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Database: PDB
Entry: 2WU2
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HEADER    OXIDOREDUCTASE                          28-SEP-09   2WU2              
TITLE     CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE     
TITLE    2 (SQR) SDHC HIS84MET 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 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT;           
COMPND  15 CHAIN: C, G, K;                                                      
COMPND  16 SYNONYM: CYTOCHROME B-556;                                           
COMPND  17 EC: 1.3.5.1;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 OTHER_DETAILS: RESIDUES 8-129 MODELLED;                              
COMPND  20 MOL_ID: 4;                                                           
COMPND  21 MOLECULE: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR        
COMPND  22  PROTEIN SUBUNIT;                                                    
COMPND  23 CHAIN: D, H, L;                                                      
COMPND  24 EC: 1.3.5.1;                                                         
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MUTATION: YES;                                                       
COMPND  27 OTHER_DETAILS: RESIDUES 11-115 MODELLED                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 562;                                                 
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  19 ORGANISM_TAXID: 562;                                                 
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  22 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PFAS;                                     
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  27 ORGANISM_TAXID: 562;                                                 
SOURCE  28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  30 EXPRESSION_SYSTEM_STRAIN: DW35;                                      
SOURCE  31 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  32 EXPRESSION_SYSTEM_PLASMID: PFAS                                      
KEYWDS    CELL INNER MEMBRANE, TRICARBOXYLIC ACID CYCLE, METAL-BINDING,         
KEYWDS   2 TRANSMEMBRANE, TRANSPORT, FLAVOPROTEIN, OXIDOREDUCTASE, ELECTRON     
KEYWDS   3 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.RUPRECHT,V.YANKOVSKAYA,E.MAKLASHINA,S.IWATA,G.CECCHINI              
REVDAT   1   25-AUG-10 2WU2    0                                                
JRNL        AUTH   J.RUPRECHT,V.YANKOVSKAYA,E.MAKLASHINA,S.IWATA,G.CECCHINI     
JRNL        TITL   CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE:QUINONE           
JRNL        TITL 2 OXIDOREDUCTASE (SQR) SDHC HIS84MET MUTANT                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.70                          
REMARK   3   NUMBER OF REFLECTIONS             : 146098                         
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) : 0.17876                         
REMARK   3   R VALUE            (WORKING SET) : 0.17689                         
REMARK   3   FREE R VALUE                     : 0.21431                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 7724                            
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) : 2.502                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.567                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10366                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.231                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 547                          
REMARK   3   BIN FREE R VALUE                    : 0.279                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 24519                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 423                                     
REMARK   3   SOLVENT ATOMS            :   1018                                  
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.086                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.51                                                
REMARK   3    B22 (A**2) : 1.27                                                 
REMARK   3    B33 (A**2) : 0.23                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.353         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.158         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.601        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
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): 25551 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 34647 ; 1.444 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3147 ; 5.758 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1107 ;35.392 ;23.388       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4209 ;15.146 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   192 ;21.099 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3834 ; 0.137 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19269 ; 0.006 ; 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): 15654 ; 0.444 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 25155 ; 0.897 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9897 ; 1.953 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9441 ; 2.889 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A E I                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     588      1                      
REMARK   3           1     E      1       E     588      1                      
REMARK   3           1     I      1       I     588      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   4522 ;  0.07 ;  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 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      1    E (A**2):   4522 ;  0.13 ;  0.50           
REMARK   3   TIGHT THERMAL      1    I (A**2):   4522 ;  0.13 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B F J                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B     238      1                      
REMARK   3           1     F      1       F     238      1                      
REMARK   3           1     J      1       J     238      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   1869 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    F    (A):   1869 ;  0.05 ;  0.05           
REMARK   3   TIGHT POSITIONAL   2    J    (A):   1869 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      2    B (A**2):   1869 ;  0.17 ;  0.50           
REMARK   3   TIGHT THERMAL      2    F (A**2):   1869 ;  0.15 ;  0.50           
REMARK   3   TIGHT THERMAL      2    J (A**2):   1869 ;  0.14 ;  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):    946 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    G    (A):    946 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   3    K    (A):    946 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      3    C (A**2):    946 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      3    G (A**2):    946 ;  0.08 ;  0.50           
REMARK   3   TIGHT THERMAL      3    K (A**2):    946 ;  0.08 ;  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):    836 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    H    (A):    836 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   4    L    (A):    836 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      4    D (A**2):    836 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      4    H (A**2):    836 ;  0.10 ;  0.50           
REMARK   3   TIGHT THERMAL      4    L (A**2):    836 ;  0.10 ;  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):   1.8560 -11.4940 -24.5140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0252 T22:   0.0512                                     
REMARK   3      T33:   0.1148 T12:  -0.0113                                     
REMARK   3      T13:   0.0349 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9102 L22:   1.3136                                     
REMARK   3      L33:   1.4094 L12:  -0.0826                                     
REMARK   3      L13:   0.0888 L23:  -0.1145                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0366 S12:  -0.1041 S13:   0.0041                       
REMARK   3      S21:   0.1620 S22:  -0.0710 S23:   0.2017                       
REMARK   3      S31:  -0.0376 S32:  -0.1675 S33:   0.0344                       
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 :   E     1        E   588                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7420 -72.3730 -26.8720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2932 T22:   0.0329                                     
REMARK   3      T33:   0.1419 T12:  -0.0550                                     
REMARK   3      T13:  -0.0714 T23:   0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1033 L22:   1.4231                                     
REMARK   3      L33:   1.3711 L12:   0.3243                                     
REMARK   3      L13:   0.2020 L23:   0.4881                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1590 S12:  -0.0673 S13:  -0.1566                       
REMARK   3      S21:   0.4039 S22:  -0.0821 S23:   0.0917                       
REMARK   3      S31:   0.2862 S32:  -0.1005 S33:  -0.0768                       
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 :   I     1        I   588                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8890 -40.0800 -79.7110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2587 T22:   0.1891                                     
REMARK   3      T33:   0.0764 T12:   0.0248                                     
