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Database: PDB
Entry: 4OTY
LinkDB: 4OTY
Original site: 4OTY 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 14-FEB-14   4OTY              
TITLE     CRYSTAL STRUCTURE OF LUMIRACOXIB BOUND TO THE APO-MOUSE-              
TITLE    2 CYCLOOXYGENASE-2                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, GLUCOCORTICOID-REGULATED           
COMPND   5 INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, MACROPHAGE ACTIVATION-         
COMPND   6 ASSOCIATED MARKER PROTEIN P71/73, PES-2, PHS II, PROSTAGLANDIN H2    
COMPND   7 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PROSTAGLANDIN-ENDOPEROXIDE       
COMPND   8 SYNTHASE 2, TIS10 PROTEIN;                                           
COMPND   9 EC: 1.14.99.1;                                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PTGS2, COX-2, COX2, PGHS-B, TIS10;                             
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PVL-1393                                  
KEYWDS    PROTEIN-DRUG COMPLEX, OXIDOREDUCTASE, NSAIDS, HEME, GLYCOSYLATION,    
KEYWDS   2 MONOTOPIC MEMBRANE PROTEIN, DRUG COMPLEX, OXIDOREDUCTASE-            
KEYWDS   3 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.XU,M.A.WINDSOR,S.BANERJEE,L.J.MARNETT                               
REVDAT   1   26-FEB-14 4OTY    0                                                
SPRSDE     26-FEB-14 4OTY      4LLZ                                             
JRNL        AUTH   M.A.WINDSOR,P.L.VALK,S.XU,S.BANERJEE,L.J.MARNETT             
JRNL        TITL   EXPLORING THE MOLECULAR DETERMINANTS OF SUBSTRATE-SELECTIVE  
JRNL        TITL 2 INHIBITION OF CYCLOOXYGENASE-2 BY LUMIRACOXIB.               
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  5860 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   24060487                                                     
JRNL        DOI    10.1016/J.BMCL.2013.08.097                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 61543                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1876                            
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 43.1279 -  5.5310    0.99     4803   145  0.1675 0.1988        
REMARK   3     2  5.5310 -  4.3915    1.00     4667   154  0.1430 0.1857        
REMARK   3     3  4.3915 -  3.8368    1.00     4636   154  0.1486 0.1771        
REMARK   3     4  3.8368 -  3.4861    1.00     4612   137  0.1645 0.1982        
REMARK   3     5  3.4861 -  3.2363    1.00     4583   162  0.1975 0.2551        
REMARK   3     6  3.2363 -  3.0456    1.00     4563   154  0.2119 0.2562        
REMARK   3     7  3.0456 -  2.8931    1.00     4585   165  0.2191 0.2769        
REMARK   3     8  2.8931 -  2.7672    1.00     4562   150  0.2206 0.2667        
REMARK   3     9  2.7672 -  2.6607    1.00     4558   134  0.2197 0.2661        
REMARK   3    10  2.6607 -  2.5689    1.00     4585   130  0.2231 0.2867        
REMARK   3    11  2.5689 -  2.4886    1.00     4595   131  0.2245 0.2913        
REMARK   3    12  2.4886 -  2.4174    1.00     4509   138  0.2383 0.3034        
REMARK   3    13  2.4174 -  2.3538    0.96     4409   122  0.2478 0.2857        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.75                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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           9385                                  
REMARK   3   ANGLE     :  0.815          12725                                  
REMARK   3   CHIRALITY :  0.046           1366                                  
REMARK   3   PLANARITY :  0.004           1640                                  
REMARK   3   DIHEDRAL  : 13.618           3461                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 33 through 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -25.6766  64.1701  31.5233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5943 T22:   0.2620                                     
REMARK   3      T33:   0.8141 T12:  -0.1009                                     
REMARK   3      T13:  -0.0289 T23:   0.1372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1490 L22:  -0.0557                                     
REMARK   3      L33:   0.4756 L12:  -0.0578                                     
REMARK   3      L13:  -0.1627 L23:  -0.0783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0531 S12:   0.3675 S13:   0.7171                       
REMARK   3      S21:  -0.0533 S22:   0.0041 S23:  -0.2038                       
REMARK   3      S31:  -0.5580 S32:  -0.1009 S33:  -0.0438                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 94 through 123 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3407  48.1283  28.8831              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4833 T22:   0.6262                                     
REMARK   3      T33:   0.5701 T12:  -0.1237                                     
REMARK   3      T13:  -0.0301 T23:   0.1578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0177 L22:   0.0425                                     
REMARK   3      L33:   0.0088 L12:   0.0078                                     
REMARK   3      L13:  -0.0450 L23:  -0.0217                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1490 S12:   0.1577 S13:   0.2257                       
REMARK   3      S21:   0.1442 S22:  -0.0234 S23:  -0.1558                       
REMARK   3      S31:  -0.1832 S32:   0.2917 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 124 through 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6752  41.9107  26.1587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3167 T22:   0.2920                                     
REMARK   3      T33:   0.2813 T12:   0.0267                                     
REMARK   3      T13:   0.0171 T23:   0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4046 L22:  -0.0556                                     
REMARK   3      L33:   0.2866 L12:   0.0283                                     
REMARK   3      L13:   0.1696 L23:   0.1859                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0249 S12:   0.1134 S13:   0.1599                       
REMARK   3      S21:   0.0488 S22:  -0.0611 S23:  -0.0083                       
REMARK   3      S31:  -0.0959 S32:   0.0611 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 219 through 583 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.5046  30.9817  27.9061              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2937 T22:   0.3023                                     
