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Entry: 2WU5
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HEADER    OXIDOREDUCTASE                          29-SEP-09   2WU5              
TITLE     CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE     
TITLE    2 (SQR) SDHD HIS71MET 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 2WU5    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) SDHD HIS71MET MUTANT                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.803                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.827                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.01                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.49                          
REMARK   3   NUMBER OF REFLECTIONS             : 106952                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2153                          
REMARK   3   R VALUE            (WORKING SET) : 0.2134                          
REMARK   3   FREE R VALUE                     : 0.2515                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 5417                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.8338 -  8.6916    0.96     3653   170  0.2384 0.2534        
REMARK   3     2  8.6916 -  6.9059    0.99     3593   189  0.1988 0.1963        
REMARK   3     3  6.9059 -  6.0350    0.99     3551   193  0.2152 0.2321        
REMARK   3     4  6.0350 -  5.4842    0.99     3540   184  0.2028 0.1978        
REMARK   3     5  5.4842 -  5.0916    1.00     3548   181  0.1920 0.2346        
REMARK   3     6  5.0916 -  4.7917    1.00     3526   187  0.1864 0.2068        
REMARK   3     7  4.7917 -  4.5520    1.00     3532   184  0.1839 0.2296        
REMARK   3     8  4.5520 -  4.3540    1.00     3515   180  0.1838 0.2075        
REMARK   3     9  4.3540 -  4.1864    1.00     3498   201  0.1987 0.2420        
REMARK   3    10  4.1864 -  4.0421    1.00     3490   171  0.1973 0.2524        
REMARK   3    11  4.0421 -  3.9157    1.00     3462   204  0.1961 0.2239        
REMARK   3    12  3.9157 -  3.8039    0.99     3507   188  0.1873 0.2264        
REMARK   3    13  3.8039 -  3.7038    0.99     3441   184  0.1929 0.2475        
REMARK   3    14  3.7038 -  3.6134    0.99     3475   179  0.1896 0.2404        
REMARK   3    15  3.6134 -  3.5313    0.99     3424   187  0.1968 0.2292        
REMARK   3    16  3.5313 -  3.4562    0.99     3462   187  0.1998 0.2833        
REMARK   3    17  3.4562 -  3.3871    0.98     3414   186  0.2060 0.2242        
REMARK   3    18  3.3871 -  3.3232    0.97     3385   178  0.2078 0.2666        
REMARK   3    19  3.3232 -  3.2638    0.97     3376   193  0.2179 0.2735        
REMARK   3    20  3.2638 -  3.2085    0.96     3316   198  0.2283 0.2887        
REMARK   3    21  3.2085 -  3.1568    0.96     3300   180  0.2280 0.2885        
REMARK   3    22  3.1568 -  3.1082    0.95     3319   174  0.2478 0.3136        
REMARK   3    23  3.1082 -  3.0625    0.94     3234   187  0.2486 0.2916        
REMARK   3    24  3.0625 -  3.0194    0.93     3216   164  0.2460 0.3189        
REMARK   3    25  3.0194 -  2.9786    0.93     3234   189  0.2499 0.3337        
REMARK   3    26  2.9786 -  2.9399    0.92     3195   141  0.2568 0.3058        
REMARK   3    27  2.9399 -  2.9032    0.90     3177   163  0.2605 0.3377        
REMARK   3    28  2.9032 -  2.8682    0.89     3067   162  0.2636 0.3338        
REMARK   3    29  2.8682 -  2.8349    0.88     3061   163  0.2644 0.3333        
REMARK   3    30  2.8349 -  2.8030    0.88     3024   170  0.2880 0.3638        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.327                                         
REMARK   3   B_SOL              : 39.970                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.35             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.76            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.32                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -18.6210                                             
REMARK   3    B22 (A**2) : -11.3313                                             
REMARK   3    B33 (A**2) : -3.4983                                              
REMARK   3    B12 (A**2) : -0.0000                                              
REMARK   3    B13 (A**2) : -0.0000                                              
REMARK   3    B23 (A**2) : -0.0000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          25555                                  
REMARK   3   ANGLE     :  0.565          34647                                  
REMARK   3   CHIRALITY :  0.039           3831                                  
REMARK   3   PLANARITY :  0.002           4437                                  
REMARK   3   DIHEDRAL  : 15.475           9240                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.5439 -11.3503 -24.2218              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0146 T22:   0.0205                                     
REMARK   3      T33:   0.0453 T12:   0.0249                                     
REMARK   3      T13:   0.0069 T23:   0.0755                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1172 L22:   0.6689                                     
REMARK   3      L33:   0.3155 L12:  -0.0242                                     
REMARK   3      L13:   0.0446 L23:   0.1393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0242 S12:   0.1250 S13:   0.0304                       
REMARK   3      S21:   0.1269 S22:  -0.1543 S23:   0.2932                       
REMARK   3      S31:   0.1160 S32:  -0.1092 S33:   0.0459                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  28.9760  -8.7535 -30.3883              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0796 T22:   0.1962                                     
REMARK   3      T33:   0.1532 T12:  -0.0254                                     
REMARK   3      T13:  -0.0386 T23:   0.1092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5481 L22:   0.7038                                     
REMARK   3      L33:   0.3871 L12:  -0.2682                                     
REMARK   3      L13:   0.4022 L23:  -0.2630                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0553 S12:   0.3210 S13:   0.2015                       
REMARK   3      S21:   0.0568 S22:  -0.0514 S23:  -0.1511                       
REMARK   3      S31:  -0.0051 S32:   0.2483 S33:   0.1050                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  60.9567  -5.7010 -31.4346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1184 T22:   0.3966                                     
REMARK   3      T33:   0.4908 T12:  -0.0624                                     
REMARK   3      T13:  -0.0853 T23:   0.1932                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1007 L22:   0.8172                                     
REMARK   3      L33:   0.9898 L12:   0.0313                                     
REMARK   3      L13:   0.3128 L23:  -0.0376                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0566 S12:   0.4089 S13:   0.1958                       
REMARK   3      S21:  -0.0024 S22:  -0.0473 S23:  -0.4919                       
REMARK   3      S31:  -0.0399 S32:   0.3129 S33:   0.1235                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  67.0466 -17.7337 -37.9493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0419 T22:   0.6139                                     
REMARK   3      T33:   0.4460 T12:  -0.0127                                     
REMARK   3      T13:   0.0305 T23:   0.1887                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0206 L22:   0.8906                                     
REMARK   3      L33:   1.1799 L12:  -0.1061                                     
REMARK   3      L13:  -0.1342 L23:   0.3416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0905 S12:   0.4238 S13:   0.0285                       
REMARK   3      S21:  -0.0196 S22:   0.1637 S23:  -0.4462                       
REMARK   3      S31:   0.0533 S32:   0.6077 S33:  -0.0502                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN E                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6564 -72.3672 -27.1661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2524 T22:  -0.1844                                     
REMARK   3      T33:  -0.0275 T12:  -0.1222                                     
REMARK   3      T13:  -0.2201 T23:  -0.3149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4649 L22:   1.1080                                     
REMARK   3      L33:   0.3721 L12:   0.1557                                     
REMARK   3      L13:   0.2195 L23:   0.4148                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1679 S12:  -0.0432 S13:  -0.4404                       
REMARK   3      S21:   0.5867 S22:   0.0463 S23:   0.2724                       
REMARK   3      S31:   0.1030 S32:  -0.0745 S33:  -0.1083                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN F                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  38.6248 -61.2289 -26.8333              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2345 T22:   0.2003                                     
REMARK   3      T33:   0.1552 T12:   0.1115                                     
REMARK   3      T13:  -0.2157 T23:  -0.1222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6406 L22:   0.5252                                     
REMARK   3      L33:   0.5882 L12:   0.3229                                     
REMARK   3      L13:   0.2853 L23:   0.5110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1223 S12:   0.2486 S13:  -0.1803                       
REMARK   3      S21:   0.2082 S22:   0.0397 S23:  -0.2632                       
REMARK   3      S31:   0.2303 S32:   0.1435 S33:  -0.2183                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN G                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  69.8470 -53.6098 -29.5882              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0953 T22:   0.2238                                     
REMARK   3      T33:   0.3146 T12:   0.2404                                     
REMARK   3      T13:  -0.2525 T23:  -0.0634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5037 L22:   0.8812                                     
REMARK   3      L33:   0.3528 L12:  -0.5454                                     