REMARK   3      T13:  -0.1013 T23:  -0.0343                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4480 L22:   1.6438                                     
REMARK   3      L33:   1.1918 L12:  -0.0337                                     
REMARK   3      L13:   0.3421 L23:   0.1546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0707 S12:   0.1712 S13:  -0.0485                       
REMARK   3      S21:  -0.4130 S22:   0.0113 S23:   0.2074                       
REMARK   3      S31:   0.0682 S32:  -0.1362 S33:  -0.0820                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0270  -9.3880 -30.5370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0211 T22:   0.0497                                     
REMARK   3      T33:   0.1243 T12:  -0.0107                                     
REMARK   3      T13:  -0.0344 T23:  -0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4168 L22:   1.4475                                     
REMARK   3      L33:   1.5073 L12:  -0.0130                                     
REMARK   3      L13:  -0.0728 L23:  -0.3068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0163 S12:  -0.0089 S13:   0.1055                       
REMARK   3      S21:   0.1574 S22:  -0.0507 S23:  -0.2483                       
REMARK   3      S31:  -0.0943 S32:   0.1767 S33:   0.0343                       
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 :   F     1        F   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5070 -61.1350 -26.8580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2063 T22:   0.0876                                     
REMARK   3      T33:   0.1741 T12:   0.0500                                     
REMARK   3      T13:  -0.1491 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5144 L22:   1.2320                                     
REMARK   3      L33:   1.0583 L12:   0.4676                                     
REMARK   3      L13:   0.3437 L23:   0.4060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1134 S12:   0.0041 S13:  -0.0771                       
REMARK   3      S21:   0.2743 S22:   0.0025 S23:  -0.2490                       
REMARK   3      S31:   0.2348 S32:   0.1960 S33:  -0.1159                       
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 :   J     1        J   238                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.5310 -38.9630 -74.5650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2032 T22:   0.2001                                     
REMARK   3      T33:   0.0594 T12:   0.0595                                     
REMARK   3      T13:   0.0521 T23:  -0.0466                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7828 L22:   1.4706                                     
REMARK   3      L33:   0.9440 L12:  -0.2036                                     
REMARK   3      L13:   0.0881 L23:  -0.0512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0755 S12:   0.2075 S13:  -0.0059                       
REMARK   3      S21:  -0.3386 S22:  -0.0161 S23:  -0.2169                       
REMARK   3      S31:   0.0802 S32:   0.2344 S33:  -0.0594                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     8        C   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.9700  -5.5570 -31.5020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0849 T22:   0.2681                                     
REMARK   3      T33:   0.5484 T12:  -0.0871                                     
REMARK   3      T13:  -0.0540 T23:  -0.0916                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1288 L22:   1.0514                                     
REMARK   3      L33:   0.9595 L12:  -1.2374                                     
REMARK   3      L13:  -0.0379 L23:   0.1825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0334 S12:  -0.3792 S13:   0.6793                       
REMARK   3      S21:   0.0880 S22:   0.0871 S23:  -0.5516                       
REMARK   3      S31:  -0.1024 S32:   0.3323 S33:  -0.0537                       
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 :   G     8        G   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.0020 -54.1070 -29.3580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1910 T22:   0.3270                                     
REMARK   3      T33:   0.6850 T12:   0.1368                                     
REMARK   3      T13:  -0.2407 T23:  -0.0167                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5363 L22:   1.9541                                     
REMARK   3      L33:   1.5489 L12:   1.3869                                     
REMARK   3      L13:  -1.2184 L23:  -0.6272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0740 S12:  -0.0826 S13:  -0.5809                       
REMARK   3      S21:   0.1807 S22:  -0.1357 S23:  -0.8693                       
REMARK   3      S31:   0.2689 S32:   0.4722 S33:   0.0617                       
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 :   K     8        K   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.9440 -32.0100 -73.1180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2566 T22:   0.7329                                     
REMARK   3      T33:   0.4135 T12:   0.0301                                     
REMARK   3      T13:   0.2506 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2526 L22:   1.7822                                     
REMARK   3      L33:   2.0704 L12:   1.4095                                     
REMARK   3      L13:   1.5325 L23:   0.7652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1339 S12:   0.7686 S13:   0.1848                       
REMARK   3      S21:  -0.3925 S22:   0.1899 S23:  -0.4635                       
REMARK   3      S31:  -0.1408 S32:   0.7976 S33:  -0.0560                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    11        D   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.0000 -18.1570 -38.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0215 T22:   0.3213                                     
REMARK   3      T33:   0.4478 T12:  -0.0261                                     
REMARK   3      T13:  -0.0012 T23:  -0.0855                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4915 L22:   1.0284                                     
REMARK   3      L33:   1.4780 L12:  -0.2914                                     
REMARK   3      L13:   0.2058 L23:  -0.0177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0110 S12:   0.1043 S13:  -0.0307                       
REMARK   3      S21:  -0.0425 S22:   0.1340 S23:  -0.3912                       
REMARK   3      S31:  -0.1340 S32:   0.4749 S33:  -0.1450                       
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 :   H    11        H   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.3270 -41.3820 -37.7890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0386 T22:   0.3580                                     
REMARK   3      T33:   0.5920 T12:   0.0857                                     
REMARK   3      T13:  -0.0778 T23:  -0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7062 L22:   2.6272                                     
REMARK   3      L33:   2.8656 L12:   0.7887                                     
REMARK   3      L13:  -0.4532 L23:   0.0147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0042 S12:   0.1020 S13:  -0.0612                       
REMARK   3      S21:   0.0200 S22:   0.0683 S23:  -0.8424                       
REMARK   3      S31:   0.1650 S32:   0.5343 S33:  -0.0724                       
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):  68.6820 -29.9710 -58.3430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0729 T22:   0.5547                                     
REMARK   3      T33:   0.4160 T12:   0.0050                                     
REMARK   3      T13:   0.1277 T23:  -0.0840                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5832 L22:   3.0222                                     
REMARK   3      L33:   1.3856 L12:   0.2711                                     
REMARK   3      L13:   1.0827 L23:   0.4643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0579 S12:   0.2477 S13:   0.0868                       
REMARK   3      S21:  -0.2608 S22:   0.0638 S23:  -0.7192                       
REMARK   3      S31:  -0.0305 S32:   0.5131 S33:  -0.0059                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. DENSITY FOR THE N-TERMINUS OF SDH C (RESIDUES 1-7 OF     
REMARK   3  CHAINS C, G, K) AND THE N-TERMINUS OF SDHD (RESIDUES 1-10 OF        
REMARK   3  CHAINS D, H AND L) WAS WEAK AND THESE REGIONS ARE NOT INCLUDED IN   
REMARK   3  THE MODEL. THE SIDE CHAIN OF SDHD TRP113 IS TRUNCATED AT THE        
REMARK   3  CBETA ATOM SINCE DENSITY FOR THE SIDE CHAIN WAS POOR. ATOM RECORD   
REMARK   3  CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD           
REMARK   3  CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.                         
REMARK   4                                                                      
REMARK   4 2WU2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41275.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 153926                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.74                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 6.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.7                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.50                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2WDQ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 0.1M MGSO4, 11%        
