIX1   7  0.951760  0.281270  0.122640       17.17110    1                    
MTRIX2   7  0.245330 -0.457460 -0.854710      -98.24440    1                    
MTRIX3   7 -0.184300  0.843570 -0.504400      -29.04328    1                    
MTRIX1   8  0.948250  0.256160 -0.187640        2.78004    1                    
MTRIX2   8  0.289280 -0.453200  0.843170      -25.55106    1                    
MTRIX3   8  0.130950 -0.853810 -0.503840     -101.16541    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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