REMARK   3      L13:   0.3648 L23:  -0.2365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0255 S12:   0.2723 S13:   0.0644                       
REMARK   3      S21:   0.0263 S22:  -0.1275 S23:  -0.3866                       
REMARK   3      S31:   0.1021 S32:   0.1867 S33:   0.0693                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN H                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  71.4022 -41.1047 -37.5828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1784 T22:   0.3952                                     
REMARK   3      T33:   0.3545 T12:   0.1329                                     
REMARK   3      T13:  -0.2311 T23:   0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3962 L22:   2.1750                                     
REMARK   3      L33:   0.6098 L12:  -0.2844                                     
REMARK   3      L13:   0.3823 L23:   0.2055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0748 S12:   0.6214 S13:   0.2217                       
REMARK   3      S21:  -0.0132 S22:   0.0053 S23:  -0.9385                       
REMARK   3      S31:   0.1104 S32:   0.3482 S33:  -0.0853                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN I                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9018 -40.0618 -80.1364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4594 T22:   0.9347                                     
REMARK   3      T33:  -0.1452 T12:   0.1837                                     
REMARK   3      T13:  -0.3233 T23:  -0.0394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8045 L22:   1.4198                                     
REMARK   3      L33:   0.0067 L12:   0.0351                                     
REMARK   3      L13:   0.1234 L23:   0.0821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1530 S12:   0.9054 S13:   0.2623                       
REMARK   3      S21:  -1.1299 S22:   0.1486 S23:  -0.0727                       
REMARK   3      S31:   0.0236 S32:   0.0290 S33:  -0.1342                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN J                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  33.6884 -38.8354 -75.0103              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4123 T22:   0.9986                                     
REMARK   3      T33:  -0.0067 T12:   0.1936                                     
REMARK   3      T13:   0.0798 T23:  -0.0664                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7781 L22:   1.3181                                     
REMARK   3      L33:   0.0447 L12:  -0.1257                                     
REMARK   3      L13:   0.0105 L23:  -0.2528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1542 S12:   0.7005 S13:  -0.0982                       
REMARK   3      S21:  -0.8165 S22:  -0.0421 S23:  -0.0554                       
REMARK   3      S31:   0.0651 S32:  -0.0504 S33:  -0.0830                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN K                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  65.0360 -31.6568 -72.7062              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5580 T22:   1.1990                                     
REMARK   3      T33:   0.5568 T12:   0.0646                                     
REMARK   3      T13:   0.2725 T23:  -0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9918 L22:   0.2226                                     
REMARK   3      L33:   0.8426 L12:   0.3117                                     
REMARK   3      L13:  -0.9134 L23:  -0.3012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:  -0.0857 S13:  -0.0470                       
REMARK   3      S21:  -0.2202 S22:   0.0654 S23:  -0.1643                       
REMARK   3      S31:  -0.0642 S32:   0.2400 S33:  -0.0581                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN L                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  68.9129 -29.7560 -58.3853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2229 T22:   1.1083                                     
REMARK   3      T33:   0.3558 T12:   0.1835                                     
REMARK   3      T13:   0.1682 T23:   0.0199                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0050 L22:   0.7591                                     
REMARK   3      L33:   0.4272 L12:  -0.0693                                     
REMARK   3      L13:   0.0109 L23:  -0.2850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0679 S12:  -0.1882 S13:   0.0278                       
REMARK   3      S21:  -0.1678 S22:  -0.3393 S23:  -0.3087                       
REMARK   3      S31:   0.0070 S32:   0.3460 S33:   0.2257                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 4                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:588 )                 
REMARK   3     SELECTION          : CHAIN E AND (RESSEQ 1:588 )                 
REMARK   3     ATOM PAIRS NUMBER  : 4522                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:588 )                 
REMARK   3     SELECTION          : CHAIN I AND (RESSEQ 1:588 )                 
REMARK   3     ATOM PAIRS NUMBER  : 4522                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:238 )                 
REMARK   3     SELECTION          : CHAIN F AND (RESSEQ 1:238 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1869                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B AND (RESSEQ 1:238 )                 
REMARK   3     SELECTION          : CHAIN J AND (RESSEQ 1:238 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1869                                        
REMARK   3     RMSD               : 0.003                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C AND (RESSEQ 8:129 )                 
REMARK   3     SELECTION          : CHAIN G AND (RESSEQ 8:129 )                 
REMARK   3     ATOM PAIRS NUMBER  : 948                                         
REMARK   3     RMSD               : 0.002                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C AND (RESSEQ 8:129 )                 
REMARK   3     SELECTION          : CHAIN K AND (RESSEQ 8:129 )                 
REMARK   3     ATOM PAIRS NUMBER  : 948                                         
REMARK   3     RMSD               : 0.002                                       
REMARK   3   NCS GROUP : 4                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 11:115 )                
REMARK   3     SELECTION          : CHAIN H AND (RESSEQ 11:115 )                
REMARK   3     ATOM PAIRS NUMBER  : 834                                         
REMARK   3     RMSD               : 0.004                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN D AND (RESSEQ 11:115 )                
REMARK   3     SELECTION          : CHAIN L AND (RESSEQ 11:115 )                
REMARK   3     ATOM PAIRS NUMBER  : 834                                         
REMARK   3     RMSD               : 0.034                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DENSITY FOR THE N-TERMINUS OF SDH C       
REMARK   3  (RESIDUES 1-7 OF CHAINS C, G, K) AND THE N-TERMINUS OF SDHD         
REMARK   3  (RESIDUES 1-10 OF CHAINS D, H AND L) WAS WEAK AND THESE REGIONS     
REMARK   3  ARE NOT INCLUDED IN THE MODEL. THE SIDE CHAIN OF SDHD TRP113 IS     
REMARK   3  TRUNCATED AT THE CBETA ATOM SINCE DENSITY FOR THE SIDE CHAIN WAS    
REMARK   3  POOR.                                                               
REMARK   4                                                                      
REMARK   4 2WU5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-SEP-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41283.                                       
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   : 110749                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.80                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.97                              
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  : 12.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.57                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.90                               
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   (%): 60.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.5, 0.1M MGSO4, 11.5%      
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       60.03000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      101.71000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.91000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      101.71000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.03000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.91000            
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: 15570 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.6 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: 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: 15630 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.1 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: 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: 15500 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.4 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, HIS  71 TO MET                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, HIS  71 TO MET                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, HIS  71 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: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  50      -70.28   -113.67                                   
REMARK 500    ALA A 138     -129.71     56.23                                   
REMARK 500    LEU A 167      -67.68    -91.75                                   
REMARK 500    ALA A 205       48.32   -155.38                                   
REMARK 500    ALA A 249      -38.39   -133.20                                   
REMARK 500    LYS A 281     -127.39     56.28                                   
REMARK 500    HIS A 354      -54.93   -131.22                                   
REMARK 500    ASN A 398      113.65   -166.21                                   
REMARK 500    PHE A 471       35.59   -142.06                                   
REMARK 500    SER A 472     -148.95    -88.37                                   
REMARK 500    VAL B  14      -50.26   -131.19                                   