REMARK 280  PEG4000, 1MM CARBOXIN                                               
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       60.01650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.36000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.68150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.36000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.01650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.68150            
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: 15540 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -157.9 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: 15580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -157.4 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: 15550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.1 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 C, HIS  84 TO MET                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, HIS  84 TO MET                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN K, HIS  84 TO MET                        
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    VAL A  47   CB  -  CA  -  C   ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ARG B 180   CG  -  CD  -  NE  ANGL. DEV. =  13.0 DEGREES          
REMARK 500    VAL E  47   CB  -  CA  -  C   ANGL. DEV. = -11.6 DEGREES          
REMARK 500    VAL I  47   CB  -  CA  -  C   ANGL. DEV. = -11.5 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    PHE A 126       63.37     60.09                                   
REMARK 500    ALA A 138     -121.79     43.67                                   
REMARK 500    ALA A 201       42.91   -146.04                                   
REMARK 500    ALA A 205       31.19   -157.21                                   
REMARK 500    ALA A 249      -32.71   -133.18                                   
REMARK 500    LYS A 281     -127.83     54.41                                   
REMARK 500    HIS A 354      -47.49   -134.12                                   
REMARK 500    ASN A 398      114.45   -168.55                                   
REMARK 500    SER A 472     -153.59    -87.20                                   
REMARK 500    SER B  54      -68.11   -154.05                                   
REMARK 500    ARG B  56       19.49     54.75                                   
REMARK 500    ASP B  63       46.30   -103.30                                   
REMARK 500    ASP B 102     -109.31     42.28                                   
REMARK 500    LYS B 118       71.15     47.95                                   
REMARK 500    ARG B 131     -115.22   -130.31                                   
REMARK 500    ASN B 165       57.39   -141.29                                   
REMARK 500    GLU D  42      113.91    -37.99                                   
REMARK 500    GLN E  50      -65.85   -108.75                                   
REMARK 500    ALA E 138     -125.96     50.63                                   
REMARK 500    ALA E 201       43.40   -140.73                                   
REMARK 500    ALA E 205       27.25   -157.02                                   
REMARK 500    ALA E 249      -35.36   -133.97                                   
REMARK 500    LYS E 281     -130.75     49.66                                   
REMARK 500    ASN E 398      113.56   -169.74                                   
REMARK 500    SER E 472     -154.76    -88.93                                   
REMARK 500    VAL F  14      -45.05   -132.43                                   
REMARK 500    SER F  54      -73.69   -150.65                                   
REMARK 500    ASP F  63       50.38   -104.79                                   
REMARK 500    ARG F 101      132.62   -173.22                                   
REMARK 500    ASP F 102     -107.76     40.31                                   
REMARK 500    ARG F 131     -116.51   -132.37                                   
REMARK 500    ASN F 165       59.95   -142.28                                   
REMARK 500    LEU G  13       39.79   -140.47                                   
REMARK 500    GLN I  50      -62.41   -106.47                                   
REMARK 500    PHE I 126       65.98     61.85                                   
REMARK 500    ALA I 138     -121.89     45.44                                   
REMARK 500    ALA I 201       41.97   -141.12                                   
REMARK 500    ALA I 205       28.72   -157.72                                   
REMARK 500    ALA I 249      -33.62   -139.79                                   
REMARK 500    LYS I 281     -128.92     54.43                                   
REMARK 500    ASN I 398      111.05   -169.21                                   
REMARK 500    SER I 472     -158.28    -86.76                                   
REMARK 500    SER J  54      -70.97   -150.07                                   
REMARK 500    GLU J  57       18.43   -142.76                                   
REMARK 500    ASP J  63       44.86   -107.35                                   
REMARK 500    PRO J  85      128.71    -39.86                                   
REMARK 500    ASP J 102     -106.45     36.90                                   
REMARK 500    ARG J 131     -115.55   -133.33                                   
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    95.1                                              
REMARK 620 3 MET A 357   O   100.6  68.6                                        
REMARK 620 4 GLU A 388   O    84.7  94.3 162.4                                  
REMARK 620 5 MET A 356   O   174.5  79.6  78.5  94.6                            
REMARK 620 N                    1     2     3     4                             
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 357   O                                                      
REMARK 620 2 GLY E 358   O    69.6                                              
REMARK 620 3 ALA E 390   O    99.9  91.8                                        
REMARK 620 4 MET E 356   O    79.2  82.5 174.2                                  
REMARK 620 5 GLU E 388   O   164.0  96.1  87.4  92.1                            
REMARK 620 N                    1     2     3     4                             
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 MET I 356   O                                                      
REMARK 620 2 MET I 357   O    78.8                                              
REMARK 620 3 GLY I 358   O    79.3  68.4                                        
REMARK 620 4 GLU I 388   O    96.7 160.2  91.9                                  
REMARK 620 5 ALA I 390   O   168.9  98.2  89.6  82.5                            
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 CYS B  60   SG  103.1                                              
REMARK 620 3 FES B 302  FE2  120.3 136.2                                        
REMARK 620 4 FES B 302   S1  102.5 118.8  49.2                                  
REMARK 620 5 FES B 302   S2  122.0 112.5  49.7  98.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  63   OD1                                                    
REMARK 620 2 FES B 302  FE1  119.9                                              
REMARK 620 3 FES B 302   S1  111.4  49.8                                        
REMARK 620 4 FES B 302   S2  100.7  49.8  99.2                                  
REMARK 620 5 CYS B  75   SG  126.8 113.3 100.7 115.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES F 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  55   SG                                                     
REMARK 620 2 FES F 302  FE2  117.9                                              
REMARK 620 3 FES F 302   S1  110.3  49.9                                        
REMARK 620 4 FES F 302   S2  113.0  49.4  98.7                                  
REMARK 620 5 CYS F  60   SG  107.1 134.9 116.9 110.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES F 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FES F 302  FE1                                                     
REMARK 620 2 FES F 302   S1   49.4                                              
REMARK 620 3 FES F 302   S2   51.5 100.2                                        
REMARK 620 4 ASP F  63   OD1 122.6 107.0 105.4                                  
REMARK 620 5 CYS F  75   SG  116.4 103.6 117.9 120.3                            
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 CYS J  60   SG  109.9                                              
REMARK 620 3 FES J 302  FE2  118.0 131.4                                        
REMARK 620 4 FES J 302   S1  103.4 113.8  48.2                                  
REMARK 620 5 FES J 302   S2  118.3 115.1  47.0  94.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES J 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J  75   SG                                                     
REMARK 620 2 FES J 302  FE1  115.3                                              
REMARK 620 3 FES J 302   S1  101.1  49.3                                        
REMARK 620 4 FES J 302   S2  116.1  50.0  99.1                                  
REMARK 620 5 ASP J  63   OD1 124.8 120.0 113.9  99.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 155   SG                                                     
REMARK 620 2 SF4 B 303  FE3  144.6                                              
REMARK 620 3 SF4 B 303  FE2  145.1  59.6                                        
REMARK 620 4 SF4 B 303  FE4  143.1  62.1  60.6                                  
REMARK 620 5 SF4 B 303   S3  112.0 103.5  54.9  54.2                            
