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Entry: 2WYA
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HEADER    TRANSFERASE                             13-NOV-09   2WYA              
TITLE     CRYSTAL STRUCTURE OF HUMAN MITOCHONDRIAL 3-HYDROXY-3-                 
TITLE    2 METHYLGLUTARYL-COENZYME A SYNTHASE 2 (HMGCS2)                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROXYMETHYLGLUTARYL-COA SYNTHASE,                        
COMPND   3  MITOCHONDRIAL;                                                      
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 FRAGMENT: RESIDUES 51-508;                                           
COMPND   6 SYNONYM: HMG-COA SYNTHASE, 3-HYDROXY-3-METHYLGLUTARYL                
COMPND   7  COENZYME A SYNTHASE;                                                
COMPND   8 EC: 2.3.3.10;                                                        
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGANELLE: MITOCHONDRIA;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PNH-TRXT                                  
KEYWDS    STEROID BIOSYNTHESIS, CHOLESTEROL BIOSYNTHESIS,                       
KEYWDS   2 MITOCHONDRIA, MITOCHONDRION, PHOSPHOPROTEIN, MELAVONATE              
KEYWDS   3 PATHWAY, STEROL BIOSYNTHESIS, THIOLASE, ACETYLATION,                 
KEYWDS   4 TRANSFERASE, LIPID SYNTHESIS, TRANSIT PEPTIDE, DISEASE               
KEYWDS   5 MUTATION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.W.YUE,N.SHAFQAT,P.SAVITSKY,A.K.ROOS,C.COOPER,J.W.MURRAY,            
AUTHOR   2 F.VON DELFT,C.ARROWSMITH,M.WIKSTROM,A.EDWARDS,C.BOUNTRA,             
AUTHOR   3 U.OPPERMANN                                                          
REVDAT   3   05-MAY-10 2WYA    1       JRNL                                     
REVDAT   2   14-APR-10 2WYA    1       JRNL   REMARK                            
REVDAT   1   24-NOV-09 2WYA    0                                                
SPRSDE     24-NOV-09 2WYA      2V4W                                             
JRNL        AUTH   N.SHAFQAT,A.TURNBULL,J.ZSCHOCKE,U.OPPERMANN,                 
JRNL        AUTH 2 W.W.YUE                                                      
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN HMG-COA SYNTHASE                 
JRNL        TITL 2 ISOFORMS PROVIDE INSIGHTS INTO INHERITED                     
JRNL        TITL 3 KETOGENESIS DISORDERS AND INHIBITOR DESIGN.                  
JRNL        REF    J.MOL.BIOL.                   V. 398   497 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20346956                                                     
JRNL        DOI    10.1016/J.JMB.2010.03.034                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 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-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.700                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.358                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.33                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.93                          
REMARK   3   NUMBER OF REFLECTIONS             : 428484                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1616                          
REMARK   3   R VALUE            (WORKING SET) : 0.1614                          
REMARK   3   FREE R VALUE                     : 0.1840                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 3902                            
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 31.3637 -  5.1548    0.98    15411   147  0.1722 0.1838        
REMARK   3     2  5.1548 -  4.0944    0.99    15512   153  0.1317 0.1288        
REMARK   3     3  4.0944 -  3.5777    0.99    15485   156  0.1361 0.1714        
REMARK   3     4  3.5777 -  3.2509    0.99    15436   138  0.1494 0.1753        
REMARK   3     5  3.2509 -  3.0181    0.98    15367   132  0.1564 0.1910        
REMARK   3     6  3.0181 -  2.8403    0.98    15441   144  0.1502 0.1704        
REMARK   3     7  2.8403 -  2.6982    0.98    15318   150  0.1493 0.1566        
REMARK   3     8  2.6982 -  2.5808    0.98    15379   124  0.1546 0.1802        
REMARK   3     9  2.5808 -  2.4814    0.98    15351   136  0.1553 0.2037        
REMARK   3    10  2.4814 -  2.3959    0.98    15225   150  0.1505 0.1966        
REMARK   3    11  2.3959 -  2.3210    0.98    15291   140  0.1472 0.1504        
REMARK   3    12  2.3210 -  2.2546    0.97    15198   154  0.1394 0.1508        
REMARK   3    13  2.2546 -  2.1953    0.97    15159   128  0.1445 0.1407        
REMARK   3    14  2.1953 -  2.1418    0.97    15138   150  0.1476 0.1854        
REMARK   3    15  2.1418 -  2.0931    0.97    15298   124  0.1499 0.1657        
REMARK   3    16  2.0931 -  2.0485    0.97    15236   142  0.1491 0.1600        
REMARK   3    17  2.0485 -  2.0076    0.97    15087   142  0.1507 0.1639        
REMARK   3    18  2.0076 -  1.9697    0.97    15165   147  0.1622 0.1806        
REMARK   3    19  1.9697 -  1.9345    0.96    15049   108  0.1685 0.1898        
REMARK   3    20  1.9345 -  1.9017    0.96    15069   116  0.1741 0.2072        
REMARK   3    21  1.9017 -  1.8711    0.96    15113   130  0.1847 0.2461        
REMARK   3    22  1.8711 -  1.8423    0.96    15009   134  0.1916 0.2204        
REMARK   3    23  1.8423 -  1.8152    0.96    15080   132  0.1949 0.2348        
REMARK   3    24  1.8152 -  1.7896    0.96    15058   144  0.2114 0.2347        
REMARK   3    25  1.7896 -  1.7654    0.96    15026   154  0.2156 0.2837        
REMARK   3    26  1.7654 -  1.7425    0.96    14912   120  0.2305 0.2214        
REMARK   3    27  1.7425 -  1.7207    0.94    14874   133  0.2404 0.2504        
REMARK   3    28  1.7207 -  1.7000    0.90    13895   174  0.2575 0.2868        
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              : 0.400                                         
REMARK   3   B_SOL              : 59.486                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.19             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.59            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.4143                                              
REMARK   3    B22 (A**2) : 2.3857                                               
REMARK   3    B33 (A**2) : 0.0286                                               
REMARK   3    B12 (A**2) : -0.2111                                              
REMARK   3    B13 (A**2) : 1.4191                                               
REMARK   3    B23 (A**2) : 1.7399                                               
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      :  0.007          14969                                  
REMARK   3   ANGLE     :  1.138          20371                                  
REMARK   3   CHIRALITY :  0.079           2225                                  
REMARK   3   PLANARITY :  0.005           2633                                  
REMARK   3   DIHEDRAL  : 19.555           5615                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 49:204)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -12.2921  40.3885  12.5831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0682 T22:   0.0679                                     
REMARK   3      T33:   0.0705 T12:   0.0015                                     
REMARK   3      T13:  -0.0135 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5131 L22:   0.4737                                     
REMARK   3      L33:   0.4337 L12:   0.0808                                     
REMARK   3      L13:  -0.2023 L23:  -0.2561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0057 S12:   0.0727 S13:   0.0796                       
REMARK   3      S21:   0.0289 S22:   0.0309 S23:   0.0563                       
REMARK   3      S31:  -0.0732 S32:  -0.0530 S33:  -0.0221                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 205:287)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.9594  32.7699  13.1274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0714 T22:   0.0988                                     