REMARK 500    SER B  54      -77.38   -160.64                                   
REMARK 500    ARG B  56       16.32     45.18                                   
REMARK 500    ASP B 102     -109.44     50.06                                   
REMARK 500    LYS B 118       76.18     50.66                                   
REMARK 500    ARG B 131     -105.19   -124.87                                   
REMARK 500    ASP B 199     -178.96    -63.85                                   
REMARK 500    SER D  40       -8.94   -155.12                                   
REMARK 500    GLN E  50      -70.12   -113.90                                   
REMARK 500    ALA E 138     -129.66     56.24                                   
REMARK 500    LEU E 167      -67.49    -92.10                                   
REMARK 500    ALA E 205       48.22   -155.41                                   
REMARK 500    ALA E 249      -38.59   -133.31                                   
REMARK 500    LYS E 281     -127.51     56.36                                   
REMARK 500    HIS E 354      -54.96   -131.62                                   
REMARK 500    ASN E 398      113.65   -166.36                                   
REMARK 500    PHE E 471       35.45   -141.88                                   
REMARK 500    SER E 472     -148.72    -87.91                                   
REMARK 500    VAL F  14      -50.08   -131.40                                   
REMARK 500    SER F  54      -77.45   -160.79                                   
REMARK 500    ARG F  56       16.56     45.05                                   
REMARK 500    ASP F 102     -109.33     49.97                                   
REMARK 500    LYS F 118       76.20     50.58                                   
REMARK 500    ARG F 131     -105.18   -125.02                                   
REMARK 500    ASP F 199     -178.69    -63.97                                   
REMARK 500    SER H  40       -8.81   -155.13                                   
REMARK 500    GLN I  50      -70.22   -113.59                                   
REMARK 500    ALA I 138     -129.49     56.24                                   
REMARK 500    LEU I 167      -67.67    -92.06                                   
REMARK 500    ALA I 205       48.11   -155.42                                   
REMARK 500    ALA I 249      -38.37   -133.24                                   
REMARK 500    LYS I 281     -127.46     56.12                                   
REMARK 500    HIS I 354      -54.88   -131.36                                   
REMARK 500    ASN I 398      113.67   -166.55                                   
REMARK 500    PHE I 471       35.45   -141.82                                   
REMARK 500    SER I 472     -148.76    -88.09                                   
REMARK 500    VAL J  14      -50.42   -131.24                                   
REMARK 500    SER J  54      -77.57   -160.80                                   
REMARK 500    ARG J  56       16.30     45.19                                   
REMARK 500    ASP J 102     -109.47     49.91                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1590  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 390   O                                                      
REMARK 620 2 GLY A 358   O    99.2                                              
REMARK 620 3 MET A 356   O   169.8  71.9                                        
REMARK 620 4 GLU A 388   O    95.5  80.6  78.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA E1590  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET E 356   O                                                      
REMARK 620 2 GLY E 358   O    70.0                                              
REMARK 620 3 GLU E 388   O    78.2  76.9                                        
REMARK 620 4 ALA E 390   O   161.7  92.9  92.1                                  
REMARK 620 N                    1     2     3                                   
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 GLU I 388   O    78.6                                              
REMARK 620 3 ALA I 390   O   154.8  89.3                                        
REMARK 620 N                    1     2                                         
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  103.2                                              
REMARK 620 3 FES B 302  FE2  121.0 135.4                                        
REMARK 620 4 FES B 302   S1  106.9 118.9  45.5                                  
REMARK 620 5 FES B 302   S2  119.9 117.3  45.4  90.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES B 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 FES B 302  FE1                                                     
REMARK 620 2 FES B 302   S1   45.4                                              
REMARK 620 3 FES B 302   S2   45.5  90.8                                        
REMARK 620 4 ASP B  63   OD1 120.3 113.0 104.4                                  
REMARK 620 5 CYS B  75   SG  113.1 103.4 113.0 126.6                            
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 ASP F  63   OD1                                                    
REMARK 620 2 CYS F  75   SG  130.8                                              
REMARK 620 3 FES F 302  FE2  117.0 112.0                                        
REMARK 620 4 FES F 302   S1  112.4 104.2  45.5                                  
REMARK 620 5 FES F 302   S2  102.1 109.3  45.4  90.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES F 302  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F  55   SG                                                     
REMARK 620 2 FES F 302  FE1  121.8                                              
REMARK 620 3 FES F 302   S1  107.1  45.5                                        
REMARK 620 4 FES F 302   S2  119.3  45.5  90.8                                  
REMARK 620 5 CYS F  60   SG   99.8 137.8 119.4 120.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES J 302  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J  63   OD2                                                    
REMARK 620 2 CYS J  75   SG   93.2                                              
REMARK 620 3 ASP J  63   OD1  53.0 125.5                                        
REMARK 620 4 FES J 302  FE2  137.2 109.2 124.7                                  
REMARK 620 5 FES J 302   S1  170.3  93.8 117.2  45.4                            
REMARK 620 6 FES J 302   S2   92.2 115.8 107.8  45.5  90.8                      
REMARK 620 N                    1     2     3     4     5                       
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  55   SG                                                     
REMARK 620 2 CYS J  60   SG  100.1                                              
REMARK 620 3 FES J 302  FE1  123.1 130.5                                        
REMARK 620 4 FES J 302   S1   97.3 112.3  45.3                                  
REMARK 620 5 FES J 302   S2  132.3 120.0  45.5  90.8                            
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 SF4 B 303  FE4                                                     
REMARK 620 2 CYS B 155   SG  143.7                                              
REMARK 620 3 SF4 B 303  FE2   59.9 140.2                                        
REMARK 620 4 SF4 B 303  FE3   59.9 149.9  59.9                                  
REMARK 620 5 SF4 B 303   S2   53.8 118.0 101.6  53.8                            
REMARK 620 6 SF4 B 303   S3   53.8 108.4  53.7 101.6 105.1                      
REMARK 620 7 SF4 B 303   S4  101.6 114.2  53.7  53.8 105.1 104.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B 303  FE4                                                     
REMARK 620 2 SF4 B 303   S1   53.8                                              
REMARK 620 3 SF4 B 303  FE1   59.9 101.7                                        
REMARK 620 4 SF4 B 303  FE3   60.0  53.8  60.0                                  
REMARK 620 5 SF4 B 303   S3   53.8 105.1  53.8 101.8                            
REMARK 620 6 SF4 B 303   S4  101.6 105.2  53.6  53.8 104.9                      
REMARK 620 7 CYS B 216   SG  139.8 113.9 143.8 150.1 108.0 118.5                
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  FE4  138.5                                              
REMARK 620 3 SF4 B 303   S1  127.2  53.8                                        
REMARK 620 4 SF4 B 303  FE1  129.2  60.0 101.8                                  
REMARK 620 5 SF4 B 303  FE2  160.7  60.0  53.8  60.1                            
REMARK 620 6 SF4 B 303   S2   96.4  53.8 105.1  53.7 101.8                      
REMARK 620 7 SF4 B 303   S4  115.0 101.6 105.2  53.7  53.8 105.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 303  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 B 303   S1                                                     
REMARK 620 2 CYS B 152   SG  120.3                                              
REMARK 620 3 SF4 B 303  FE1  101.9 136.4                                        
REMARK 620 4 SF4 B 303  FE2   53.8 138.7  60.2                                  
REMARK 620 5 SF4 B 303  FE3   53.9 156.6  60.1  60.0                            
REMARK 620 6 SF4 B 303   S2  105.2 117.6  53.8 101.9  53.9                      
REMARK 620 7 SF4 B 303   S3  105.1 101.5  53.9  53.8 101.8 105.2                
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   S2   53.8                                              
REMARK 620 3 SF4 F 303  FE2   59.9 101.7                                        
REMARK 620 4 SF4 F 303  FE3   59.9  53.7  60.0                                  
REMARK 620 5 SF4 F 303   S3   53.8 105.1  53.7 101.7                            
REMARK 620 6 SF4 F 303   S4  101.6 105.0  53.9  53.7 105.2                      
REMARK 620 7 CYS F 155   SG  148.2 113.7 144.4 141.3 116.9 110.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 F 303  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SF4 F 303  FE4                                                     
REMARK 620 2 CYS F 152   SG  156.7                                              
REMARK 620 3 SF4 F 303  FE3   60.0 136.3                                        
REMARK 620 4 SF4 F 303   S1   53.8 117.6  53.7                                  
REMARK 620 5 SF4 F 303  FE1   60.1 138.6  60.1 101.8                            
REMARK 620 6 SF4 F 303   S3   53.9 120.4 101.9 105.2  53.9                      