REMARK 620 6 SF4 B 303   S2  113.1  54.9 101.8  54.1 105.9                      
REMARK 620 7 SF4 B 303   S4  113.5  54.4  52.8 103.3 104.3 107.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 149   SG                                                     
REMARK 620 2 SF4 B 303  FE1  134.1                                              
REMARK 620 3 SF4 B 303  FE2  137.1  61.5                                        
REMARK 620 4 SF4 B 303  FE4  159.7  58.8  60.2                                  
REMARK 620 5 SF4 B 303   S1  122.1 102.4  54.1  54.3                            
REMARK 620 6 SF4 B 303   S2  118.4  53.5 102.2  52.4 103.5                      
REMARK 620 7 SF4 B 303   S4   98.2  56.1  53.9 102.0 105.5 107.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B 303  FE1                                                     
REMARK 620 2 SF4 B 303  FE3   58.9                                              
REMARK 620 3 SF4 B 303  FE4   58.2  61.0                                        
REMARK 620 4 SF4 B 303   S1  100.2  54.0  54.7                                  
REMARK 620 5 SF4 B 303   S3   53.1 101.4  52.8 105.3                            
REMARK 620 6 SF4 B 303   S4   55.2  54.8 103.3 106.2 104.8                      
REMARK 620 7 CYS B 152   SG  133.6 160.0 137.1 124.2  98.1 115.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B 303  FE1                                                     
REMARK 620 2 SF4 B 303  FE3   59.1                                              
REMARK 620 3 SF4 B 303  FE2   61.1  58.8                                        
REMARK 620 4 SF4 B 303   S1  101.4  52.8  53.2                                  
REMARK 620 5 SF4 B 303   S3   54.9 101.6  55.3 106.2                            
REMARK 620 6 SF4 B 303   S2   54.0  53.7 102.1 103.2 106.4                      
REMARK 620 7 CYS B 216   SG  147.6 148.1 138.4 110.8 109.8 119.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE4                                                     
REMARK 620 2 SF4 F 303  FE2   62.9                                              
REMARK 620 3 SF4 F 303   S3   56.8  55.4                                        
REMARK 620 4 SF4 F 303   S2   54.4 103.1 109.3                                  
REMARK 620 5 SF4 F 303  FE3   60.7  59.4 103.4  53.8                            
REMARK 620 6 SF4 F 303   S4  103.6  53.4 105.8 103.7  53.3                      
REMARK 620 7 CYS F 155   SG  143.5 146.8 115.0 109.7 141.6 112.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE4                                                     
REMARK 620 2 SF4 F 303  FE2   61.4                                              
REMARK 620 3 SF4 F 303   S1   54.3  54.7                                        
REMARK 620 4 CYS F 216   SG  154.2 135.5 114.7                                  
REMARK 620 5 SF4 F 303   S2   53.2 102.3 105.0 121.4                            
REMARK 620 6 SF4 F 303   S4  101.1  53.0 105.7 104.6 103.9                      
REMARK 620 7 SF4 F 303  FE1   57.6  58.4  99.5 144.2  53.9  53.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE4                                                     
REMARK 620 2 CYS F 152   SG  155.4                                              
REMARK 620 3 SF4 F 303   S1   53.7 122.0                                        
REMARK 620 4 SF4 F 303   S3   54.8 112.6 104.6                                  
REMARK 620 5 SF4 F 303  FE3   60.2 140.9  54.1 105.1                            
REMARK 620 6 SF4 F 303   S4  101.6 102.5 107.0 107.2  54.9                      
REMARK 620 7 SF4 F 303  FE1   58.4 135.7 102.1  54.7  62.2  55.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE2                                                     
REMARK 620 2 SF4 F 303   S1   53.2                                              
REMARK 620 3 CYS F 149   SG  133.4 114.6                                        
REMARK 620 4 SF4 F 303   S3   53.1 102.6  98.9                                  
REMARK 620 5 SF4 F 303   S2  100.9 105.2 124.7 108.3                            
REMARK 620 6 SF4 F 303  FE3   58.4  53.2 157.6 102.2  54.5                      
REMARK 620 7 SF4 F 303  FE1   58.7 101.9 139.4  54.4  55.9  61.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 J 303  FE2                                                     
REMARK 620 2 SF4 J 303  FE3   61.7                                              
REMARK 620 3 SF4 J 303  FE4   61.2  58.0                                        
REMARK 620 4 SF4 J 303   S4   57.6  53.2 102.2                                  
REMARK 620 5 CYS J 155   SG  146.2 145.1 142.0 115.4                            
REMARK 620 6 SF4 J 303   S2  104.3  53.5  54.0 102.4 109.4                      
REMARK 620 7 SF4 J 303   S3   55.4 101.7  53.6 111.9 112.6 104.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 J 303  FE3                                                     
REMARK 620 2 SF4 J 303  FE4   58.6                                              
REMARK 620 3 SF4 J 303   S1   53.2  54.2                                        
REMARK 620 4 SF4 J 303   S4   53.3 101.6 103.0                                  
REMARK 620 5 CYS J 149   SG  134.7 158.6 116.2  99.4                            
REMARK 620 6 SF4 J 303  FE1   62.9  62.0 105.2  56.0 136.2                      
REMARK 620 7 SF4 J 303   S3  103.9  54.3 104.4 111.9 120.8  57.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 152   SG                                                     
REMARK 620 2 SF4 J 303  FE2  157.5                                              
REMARK 620 3 SF4 J 303  FE4  141.5  59.7                                        
REMARK 620 4 SF4 J 303   S1  125.2  54.4  55.0                                  
REMARK 620 5 SF4 J 303   S4  111.4  55.0 103.8 105.6                            
REMARK 620 6 SF4 J 303  FE1  134.6  55.4  59.7  99.9  53.3                      
REMARK 620 7 SF4 J 303   S2  102.5  98.1  54.5 108.2 101.4  52.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 J 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 J 303  FE2                                                     
REMARK 620 2 SF4 J 303  FE3   61.7                                              
REMARK 620 3 SF4 J 303   S1   55.2  54.7                                        
REMARK 620 4 CYS J 216   SG  148.4 142.0 115.0                                  
REMARK 620 5 SF4 J 303  FE1   56.8  62.2 101.7 143.3                            
REMARK 620 6 SF4 J 303   S2  100.2  55.2 108.7 111.2  53.5                      
REMARK 620 7 SF4 J 303   S3   53.9 106.1 104.9 111.8  54.7 104.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 159   SG                                                     
REMARK 620 2 F3S B 304   S3  113.5                                              
REMARK 620 3 F3S B 304   S1  110.9 101.7                                        
REMARK 620 4 F3S B 304  FE3  139.6  49.7  54.3                                  
REMARK 620 5 F3S B 304   S2  113.4 114.5 101.5 106.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S B 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 206   SG                                                     
REMARK 620 2 F3S B 304  FE1  154.9                                              
REMARK 620 3 F3S B 304   S3  120.1  51.9                                        
REMARK 620 4 F3S B 304   S1  121.0  50.5 100.2                                  
REMARK 620 5 F3S B 304  FE4  146.6  51.7  92.9  50.3                            
REMARK 620 6 F3S B 304   S4  103.3 101.0 116.1  93.9  52.6                      
REMARK 620 N                    1     2     3     4     5                       
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   S1  112.1                                              
REMARK 620 3 F3S B 304  FE3  132.6  59.6                                        
REMARK 620 4 F3S B 304   S2  104.6 112.6 122.0                                  
REMARK 620 5 F3S B 304   S4   85.8 105.7  57.4 132.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S F 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S F 304  FE3                                                     
REMARK 620 2 F3S F 304  FE4   56.0                                              
REMARK 620 3 F3S F 304   S3   53.4  53.5                                        
REMARK 620 4 F3S F 304   S1   52.9 107.8  91.3                                  
REMARK 620 5 F3S F 304   S2   96.8  53.4 104.8 125.4                            
REMARK 620 6 CYS F 159   SG  146.8 144.6 111.7 104.2 116.4                      
REMARK 620 N                    1     2     3     4     5                       
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 212   SG                                                     
REMARK 620 2 F3S F 304   S3  102.0                                              
REMARK 620 3 F3S F 304   S4  102.3 107.0                                        
REMARK 620 4 F3S F 304  FE1  137.2  58.2 119.2                                  
REMARK 620 5 F3S F 304   S1   92.9  99.1 146.1  58.5                            
REMARK 620 N                    1     2     3     4                             
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 F3S F 304   S3                                                     
REMARK 620 2 F3S F 304   S4   99.5                                              
REMARK 620 3 F3S F 304  FE1   56.1 109.4                                        
REMARK 620 4 CYS F 206   SG  122.0  97.0 153.5                                  
REMARK 620 5 F3S F 304   S2  107.2 118.0  53.4 112.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S J 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS J 159   SG                                                     