REMARK   3      T33:   0.0643 T12:   0.0025                                     
REMARK   3      T13:  -0.0147 T23:  -0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3539 L22:   0.3486                                     
REMARK   3      L33:   0.1638 L12:   0.2363                                     
REMARK   3      L13:  -0.1487 L23:  -0.1743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0373 S12:   0.0622 S13:  -0.0427                       
REMARK   3      S21:  -0.0088 S22:   0.0062 S23:  -0.0612                       
REMARK   3      S31:  -0.0272 S32:   0.0739 S33:   0.0120                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 288:424)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2384  38.7797   4.5469              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0594 T22:   0.1244                                     
REMARK   3      T33:   0.0806 T12:  -0.0120                                     
REMARK   3      T13:  -0.0018 T23:   0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6457 L22:   0.7883                                     
REMARK   3      L33:   0.2508 L12:   0.0011                                     
REMARK   3      L13:   0.1599 L23:  -0.2291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0425 S12:   0.2003 S13:   0.0499                       
REMARK   3      S21:  -0.0081 S22:  -0.0107 S23:  -0.1646                       
REMARK   3      S31:  -0.0167 S32:   0.0858 S33:   0.0475                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 425:508)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7247  51.1439  13.9484              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1049 T22:   0.0606                                     
REMARK   3      T33:   0.1256 T12:   0.0242                                     
REMARK   3      T13:   0.0076 T23:   0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8658 L22:   0.4643                                     
REMARK   3      L33:   0.3273 L12:   0.0516                                     
REMARK   3      L13:   0.0016 L23:  -0.2969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0140 S12:   0.0732 S13:   0.2243                       
REMARK   3      S21:   0.0643 S22:   0.0552 S23:   0.1663                       
REMARK   3      S31:  -0.1567 S32:  -0.0556 S33:  -0.0493                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 49:257)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.9214  73.2822 -16.8503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0700 T22:   0.0603                                     
REMARK   3      T33:   0.0639 T12:   0.0168                                     
REMARK   3      T13:   0.0094 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5414 L22:   0.4643                                     
REMARK   3      L33:   0.3382 L12:   0.2382                                     
REMARK   3      L13:  -0.1711 L23:  -0.1322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0240 S12:  -0.0364 S13:  -0.0695                       
REMARK   3      S21:   0.0590 S22:   0.0005 S23:   0.0064                       
REMARK   3      S31:  -0.0162 S32:   0.0340 S33:   0.0163                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 258:444)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.0299  63.6407 -20.5049              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0670 T22:   0.0692                                     
REMARK   3      T33:   0.1522 T12:  -0.0030                                     
REMARK   3      T13:   0.0159 T23:   0.0044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7297 L22:   0.2407                                     
REMARK   3      L33:   0.7001 L12:  -0.0200                                     
REMARK   3      L13:  -0.1563 L23:  -0.1088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0538 S12:   0.0285 S13:  -0.1806                       
REMARK   3      S21:   0.0142 S22:   0.0448 S23:   0.1180                       
REMARK   3      S31:   0.0641 S32:  -0.1284 S33:   0.0095                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 445:460)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0278  68.7872   2.8765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1755 T22:   0.1648                                     
REMARK   3      T33:   0.0976 T12:   0.0294                                     
REMARK   3      T13:   0.0135 T23:   0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5933 L22:   0.4357                                     
REMARK   3      L33:   0.1709 L12:   0.1435                                     
REMARK   3      L13:   0.0217 L23:  -0.0291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0225 S12:  -0.3326 S13:  -0.0486                       
REMARK   3      S21:   0.1394 S22:  -0.0561 S23:   0.0178                       
REMARK   3      S31:  -0.1182 S32:   0.0543 S33:   0.0354                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 461:508)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5852  81.7155  -3.0916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1773 T22:   0.2014                                     
REMARK   3      T33:   0.0989 T12:  -0.0186                                     
REMARK   3      T13:  -0.0255 T23:  -0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4066 L22:   0.3995                                     
REMARK   3      L33:   0.1759 L12:   0.0865                                     
REMARK   3      L13:  -0.1777 L23:  -0.0441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0058 S12:  -0.2586 S13:   0.0166                       
REMARK   3      S21:   0.2580 S22:  -0.0640 S23:  -0.0678                       
REMARK   3      S31:  -0.1086 S32:   0.1952 S33:   0.0412                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 49:205)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7448  91.5091 -35.3088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0770 T22:   0.0869                                     
REMARK   3      T33:   0.0830 T12:   0.0005                                     
REMARK   3      T13:  -0.0126 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5673 L22:   0.3549                                     
REMARK   3      L33:   0.4145 L12:   0.1519                                     
REMARK   3      L13:  -0.3033 L23:  -0.2783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0065 S12:   0.1196 S13:   0.0901                       
REMARK   3      S21:   0.0112 S22:   0.0327 S23:   0.0556                       
REMARK   3      S31:  -0.0709 S32:  -0.0524 S33:  -0.0137                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 206:286)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  14.2519  84.0299 -33.7537              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0697 T22:   0.1066                                     
REMARK   3      T33:   0.0526 T12:  -0.0025                                     
REMARK   3      T13:  -0.0117 T23:  -0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4236 L22:   0.2993                                     
REMARK   3      L33:   0.2554 L12:   0.1922                                     
REMARK   3      L13:  -0.2643 L23:  -0.2081                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0354 S12:   0.0840 S13:  -0.0001                       
REMARK   3      S21:  -0.0172 S22:   0.0220 S23:  -0.0261                       
REMARK   3      S31:  -0.0128 S32:   0.0791 S33:   0.0022                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 287:424)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7579  88.9895 -43.0455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0698 T22:   0.1384                                     
REMARK   3      T33:   0.0750 T12:  -0.0226                                     