REMARK 620 7 SF4 F 303   S4  101.8 101.4  53.8 105.0  53.9 105.3                
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   S2   53.8                                              
REMARK 620 3 SF4 F 303  FE2   59.9 101.5                                        
REMARK 620 4 SF4 F 303   S1   53.8 105.1  53.8                                  
REMARK 620 5 SF4 F 303  FE1   60.0  53.7  59.8 101.7                            
REMARK 620 6 CYS F 216   SG  148.7 119.8 138.7 111.5 146.2                      
REMARK 620 7 SF4 F 303   S4  101.7 104.9  53.8 105.1  53.7 109.2                
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   S2                                                     
REMARK 620 2 SF4 F 303  FE2  101.6                                              
REMARK 620 3 SF4 F 303  FE3   53.8  60.1                                        
REMARK 620 4 SF4 F 303   S1  105.1  53.9  53.8                                  
REMARK 620 5 CYS F 149   SG  120.2 135.6 159.9 120.7                            
REMARK 620 6 SF4 F 303  FE1   53.7  59.9  60.1 101.7 135.2                      
REMARK 620 7 SF4 F 303   S3  105.0  53.7 101.8 105.1  98.3  53.8                
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   59.9                                              
REMARK 620 3 SF4 J 303  FE4   59.9  59.8                                        
REMARK 620 4 SF4 J 303   S2  101.6  53.7  53.8                                  
REMARK 620 5 SF4 J 303   S3   53.7 101.6  53.8 105.1                            
REMARK 620 6 CYS J 155   SG  141.3 148.4 144.4 117.0 109.9                      
REMARK 620 7 SF4 J 303   S4   53.7  53.7 101.5 105.0 105.0 113.9                
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 CYS J 152   SG                                                     
REMARK 620 2 SF4 J 303  FE3  137.5                                              
REMARK 620 3 SF4 J 303  FE4  155.9  60.0                                        
REMARK 620 4 SF4 J 303   S1  117.9  53.8  53.8                                  
REMARK 620 5 SF4 J 303   S3  119.5 101.8  53.9 105.2                            
REMARK 620 6 SF4 J 303  FE1  138.7  60.1  60.1 101.9  53.7                      
REMARK 620 7 SF4 J 303   S4  102.3  53.8 101.8 105.1 105.1  53.8                
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 216   SG                                                     
REMARK 620 2 SF4 J 303  FE2  141.5                                              
REMARK 620 3 SF4 J 303  FE4  150.0  60.0                                        
REMARK 620 4 SF4 J 303   S1  115.8  53.8  53.8                                  
REMARK 620 5 SF4 J 303   S2  116.5 101.6  53.9 105.3                            
REMARK 620 6 SF4 J 303  FE1  142.1  60.0  60.0 101.8  53.6                      
REMARK 620 7 SF4 J 303   S4  108.2  53.8 101.8 105.1 105.0  53.8                
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   60.1                                              
REMARK 620 3 SF4 J 303   S1   53.8  53.9                                        
REMARK 620 4 SF4 J 303   S2  101.7  53.8 105.3                                  
REMARK 620 5 SF4 J 303   S3   53.8 101.8 105.1 104.9                            
REMARK 620 6 CYS J 149   SG  133.5 161.4 119.9 122.0  96.8                      
REMARK 620 7 SF4 J 303  FE1   60.1  60.1 101.9  53.6  53.7 135.0                
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  FE3  144.7                                              
REMARK 620 3 F3S B 304   S1  109.7  53.4                                        
REMARK 620 4 F3S B 304   S3  116.5  53.4 103.5                                  
REMARK 620 5 F3S B 304   S2  114.0 101.3 108.9 103.5                            
REMARK 620 6 F3S B 304  FE4  146.6  60.2 103.7  52.9  53.0                      
REMARK 620 N                    1     2     3     4     5                       
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 212   SG                                                     
REMARK 620 2 F3S B 304   S1  114.8                                              
REMARK 620 3 F3S B 304   S3  118.4 103.3                                        
REMARK 620 4 F3S B 304  FE1  151.6  53.3  53.3                                  
REMARK 620 5 F3S B 304  FE4  141.2 103.7  52.9  60.3                            
REMARK 620 6 F3S B 304   S4  106.0 110.6 103.0 102.3  52.9                      
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 F3S B 304  FE3                                                     
REMARK 620 2 F3S B 304   S3   53.1                                              
REMARK 620 3 CYS B 206   SG  141.9 116.0                                        
REMARK 620 4 F3S B 304  FE1   59.5  52.9 149.5                                  
REMARK 620 5 F3S B 304   S2  100.6 103.5 117.3  52.9                            
REMARK 620 6 F3S B 304   S4   53.0 103.4 108.7 101.7 106.7                      
REMARK 620 N                    1     2     3     4     5                       
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   60.1                                              
REMARK 620 3 F3S F 304   S3   53.3  52.9                                        
REMARK 620 4 F3S F 304   S1   53.2 103.7 103.2                                  
REMARK 620 5 F3S F 304   S2  101.9  53.0 103.3 110.1                            
REMARK 620 6 CYS F 159   SG  142.8 145.2 113.2 110.9 115.3                      
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  FE4  143.4                                              
REMARK 620 3 F3S F 304   S3  123.7  53.0                                        
REMARK 620 4 F3S F 304   S4  103.8  52.9 103.0                                  
REMARK 620 5 F3S F 304  FE1  153.3  60.3  53.3 102.4                            
REMARK 620 6 F3S F 304   S1  111.6 103.8 103.2 111.0  53.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S F 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S F 304  FE3                                                     
REMARK 620 2 F3S F 304   S3   53.1                                              
REMARK 620 3 F3S F 304   S4   53.1 103.3                                        
REMARK 620 4 F3S F 304  FE1   59.6  53.0 102.0                                  
REMARK 620 5 CYS F 206   SG  137.3 115.0 104.7 152.9                            
REMARK 620 6 F3S F 304   S2  101.4 103.4 108.0  53.0 121.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S J 304  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S J 304   S1                                                     
REMARK 620 2 CYS J 159   SG  106.8                                              
REMARK 620 3 F3S J 304  FE3   53.1 143.3                                        
REMARK 620 4 F3S J 304  FE4  102.3 150.9  59.6                                  
REMARK 620 5 F3S J 304   S2  108.1 114.9 101.3  53.1                            
REMARK 620 6 F3S J 304   S3  103.2 119.2  53.1  53.0 103.6                      
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 CYS J 212   SG                                                     
REMARK 620 2 F3S J 304   S1  108.2                                              
REMARK 620 3 F3S J 304  FE1  149.2  53.1                                        
REMARK 620 4 F3S J 304  FE4  147.7 103.0  60.4                                  
REMARK 620 5 F3S J 304   S3  124.3 103.3  53.2  53.4                            
REMARK 620 6 F3S J 304   S4  105.9 111.8 104.1  53.3 103.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             F3S J 304  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 F3S J 304  FE1                                                     
REMARK 620 2 F3S J 304  FE3   60.0                                              
REMARK 620 3 F3S J 304   S2   52.9 101.5                                        
REMARK 620 4 F3S J 304   S3   53.0  53.3 103.4                                  
REMARK 620 5 CYS J 206   SG  143.5 135.5 122.5 105.4                            
REMARK 620 6 F3S J 304   S4  103.7  53.3 110.0 103.1 110.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HEM C 305   NA                                                     
REMARK 620 2 HEM C 305   ND   91.0                                              
REMARK 620 3 HEM C 305   NB   88.7 175.7                                        
REMARK 620 4 HEM C 305   NC  178.0  91.0  89.4                                  
REMARK 620 5 HIS C  84   NE2  92.9  79.3  96.5  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G 305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET H  71   SD                                                     
REMARK 620 2 HEM G 305   NA   85.2                                              
REMARK 620 3 HEM G 305   ND   93.1  90.6                                        
REMARK 620 4 HEM G 305   NC   96.2 178.0  90.8                                  
REMARK 620 5 HIS G  84   NE2 173.3  88.1  86.9  90.5                            
REMARK 620 6 HEM G 305   NB   92.9  89.2 174.0  89.3  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K 305  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  84   NE2                                                    
REMARK 620 2 HEM K 305   NA   93.9                                              
REMARK 620 3 HEM K 305   NB   89.7  88.8                                        
REMARK 620 4 HEM K 305   NC   86.5 177.9  89.1                                  
REMARK 620 5 HEM K 305   ND   84.2  91.2 173.9  90.9                            
REMARK 620 N                    1     2     3     4                             
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 HEM C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES F 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S F 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES J 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 J 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S J 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE C1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE G1130                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE K1130                 
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 TEO A1589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO I1589                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A1590                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E1590                  