REMARK 620 2 F3S J 304   S2  107.2                                              
REMARK 620 3 F3S J 304  FE3  144.6 105.8                                        
REMARK 620 4 F3S J 304  FE4  147.4  54.2  54.0                                  
REMARK 620 5 F3S J 304   S1  110.6  97.1  52.3  54.4                            
REMARK 620 6 F3S J 304   S3  117.9 121.4  50.8  94.2  99.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S J 304  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S J 304  FE1                                                     
REMARK 620 2 F3S J 304   S1   52.7                                              
REMARK 620 3 CYS J 206   SG  146.6 117.6                                        
REMARK 620 4 F3S J 304   S4  107.0 100.1 106.2                                  
REMARK 620 5 F3S J 304   S3   49.8  99.3 113.7 119.7                            
REMARK 620 N                    1     2     3     4                             
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 212   SG                                                     
REMARK 620 2 F3S J 304   S2   97.5                                              
REMARK 620 3 F3S J 304  FE1  142.0  59.4                                        
REMARK 620 4 F3S J 304   S1  105.7 105.0  59.2                                  
REMARK 620 5 F3S J 304   S4   91.6 141.2 125.7 108.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C1130  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  71   NE2                                                    
REMARK 620 2 HEM C1130   NA   85.1                                              
REMARK 620 3 HEM C1130   NB   87.8  80.2                                        
REMARK 620 4 HEM C1130   NC   97.5 171.8  92.0                                  
REMARK 620 5 HEM C1130   ND   97.1  97.2 174.2  90.2                            
REMARK 620 6 MET C  84   SD  172.6  89.4  96.1  88.6  78.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G1130  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET G  84   SD                                                     
REMARK 620 2 HEM G1130   ND   83.1                                              
REMARK 620 3 HIS H  71   NE2 175.3  95.7                                        
REMARK 620 4 HEM G1130   NC   93.2  91.4  91.3                                  
REMARK 620 5 HEM G1130   NA   86.1  93.5  89.5 174.9                            
REMARK 620 6 HEM G1130   NB   91.3 174.4  89.9  89.4  85.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K1130  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET K  84   SD                                                     
REMARK 620 2 HIS L  71   NE2 174.2                                              
REMARK 620 3 HEM K1130   NA   91.6  90.5                                        
REMARK 620 4 HEM K1130   NB   92.6  93.0  85.7                                  
REMARK 620 5 HEM K1130   NC   87.4  90.8 177.2  91.7                            
REMARK 620 6 HEM K1130   ND   80.9  93.4  95.5 173.4  86.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES F 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S F 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES J 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 J 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S J 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE C1131                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO A1589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1590                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE G1131                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO E1589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E1590                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE K1131                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO I1589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA I1590                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WP9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE                  
REMARK 900 OXIDOREDUCTASE (SQR) SDHB HIS207THR MUTANT                           
REMARK 900 RELATED ID: 2WDQ   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH                 
REMARK 900 CARBOXIN BOUND                                                       
REMARK 900 RELATED ID: 2WDR   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH                 
REMARK 900 PENTACHLOROPHENOL BOUND                                              
REMARK 900 RELATED ID: 1NEK   RELATED DB: PDB                                   
REMARK 900 SUCCINATE DEHYDOGENASE FROM E.COLI                                   
REMARK 900 RELATED ID: 1NEN   RELATED DB: PDB                                   
REMARK 900 MOLECULAR ARCHITECTURE OF SUCCINATE DEHYDROGENASE                    
REMARK 900 (COMPLEXII) PREVENTS REACTIVE OXYGEN SPECIES GENERATION              
REMARK 900 RELATED ID: 2ACZ   RELATED DB: PDB                                   
REMARK 900 COMPLEX II (SUCCINATE DEHYDROGENASE) FROM E. COLI                    
REMARK 900 WITHATPENIN A5 INHIBITOR CO-CRYSTALLIZED AT THE                      
REMARK 900 UBIQUINONEBINDING SITE                                               
REMARK 900 RELATED ID: 2WU5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE                  
REMARK 900 OXIDOREDUCTASE (SQR) SDHD HIS71MET MUTANT                            
REMARK 900 RELATED ID: 2WDV   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH AN              
REMARK 900 EMPTY QUINONE-BINDING POCKET                                         
DBREF  2WU2 A    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WU2 B    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WU2 C    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WU2 D    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WU2 E    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WU2 F    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WU2 G    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WU2 H    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WU2 I    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WU2 J    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WU2 K    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WU2 L    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
SEQADV 2WU2 MET C   84  UNP  P69054    HIS    84 ENGINEERED MUTATION            
SEQADV 2WU2 MET G   84  UNP  P69054    HIS    84 ENGINEERED MUTATION            
SEQADV 2WU2 MET K   84  UNP  P69054    HIS    84 ENGINEERED MUTATION            
SEQRES   1 A  588  MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE          
SEQRES   2 A  588  GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE          
SEQRES   3 A  588  SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL          
SEQRES   4 A  588  PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY          
SEQRES   5 A  588  ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP          
SEQRES   6 A  588  GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR          
SEQRES   7 A  588  ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR          
SEQRES   8 A  588  GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU          
SEQRES   9 A  588  PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG          
SEQRES  10 A  588  PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN          
SEQRES  11 A  588  ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS          
SEQRES  12 A  588  ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN          
SEQRES  13 A  588  HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU          
SEQRES  14 A  588  VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA          
SEQRES  15 A  588  LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA          
SEQRES  16 A  588  ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE          
SEQRES  17 A  588  TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP          
SEQRES  18 A  588  GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN          
SEQRES  19 A  588  ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA          
SEQRES  20 A  588  GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU          
SEQRES  21 A  588  GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET          
SEQRES  22 A  588  GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG          
SEQRES  23 A  588  ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU          
SEQRES  24 A  588  GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS          
SEQRES  25 A  588  LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER          
SEQRES  26 A  588  ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA          
SEQRES  27 A  588  HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO          
SEQRES  28 A  588  THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL          
SEQRES  29 A  588  THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP          
SEQRES  30 A  588  VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA          
SEQRES  31 A  588  CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN          
SEQRES  32 A  588  SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY          
SEQRES  33 A  588  LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU          
SEQRES  34 A  588  ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP          
SEQRES  35 A  588  ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP          
SEQRES  36 A  588  PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN          