REMARK   3      T13:   0.0040 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6647 L22:   0.8484                                     
REMARK   3      L33:   0.4130 L12:  -0.0089                                     
REMARK   3      L13:   0.0943 L23:  -0.2113                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0422 S12:   0.2034 S13:   0.0621                       
REMARK   3      S21:  -0.0366 S22:   0.0096 S23:  -0.1597                       
REMARK   3      S31:  -0.0407 S32:   0.0933 S33:   0.0299                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN C AND RESID 425:508)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3153 102.1668 -35.0628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1230 T22:   0.0866                                     
REMARK   3      T33:   0.1732 T12:   0.0308                                     
REMARK   3      T13:   0.0186 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8471 L22:   0.4505                                     
REMARK   3      L33:   0.5033 L12:   0.1544                                     
REMARK   3      L13:  -0.0675 L23:  -0.4159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0497 S12:   0.1089 S13:   0.2793                       
REMARK   3      S21:   0.0904 S22:   0.0618 S23:   0.1712                       
REMARK   3      S31:  -0.1987 S32:  -0.0871 S33:  -0.0785                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 49:205)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.9813  19.1698  29.7818              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0758 T22:   0.0747                                     
REMARK   3      T33:   0.0709 T12:   0.0134                                     
REMARK   3      T13:   0.0036 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6317 L22:   0.5787                                     
REMARK   3      L33:   0.2285 L12:   0.2898                                     
REMARK   3      L13:  -0.0413 L23:  -0.2465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0189 S12:  -0.0921 S13:  -0.0966                       
REMARK   3      S21:   0.0902 S22:  -0.0225 S23:  -0.0074                       
REMARK   3      S31:  -0.0246 S32:   0.0285 S33:   0.0046                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 206:314)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -26.8720  18.5706  22.9826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0693 T22:   0.0759                                     
REMARK   3      T33:   0.1302 T12:   0.0088                                     
REMARK   3      T13:  -0.0004 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4890 L22:   0.4435                                     
REMARK   3      L33:   0.3641 L12:   0.2061                                     
REMARK   3      L13:  -0.1509 L23:  -0.2057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0057 S12:   0.0144 S13:  -0.0805                       
REMARK   3      S21:   0.0043 S22:   0.0464 S23:   0.1461                       
REMARK   3      S31:   0.0083 S32:  -0.0733 S33:  -0.0089                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 315:362)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -45.2064  13.1482  25.0077              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0656 T22:   0.1934                                     
REMARK   3      T33:   0.2439 T12:   0.0047                                     
REMARK   3      T13:   0.0095 T23:   0.0345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0801 L22:   0.1861                                     
REMARK   3      L33:   0.2250 L12:  -0.0575                                     
REMARK   3      L13:  -0.0285 L23:  -0.0588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1029 S12:  -0.0300 S13:  -0.3082                       
REMARK   3      S21:   0.0719 S22:   0.1283 S23:   0.2147                       
REMARK   3      S31:  -0.0539 S32:  -0.2846 S33:  -0.0119                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 363:508)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -13.2444  15.2249  35.4762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0978 T22:   0.0895                                     
REMARK   3      T33:   0.0877 T12:   0.0146                                     
REMARK   3      T13:   0.0062 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9450 L22:   0.5926                                     
REMARK   3      L33:   0.5070 L12:   0.1318                                     
REMARK   3      L13:  -0.0308 L23:  -0.2973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0250 S12:  -0.1923 S13:  -0.1745                       
REMARK   3      S21:   0.1180 S22:  -0.0379 S23:   0.0227                       
REMARK   3      S31:   0.0210 S32:   0.0365 S33:   0.0030                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 49:508 )                
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 49:508 )                
REMARK   3     ATOM PAIRS NUMBER  : 3554                                        
REMARK   3     RMSD               : 0.058                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 49:508 )                
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 49:508 )                
REMARK   3     ATOM PAIRS NUMBER  : 3519                                        
REMARK   3     RMSD               : 0.054                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 49:508 )                
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 49:508 )                
REMARK   3     ATOM PAIRS NUMBER  : 3536                                        
REMARK   3     RMSD               : 0.064                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2WYA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41725.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9989                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 212827                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 3.8                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.10                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.38                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.00                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2P8U                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.1M BISTRIS PH             
REMARK 280  6.5, 0.2M AMMONIUM SULPHATE                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     SER A  49    OG                                                  
REMARK 470     LYS A  52    CG   CD   CE   NZ                                   
REMARK 470     LYS A 256    NZ                                                  
REMARK 470     LYS A 275    CE   NZ                                             
REMARK 470     GLN A 283    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 333    CG   CD   CE   NZ                                   
REMARK 470     LYS A 342    CE   NZ                                             
REMARK 470     TYR A 347    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 350    CG   CD   CE   NZ                                   
REMARK 470     LYS A 354    CG   CD   CE   NZ                                   
REMARK 470     GLU A 462    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 472    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     GLU A 497    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 502    CD   CE   NZ                                        
REMARK 470     SER B  49    OG                                                  
REMARK 470     LYS B  52    CG   CD   CE   NZ                                   
REMARK 470     GLU B  80    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 256    CD   CE   NZ                                        
REMARK 470     LYS B 275    CD   CE   NZ                                        