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: 1NEN   RELATED DB: PDB                                   
REMARK 900 MOLECULAR ARCHITECTURE OF SUCCINATE DEHYDROGENASE                    
REMARK 900 (COMPLEXII) PREVENTS REACTIVE OXYGEN SPECIES GENERATION              
REMARK 900 RELATED ID: 1NEK   RELATED DB: PDB                                   
REMARK 900 SUCCINATE DEHYDOGENASE FROM E.COLI                                   
REMARK 900 RELATED ID: 2WU2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE                  
REMARK 900 OXIDOREDUCTASE (SQR) SDHC HIS84MET MUTANT                            
REMARK 900 RELATED ID: 2ACZ   RELATED DB: PDB                                   
REMARK 900 COMPLEX II (SUCCINATE DEHYDROGENASE) FROM E. COLI                    
REMARK 900 WITHATPENIN A5 INHIBITOR CO-CRYSTALLIZED AT THE                      
REMARK 900 UBIQUINONEBINDING SITE                                               
REMARK 900 RELATED ID: 2WDV   RELATED DB: PDB                                   
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH AN              
REMARK 900 EMPTY QUINONE-BINDING POCKET                                         
DBREF  2WU5 A    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WU5 B    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WU5 C    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WU5 D    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WU5 E    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WU5 F    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WU5 G    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WU5 H    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
DBREF  2WU5 I    1   588  UNP    P0AC41   DHSA_ECOLI       1    588             
DBREF  2WU5 J    1   238  UNP    P07014   DHSB_ECOLI       1    238             
DBREF  2WU5 K    1   129  UNP    P69054   DHSC_ECOLI       1    129             
DBREF  2WU5 L    1   115  UNP    P0AC44   DHSD_ECOLI       1    115             
SEQADV 2WU5 MET D   71  UNP  P0AC44    HIS    71 ENGINEERED MUTATION            
SEQADV 2WU5 MET H   71  UNP  P0AC44    HIS    71 ENGINEERED MUTATION            
SEQADV 2WU5 MET L   71  UNP  P0AC44    HIS    71 ENGINEERED MUTATION            
SEQRES   1 A  588  MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE          
SEQRES   2 A  588  GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE          
SEQRES   3 A  588  SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL          
SEQRES   4 A  588  PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY          
SEQRES   5 A  588  ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP          
SEQRES   6 A  588  GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR          
SEQRES   7 A  588  ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR          
SEQRES   8 A  588  GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU          
SEQRES   9 A  588  PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG          
SEQRES  10 A  588  PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN          
SEQRES  11 A  588  ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS          
SEQRES  12 A  588  ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN          
SEQRES  13 A  588  HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU          
SEQRES  14 A  588  VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA          
SEQRES  15 A  588  LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA          
SEQRES  16 A  588  ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE          
SEQRES  17 A  588  TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP          
SEQRES  18 A  588  GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN          
SEQRES  19 A  588  ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA          
SEQRES  20 A  588  GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU          
SEQRES  21 A  588  GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET          
SEQRES  22 A  588  GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG          
SEQRES  23 A  588  ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU          
SEQRES  24 A  588  GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS          
SEQRES  25 A  588  LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER          
SEQRES  26 A  588  ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA          
SEQRES  27 A  588  HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO          
SEQRES  28 A  588  THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL          
SEQRES  29 A  588  THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP          
SEQRES  30 A  588  VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA          
SEQRES  31 A  588  CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN          
SEQRES  32 A  588  SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY          
SEQRES  33 A  588  LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU          
SEQRES  34 A  588  ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP          
SEQRES  35 A  588  ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP          
SEQRES  36 A  588  PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN          
SEQRES  37 A  588  HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA          
SEQRES  38 A  588  LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU          
SEQRES  39 A  588  LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN          
SEQRES  40 A  588  THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET          
SEQRES  41 A  588  GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG          
SEQRES  42 A  588  THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO          
SEQRES  43 A  588  ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR          
SEQRES  44 A  588  LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN          
SEQRES  45 A  588  MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE          
SEQRES  46 A  588  ARG THR TYR                                                  
SEQRES   1 B  238  MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP          
SEQRES   2 B  238  VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU          
SEQRES   3 B  238  ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU          
SEQRES   4 B  238  ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG          
SEQRES   5 B  238  ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU          
SEQRES   6 B  238  ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO          
SEQRES   7 B  238  ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE          
SEQRES   8 B  238  ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL          
SEQRES   9 B  238  VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE          
SEQRES  10 B  238  LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA          
SEQRES  11 B  238  ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU          
SEQRES  12 B  238  ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER          
SEQRES  13 B  238  THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE          
SEQRES  14 B  238  ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU          
SEQRES  15 B  238  ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP          
SEQRES  16 B  238  GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER          
SEQRES  17 B  238  ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN          
SEQRES  18 B  238  PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU          
SEQRES  19 B  238  GLN ARG ASN ALA                                              
SEQRES   1 C  129  MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU          
SEQRES   2 C  129  ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA          
SEQRES   3 C  129  SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL          
SEQRES   4 C  129  ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU          
SEQRES   5 C  129  SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET          
SEQRES   6 C  129  GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU          
SEQRES   7 C  129  THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS          
SEQRES   8 C  129  MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU          
SEQRES   9 C  129  ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR          
SEQRES  10 C  129  VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP              
SEQRES   1 D  115  MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL          
SEQRES   2 D  115  HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU          
SEQRES   3 D  115  THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR          
SEQRES   4 D  115  SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE          
SEQRES   5 D  115  ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU          
SEQRES   6 D  115  PHE SER ILE LEU ILE MET 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 HIS VAL VAL VAL GLY ILE ARG HIS          
SEQRES   8 G  129  MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU          
SEQRES   9 G  129  ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR          
SEQRES  10 G  129  VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP              
SEQRES   1 H  115  MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL          
SEQRES   2 H  115  HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU          
SEQRES   3 H  115  THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR          
SEQRES   4 H  115  SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE          
SEQRES   5 H  115  ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU          
SEQRES   6 H  115  PHE SER ILE LEU ILE MET 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 HIS VAL VAL VAL GLY ILE ARG HIS          
SEQRES   8 K  129  MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU          
SEQRES   9 K  129  ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR          
SEQRES  10 K  129  VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP              
SEQRES   1 L  115  MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL          
SEQRES   2 L  115  HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU          
SEQRES   3 L  115  THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR          