SEQRES  37 A  588  HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA          
SEQRES  38 A  588  LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU          
SEQRES  39 A  588  LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN          
SEQRES  40 A  588  THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET          
SEQRES  41 A  588  GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG          
SEQRES  42 A  588  THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO          
SEQRES  43 A  588  ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR          
SEQRES  44 A  588  LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN          
SEQRES  45 A  588  MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE          
SEQRES  46 A  588  ARG THR TYR                                                  
SEQRES   1 B  238  MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP          
SEQRES   2 B  238  VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU          
SEQRES   3 B  238  ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU          
SEQRES   4 B  238  ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG          
SEQRES   5 B  238  ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU          
SEQRES   6 B  238  ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO          
SEQRES   7 B  238  ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE          
SEQRES   8 B  238  ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL          
SEQRES   9 B  238  VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE          
SEQRES  10 B  238  LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA          
SEQRES  11 B  238  ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU          
SEQRES  12 B  238  ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER          
SEQRES  13 B  238  THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE          
SEQRES  14 B  238  ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU          
SEQRES  15 B  238  ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP          
SEQRES  16 B  238  GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER          
SEQRES  17 B  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 B  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 B  238  GLN ARG ASN ALA                                              
SEQRES   1 C  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 C  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 C  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 C  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 C  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 C  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 C  129  THR ALA LEU ALA TYR MET 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 HIS SER          
SEQRES  17 F  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 F  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 F  238  GLN ARG ASN ALA                                              
SEQRES   1 G  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 G  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 G  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 G  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 G  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 G  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 G  129  THR ALA LEU ALA TYR MET 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 HIS SER          
SEQRES  17 J  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 J  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 J  238  GLN ARG ASN ALA                                              
SEQRES   1 K  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 K  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 K  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 K  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 K  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 K  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 K  129  THR ALA LEU ALA TYR MET 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  C1130      43                                                       
HET    CBE  C1131      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  G1130      43                                                       
HET    CBE  G1131      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  K1130      43                                                       
HET    CBE  K1131      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-                     
HETNAM   2 CBE  3-CARBOXAMIDE                                                   
HETSYN     HEM HEME                                                             
HETSYN     CBE 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-                             
HETSYN   2 CBE  CARBOXANILID                                                    
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  21  HOH   *1018(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  SER A  440  1                                   8    
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 PRO B   78  ASN B   83  1                                   6    
HELIX   25  25 MET B  107  ILE B  117  1                                  11    
HELIX   26  26 MET B  136  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 ILE B  170  ILE B  183  1                                  14    
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  SER D   40  1                                  30    
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  GLY D  114  1                                  29    
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  ALA E  338  1                                  12    
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 ASP E  549  LEU E  554  1                                   6    
HELIX   64  64 MET F   34  ASP F   46  1                                  13    
HELIX   65  65 CYS F   75  THR F   77  5                                   3    
HELIX   66  66 PRO F   78  ASN F   83  1                                   6    
HELIX   67  67 MET F  107  ILE F  117  1                                  11    
HELIX   68  68 MET F  136  LYS F  142  1                                   7    
HELIX   69  69 CYS F  155  SER F  158  5                                   4    
HELIX   70  70 CYS F  159  ASN F  165  1                                   7    
HELIX   71  71 GLY F  171  ILE F  183  1                                  13    
HELIX   72  72 GLU F  189  GLY F  196  1                                   8    
HELIX   73  73 MET F  210  CYS F  216  1                                   7    
HELIX   74  74 ASN F  221  ALA F  238  1                                  18    
HELIX   75  75 ASP G   14  ILE G   18  5                                   5    
HELIX   76  76 PRO G   21  SER G   54  1                                  34    
HELIX   77  77 SER G   54  GLY G   66  1                                  13    
HELIX   78  78 SER G   67  PHE G   96  1                                  30    
HELIX   79  79 THR G  102  TRP G  129  1                                  28    
HELIX   80  80 ASN H   11  SER H   40  1                                  30    
HELIX   81  81 THR H   44  SER H   54  1                                  11    
HELIX   82  82 SER H   54  VAL H   84  1                                  31    
HELIX   83  83 PRO H   86  GLY H  114  1                                  29    
HELIX   84  84 GLY I   16  SER I   29  1                                  14    
HELIX   85  85 PHE I   40  SER I   44  5                                   5    
HELIX   86  86 SER I   44  ALA I   49  5                                   6    
HELIX   87  87 ASN I   64  SER I   76  1                                  13    
HELIX   88  88 ASP I   81  MET I  102  1                                  22    
HELIX   89  89 ARG I  140  ASN I  156  1                                  17    
HELIX   90  90 ALA I  205  TYR I  209  5                                   5    
HELIX   91  91 GLY I  220  ALA I  229  1                                  10    
HELIX   92  92 GLU I  255  GLU I  260  1                                   6    
HELIX   93  93 PHE I  272  ALA I  277  1                                   6    
HELIX   94  94 ALA I  280  ALA I  284  5                                   5    
HELIX   95  95 GLY I  285  GLU I  299  1                                  15    
HELIX   96  96 LEU I  315  LEU I  318  5                                   4    
HELIX   97  97 GLY I  319  LEU I  327  1                                   9    
HELIX   98  98 LEU I  327  ALA I  338  1                                  12    
HELIX   99  99 GLY I  402  GLY I  427  1                                  26    
HELIX  100 100 SER I  433  SER I  440  1                                   8    
HELIX  101 101 LEU I  441  ASN I  450  1                                  10    
HELIX  102 102 ASP I  455  PHE I  471  1                                  17    
HELIX  103 103 GLU I  476  LYS I  495  1                                  20    
HELIX  104 104 ASN I  507  ARG I  533  1                                  27    
HELIX  105 105 MET J   34  ASP J   46  1                                  13    
HELIX  106 106 CYS J   75  THR J   77  5                                   3    
HELIX  107 107 PRO J   78  ASN J   83  1                                   6    
HELIX  108 108 MET J  107  ILE J  117  1                                  11    
HELIX  109 109 MET J  136  GLU J  141  1                                   6    
HELIX  110 110 LYS J  142  ASP J  144  5                                   3    