REMARK 470     LYS B 282    CE   NZ                                             
REMARK 470     LYS B 333    CG   CD   CE   NZ                                   
REMARK 470     LYS B 342    CE   NZ                                             
REMARK 470     LYS B 350    CD   CE   NZ                                        
REMARK 470     LYS B 354    CG   CD   CE   NZ                                   
REMARK 470     GLU B 462    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 502    CD   CE   NZ                                        
REMARK 470     LYS C  52    CG   CD   CE   NZ                                   
REMARK 470     ASN C  78    CG   OD1  ND2                                       
REMARK 470     GLU C  80    CD   OE1  OE2                                       
REMARK 470     LYS C 275    CE   NZ                                             
REMARK 470     GLN C 283    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 333    CG   CD   CE   NZ                                   
REMARK 470     LYS C 342    CE   NZ                                             
REMARK 470     TYR C 347    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS C 350    CD   CE   NZ                                        
REMARK 470     LYS C 354    CD   CE   NZ                                        
REMARK 470     LYS C 453    CD   CE   NZ                                        
REMARK 470     GLU C 462    CG   CD   OE1  OE2                                  
REMARK 470     HIS C 472    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 473    CG   CD   CE   NZ                                   
REMARK 470     ASN C 483    CG   OD1  ND2                                       
REMARK 470     LYS C 502    CG   CD   CE   NZ                                   
REMARK 470     SER D  49    OG                                                  
REMARK 470     LYS D  52    CG   CD   CE   NZ                                   
REMARK 470     LYS D 256    CE   NZ                                             
REMARK 470     LYS D 275    CD   CE   NZ                                        
REMARK 470     LYS D 282    CG   CD   CE   NZ                                   
REMARK 470     LEU D 331    CG   CD1  CD2                                       
REMARK 470     LYS D 333    CD   CE   NZ                                        
REMARK 470     LYS D 342    CE   NZ                                             
REMARK 470     TYR D 347    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS D 350    CD   CE   NZ                                        
REMARK 470     LYS D 453    CD   CE   NZ                                        
REMARK 470     GLU D 462    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 469    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 502    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 406   CZ    ARG A 406   NH1    -0.088                       
REMARK 500    ARG A 406   CZ    ARG A 406   NH2    -0.090                       
REMARK 500    ARG B 406   CZ    ARG B 406   NH1    -0.100                       
REMARK 500    ARG B 406   CZ    ARG B 406   NH2    -0.090                       
REMARK 500    ARG C 406   CZ    ARG C 406   NH1    -0.090                       
REMARK 500    ARG C 406   CZ    ARG C 406   NH2    -0.096                       
REMARK 500    GLU C 497   CD    GLU C 497   OE2     0.077                       
REMARK 500    ARG D 406   CZ    ARG D 406   NH1    -0.102                       
REMARK 500    ARG D 406   CZ    ARG D 406   NH2    -0.085                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 406   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 406   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 406   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    VAL B  79   CG1 -  CB  -  CG2 ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG B 406   NE  -  CZ  -  NH2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG B 406   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ASP C 136   CB  -  CG  -  OD1 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ASP C 136   CB  -  CG  -  OD2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ASP C 136   OD1 -  CG  -  OD2 ANGL. DEV. = -19.6 DEGREES          
REMARK 500    ARG C 406   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG C 406   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG C 406   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.5 DEGREES          
REMARK 500    ARG D 406   NE  -  CZ  -  NH2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG D 406   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 160     -128.14   -137.03                                   
REMARK 500    ALA A 165     -133.40     45.91                                   
REMARK 500    LEU A 230       67.80   -110.20                                   
REMARK 500    TYR A 382     -117.15     55.90                                   
REMARK 500    ILE B 160     -128.73   -137.81                                   
REMARK 500    ALA B 165     -134.34     46.50                                   
REMARK 500    LEU B 230       67.63   -109.99                                   
REMARK 500    THR B 368      -35.10   -132.06                                   
REMARK 500    TYR B 382     -116.64     56.20                                   
REMARK 500    ILE C 160     -127.61   -136.37                                   
REMARK 500    ALA C 165     -133.87     46.42                                   
REMARK 500    LEU C 230       66.79   -109.51                                   
REMARK 500    THR C 368      -34.14   -131.79                                   
REMARK 500    TYR C 382     -116.34     54.92                                   
REMARK 500    ILE D 160     -128.38   -137.00                                   
REMARK 500    ALA D 165     -132.74     47.75                                   
REMARK 500    LEU D 230       66.97   -108.65                                   
REMARK 500    THR D 368      -34.72   -131.80                                   
REMARK 500    TYR D 382     -116.13     56.53                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL B 508        22.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HMG C1509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HMG D1509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HMG A1509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HMG B1509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1510                 
DBREF  2WYA A   49    50  PDB    2WYA     2WYA            49     50             
DBREF  2WYA A   51   508  UNP    P54868   HMCS2_HUMAN     51    508             
DBREF  2WYA B   49    50  PDB    2WYA     2WYA            49     50             
DBREF  2WYA B   51   508  UNP    P54868   HMCS2_HUMAN     51    508             
DBREF  2WYA C   49    50  PDB    2WYA     2WYA            49     50             
DBREF  2WYA C   51   508  UNP    P54868   HMCS2_HUMAN     51    508             
DBREF  2WYA D   49    50  PDB    2WYA     2WYA            49     50             
DBREF  2WYA D   51   508  UNP    P54868   HMCS2_HUMAN     51    508             
SEQRES   1 A  460  SER MET PRO LYS ASP VAL GLY ILE LEU ALA LEU GLU VAL          
SEQRES   2 A  460  TYR PHE PRO ALA GLN TYR VAL ASP GLN THR ASP LEU GLU          
SEQRES   3 A  460  LYS TYR ASN ASN VAL GLU ALA GLY LYS TYR THR VAL GLY          
SEQRES   4 A  460  LEU GLY GLN THR ARG MET GLY PHE CYS SER VAL GLN GLU          
SEQRES   5 A  460  ASP ILE ASN SER LEU CYS LEU THR VAL VAL GLN ARG LEU          
SEQRES   6 A  460  MET GLU ARG ILE GLN LEU PRO TRP ASP SER VAL GLY ARG          
SEQRES   7 A  460  LEU GLU VAL GLY THR GLU THR ILE ILE ASP LYS SER LYS          
SEQRES   8 A  460  ALA VAL LYS THR VAL LEU MET GLU LEU PHE GLN ASP SER          
SEQRES   9 A  460  GLY ASN THR ASP ILE GLU GLY ILE ASP THR THR ASN ALA          
SEQRES  10 A  460  CYS TYR GLY GLY THR ALA SER LEU PHE ASN ALA ALA ASN          