SEQRES   4 L  115  SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE          
SEQRES   5 L  115  ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU          
SEQRES   6 L  115  PHE SER ILE LEU ILE MET 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  C 305      43                                                       
HET    CBE  C1130      16                                                       
HET    FAD  E 601      53                                                       
HET    TEO  E1589       9                                                       
HET     NA  E1590       1                                                       
HET    FES  F 302       4                                                       
HET    SF4  F 303       8                                                       
HET    F3S  F 304       7                                                       
HET    HEM  G 305      43                                                       
HET    CBE  G1130      16                                                       
HET    FAD  I 601      53                                                       
HET    TEO  I1589       9                                                       
HET     NA  I1590       1                                                       
HET    FES  J 302       4                                                       
HET    SF4  J 303       8                                                       
HET    F3S  J 304       7                                                       
HET    HEM  K 305      43                                                       
HET    CBE  K1130      16                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     TEO MALATE LIKE INTERMEDIATE                                         
HETNAM      NA SODIUM ION                                                       
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     F3S FE3-S4 CLUSTER                                                   
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CBE 2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE        
HETSYN     HEM HEME                                                             
HETSYN     CBE 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-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   *222(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  ASN A  156  1                                  17    
HELIX    7   7 ALA A  205  TYR A  209  5                                   5    
HELIX    8   8 GLY A  220  ALA A  229  1                                  10    
HELIX    9   9 GLU A  255  GLU A  260  1                                   6    
HELIX   10  10 PHE A  272  ALA A  277  1                                   6    
HELIX   11  11 ALA A  280  ALA A  284  5                                   5    
HELIX   12  12 GLY A  285  GLU A  299  1                                  15    
HELIX   13  13 LEU A  315  LEU A  318  5                                   4    
HELIX   14  14 GLY A  319  LEU A  327  1                                   9    
HELIX   15  15 LEU A  327  ALA A  338  1                                  12    
HELIX   16  16 GLY A  402  HIS A  418  1                                  17    
HELIX   17  17 HIS A  418  GLY A  427  1                                  10    
HELIX   18  18 SER A  433  SER A  440  1                                   8    
HELIX   19  19 LEU A  441  ASN A  450  1                                  10    
HELIX   20  20 ASP A  455  PHE A  471  1                                  17    
HELIX   21  21 GLU A  476  LYS A  495  1                                  20    
HELIX   22  22 ASN A  507  ARG A  533  1                                  27    
HELIX   23  23 MET B   34  ASP B   46  1                                  13    
HELIX   24  24 ILE B   79  LEU B   82  5                                   4    
HELIX   25  25 MET B  107  ILE B  117  1                                  11    
HELIX   26  26 MET B  136  LYS B  142  1                                   7    
HELIX   27  27 CYS B  155  SER B  158  5                                   4    
HELIX   28  28 CYS B  159  ASN B  165  1                                   7    
HELIX   29  29 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  LEU C  127  1                                  26    
HELIX   38  38 ASN D   11  ALA D   38  1                                  28    
HELIX   39  39 THR D   44  PHE D   52  1                                   9    
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  HIS E  418  1                                  17    
HELIX   58  58 HIS E  418  GLY E  427  1                                  10    
HELIX   59  59 SER E  433  SER E  440  1                                   8    
HELIX   60  60 LEU E  441  ASN E  450  1                                  10    
HELIX   61  61 ASP E  455  PHE E  471  1                                  17    
HELIX   62  62 GLU E  476  LYS E  495  1                                  20    
HELIX   63  63 ASN E  507  ARG E  533  1                                  27    
HELIX   64  64 MET F   34  ASP F   46  1                                  13    
HELIX   65  65 ILE F   79  LEU F   82  5                                   4    
HELIX   66  66 MET F  107  ILE F  117  1                                  11    
HELIX   67  67 MET F  136  LYS F  142  1                                   7    
HELIX   68  68 CYS F  155  SER F  158  5                                   4    
HELIX   69  69 CYS F  159  ASN F  165  1                                   7    
HELIX   70  70 ILE F  170  ILE F  183  1                                  14    
HELIX   71  71 GLU F  189  GLY F  196  1                                   8    
HELIX   72  72 MET F  210  CYS F  216  1                                   7    
HELIX   73  73 ASN F  221  ALA F  238  1                                  18    
HELIX   74  74 ASP G   14  ILE G   18  5                                   5    
HELIX   75  75 PRO G   21  SER G   54  1                                  34    
HELIX   76  76 SER G   54  SER G   67  1                                  14    
HELIX   77  77 SER G   67  PHE G   96  1                                  30    
HELIX   78  78 THR G  102  LEU G  127  1                                  26    
HELIX   79  79 ASN H   11  ALA H   38  1                                  28    
HELIX   80  80 THR H   44  PHE H   52  1                                   9    
HELIX   81  81 SER H   54  VAL H   84  1                                  31    
HELIX   82  82 PRO H   86  GLY H  114  1                                  29    
HELIX   83  83 GLY I   16  SER I   29  1                                  14    
HELIX   84  84 PHE I   40  SER I   44  5                                   5    
HELIX   85  85 SER I   44  ALA I   49  5                                   6    
HELIX   86  86 ASN I   64  SER I   76  1                                  13    
HELIX   87  87 ASP I   81  MET I  102  1                                  22    
HELIX   88  88 ARG I  140  ASN I  156  1                                  17    
HELIX   89  89 ALA I  205  TYR I  209  5                                   5    
HELIX   90  90 GLY I  220  ALA I  229  1                                  10    
HELIX   91  91 GLU I  255  GLU I  260  1                                   6    
HELIX   92  92 PHE I  272  ALA I  277  1                                   6    
HELIX   93  93 ALA I  280  ALA I  284  5                                   5    
HELIX   94  94 GLY I  285  GLU I  299  1                                  15    
HELIX   95  95 LEU I  315  LEU I  318  5                                   4    
HELIX   96  96 GLY I  319  LEU I  327  1                                   9    
HELIX   97  97 LEU I  327  ALA I  338  1                                  12    
HELIX   98  98 GLY I  402  HIS I  418  1                                  17    
HELIX   99  99 HIS I  418  GLY I  427  1                                  10    
HELIX  100 100 SER I  433  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 ILE J   79  LEU J   82  5                                   4    
HELIX  107 107 MET J  107  ILE J  117  1                                  11    
HELIX  108 108 MET J  136  LYS J  142  1                                   7    
HELIX  109 109 CYS J  155  SER J  158  5                                   4    
HELIX  110 110 CYS J  159  ASN J  165  1                                   7    
HELIX  111 111 ILE J  170  ILE J  183  1                                  14    
HELIX  112 112 GLU J  189  GLY J  196  1                                   8    
HELIX  113 113 MET J  210  CYS J  216  1                                   7    
HELIX  114 114 ASN J  221  ALA J  238  1                                  18    
HELIX  115 115 ASP K   14  ILE K   18  5                                   5    
HELIX  116 116 PRO K   21  SER K   54  1                                  34    
HELIX  117 117 SER K   54  SER K   67  1                                  14    
HELIX  118 118 SER K   67  PHE K   96  1                                  30    
HELIX  119 119 THR K  102  LEU K  127  1                                  26    
HELIX  120 120 ASN L   11  ALA L   38  1                                  28    
HELIX  121 121 THR L   44  PHE L   52  1                                   9    
HELIX  122 122 SER L   54  VAL L   84  1                                  31    
HELIX  123 123 PRO L   86  GLY L  114  1                                  29    
SHEET    1  AA 6 THR A 159  SER A 162  0                                        
SHEET    2  AA 6 CYS A  33  SER A  37  1  O  CYS A  33   N  THR A 159           
SHEET    3  AA 6 VAL A   5  ILE A  13  1  O  ALA A  10   N  ALA A  34           
SHEET    4  AA 6 VAL A 190  LEU A 200  1  O  TYR A 192   N  ARG A   6           
SHEET    5  AA 6 ASP A 377  ALA A 385 -1  O  GLY A 382   N  THR A 198           
SHEET    6  AA 6 GLN A 367  VAL A 371  1  O  ALA A 368   N  VAL A 380           
SHEET    1  AB 6 THR A 159  SER A 162  0                                        
SHEET    2  AB 6 CYS A  33  SER A  37  1  O  CYS A  33   N  THR A 159           
SHEET    3  AB 6 VAL A   5  ILE A  13  1  O  ALA A  10   N  ALA A  34           
SHEET    4  AB 6 VAL A 190  LEU A 200  1  O  TYR A 192   N  ARG A   6           
SHEET    5  AB 6 VAL A 177  CYS A 184 -1  O  VAL A 178   N  ALA A 195           
SHEET    6  AB 6 TRP A 164  LYS A 171 -1  O  TYR A 165   N  LEU A 183           