HELIX  111 111 CYS J  155  SER J  158  5                                   4    
HELIX  112 112 CYS J  159  ASN J  165  1                                   7    
HELIX  113 113 GLY J  171  ILE J  183  1                                  13    
HELIX  114 114 GLU J  189  GLY J  196  1                                   8    
HELIX  115 115 MET J  210  CYS J  216  1                                   7    
HELIX  116 116 ASN J  221  ALA J  238  1                                  18    
HELIX  117 117 ASP K   14  ILE K   18  5                                   5    
HELIX  118 118 PRO K   21  SER K   54  1                                  34    
HELIX  119 119 SER K   54  SER K   67  1                                  14    
HELIX  120 120 SER K   67  PHE K   96  1                                  30    
HELIX  121 121 THR K  102  TRP K  129  1                                  28    
HELIX  122 122 ASN L   11  SER L   40  1                                  30    
HELIX  123 123 THR L   44  SER L   54  1                                  11    
HELIX  124 124 SER L   54  VAL L   84  1                                  31    
HELIX  125 125 PRO L   86  GLY L  114  1                                  29    
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 HIS A 556  LEU A 560 -1  O  TYR A 559   N  VAL A 233           
SHEET    3  AD 3 SER A 565  ARG A 569 -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 HIS E 556  LEU E 560 -1  O  TYR E 559   N  VAL E 233           
SHEET    3  ED 3 SER E 565  ARG E 569 -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  PRO F  93  1  O  ILE F  89   N  SER F   6           
SHEET    4  FA 5 GLY F  64  MET F  67 -1  O  ASN F  66   N  ARG F  92           
SHEET    5  FA 5 LYS F  70  LEU F  73 -1  O  LYS F  70   N  MET F  67           
SHEET    1  FB 2 VAL F  99  ARG F 101  0                                        
SHEET    2  FB 2 VAL F 104  VAL F 105 -1  O  VAL F 104   N  ILE F 100           
SHEET    1  IA 6 THR I 159  SER I 162  0                                        
SHEET    2  IA 6 CYS I  33  SER I  37  1  O  CYS I  33   N  THR I 159           
SHEET    3  IA 6 VAL I   5  ILE I  13  1  O  ALA I  10   N  ALA I  34           
SHEET    4  IA 6 VAL I 190  LEU I 200  1  O  TYR I 192   N  ARG I   6           
SHEET    5  IA 6 ASP I 377  ALA I 385 -1  O  GLY I 382   N  THR I 198           
SHEET    6  IA 6 GLN I 367  VAL I 371  1  O  ALA I 368   N  VAL I 380           
SHEET    1  IB 6 THR I 159  SER I 162  0                                        
SHEET    2  IB 6 CYS I  33  SER I  37  1  O  CYS I  33   N  THR I 159           
SHEET    3  IB 6 VAL I   5  ILE I  13  1  O  ALA I  10   N  ALA I  34           
SHEET    4  IB 6 VAL I 190  LEU I 200  1  O  TYR I 192   N  ARG I   6           
SHEET    5  IB 6 VAL I 177  CYS I 184 -1  O  VAL I 178   N  ALA I 195           
SHEET    6  IB 6 TRP I 164  LYS I 171 -1  O  TYR I 165   N  LEU I 183           
SHEET    1  IC 3 ILE I  53  THR I  54  0                                        
SHEET    2  IC 3 GLN I 130  ALA I 135 -1  O  ALA I 135   N  ILE I  53           
SHEET    3  IC 3 GLN I 116  SER I 123 -1  O  ARG I 117   N  THR I 134           
SHEET    1  ID 3 VAL I 233  GLN I 234  0                                        
SHEET    2  ID 3 CYS I 555  LEU I 560 -1  O  TYR I 559   N  VAL I 233           
SHEET    3  ID 3 SER I 565  SER I 570 -1  O  SER I 565   N  LEU I 560           
SHEET    1  IE 4 TRP I 239  ILE I 246  0                                        
SHEET    2  IE 4 ILE I 347  MET I 356 -1  O  ILE I 350   N  GLY I 245           
SHEET    3  IE 4 ALA I 311  LYS I 314 -1  O  ALA I 311   N  VAL I 349           
SHEET    4  IE 4 TYR I 263  LEU I 265 -1  O  TYR I 263   N  LYS I 314           
SHEET    1  IF 2 ILE I 360  PRO I 361  0                                        
SHEET    2  IF 2 ALA I 390  CYS I 391  1  N  CYS I 391   O  ILE I 360           
SHEET    1  JA 5 ARG J  19  GLU J  26  0                                        
SHEET    2  JA 5 ARG J   2  ARG J   9 -1  O  LEU J   3   N  LEU J  25           
SHEET    3  JA 5 ILE J  89  ARG J  92  1  O  ILE J  89   N  SER J   6           
SHEET    4  JA 5 GLY J  64  MET J  67 -1  O  ASN J  66   N  ARG J  92           
SHEET    5  JA 5 LYS J  70  LEU J  73 -1  O  LYS J  70   N  MET J  67           
SHEET    1  JB 2 VAL J  99  ARG J 101  0                                        
SHEET    2  JB 2 VAL J 104  VAL J 105 -1  O  VAL J 104   N  ILE J 100           
LINK         NE2 HIS A  45                 C8M FAD A 601     1555   1555  1.50  
LINK        NA    NA A1590                 O   ALA A 390     1555   1555  2.44  
LINK        NA    NA A1590                 O   GLY A 358     1555   1555  2.44  
LINK        NA    NA A1590                 O   MET A 357     1555   1555  3.05  
LINK        NA    NA A1590                 O   GLU A 388     1555   1555  2.45  
LINK        NA    NA A1590                 O   MET A 356     1555   1555  2.64  
LINK         SG  CYS B  55                FE1  FES B 302     1555   1555  2.25  
LINK         SG  CYS B  60                FE1  FES B 302     1555   1555  2.21  
LINK         OD1 ASP B  63                FE2  FES B 302     1555   1555  1.81  
LINK         SG  CYS B  75                FE2  FES B 302     1555   1555  2.25  
LINK         SG  CYS B 149                FE3  SF4 B 303     1555   1555  2.30  
LINK         SG  CYS B 152                FE2  SF4 B 303     1555   1555  2.30  
LINK         SG  CYS B 155                FE1  SF4 B 303     1555   1555  2.35  
LINK         SG  CYS B 159                FE1  F3S B 304     1555   1555  2.26  
LINK         SG  CYS B 206                FE3  F3S B 304     1555   1555  2.30  
LINK         SG  CYS B 212                FE4  F3S B 304     1555   1555  2.30  
LINK         SG  CYS B 216                FE4  SF4 B 303     1555   1555  2.30  
LINK         SD  MET C  84                FE   HEM C1130     1555   1555  2.30  
LINK         NE2 HIS D  71                FE   HEM C1130     1555   1555  1.93  
LINK         NE2 HIS E  45                 C8M FAD E 601     1555   1555  1.50  
LINK        NA    NA E1590                 O   MET E 357     1555   1555  2.92  
LINK        NA    NA E1590                 O   GLY E 358     1555   1555  2.35  
LINK        NA    NA E1590                 O   GLU E 388     1555   1555  2.44  
LINK        NA    NA E1590                 O   ALA E 390     1555   1555  2.44  
LINK        NA    NA E1590                 O   MET E 356     1555   1555  2.60  
LINK         SG  CYS F  55                FE1  FES F 302     1555   1555  2.31  
LINK         SG  CYS F  60                FE1  FES F 302     1555   1555  2.26  
LINK         OD1 ASP F  63                FE2  FES F 302     1555   1555  1.85  
LINK         SG  CYS F  75                FE2  FES F 302     1555   1555  2.27  
LINK         SG  CYS F 149                FE4  SF4 F 303     1555   1555  2.31  
LINK         SG  CYS F 152                FE2  SF4 F 303     1555   1555  2.34  
LINK         SG  CYS F 155                FE1  SF4 F 303     1555   1555  2.29  
LINK         SG  CYS F 159                FE1  F3S F 304     1555   1555  2.27  
LINK         SG  CYS F 206                FE4  F3S F 304     1555   1555  2.31  
LINK         SG  CYS F 212                FE3  F3S F 304     1555   1555  2.29  
LINK         SG  CYS F 216                FE3  SF4 F 303     1555   1555  2.29  
LINK         SD  MET G  84                FE   HEM G1130     1555   1555  2.28  
LINK         NE2 HIS H  71                FE   HEM G1130     1555   1555  1.92  
LINK         NE2 HIS I  45                 C8M FAD I 601     1555   1555  1.49  
LINK        NA    NA I1590                 O   ALA I 390     1555   1555  2.48  
LINK        NA    NA I1590                 O   GLU I 388     1555   1555  2.43  
LINK        NA    NA I1590                 O   GLY I 358     1555   1555  2.52  
LINK        NA    NA I1590                 O   MET I 357     1555   1555  3.03  
LINK        NA    NA I1590                 O   MET I 356     1555   1555  2.52  
LINK         SG  CYS J  55                FE1  FES J 302     1555   1555  2.30  
LINK         SG  CYS J  60                FE1  FES J 302     1555   1555  2.27  
LINK         OD1 ASP J  63                FE2  FES J 302     1555   1555  1.81  
LINK         SG  CYS J  75                FE2  FES J 302     1555   1555  2.28  
LINK         SG  CYS J 149                FE2  SF4 J 303     1555   1555  2.31  
LINK         SG  CYS J 152                FE3  SF4 J 303     1555   1555  2.28  
LINK         SG  CYS J 155                FE1  SF4 J 303     1555   1555  2.32  
LINK         SG  CYS J 159                FE1  F3S J 304     1555   1555  2.32  
LINK         SG  CYS J 206                FE3  F3S J 304     1555   1555  2.31  
LINK         SG  CYS J 212                FE4  F3S J 304     1555   1555  2.28  
LINK         SG  CYS J 216                FE4  SF4 J 303     1555   1555  2.32  
LINK         SD  MET K  84                FE   HEM K1130     1555   1555  2.31  
LINK         NE2 HIS L  71                FE   HEM K1130     1555   1555  1.93  
CISPEP   1 VAL A  392    SER A  393          0        -3.42                     
CISPEP   2 VAL E  392    SER E  393          0        -6.87                     
CISPEP   3 VAL I  392    SER I  393          0        -6.59                     
SITE     1 AC1 43 ILE A  13  GLY A  14  ALA A  15  GLY A  16                    
SITE     2 AC1 43 GLY A  17  ALA A  18  SER A  37  LYS A  38                    
SITE     3 AC1 43 VAL A  39  SER A  44  HIS A  45  THR A  46                    
SITE     4 AC1 43 SER A  48  ALA A  49  GLN A  50  GLY A  51                    
SITE     5 AC1 43 GLY A  52  TRP A 164  TYR A 165  ALA A 166                    