SEQRES  11 A  460  TRP MET GLU SER SER SER TRP ASP GLY ARG TYR ALA MET          
SEQRES  12 A  460  VAL VAL CYS GLY ASP ILE ALA VAL TYR PRO SER GLY ASN          
SEQRES  13 A  460  ALA ARG PRO THR GLY GLY ALA GLY ALA VAL ALA MET LEU          
SEQRES  14 A  460  ILE GLY PRO LYS ALA PRO LEU ALA LEU GLU ARG GLY LEU          
SEQRES  15 A  460  ARG GLY THR HIS MET GLU ASN VAL TYR ASP PHE TYR LYS          
SEQRES  16 A  460  PRO ASN LEU ALA SER GLU TYR PRO ILE VAL ASP GLY LYS          
SEQRES  17 A  460  LEU SER ILE GLN CYS TYR LEU ARG ALA LEU ASP ARG CYS          
SEQRES  18 A  460  TYR THR SER TYR ARG LYS LYS ILE GLN ASN GLN TRP LYS          
SEQRES  19 A  460  GLN ALA GLY SER ASP ARG PRO PHE THR LEU ASP ASP LEU          
SEQRES  20 A  460  GLN TYR MET ILE PHE HIS THR PRO PHE CYS LYS MET VAL          
SEQRES  21 A  460  GLN LYS SER LEU ALA ARG LEU MET PHE ASN ASP PHE LEU          
SEQRES  22 A  460  SER ALA SER SER ASP THR GLN THR SER LEU TYR LYS GLY          
SEQRES  23 A  460  LEU GLU ALA PHE GLY GLY LEU LYS LEU GLU ASP THR TYR          
SEQRES  24 A  460  THR ASN LYS ASP LEU ASP LYS ALA LEU LEU LYS ALA SER          
SEQRES  25 A  460  GLN ASP MET PHE ASP LYS LYS THR LYS ALA SER LEU TYR          
SEQRES  26 A  460  LEU SER THR HIS ASN GLY ASN MET TYR THR SER SER LEU          
SEQRES  27 A  460  TYR GLY CYS LEU ALA SER LEU LEU SER HIS HIS SER ALA          
SEQRES  28 A  460  GLN GLU LEU ALA GLY SER ARG ILE GLY ALA PHE SER TYR          
SEQRES  29 A  460  GLY SER GLY LEU ALA ALA SER PHE PHE SER PHE ARG VAL          
SEQRES  30 A  460  SER GLN ASP ALA ALA PRO GLY SER PRO LEU ASP LYS LEU          
SEQRES  31 A  460  VAL SER SER THR SER ASP LEU PRO LYS ARG LEU ALA SER          
SEQRES  32 A  460  ARG LYS CYS VAL SER PRO GLU GLU PHE THR GLU ILE MET          
SEQRES  33 A  460  ASN GLN ARG GLU GLN PHE TYR HIS LYS VAL ASN PHE SER          
SEQRES  34 A  460  PRO PRO GLY ASP THR ASN SER LEU PHE PRO GLY THR TRP          
SEQRES  35 A  460  TYR LEU GLU ARG VAL ASP GLU GLN HIS ARG ARG LYS TYR          
SEQRES  36 A  460  ALA ARG ARG PRO VAL                                          
SEQRES   1 B  460  SER MET PRO LYS ASP VAL GLY ILE LEU ALA LEU GLU VAL          
SEQRES   2 B  460  TYR PHE PRO ALA GLN TYR VAL ASP GLN THR ASP LEU GLU          
SEQRES   3 B  460  LYS TYR ASN ASN VAL GLU ALA GLY LYS TYR THR VAL GLY          
SEQRES   4 B  460  LEU GLY GLN THR ARG MET GLY PHE CYS SER VAL GLN GLU          
SEQRES   5 B  460  ASP ILE ASN SER LEU CYS LEU THR VAL VAL GLN ARG LEU          
SEQRES   6 B  460  MET GLU ARG ILE GLN LEU PRO TRP ASP SER VAL GLY ARG          
SEQRES   7 B  460  LEU GLU VAL GLY THR GLU THR ILE ILE ASP LYS SER LYS          
SEQRES   8 B  460  ALA VAL LYS THR VAL LEU MET GLU LEU PHE GLN ASP SER          
SEQRES   9 B  460  GLY ASN THR ASP ILE GLU GLY ILE ASP THR THR ASN ALA          
SEQRES  10 B  460  CYS TYR GLY GLY THR ALA SER LEU PHE ASN ALA ALA ASN          
SEQRES  11 B  460  TRP MET GLU SER SER SER TRP ASP GLY ARG TYR ALA MET          
SEQRES  12 B  460  VAL VAL CYS GLY ASP ILE ALA VAL TYR PRO SER GLY ASN          
SEQRES  13 B  460  ALA ARG PRO THR GLY GLY ALA GLY ALA VAL ALA MET LEU          
SEQRES  14 B  460  ILE GLY PRO LYS ALA PRO LEU ALA LEU GLU ARG GLY LEU          
SEQRES  15 B  460  ARG GLY THR HIS MET GLU ASN VAL TYR ASP PHE TYR LYS          
SEQRES  16 B  460  PRO ASN LEU ALA SER GLU TYR PRO ILE VAL ASP GLY LYS          
SEQRES  17 B  460  LEU SER ILE GLN CYS TYR LEU ARG ALA LEU ASP ARG CYS          
SEQRES  18 B  460  TYR THR SER TYR ARG LYS LYS ILE GLN ASN GLN TRP LYS          
SEQRES  19 B  460  GLN ALA GLY SER ASP ARG PRO PHE THR LEU ASP ASP LEU          
SEQRES  20 B  460  GLN TYR MET ILE PHE HIS THR PRO PHE CYS LYS MET VAL          
SEQRES  21 B  460  GLN LYS SER LEU ALA ARG LEU MET PHE ASN ASP PHE LEU          
SEQRES  22 B  460  SER ALA SER SER ASP THR GLN THR SER LEU TYR LYS GLY          
SEQRES  23 B  460  LEU GLU ALA PHE GLY GLY LEU LYS LEU GLU ASP THR TYR          
SEQRES  24 B  460  THR ASN LYS ASP LEU ASP LYS ALA LEU LEU LYS ALA SER          
SEQRES  25 B  460  GLN ASP MET PHE ASP LYS LYS THR LYS ALA SER LEU TYR          
SEQRES  26 B  460  LEU SER THR HIS ASN GLY ASN MET TYR THR SER SER LEU          
SEQRES  27 B  460  TYR GLY CYS LEU ALA SER LEU LEU SER HIS HIS SER ALA          
SEQRES  28 B  460  GLN GLU LEU ALA GLY SER ARG ILE GLY ALA PHE SER TYR          
SEQRES  29 B  460  GLY SER GLY LEU ALA ALA SER PHE PHE SER PHE ARG VAL          
SEQRES  30 B  460  SER GLN ASP ALA ALA PRO GLY SER PRO LEU ASP LYS LEU          
SEQRES  31 B  460  VAL SER SER THR SER ASP LEU PRO LYS ARG LEU ALA SER          
SEQRES  32 B  460  ARG LYS CYS VAL SER PRO GLU GLU PHE THR GLU ILE MET          
SEQRES  33 B  460  ASN GLN ARG GLU GLN PHE TYR HIS LYS VAL ASN PHE SER          
SEQRES  34 B  460  PRO PRO GLY ASP THR ASN SER LEU PHE PRO GLY THR TRP          
SEQRES  35 B  460  TYR LEU GLU ARG VAL ASP GLU GLN HIS ARG ARG LYS TYR          
SEQRES  36 B  460  ALA ARG ARG PRO VAL                                          
SEQRES   1 C  460  SER MET PRO LYS ASP VAL GLY ILE LEU ALA LEU GLU VAL          
SEQRES   2 C  460  TYR PHE PRO ALA GLN TYR VAL ASP GLN THR ASP LEU GLU          
SEQRES   3 C  460  LYS TYR ASN ASN VAL GLU ALA GLY LYS TYR THR VAL GLY          
SEQRES   4 C  460  LEU GLY GLN THR ARG MET GLY PHE CYS SER VAL GLN GLU          
SEQRES   5 C  460  ASP ILE ASN SER LEU CYS LEU THR VAL VAL GLN ARG LEU          
SEQRES   6 C  460  MET GLU ARG ILE GLN LEU PRO TRP ASP SER VAL GLY ARG          
SEQRES   7 C  460  LEU GLU VAL GLY THR GLU THR ILE ILE ASP LYS SER LYS          
SEQRES   8 C  460  ALA VAL LYS THR VAL LEU MET GLU LEU PHE GLN ASP SER          
SEQRES   9 C  460  GLY ASN THR ASP ILE GLU GLY ILE ASP THR THR ASN ALA          
SEQRES  10 C  460  CYS TYR GLY GLY THR ALA SER LEU PHE ASN ALA ALA ASN          
SEQRES  11 C  460  TRP MET GLU SER SER SER TRP ASP GLY ARG TYR ALA MET          
SEQRES  12 C  460  VAL VAL CYS GLY ASP ILE ALA VAL TYR PRO SER GLY ASN          
SEQRES  13 C  460  ALA ARG PRO THR GLY GLY ALA GLY ALA VAL ALA MET LEU          
SEQRES  14 C  460  ILE GLY PRO LYS ALA PRO LEU ALA LEU GLU ARG GLY LEU          
SEQRES  15 C  460  ARG GLY THR HIS MET GLU ASN VAL TYR ASP PHE TYR LYS          
SEQRES  16 C  460  PRO ASN LEU ALA SER GLU TYR PRO ILE VAL ASP GLY LYS          
SEQRES  17 C  460  LEU SER ILE GLN CYS TYR LEU ARG ALA LEU ASP ARG CYS          
SEQRES  18 C  460  TYR THR SER TYR ARG LYS LYS ILE GLN ASN GLN TRP LYS          
SEQRES  19 C  460  GLN ALA GLY SER ASP ARG PRO PHE THR LEU ASP ASP LEU          
SEQRES  20 C  460  GLN TYR MET ILE PHE HIS THR PRO PHE CYS LYS MET VAL          
SEQRES  21 C  460  GLN LYS SER LEU ALA ARG LEU MET PHE ASN ASP PHE LEU          
SEQRES  22 C  460  SER ALA SER SER ASP THR GLN THR SER LEU TYR LYS GLY          
SEQRES  23 C  460  LEU GLU ALA PHE GLY GLY LEU LYS LEU GLU ASP THR TYR          
SEQRES  24 C  460  THR ASN LYS ASP LEU ASP LYS ALA LEU LEU LYS ALA SER          
SEQRES  25 C  460  GLN ASP MET PHE ASP LYS LYS THR LYS ALA SER LEU TYR          
SEQRES  26 C  460  LEU SER THR HIS ASN GLY ASN MET TYR THR SER SER LEU          
SEQRES  27 C  460  TYR GLY CYS LEU ALA SER LEU LEU SER HIS HIS SER ALA          
SEQRES  28 C  460  GLN GLU LEU ALA GLY SER ARG ILE GLY ALA PHE SER TYR          
SEQRES  29 C  460  GLY SER GLY LEU ALA ALA SER PHE PHE SER PHE ARG VAL          
SEQRES  30 C  460  SER GLN ASP ALA ALA PRO GLY SER PRO LEU ASP LYS LEU          
SEQRES  31 C  460  VAL SER SER THR SER ASP LEU PRO LYS ARG LEU ALA SER          
SEQRES  32 C  460  ARG LYS CYS VAL SER PRO GLU GLU PHE THR GLU ILE MET          
SEQRES  33 C  460  ASN GLN ARG GLU GLN PHE TYR HIS LYS VAL ASN PHE SER          
SEQRES  34 C  460  PRO PRO GLY ASP THR ASN SER LEU PHE PRO GLY THR TRP          
SEQRES  35 C  460  TYR LEU GLU ARG VAL ASP GLU GLN HIS ARG ARG LYS TYR          
SEQRES  36 C  460  ALA ARG ARG PRO VAL                                          
SEQRES   1 D  460  SER MET PRO LYS ASP VAL GLY ILE LEU ALA LEU GLU VAL          