SHEET    1  AC 3 ILE A  53  THR A  54  0                                        
SHEET    2  AC 3 THR A 134  ALA A 135 -1  O  ALA A 135   N  ILE A  53           
SHEET    3  AC 3 GLN A 116  ARG A 117 -1  O  ARG A 117   N  THR A 134           
SHEET    1  AD 3 VAL A 233  GLN A 234  0                                        
SHEET    2  AD 3 CYS A 555  LEU A 560 -1  O  TYR A 559   N  VAL A 233           
SHEET    3  AD 3 SER A 565  SER A 570 -1  O  SER A 565   N  LEU A 560           
SHEET    1  AE 4 TRP A 239  ILE A 246  0                                        
SHEET    2  AE 4 ILE A 347  MET A 356 -1  O  ILE A 350   N  GLY A 245           
SHEET    3  AE 4 ALA A 311  LYS A 314 -1  O  ALA A 311   N  VAL A 349           
SHEET    4  AE 4 TYR A 263  LEU A 265 -1  O  TYR A 263   N  LYS A 314           
SHEET    1  AF 2 ILE A 360  PRO A 361  0                                        
SHEET    2  AF 2 ALA A 390  CYS A 391  1  N  CYS A 391   O  ILE A 360           
SHEET    1  BA 5 ARG B  19  GLU B  26  0                                        
SHEET    2  BA 5 ARG B   2  ARG B   9 -1  O  LEU B   3   N  LEU B  25           
SHEET    3  BA 5 ILE B  89  ARG B  92  1  O  ILE B  89   N  SER B   6           
SHEET    4  BA 5 GLY B  64  MET B  67 -1  O  ASN B  66   N  ARG B  92           
SHEET    5  BA 5 LYS B  70  LEU B  73 -1  O  LYS B  70   N  MET B  67           
SHEET    1  BB 2 VAL B  99  ARG B 101  0                                        
SHEET    2  BB 2 VAL B 104  VAL B 105 -1  O  VAL B 104   N  ILE B 100           
SHEET    1  EA 6 THR E 159  SER E 162  0                                        
SHEET    2  EA 6 CYS E  33  SER E  37  1  O  CYS E  33   N  THR E 159           
SHEET    3  EA 6 VAL E   5  ILE E  13  1  O  ALA E  10   N  ALA E  34           
SHEET    4  EA 6 VAL E 190  LEU E 200  1  O  TYR E 192   N  ARG E   6           
SHEET    5  EA 6 ASP E 377  ALA E 385 -1  O  GLY E 382   N  THR E 198           
SHEET    6  EA 6 GLN E 367  VAL E 371  1  O  ALA E 368   N  VAL E 380           
SHEET    1  EB 6 THR E 159  SER E 162  0                                        
SHEET    2  EB 6 CYS E  33  SER E  37  1  O  CYS E  33   N  THR E 159           
SHEET    3  EB 6 VAL E   5  ILE E  13  1  O  ALA E  10   N  ALA E  34           
SHEET    4  EB 6 VAL E 190  LEU E 200  1  O  TYR E 192   N  ARG E   6           
SHEET    5  EB 6 VAL E 177  CYS E 184 -1  O  VAL E 178   N  ALA E 195           
SHEET    6  EB 6 TRP E 164  LYS E 171 -1  O  TYR E 165   N  LEU E 183           
SHEET    1  EC 3 ILE E  53  THR E  54  0                                        
SHEET    2  EC 3 THR E 134  ALA E 135 -1  O  ALA E 135   N  ILE E  53           
SHEET    3  EC 3 GLN E 116  ARG E 117 -1  O  ARG E 117   N  THR E 134           
SHEET    1  ED 3 VAL E 233  GLN E 234  0                                        
SHEET    2  ED 3 CYS E 555  LEU E 560 -1  O  TYR E 559   N  VAL E 233           
SHEET    3  ED 3 SER E 565  SER E 570 -1  O  SER E 565   N  LEU E 560           
SHEET    1  EE 4 TRP E 239  ILE E 246  0                                        
SHEET    2  EE 4 ILE E 347  MET E 356 -1  O  ILE E 350   N  GLY E 245           
SHEET    3  EE 4 ALA E 311  LYS E 314 -1  O  ALA E 311   N  VAL E 349           
SHEET    4  EE 4 TYR E 263  LEU E 265 -1  O  TYR E 263   N  LYS E 314           
SHEET    1  EF 2 ILE E 360  PRO E 361  0                                        
SHEET    2  EF 2 ALA E 390  CYS E 391  1  N  CYS E 391   O  ILE E 360           
SHEET    1  FA 5 ARG F  19  GLU F  26  0                                        
SHEET    2  FA 5 ARG F   2  ARG F   9 -1  O  LEU F   3   N  LEU F  25           
SHEET    3  FA 5 ILE F  89  ARG F  92  1  O  ILE F  89   N  SER F   6           
SHEET    4  FA 5 GLY F  64  MET F  67 -1  O  ASN F  66   N  ARG F  92           
SHEET    5  FA 5 LYS F  70  LEU F  73 -1  O  LYS F  70   N  MET F  67           
SHEET    1  FB 2 VAL F  99  ARG F 101  0                                        
SHEET    2  FB 2 VAL F 104  VAL F 105 -1  O  VAL F 104   N  ILE F 100           
SHEET    1  IA 6 THR I 159  SER I 162  0                                        
SHEET    2  IA 6 CYS I  33  SER I  37  1  O  CYS I  33   N  THR I 159           
SHEET    3  IA 6 VAL I   5  ILE I  13  1  O  ALA I  10   N  ALA I  34           
SHEET    4  IA 6 VAL I 190  LEU I 200  1  O  TYR I 192   N  ARG I   6           
SHEET    5  IA 6 ASP I 377  ALA I 385 -1  O  GLY I 382   N  THR I 198           
SHEET    6  IA 6 GLN I 367  VAL I 371  1  O  ALA I 368   N  VAL I 380           
SHEET    1  IB 6 THR I 159  SER I 162  0                                        
SHEET    2  IB 6 CYS I  33  SER I  37  1  O  CYS I  33   N  THR I 159           
SHEET    3  IB 6 VAL I   5  ILE I  13  1  O  ALA I  10   N  ALA I  34           
SHEET    4  IB 6 VAL I 190  LEU I 200  1  O  TYR I 192   N  ARG I   6           
SHEET    5  IB 6 VAL I 177  CYS I 184 -1  O  VAL I 178   N  ALA I 195           
SHEET    6  IB 6 TRP I 164  LYS I 171 -1  O  TYR I 165   N  LEU I 183           
SHEET    1  IC 3 ILE I  53  THR I  54  0                                        
SHEET    2  IC 3 THR I 134  ALA I 135 -1  O  ALA I 135   N  ILE I  53           
SHEET    3  IC 3 GLN I 116  ARG I 117 -1  O  ARG I 117   N  THR I 134           
SHEET    1  ID 3 VAL I 233  GLN I 234  0                                        
SHEET    2  ID 3 CYS I 555  LEU I 560 -1  O  TYR I 559   N  VAL I 233           
SHEET    3  ID 3 SER I 565  SER I 570 -1  O  SER I 565   N  LEU I 560           
SHEET    1  IE 4 TRP I 239  ILE I 246  0                                        
SHEET    2  IE 4 ILE I 347  MET I 356 -1  O  ILE I 350   N  GLY I 245           
SHEET    3  IE 4 ALA I 311  LYS I 314 -1  O  ALA I 311   N  VAL I 349           
SHEET    4  IE 4 TYR I 263  LEU I 265 -1  O  TYR I 263   N  LYS I 314           
SHEET    1  IF 2 ILE I 360  PRO I 361  0                                        
SHEET    2  IF 2 ALA I 390  CYS I 391  1  N  CYS I 391   O  ILE I 360           
SHEET    1  JA 5 ARG J  19  GLU J  26  0                                        
SHEET    2  JA 5 ARG J   2  ARG J   9 -1  O  LEU J   3   N  LEU J  25           
SHEET    3  JA 5 ILE J  89  ARG J  92  1  O  ILE J  89   N  SER J   6           
SHEET    4  JA 5 GLY J  64  MET J  67 -1  O  ASN J  66   N  ARG J  92           
SHEET    5  JA 5 LYS J  70  LEU J  73 -1  O  LYS J  70   N  MET J  67           
SHEET    1  JB 2 VAL J  99  ARG J 101  0                                        
SHEET    2  JB 2 VAL J 104  VAL J 105 -1  O  VAL J 104   N  ILE J 100           
LINK         NE2 HIS A  45                 C8M FAD A 601     1555   1555  1.65  
LINK        NA    NA A1590                 O   ALA A 390     1555   1555  2.30  
LINK        NA    NA A1590                 O   GLY A 358     1555   1555  2.85  
LINK        NA    NA A1590                 O   MET A 356     1555   1555  3.01  
LINK        NA    NA A1590                 O   GLU A 388     1555   1555  3.10  
LINK         SG  CYS B  55                FE1  FES B 302     1555   1555  2.19  
LINK         SG  CYS B  60                FE1  FES B 302     1555   1555  2.09  
LINK         OD1 ASP B  63                FE2  FES B 302     1555   1555  1.85  
LINK         SG  CYS B  75                FE2  FES B 302     1555   1555  2.19  
LINK         SG  CYS B 149                FE3  SF4 B 303     1555   1555  2.28  
LINK         SG  CYS B 152                FE4  SF4 B 303     1555   1555  2.29  
LINK         SG  CYS B 155                FE1  SF4 B 303     1555   1555  2.38  
LINK         SG  CYS B 159                FE1  F3S B 304     1555   1555  2.23  
LINK         SG  CYS B 206                FE4  F3S B 304     1555   1555  2.24  
LINK         SG  CYS B 212                FE3  F3S B 304     1555   1555  2.33  
LINK         SG  CYS B 216                FE2  SF4 B 303     1555   1555  2.32  
LINK         NE2 HIS C  84                FE   HEM C 305     1555   1555  2.04  
LINK         SD  MET D  71                FE   HEM C 305     1555   1555  2.56  
LINK         NE2 HIS E  45                 C8M FAD E 601     1555   1555  1.52  
LINK        NA    NA E1590                 O   GLY E 358     1555   1555  3.06  
LINK        NA    NA E1590                 O   MET E 356     1555   1555  2.97  
LINK        NA    NA E1590                 O   GLU E 388     1555   1555  3.16  
LINK        NA    NA E1590                 O   ALA E 390     1555   1555  2.40  
LINK         SG  CYS F  55                FE2  FES F 302     1555   1555  2.25  
LINK         SG  CYS F  60                FE2  FES F 302     1555   1555  2.14  
LINK         OD1 ASP F  63                FE1  FES F 302     1555   1555  1.83  
LINK         SG  CYS F  75                FE1  FES F 302     1555   1555  2.14  
LINK         SG  CYS F 149                FE4  SF4 F 303     1555   1555  2.28  
LINK         SG  CYS F 152                FE2  SF4 F 303     1555   1555  2.35  
LINK         SG  CYS F 155                FE1  SF4 F 303     1555   1555  2.23  
LINK         SG  CYS F 159                FE1  F3S F 304     1555   1555  2.17  
LINK         SG  CYS F 206                FE4  F3S F 304     1555   1555  2.26  
LINK         SG  CYS F 212                FE3  F3S F 304     1555   1555  2.38  
LINK         SG  CYS F 216                FE3  SF4 F 303     1555   1555  2.36  
LINK         NE2 HIS G  84                FE   HEM G 305     1555   1555  2.05  
LINK         SD  MET H  71                FE   HEM G 305     1555   1555  2.49  
LINK         NE2 HIS I  45                 C8M FAD I 601     1555   1555  1.55  
LINK        NA    NA I1590                 O   MET I 356     1555   1555  2.91  
LINK        NA    NA I1590                 O   GLU I 388     1555   1555  3.18  
LINK        NA    NA I1590                 O   ALA I 390     1555   1555  2.52  
LINK         SG  CYS J  55                FE2  FES J 302     1555   1555  2.21  
LINK         SG  CYS J  60                FE2  FES J 302     1555   1555  2.17  
LINK         OD1 ASP J  63                FE1  FES J 302     1555   1555  1.76  
LINK         CG  ASP J  63                FE1  FES J 302     1555   1555  2.49  
LINK         OD2 ASP J  63                FE1  FES J 302     1555   1555  2.74  
LINK         SG  CYS J  75                FE1  FES J 302     1555   1555  2.29  
LINK         SG  CYS J 149                FE4  SF4 J 303     1555   1555  2.37  
LINK         SG  CYS J 152                FE2  SF4 J 303     1555   1555  2.36  
LINK         SG  CYS J 155                FE1  SF4 J 303     1555   1555  2.29  