SITE     6 AC1 43 ALA A 201  THR A 202  GLY A 203  THR A 213                    
SITE     7 AC1 43 ASN A 214  ASP A 221  LEU A 252  HIS A 354                    
SITE     8 AC1 43 TYR A 355  GLY A 387  GLU A 388  ARG A 399                    
SITE     9 AC1 43 GLY A 402  ASN A 403  SER A 404  LEU A 405                    
SITE    10 AC1 43 LEU A 408  TEO A1589  HOH A2029  HOH A2117                    
SITE    11 AC1 43 HOH A2168  HOH A2277  HOH A2278                               
SITE     1 AC2 10 SER B  54  CYS B  55  ARG B  56  GLY B  58                    
SITE     2 AC2 10 VAL B  59  CYS B  60  GLY B  61  ASP B  63                    
SITE     3 AC2 10 LEU B  73  CYS B  75                                          
SITE     1 AC3  8 CYS B 149  ILE B 150  CYS B 152  ALA B 153                    
SITE     2 AC3  8 CYS B 155  CYS B 216  PRO B 217  LYS B 218                    
SITE     1 AC4  8 CYS B 159  CYS B 206  HIS B 207  ILE B 209                    
SITE     2 AC4  8 MET B 210  ASN B 211  CYS B 212  THR B 223                    
SITE     1 AC5 42 GLY E  14  ALA E  15  GLY E  16  GLY E  17                    
SITE     2 AC5 42 ALA E  18  SER E  37  LYS E  38  VAL E  39                    
SITE     3 AC5 42 SER E  44  HIS E  45  THR E  46  SER E  48                    
SITE     4 AC5 42 ALA E  49  GLN E  50  GLY E  51  GLY E  52                    
SITE     5 AC5 42 TRP E 164  TYR E 165  ALA E 166  ALA E 201                    
SITE     6 AC5 42 THR E 202  GLY E 203  THR E 213  ASN E 214                    
SITE     7 AC5 42 ASP E 221  LEU E 252  HIS E 354  TYR E 355                    
SITE     8 AC5 42 GLY E 387  GLU E 388  ARG E 399  GLY E 402                    
SITE     9 AC5 42 ASN E 403  SER E 404  LEU E 405  LEU E 408                    
SITE    10 AC5 42 TEO E1589  HOH E2075  HOH E2085  HOH E2086                    
SITE    11 AC5 42 HOH E2196  HOH E2197                                          
SITE     1 AC6  8 SER F  54  CYS F  55  ARG F  56  GLY F  58                    
SITE     2 AC6  8 CYS F  60  GLY F  61  ASP F  63  CYS F  75                    
SITE     1 AC7  9 CYS F 149  ILE F 150  CYS F 152  ALA F 153                    
SITE     2 AC7  9 CYS F 155  ALA F 173  CYS F 216  PRO F 217                    
SITE     3 AC7  9 LYS F 218                                                     
SITE     1 AC8  9 CYS F 159  PRO F 172  CYS F 206  HIS F 207                    
SITE     2 AC8  9 SER F 208  MET F 210  ASN F 211  CYS F 212                    
SITE     3 AC8  9 THR F 223                                                     
SITE     1 AC9 41 GLY I  14  ALA I  15  GLY I  16  GLY I  17                    
SITE     2 AC9 41 ALA I  18  SER I  37  LYS I  38  VAL I  39                    
SITE     3 AC9 41 SER I  44  HIS I  45  THR I  46  SER I  48                    
SITE     4 AC9 41 ALA I  49  GLN I  50  GLY I  51  GLY I  52                    
SITE     5 AC9 41 TRP I 164  TYR I 165  ALA I 166  ALA I 201                    
SITE     6 AC9 41 THR I 202  GLY I 203  THR I 213  ASN I 214                    
SITE     7 AC9 41 ASP I 221  LEU I 252  HIS I 354  TYR I 355                    
SITE     8 AC9 41 GLY I 387  GLU I 388  ARG I 399  GLY I 402                    
SITE     9 AC9 41 ASN I 403  SER I 404  LEU I 405  LEU I 408                    
SITE    10 AC9 41 TEO I1589  HOH I2071  HOH I2074  HOH I2082                    
SITE    11 AC9 41 HOH I2167                                                     
SITE     1 BC1  9 SER J  54  CYS J  55  ARG J  56  GLY J  58                    
SITE     2 BC1  9 VAL J  59  CYS J  60  GLY J  61  ASP J  63                    
SITE     3 BC1  9 CYS J  75                                                     
SITE     1 BC2  8 CYS J 149  ILE J 150  CYS J 152  ALA J 153                    
SITE     2 BC2  8 CYS J 155  CYS J 216  PRO J 217  LYS J 218                    
SITE     1 BC3  9 CYS J 159  CYS J 206  HIS J 207  SER J 208                    
SITE     2 BC3  9 ILE J 209  MET J 210  ASN J 211  CYS J 212                    
SITE     3 BC3  9 THR J 223                                                     
SITE     1 BC4 21 HIS B 207  HIS C  30  ARG C  31  THR C  37                    
SITE     2 BC4 21 PHE C  38  MET C  84  VAL C  85  GLY C  88                    
SITE     3 BC4 21 ILE C  89  HIS C  91  CBE C1131  VAL D  19                    
SITE     4 BC4 21 ARG D  20  ALA D  23  LEU D  26  THR D  27                    
SITE     5 BC4 21 ILE D  30  HIS D  71  GLY D  75  VAL D  79                    
SITE     6 BC4 21 HOH D2012                                                     
SITE     1 BC5 11 PRO B 160  SER B 161  TRP B 164  HIS B 207                    
SITE     2 BC5 11 PHE C  20  SER C  27  ILE C  28  ARG C  31                    
SITE     3 BC5 11 HEM C1130  ASP D  82  TYR D  83                               
SITE     1 BC6 12 GLY A  51  PHE A 119  HIS A 242  LEU A 252                    
SITE     2 BC6 12 THR A 254  GLU A 255  ARG A 286  HIS A 354                    
SITE     3 BC6 12 ARG A 399  GLY A 401  GLY A 402  FAD A 601                    
SITE     1 BC7  5 MET A 356  MET A 357  GLY A 358  GLU A 388                    
SITE     2 BC7  5 ALA A 390                                                     
SITE     1 BC8 21 HIS F 207  HIS G  30  ARG G  31  GLY G  34                    
SITE     2 BC8 21 MET G  84  VAL G  85  GLY G  88  ILE G  89                    
SITE     3 BC8 21 HIS G  91  CBE G1131  HOH G2007  VAL H  19                    
SITE     4 BC8 21 ARG H  20  ALA H  23  LEU H  26  THR H  27                    
SITE     5 BC8 21 ILE H  30  HIS H  71  GLY H  75  VAL H  79                    
SITE     6 BC8 21 HOH H2004                                                     
SITE     1 BC9 10 PRO F 160  SER F 161  TRP F 164  PHE G  20                    
SITE     2 BC9 10 SER G  27  ILE G  28  ARG G  31  HEM G1130                    
SITE     3 BC9 10 ASP H  82  TYR H  83                                          
SITE     1 CC1 12 GLN E  50  GLY E  51  HIS E 242  LEU E 252                    
SITE     2 CC1 12 THR E 254  GLU E 255  ARG E 286  HIS E 354                    
SITE     3 CC1 12 ARG E 399  GLY E 401  GLY E 402  FAD E 601                    
SITE     1 CC2  5 MET E 356  MET E 357  GLY E 358  GLU E 388                    
SITE     2 CC2  5 ALA E 390                                                     
SITE     1 CC3 18 HIS J 207  ARG K  31  GLY K  34  PHE K  38                    
SITE     2 CC3 18 MET K  84  VAL K  85  GLY K  88  HIS K  91                    
SITE     3 CC3 18 CBE K1131  HOH K2010  VAL L  19  ARG L  20                    
SITE     4 CC3 18 LEU L  26  THR L  27  ILE L  30  HIS L  71                    
SITE     5 CC3 18 GLY L  75  VAL L  79                                          
SITE     1 CC4  9 SER J 161  TRP J 164  PHE K  20  SER K  27                    
SITE     2 CC4  9 ILE K  28  ARG K  31  HEM K1130  ASP L  82                    
SITE     3 CC4  9 TYR L  83                                                     
SITE     1 CC5 12 GLY I  51  PHE I 119  HIS I 242  LEU I 252                    
SITE     2 CC5 12 THR I 254  GLU I 255  ARG I 286  HIS I 354                    
SITE     3 CC5 12 ARG I 399  GLY I 401  GLY I 402  FAD I 601                    
SITE     1 CC6  5 MET I 356  MET I 357  GLY I 358  GLU I 388                    
SITE     2 CC6  5 ALA I 390                                                     
CRYST1  120.033  183.363  202.720  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      0.008331  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005454  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004933        0.00000                         
MTRIX1   1  0.947310  0.259860 -0.187270        3.41661    1                    
MTRIX2   1  0.292520 -0.463700  0.836310      -26.42373    1                    
MTRIX3   1  0.130490 -0.847030 -0.515290     -101.08395    1                    
MTRIX1   2  0.950220  0.273140  0.149940       19.06854    1                    
MTRIX2   2  0.265980 -0.460380 -0.846940      -99.14578    1                    
MTRIX3   2 -0.162300  0.844660 -0.510110      -30.12042    1                    
MTRIX1   3  0.950190  0.249710 -0.186510        2.65864    1                    
MTRIX2   3  0.286610 -0.464930  0.837670      -26.24914    1                    
MTRIX3   3  0.122460 -0.849400 -0.513340     -100.98786    1                    
MTRIX1   4  0.949580  0.282940  0.135060       18.32764    1                    
MTRIX2   4  0.257620 -0.458650 -0.850460      -99.13770    1                    
MTRIX3   4 -0.178680  0.842370 -0.508410      -29.64193    1                    
MTRIX1   5  0.950010  0.247200 -0.190730        2.30747    1                    
MTRIX2   5  0.288200 -0.459260  0.840250      -25.93887    1                    
MTRIX3   5  0.120120 -0.853210 -0.507540     -100.95502    1                    
MTRIX1   6  0.947320  0.295130  0.124440       18.01566    1                    
MTRIX2   6  0.254550 -0.457900 -0.851780      -99.04029    1                    
MTRIX3   6 -0.194410  0.838580 -0.508910      -29.22209    1                    
MTRIX1   7  0.950430  0.244880 -0.191610        2.14672    1                    
MTRIX2   7  0.287330 -0.456170  0.842230      -25.66306    1                    
MTRIX3   7  0.118840 -0.855540 -0.503920     -100.90508    1                    
MTRIX1   8  0.948490  0.290800  0.125690       17.88715    1                    
MTRIX2   8  0.252220 -0.453110 -0.855030      -98.93965    1                    
MTRIX3   8 -0.191690  0.842690 -0.503110      -28.91714    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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