SEQRES   2 D  460  TYR PHE PRO ALA GLN TYR VAL ASP GLN THR ASP LEU GLU          
SEQRES   3 D  460  LYS TYR ASN ASN VAL GLU ALA GLY LYS TYR THR VAL GLY          
SEQRES   4 D  460  LEU GLY GLN THR ARG MET GLY PHE CYS SER VAL GLN GLU          
SEQRES   5 D  460  ASP ILE ASN SER LEU CYS LEU THR VAL VAL GLN ARG LEU          
SEQRES   6 D  460  MET GLU ARG ILE GLN LEU PRO TRP ASP SER VAL GLY ARG          
SEQRES   7 D  460  LEU GLU VAL GLY THR GLU THR ILE ILE ASP LYS SER LYS          
SEQRES   8 D  460  ALA VAL LYS THR VAL LEU MET GLU LEU PHE GLN ASP SER          
SEQRES   9 D  460  GLY ASN THR ASP ILE GLU GLY ILE ASP THR THR ASN ALA          
SEQRES  10 D  460  CYS TYR GLY GLY THR ALA SER LEU PHE ASN ALA ALA ASN          
SEQRES  11 D  460  TRP MET GLU SER SER SER TRP ASP GLY ARG TYR ALA MET          
SEQRES  12 D  460  VAL VAL CYS GLY ASP ILE ALA VAL TYR PRO SER GLY ASN          
SEQRES  13 D  460  ALA ARG PRO THR GLY GLY ALA GLY ALA VAL ALA MET LEU          
SEQRES  14 D  460  ILE GLY PRO LYS ALA PRO LEU ALA LEU GLU ARG GLY LEU          
SEQRES  15 D  460  ARG GLY THR HIS MET GLU ASN VAL TYR ASP PHE TYR LYS          
SEQRES  16 D  460  PRO ASN LEU ALA SER GLU TYR PRO ILE VAL ASP GLY LYS          
SEQRES  17 D  460  LEU SER ILE GLN CYS TYR LEU ARG ALA LEU ASP ARG CYS          
SEQRES  18 D  460  TYR THR SER TYR ARG LYS LYS ILE GLN ASN GLN TRP LYS          
SEQRES  19 D  460  GLN ALA GLY SER ASP ARG PRO PHE THR LEU ASP ASP LEU          
SEQRES  20 D  460  GLN TYR MET ILE PHE HIS THR PRO PHE CYS LYS MET VAL          
SEQRES  21 D  460  GLN LYS SER LEU ALA ARG LEU MET PHE ASN ASP PHE LEU          
SEQRES  22 D  460  SER ALA SER SER ASP THR GLN THR SER LEU TYR LYS GLY          
SEQRES  23 D  460  LEU GLU ALA PHE GLY GLY LEU LYS LEU GLU ASP THR TYR          
SEQRES  24 D  460  THR ASN LYS ASP LEU ASP LYS ALA LEU LEU LYS ALA SER          
SEQRES  25 D  460  GLN ASP MET PHE ASP LYS LYS THR LYS ALA SER LEU TYR          
SEQRES  26 D  460  LEU SER THR HIS ASN GLY ASN MET TYR THR SER SER LEU          
SEQRES  27 D  460  TYR GLY CYS LEU ALA SER LEU LEU SER HIS HIS SER ALA          
SEQRES  28 D  460  GLN GLU LEU ALA GLY SER ARG ILE GLY ALA PHE SER TYR          
SEQRES  29 D  460  GLY SER GLY LEU ALA ALA SER PHE PHE SER PHE ARG VAL          
SEQRES  30 D  460  SER GLN ASP ALA ALA PRO GLY SER PRO LEU ASP LYS LEU          
SEQRES  31 D  460  VAL SER SER THR SER ASP LEU PRO LYS ARG LEU ALA SER          
SEQRES  32 D  460  ARG LYS CYS VAL SER PRO GLU GLU PHE THR GLU ILE MET          
SEQRES  33 D  460  ASN GLN ARG GLU GLN PHE TYR HIS LYS VAL ASN PHE SER          
SEQRES  34 D  460  PRO PRO GLY ASP THR ASN SER LEU PHE PRO GLY THR TRP          
SEQRES  35 D  460  TYR LEU GLU ARG VAL ASP GLU GLN HIS ARG ARG LYS TYR          
SEQRES  36 D  460  ALA ARG ARG PRO VAL                                          
HET    HMG  C1509      58                                                       
HET    HMG  D1509      58                                                       
HET    HMG  A1509      58                                                       
HET    HMG  B1509      58                                                       
HET    GOL  A1510       6                                                       
HETNAM     HMG 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A                            
HETNAM     GOL GLYCEROL                                                         
HETSYN     HMG (S)-HMG-COA                                                      
FORMUL   5  HMG    4(C27 H39 N7 O20 P3 S 5-)                                    
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *1457(H2 O)                                                   
HELIX    1   1 GLN A   70  ASN A   77  1                                   8    
HELIX    2   2 GLY A   82  GLY A   89  1                                   8    
HELIX    3   3 ASP A  101  GLN A  118  1                                  18    
HELIX    4   4 PRO A  120  ASP A  122  5                                   3    
HELIX    5   5 ALA A  140  MET A  146  1                                   7    
HELIX    6   6 GLU A  147  GLY A  153  5                                   7    
HELIX    7   7 ASN A  164  CYS A  166  5                                   3    
HELIX    8   8 TYR A  167  GLU A  181  1                                  15    
HELIX    9   9 ALA A  205  GLY A  209  5                                   5    
HELIX   10  10 ASP A  254  ALA A  284  1                                  31    
HELIX   11  11 THR A  291  LEU A  295  5                                   5    
HELIX   12  12 PHE A  304  ALA A  323  1                                  20    
HELIX   13  13 SER A  324  TYR A  332  1                                   9    
HELIX   14  14 LYS A  333  GLY A  339  5                                   7    
HELIX   15  15 LYS A  342  THR A  348  5                                   7    
HELIX   16  16 ASN A  349  THR A  368  1                                  20    
HELIX   17  17 LYS A  369  SER A  371  5                                   3    
HELIX   18  18 LEU A  372  GLY A  379  1                                   8    
HELIX   19  19 MET A  381  THR A  383  5                                   3    
HELIX   20  20 SER A  384  HIS A  397  1                                  14    
HELIX   21  21 SER A  398  ALA A  403  1                                   6    
HELIX   22  22 SER A  433  SER A  441  1                                   9    
HELIX   23  23 ASP A  444  SER A  451  1                                   8    
HELIX   24  24 SER A  456  TYR A  471  1                                  16    
HELIX   25  25 ASP A  481  LEU A  485  5                                   5    
HELIX   26  26 GLN B   70  ASN B   77  1                                   8    
HELIX   27  27 GLY B   82  GLY B   89  1                                   8    
HELIX   28  28 ASP B  101  GLN B  118  1                                  18    
HELIX   29  29 PRO B  120  ASP B  122  5                                   3    
HELIX   30  30 ALA B  140  MET B  146  1                                   7    
HELIX   31  31 GLU B  147  GLY B  153  5                                   7    
HELIX   32  32 ASN B  164  CYS B  166  5                                   3    
HELIX   33  33 TYR B  167  GLU B  181  1                                  15    
HELIX   34  34 ALA B  205  GLY B  209  5                                   5    
HELIX   35  35 ASP B  254  ALA B  284  1                                  31    
HELIX   36  36 THR B  291  LEU B  295  5                                   5    
HELIX   37  37 PHE B  304  ALA B  323  1                                  20    
HELIX   38  38 SER B  324  TYR B  332  1                                   9    
HELIX   39  39 LYS B  333  GLY B  339  5                                   7    
HELIX   40  40 LYS B  342  THR B  348  5                                   7    
HELIX   41  41 ASN B  349  THR B  368  1                                  20    
HELIX   42  42 LYS B  369  SER B  371  5                                   3    
HELIX   43  43 LEU B  372  GLY B  379  1                                   8    
HELIX   44  44 MET B  381  THR B  383  5                                   3    
HELIX   45  45 SER B  384  HIS B  397  1                                  14    
HELIX   46  46 SER B  398  ALA B  403  1                                   6    
HELIX   47  47 SER B  433  SER B  441  1                                   9    
HELIX   48  48 ASP B  444  SER B  451  1                                   8    
HELIX   49  49 SER B  456  TYR B  471  1                                  16    
HELIX   50  50 ASP B  481  LEU B  485  5                                   5    
HELIX   51  51 GLN C   70  ASN C   77  1                                   8    
HELIX   52  52 GLY C   82  GLY C   89  1                                   8    
HELIX   53  53 ASP C  101  GLN C  118  1                                  18    