LINK         SG  CYS J 159                FE1  F3S J 304     1555   1555  2.28  
LINK         SG  CYS J 206                FE4  F3S J 304     1555   1555  2.21  
LINK         SG  CYS J 212                FE3  F3S J 304     1555   1555  2.35  
LINK         SG  CYS J 216                FE3  SF4 J 303     1555   1555  2.23  
LINK         NE2 HIS K  84                FE   HEM K 305     1555   1555  2.08  
LINK         SD  MET L  71                FE   HEM K 305     1555   1555  2.53  
CISPEP   1 VAL A  392    SER A  393          0         0.80                     
CISPEP   2 VAL E  392    SER E  393          0         0.83                     
CISPEP   3 VAL I  392    SER I  393          0         0.82                     
SITE     1 AC1 38 GLY A  14  ALA A  15  GLY A  16  GLY A  17                    
SITE     2 AC1 38 ALA A  18  SER A  37  LYS A  38  VAL A  39                    
SITE     3 AC1 38 SER A  44  HIS A  45  THR A  46  SER A  48                    
SITE     4 AC1 38 ALA A  49  GLN A  50  GLY A  51  GLY A  52                    
SITE     5 AC1 38 TRP A 164  TYR A 165  ALA A 166  ALA A 201                    
SITE     6 AC1 38 THR A 202  GLY A 203  THR A 213  ASN A 214                    
SITE     7 AC1 38 ASP A 221  LEU A 252  HIS A 354  TYR A 355                    
SITE     8 AC1 38 GLY A 387  GLU A 388  GLY A 402  ASN A 403                    
SITE     9 AC1 38 SER A 404  LEU A 405  LEU A 408  TEO A1589                    
SITE    10 AC1 38 HOH A2032  HOH A2066                                          
SITE     1 AC2  9 SER B  54  CYS B  55  ARG B  56  GLY B  58                    
SITE     2 AC2  9 VAL B  59  CYS B  60  GLY B  61  ASP B  63                    
SITE     3 AC2  9 CYS B  75                                                     
SITE     1 AC3  9 CYS B 149  ILE B 150  LEU B 151  CYS B 152                    
SITE     2 AC3  9 ALA B 153  CYS B 155  CYS B 216  PRO B 217                    
SITE     3 AC3  9 LYS B 218                                                     
SITE     1 AC4 10 CYS B 159  PRO B 172  CYS B 206  HIS B 207                    
SITE     2 AC4 10 SER B 208  ILE B 209  MET B 210  ASN B 211                    
SITE     3 AC4 10 CYS B 212  THR B 223                                          
SITE     1 AC5 16 HIS B 207  HIS C  30  ARG C  31  GLY C  34                    
SITE     2 AC5 16 THR C  37  PHE C  38  HIS C  84  HIS C  91                    
SITE     3 AC5 16 CBE C1130  VAL D  19  ALA D  23  LEU D  26                    
SITE     4 AC5 16 THR D  27  MET D  71  GLY D  75  GLN D  78                    
SITE     1 AC6 38 GLY E  14  ALA E  15  GLY E  16  GLY E  17                    
SITE     2 AC6 38 ALA E  18  SER E  37  LYS E  38  VAL E  39                    
SITE     3 AC6 38 SER E  44  HIS E  45  THR E  46  SER E  48                    
SITE     4 AC6 38 ALA E  49  GLN E  50  GLY E  51  GLY E  52                    
SITE     5 AC6 38 TRP E 164  TYR E 165  ALA E 166  ALA E 201                    
SITE     6 AC6 38 THR E 202  GLY E 203  THR E 213  ASN E 214                    
SITE     7 AC6 38 ASP E 221  LEU E 252  HIS E 354  TYR E 355                    
SITE     8 AC6 38 GLY E 387  GLU E 388  ARG E 399  GLY E 402                    
SITE     9 AC6 38 ASN E 403  SER E 404  LEU E 405  LEU E 408                    
SITE    10 AC6 38 TEO E1589  HOH E2015                                          
SITE     1 AC7  8 CYS F  55  ARG F  56  GLY F  58  VAL F  59                    
SITE     2 AC7  8 CYS F  60  GLY F  61  ASP F  63  CYS F  75                    
SITE     1 AC8  9 CYS F 149  ILE F 150  CYS F 152  ALA F 153                    
SITE     2 AC8  9 CYS F 154  CYS F 155  ALA F 173  CYS F 216                    
SITE     3 AC8  9 PRO F 217                                                     
SITE     1 AC9 10 CYS F 159  PRO F 172  CYS F 206  HIS F 207                    
SITE     2 AC9 10 SER F 208  ILE F 209  MET F 210  ASN F 211                    
SITE     3 AC9 10 CYS F 212  THR F 223                                          
SITE     1 BC1 19 HIS F 207  HIS G  30  ARG G  31  GLY G  34                    
SITE     2 BC1 19 THR G  37  PHE G  38  HIS G  84  VAL G  85                    
SITE     3 BC1 19 GLY G  88  HIS G  91  CBE G1130  ARG H  20                    
SITE     4 BC1 19 ALA H  23  LEU H  26  THR H  27  MET H  71                    
SITE     5 BC1 19 GLY H  75  GLN H  78  HOH H2001                               
SITE     1 BC2 37 GLY I  14  ALA I  15  GLY I  16  GLY I  17                    
SITE     2 BC2 37 ALA I  18  SER I  37  LYS I  38  VAL I  39                    
SITE     3 BC2 37 SER I  44  HIS I  45  THR I  46  SER I  48                    
SITE     4 BC2 37 ALA I  49  GLN I  50  GLY I  51  GLY I  52                    
SITE     5 BC2 37 TRP I 164  TYR I 165  ALA I 166  ALA I 201                    
SITE     6 BC2 37 THR I 202  GLY I 203  THR I 213  ASN I 214                    
SITE     7 BC2 37 ASP I 221  LEU I 252  HIS I 354  TYR I 355                    
SITE     8 BC2 37 GLY I 387  GLU I 388  GLY I 402  ASN I 403                    
SITE     9 BC2 37 SER I 404  LEU I 405  LEU I 408  TEO I1589                    
SITE    10 BC2 37 HOH I2011                                                     
SITE     1 BC3  9 SER J  54  CYS J  55  ARG J  56  GLY J  58                    
SITE     2 BC3  9 VAL J  59  CYS J  60  GLY J  61  ASP J  63                    
SITE     3 BC3  9 CYS J  75                                                     
SITE     1 BC4  8 CYS J 149  ILE J 150  CYS J 152  ALA J 153                    
SITE     2 BC4  8 CYS J 155  ALA J 173  CYS J 216  PRO J 217                    
SITE     1 BC5 11 CYS J 159  PRO J 172  CYS J 206  HIS J 207                    
SITE     2 BC5 11 SER J 208  ILE J 209  MET J 210  ASN J 211                    
SITE     3 BC5 11 CYS J 212  THR J 223  ILE J 226                               
SITE     1 BC6 17 HIS J 207  HIS K  30  ARG K  31  GLY K  34                    
SITE     2 BC6 17 THR K  37  PHE K  38  HIS K  84  VAL K  85                    
SITE     3 BC6 17 GLY K  88  HIS K  91  CBE K1130  VAL L  19                    
SITE     4 BC6 17 LEU L  26  THR L  27  MET L  71  GLY L  75                    
SITE     5 BC6 17 VAL L  79                                                     
SITE     1 BC7 11 PRO B 160  SER B 161  TRP B 164  HIS B 207                    
SITE     2 BC7 11 PHE C  20  SER C  27  ILE C  28  ARG C  31                    
SITE     3 BC7 11 HEM C 305  ASP D  82  TYR D  83                               
SITE     1 BC8  9 TRP F 164  PHE G  20  SER G  27  ILE G  28                    
SITE     2 BC8  9 ARG G  31  HEM G 305  HOH G2006  ASP H  82                    
SITE     3 BC8  9 TYR H  83                                                     
SITE     1 BC9 10 SER J 161  TRP J 164  HIS J 207  PHE K  20                    
SITE     2 BC9 10 SER K  27  ILE K  28  ARG K  31  HEM K 305                    
SITE     3 BC9 10 ASP L  82  TYR L  83                                          
SITE     1 CC1 11 GLY E  51  PHE E 119  HIS E 242  THR E 254                    
SITE     2 CC1 11 GLU E 255  ARG E 286  HIS E 354  ARG E 399                    
SITE     3 CC1 11 GLY E 401  GLY E 402  FAD E 601                               
SITE     1 CC2 11 GLY A  51  HIS A 242  LEU A 252  THR A 254                    
SITE     2 CC2 11 GLU A 255  ARG A 286  HIS A 354  ARG A 399                    
SITE     3 CC2 11 GLY A 401  GLY A 402  FAD A 601                               
SITE     1 CC3 11 GLY I  51  PHE I 119  HIS I 242  THR I 254                    
SITE     2 CC3 11 GLU I 255  ARG I 286  HIS I 354  ARG I 399                    
SITE     3 CC3 11 GLY I 401  GLY I 402  FAD I 601                               
SITE     1 CC4  5 MET A 356  MET A 357  GLY A 358  GLU A 388                    
SITE     2 CC4  5 ALA A 390                                                     
SITE     1 CC5  6 TYR E 355  MET E 356  MET E 357  GLY E 358                    
SITE     2 CC5  6 GLU E 388  ALA E 390                                          
SITE     1 CC6  6 TYR I 355  MET I 356  MET I 357  GLY I 358                    
SITE     2 CC6  6 GLU I 388  ALA I 390                                          
CRYST1  120.060  183.820  203.420  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      0.008329  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005440  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004916        0.00000                         
MTRIX1   1  0.948352  0.261599 -0.179427        3.59932    1                    
MTRIX2   1  0.286160 -0.461406  0.839772      -25.54960    1                    
MTRIX3   1  0.136895 -0.847744 -0.512435     -101.22400    1                    
MTRIX1   2  0.949003  0.275190  0.153833       19.29630    1                    
MTRIX2   2  0.270737 -0.461337 -0.844908      -99.13760    1                    
MTRIX3   2 -0.161541  0.843468 -0.512315      -30.53210    1                    
MTRIX1   3  0.950821  0.253151 -0.178478        2.96397    1                    
MTRIX2   3  0.281291 -0.464491  0.839716      -25.52650    1                    
MTRIX3   3  0.129673 -0.848624 -0.512857     -101.12100    1                    
MTRIX1   4  0.948528  0.284187  0.139759       18.54330    1                    
MTRIX2   4  0.263207 -0.462001 -0.846922      -99.08980    1                    
MTRIX3   4 -0.176116  0.840115 -0.513020      -30.31040    1                    
MTRIX1   5  0.949935  0.251144 -0.185877        2.56800    1                    
MTRIX2   5  0.285784 -0.457918  0.841807      -25.29970    1                    
MTRIX3   5  0.126299 -0.852782 -0.506765     -100.96100    1                    
MTRIX1   6  0.945986  0.296256  0.131690       18.38150    1                    
MTRIX2   6  0.262476 -0.461407 -0.847473      -98.99440    1                    
MTRIX3   6 -0.190306  0.836263 -0.514245      -29.96820    1                    
MTRIX1   7  0.950258  0.249125 -0.186939        2.41060    1                    
MTRIX2   7  0.285201 -0.454751  0.843719      -25.08070    1                    
MTRIX3   7  0.125181 -0.855066 -0.503182     -100.94600    1                    
MTRIX1   8  0.947171  0.292875  0.130732       18.12190    1                    
MTRIX2   8  0.257585 -0.451779 -0.854135      -98.79660    1                    
MTRIX3   8 -0.191093  0.842686 -0.503352      -29.09380    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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