HELIX   54  54 PRO C  120  ASP C  122  5                                   3    
HELIX   55  55 ALA C  140  MET C  146  1                                   7    
HELIX   56  56 GLU C  147  GLY C  153  5                                   7    
HELIX   57  57 ASN C  164  CYS C  166  5                                   3    
HELIX   58  58 TYR C  167  GLU C  181  1                                  15    
HELIX   59  59 ALA C  205  GLY C  209  5                                   5    
HELIX   60  60 ASP C  254  ALA C  284  1                                  31    
HELIX   61  61 THR C  291  LEU C  295  5                                   5    
HELIX   62  62 PHE C  304  ALA C  323  1                                  20    
HELIX   63  63 SER C  324  TYR C  332  1                                   9    
HELIX   64  64 LYS C  333  GLY C  339  5                                   7    
HELIX   65  65 LYS C  342  TYR C  347  5                                   6    
HELIX   66  66 ASN C  349  THR C  368  1                                  20    
HELIX   67  67 LYS C  369  SER C  371  5                                   3    
HELIX   68  68 LEU C  372  GLY C  379  1                                   8    
HELIX   69  69 MET C  381  THR C  383  5                                   3    
HELIX   70  70 SER C  384  HIS C  397  1                                  14    
HELIX   71  71 SER C  398  ALA C  403  1                                   6    
HELIX   72  72 SER C  433  SER C  441  1                                   9    
HELIX   73  73 ASP C  444  SER C  451  1                                   8    
HELIX   74  74 SER C  456  TYR C  471  1                                  16    
HELIX   75  75 ASP C  481  LEU C  485  5                                   5    
HELIX   76  76 GLN D   70  ASN D   77  1                                   8    
HELIX   77  77 GLY D   82  GLY D   89  1                                   8    
HELIX   78  78 ASP D  101  GLN D  118  1                                  18    
HELIX   79  79 PRO D  120  ASP D  122  5                                   3    
HELIX   80  80 ALA D  140  MET D  146  1                                   7    
HELIX   81  81 GLU D  147  GLY D  153  5                                   7    
HELIX   82  82 ASN D  164  CYS D  166  5                                   3    
HELIX   83  83 TYR D  167  GLU D  181  1                                  15    
HELIX   84  84 ALA D  205  GLY D  209  5                                   5    
HELIX   85  85 ASP D  254  ALA D  284  1                                  31    
HELIX   86  86 THR D  291  LEU D  295  5                                   5    
HELIX   87  87 PHE D  304  ALA D  323  1                                  20    
HELIX   88  88 SER D  324  TYR D  332  1                                   9    
HELIX   89  89 LYS D  333  GLY D  339  5                                   7    
HELIX   90  90 LYS D  342  THR D  348  5                                   7    
HELIX   91  91 ASN D  349  THR D  368  1                                  20    
HELIX   92  92 LYS D  369  SER D  371  5                                   3    
HELIX   93  93 LEU D  372  GLY D  379  1                                   8    
HELIX   94  94 MET D  381  THR D  383  5                                   3    
HELIX   95  95 SER D  384  HIS D  397  1                                  14    
HELIX   96  96 SER D  398  ALA D  403  1                                   6    
HELIX   97  97 SER D  433  SER D  441  1                                   9    
HELIX   98  98 ASP D  444  SER D  451  1                                   8    
HELIX   99  99 SER D  456  TYR D  471  1                                  16    
HELIX  100 100 ASP D  481  LEU D  485  5                                   5    
SHEET    1  AA 2 GLY A 232  MET A 235  0                                        
SHEET    2  AA 2 ALA A 417  VAL A 425 -1  O  ALA A 418   N  HIS A 234           
SHEET    1  AB 4 TYR A 297  PHE A 300  0                                        
SHEET    2  AB 4 ARG A 406  GLY A 413  1  O  GLY A 408   N  ILE A 299           
SHEET    3  AB 4 ALA A 417  VAL A 425  1  O  ALA A 417   N  GLY A 413           
SHEET    4  AB 4 GLY A 232  MET A 235 -1  O  GLY A 232   N  PHE A 420           
SHEET    1  AC18 TYR A 297  PHE A 300  0                                        
SHEET    2  AC18 ARG A 406  GLY A 413  1  O  GLY A 408   N  ILE A 299           
SHEET    3  AC18 ALA A 417  VAL A 425  1  O  ALA A 417   N  GLY A 413           
SHEET    4  AC18 LEU A 224  LEU A 226 -1  O  ALA A 225   N  ARG A 424           
SHEET    5  AC18 GLY A  55  TYR A  62 -1  O  ILE A  56   N  LEU A 224           
SHEET    6  AC18 GLY A 210  GLY A 219 -1  O  ALA A 213   N  TYR A  62           
SHEET    7  AC18 TYR A 189  ALA A 198 -1  O  ALA A 190   N  ILE A 218           
SHEET    8  AC18 VAL A 124  GLY A 130  1  N  GLY A 125   O  TYR A 189           
SHEET    9  AC18 ASP A 161  THR A 163  1  N  THR A 162   O  VAL A 129           
SHEET   10  AC18 ASP D 161  THR D 163 -1  O  ASP D 161   N  THR A 163           
SHEET   11  AC18 VAL D 124  GLY D 130  1  O  VAL D 129   N  THR D 162           
SHEET   12  AC18 TYR D 189  ALA D 198  1  O  TYR D 189   N  GLY D 125           
SHEET   13  AC18 GLY D 210  GLY D 219 -1  O  GLY D 210   N  ALA D 198           
SHEET   14  AC18 GLY D  55  TYR D  62 -1  O  GLY D  55   N  GLY D 219           
SHEET   15  AC18 LEU D 224  LEU D 226 -1  O  LEU D 224   N  ILE D  56           
SHEET   16  AC18 ALA D 417  VAL D 425 -1  O  ARG D 424   N  ALA D 225           
SHEET   17  AC18 ARG D 406  GLY D 413 -1  O  ILE D 407   N  PHE D 423           
SHEET   18  AC18 TYR D 297  PHE D 300  1  O  TYR D 297   N  GLY D 408           
SHEET    1  AD17 TYR A 297  PHE A 300  0                                        
SHEET    2  AD17 ARG A 406  GLY A 413  1  O  GLY A 408   N  ILE A 299           
SHEET    3  AD17 ALA A 417  VAL A 425  1  O  ALA A 417   N  GLY A 413           
SHEET    4  AD17 LEU A 224  LEU A 226 -1  O  ALA A 225   N  ARG A 424           
SHEET    5  AD17 GLY A  55  TYR A  62 -1  O  ILE A  56   N  LEU A 224           
SHEET    6  AD17 GLY A 210  GLY A 219 -1  O  ALA A 213   N  TYR A  62           
SHEET    7  AD17 TYR A 189  ALA A 198 -1  O  ALA A 190   N  ILE A 218           
SHEET    8  AD17 VAL A 124  GLY A 130  1  N  GLY A 125   O  TYR A 189           
SHEET    9  AD17 ASP A 161  THR A 163  1  N  THR A 162   O  VAL A 129           
SHEET   10  AD17 ASP D 161  THR D 163 -1  O  ASP D 161   N  THR A 163           
SHEET   11  AD17 VAL D 124  GLY D 130  1  O  VAL D 129   N  THR D 162           
SHEET   12  AD17 TYR D 189  ALA D 198  1  O  TYR D 189   N  GLY D 125           
SHEET   13  AD17 GLY D 210  GLY D 219 -1  O  GLY D 210   N  ALA D 198           
SHEET   14  AD17 GLY D  55  TYR D  62 -1  O  GLY D  55   N  GLY D 219           
SHEET   15  AD17 LEU D 224  LEU D 226 -1  O  LEU D 224   N  ILE D  56           
SHEET   16  AD17 ALA D 417  VAL D 425 -1  O  ARG D 424   N  ALA D 225           
SHEET   17  AD17 GLY D 232  MET D 235  1  O  GLY D 232   N  PHE D 420           
SHEET    1  AE 3 ARG A  92  GLY A  94  0                                        
SHEET    2  AE 3 GLN A  66  ASP A  69 -1  O  VAL A  68   N  MET A  93           
SHEET    3  AE 3 LYS A 453  VAL A 455  1  O  LYS A 453   N  TYR A  67           
SHEET    1  AF 2 PHE A 241  TYR A 242  0                                        
SHEET    2  AF 2 ILE A 252  VAL A 253 -1  O  ILE A 252   N  TYR A 242           
SHEET    1  AG 2 TRP A 490  VAL A 495  0                                        
SHEET    2  AG 2 ARG A 501  ARG A 505 -1  O  LYS A 502   N  GLU A 493           
SHEET    1  BA 2 GLY B 232  MET B 235  0                                        
SHEET    2  BA 2 ALA B 417  VAL B 425 -1  O  ALA B 418   N  HIS B 234           
SHEET    1  BB 4 TYR B 297  PHE B 300  0                                        
SHEET    2  BB 4 ARG B 406  GLY B 413  1  O  GLY B 408   N  ILE B 299           
SHEET    3  BB 4 ALA B 417  VAL B 425  1  O  ALA B 417   N  GLY B 413           
SHEET    4  BB 4 GLY B 232  MET B 235 -1  O  GLY B 232   N  PHE B 420           
SHEET    1  BC18 TYR B 297  PHE B 300  0                                        
SHEET    2  BC18 ARG B 406  GLY B 413  1  O  GLY B 408   N  ILE B 299           
SHEET    3  BC18 ALA B 417  VAL B 425  1  O  ALA B 417   N  GLY B 413           
SHEET    4  BC18 LEU B 224  LEU B 226 -1  O  ALA B 225   N  ARG B 424           
SHEET    5  BC18 GLY B  55  TYR B  62 -1  O  ILE B  56   N  LEU B 224           
SHEET    6  BC18 GLY B 210  GLY B 219 -1  O  ALA B 213   N  TYR B  62           
SHEET    7  BC18 TYR B 189  ALA B 198 -1  O  ALA B 190   N  ILE B 218           
SHEET    8  BC18 VAL B 124  GLY B 130  1  N  GLY B 125   O  TYR B 189           
SHEET    9  BC18 ASP B 161  THR B 163  1  N  THR B 162   O  VAL B 129           
SHEET   10  BC18 ASP C 161  THR C 163 -1  O  ASP C 161   N  THR B 163           
SHEET   11  BC18 VAL C 124  GLY C 130  1  O  VAL C 129   N  THR C 162           
SHEET   12  BC18 TYR C 189  ALA C 198  1  O  TYR C 189   N  GLY C 125           
SHEET   13  BC18 GLY C 210  GLY C 219 -1  O  GLY C 210   N  ALA C 198           
SHEET   14  BC18 GLY C  55  TYR C  62 -1  O  GLY C  55   N  GLY C 219           
SHEET   15  BC18 LEU C 224  LEU C 226 -1  O  LEU C 224   N  ILE C  56           
SHEET   16  BC18 ALA C 417  VAL C 425 -1  O  ARG C 424   N  ALA C 225           
SHEET   17  BC18 ARG C 406  GLY C 413 -1  O  ILE C 407   N  PHE C 423           
SHEET   18  BC18 TYR C 297  PHE C 300  1  O  TYR C 297   N  GLY C 408           
SHEET    1  BD17 TYR B 297  PHE B 300  0                                        
SHEET    2  BD17 ARG B 406  GLY B 413  1  O  GLY B 408   N  ILE B 299           
SHEET    3  BD17 ALA B 417  VAL B 425  1  O  ALA B 417   N  GLY B 413           
SHEET    4  BD17 LEU B 224  LEU B 226 -1  O  ALA B 225   N  ARG B 424           
SHEET    5  BD17 GLY B  55  TYR B  62 -1  O  ILE B  56   N  LEU B 224           
SHEET    6  BD17 GLY B 210  GLY B 219 -1  O  ALA B 213   N  TYR B  62           
SHEET    7  BD17 TYR B 189  ALA B 198 -1  O  ALA B 190   N  ILE B 218           
SHEET    8  BD17 VAL B 124  GLY B 130  1  N  GLY B 125   O  TYR B 189           
SHEET    9  BD17 ASP B 161  THR B 163  1  N  THR B 162   O  VAL B 129           
SHEET   10  BD17 ASP C 161  THR C 163 -1  O  ASP C 161   N  THR B 163           
SHEET   11  BD17 VAL C 124  GLY C 130  1  O  VAL C 129   N  THR C 162           
SHEET   12  BD17 TYR C 189  ALA C 198  1  O  TYR C 189   N  GLY C 125           
SHEET   13  BD17 GLY C 210  GLY C 219 -1  O  GLY C 210   N  ALA C 198           
SHEET   14  BD17 GLY C  55  TYR C  62 -1  O  GLY C  55   N  GLY C 219           
SHEET   15  BD17 LEU C 224  LEU C 226 -1  O  LEU C 224   N  ILE C  56           
SHEET   16  BD17 ALA C 417  VAL C 425 -1  O  ARG C 424   N  ALA C 225           
SHEET   17  BD17 GLY C 232  MET C 235  1  O  GLY C 232   N  PHE C 420           
SHEET    1  BE 3 ARG B  92  GLY B  94  0                                        
SHEET    2  BE 3 GLN B  66  ASP B  69 -1  O  VAL B  68   N  MET B  93           
SHEET    3  BE 3 LYS B 453  VAL B 455  1  O  LYS B 453   N  TYR B  67           
SHEET    1  BF 2 PHE B 241  TYR B 242  0                                        
SHEET    2  BF 2 ILE B 252  VAL B 253 -1  O  ILE B 252   N  TYR B 242           
SHEET    1  BG 2 TRP B 490  VAL B 495  0                                        
SHEET    2  BG 2 ARG B 501  ARG B 505 -1  O  LYS B 502   N  GLU B 493           
SHEET    1  CA 3 ARG C  92  GLY C  94  0                                        
SHEET    2  CA 3 GLN C  66  ASP C  69 -1  O  VAL C  68   N  MET C  93           
SHEET    3  CA 3 LYS C 453  VAL C 455  1  O  LYS C 453   N  TYR C  67           
SHEET    1  CB 2 PHE C 241  TYR C 242  0                                        
SHEET    2  CB 2 ILE C 252  VAL C 253 -1  O  ILE C 252   N  TYR C 242           
SHEET    1  CC 2 TRP C 490  VAL C 495  0                                        
SHEET    2  CC 2 ARG C 501  ARG C 505 -1  O  LYS C 502   N  GLU C 493           
SHEET    1  DA 3 ARG D  92  GLY D  94  0                                        
SHEET    2  DA 3 GLN D  66  ASP D  69 -1  O  VAL D  68   N  MET D  93           
SHEET    3  DA 3 LYS D 453  VAL D 455  1  O  LYS D 453   N  TYR D  67           
SHEET    1  DB 2 PHE D 241  TYR D 242  0                                        
SHEET    2  DB 2 ILE D 252  VAL D 253 -1  O  ILE D 252   N  TYR D 242           
SHEET    1  DC 2 TRP D 490  VAL D 495  0                                        
SHEET    2  DC 2 ARG D 501  ARG D 505 -1  O  LYS D 502   N  GLU D 493           
SSBOND   1 CYS C  454    CYS D  454                          1555   1564  2.05  
CISPEP   1 GLY A  415    LEU A  416          0        -3.43                     
CISPEP   2 GLY B  415    LEU B  416          0        -4.18                     
CISPEP   3 GLY C  415    LEU C  416          0        -5.32                     
CISPEP   4 GLY D  415    LEU D  416          0        -5.30                     
SITE     1 AC1 27 GLU C  80  ALA C  81  GLY C  82  LYS C  83                    
SITE     2 AC1 27 GLY C  87  GLU C 132  ALA C 165  CYS C 166                    
SITE     3 AC1 27 TYR C 200  ASN C 204  ALA C 205  THR C 208                    
SITE     4 AC1 27 PHE C 241  GLY C 255  SER C 258  HIS C 301                    
SITE     5 AC1 27 PRO C 303  PHE C 304  LYS C 310  ASN C 380                    
SITE     6 AC1 27 GLY C 413  SER C 414  HOH C2136  HOH C2355                    
SITE     7 AC1 27 HOH C2356  HOH C2357  HOH C2358                               
SITE     1 AC2 28 GLU D  80  ALA D  81  GLY D  82  LYS D  83                    
SITE     2 AC2 28 GLY D  87  GLU D 132  ALA D 165  CYS D 166                    
SITE     3 AC2 28 TYR D 200  ASN D 204  ALA D 205  THR D 208                    
SITE     4 AC2 28 PHE D 241  GLY D 255  SER D 258  HIS D 301                    
SITE     5 AC2 28 PRO D 303  PHE D 304  LYS D 306  LYS D 310                    
SITE     6 AC2 28 ASN D 380  GLY D 413  SER D 414  HOH D2128                    
SITE     7 AC2 28 HOH D2217  HOH D2348  HOH D2349  HOH D2350                    
SITE     1 AC3 28 GLU A  80  ALA A  81  GLY A  82  LYS A  83                    
SITE     2 AC3 28 GLY A  87  GLU A 132  ALA A 165  CYS A 166                    
SITE     3 AC3 28 TYR A 200  ASN A 204  ALA A 205  THR A 208                    
SITE     4 AC3 28 PHE A 241  GLY A 255  SER A 258  TYR A 262                    
SITE     5 AC3 28 HIS A 301  PRO A 303  PHE A 304  LYS A 306                    
SITE     6 AC3 28 LYS A 310  ASN A 380  GLY A 413  SER A 414                    
SITE     7 AC3 28 HOH A2144  HOH A2361  HOH A2363  HOH A2364                    
SITE     1 AC4 30 GLU B  80  ALA B  81  GLY B  82  LYS B  83                    
SITE     2 AC4 30 VAL B  86  GLY B  87  GLU B 132  ALA B 165                    
SITE     3 AC4 30 CYS B 166  TYR B 200  ASN B 204  ALA B 205                    
SITE     4 AC4 30 THR B 208  PHE B 241  GLY B 255  SER B 258                    
SITE     5 AC4 30 TYR B 262  HIS B 301  PRO B 303  PHE B 304                    
SITE     6 AC4 30 LYS B 306  LYS B 310  ASN B 380  GLY B 413                    
SITE     7 AC4 30 SER B 414  HOH B2149  HOH B2381  HOH B2382                    
SITE     8 AC4 30 HOH B2383  HOH B2384                                          
SITE     1 AC5  5 SER A 440  SER A 443  HOH A2365  HIS B 396                    
SITE     2 AC5  5 GLU B 401                                                     
CRYST1   66.410   83.514  101.442 100.00 108.08  96.30 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015058  0.001662  0.005414        0.00000                         
SCALE2      0.000000  0.012047  0.002715        0.00000                         
SCALE3      0.000000  0.000000  0.010630        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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