REMARK   3      T33:   0.2668 T12:   0.0180                                     
REMARK   3      T13:  -0.0034 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8988 L22:   0.1523                                     
REMARK   3      L33:   0.8512 L12:  -0.2764                                     
REMARK   3      L13:   0.2634 L23:   0.0172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0531 S12:   0.2261 S13:   0.0202                       
REMARK   3      S21:   0.0533 S22:  -0.0006 S23:  -0.0010                       
REMARK   3      S31:   0.0411 S32:   0.1858 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resid 33 through 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.2771  37.9112  63.2636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3838 T22:   0.5900                                     
REMARK   3      T33:   0.5475 T12:   0.0042                                     
REMARK   3      T13:  -0.0416 T23:  -0.0791                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1112 L22:   0.0134                                     
REMARK   3      L33:   0.3047 L12:  -0.0823                                     
REMARK   3      L13:   0.2216 L23:  -0.0154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0397 S12:  -0.0339 S13:   0.2244                       
REMARK   3      S21:   0.3235 S22:   0.0799 S23:  -0.1493                       
REMARK   3      S31:   0.2961 S32:   0.4893 S33:  -0.0028                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resid 94 through 123 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9904  62.4089  65.5363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5025 T22:   0.5285                                     
REMARK   3      T33:   0.8583 T12:  -0.0567                                     
REMARK   3      T13:  -0.2718 T23:  -0.1642                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0237 L22:   0.0343                                     
REMARK   3      L33:   0.0847 L12:  -0.0055                                     
REMARK   3      L13:   0.0176 L23:  -0.0083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2975 S12:   0.1838 S13:   0.3962                       
REMARK   3      S21:   0.0830 S22:   0.0652 S23:  -0.0368                       
REMARK   3      S31:  -0.2687 S32:   0.1631 S33:  -0.2049                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 124 through 181 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.1116  28.0171  65.4098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3924 T22:   0.3692                                     
REMARK   3      T33:   0.2827 T12:   0.0539                                     
REMARK   3      T13:  -0.0415 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1286 L22:   0.0182                                     
REMARK   3      L33:   0.0313 L12:   0.0422                                     
REMARK   3      L13:  -0.0178 L23:   0.0002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0502 S12:  -0.0764 S13:   0.0325                       
REMARK   3      S21:  -0.1079 S22:  -0.0199 S23:   0.0743                       
REMARK   3      S31:   0.3004 S32:   0.1905 S33:   0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 182 through 218 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.5781  42.6346  73.7845              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2721 T22:   0.6256                                     
REMARK   3      T33:   0.2910 T12:   0.0098                                     
REMARK   3      T13:   0.0001 T23:  -0.1553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0548 L22:   0.6440                                     
REMARK   3      L33:   0.1298 L12:   0.1315                                     
REMARK   3      L13:  -0.1179 L23:  -0.2543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1304 S12:  -0.4233 S13:   0.2887                       
REMARK   3      S21:  -0.3672 S22:  -0.1124 S23:   0.0858                       
REMARK   3      S31:   0.1793 S32:  -0.0528 S33:  -0.0786                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resid 219 through 390 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5389  48.5663  59.6827              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2536 T22:   0.2861                                     
REMARK   3      T33:   0.3231 T12:   0.0020                                     
REMARK   3      T13:  -0.0173 T23:  -0.0963                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5180 L22:   0.4447                                     
REMARK   3      L33:   0.4683 L12:  -0.1855                                     
REMARK   3      L13:   0.4220 L23:   0.0025                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0350 S12:  -0.2906 S13:   0.2406                       
REMARK   3      S21:  -0.1118 S22:  -0.0127 S23:  -0.0327                       
REMARK   3      S31:  -0.0110 S32:  -0.1123 S33:  -0.0036                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resid 391 through 428 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.7433  47.9820  80.3527              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4448 T22:   0.9901                                     
REMARK   3      T33:   0.4336 T12:   0.0514                                     
REMARK   3      T13:  -0.0214 T23:  -0.1783                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0204 L22:   0.0157                                     
REMARK   3      L33:   0.0200 L12:   0.0140                                     
REMARK   3      L13:  -0.0380 L23:  -0.0242                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1445 S12:  -0.5541 S13:   0.0867                       
REMARK   3      S21:  -0.0228 S22:   0.0704 S23:   0.2056                       
REMARK   3      S31:  -0.0089 S32:  -0.3821 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resid 429 through 485 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2348  36.6306  78.0541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4549 T22:   0.6126                                     
REMARK   3      T33:   0.3307 T12:   0.0050                                     
REMARK   3      T13:  -0.0750 T23:  -0.0937                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3100 L22:   0.1563                                     
REMARK   3      L33:   0.3430 L12:   0.2425                                     
REMARK   3      L13:  -0.1901 L23:  -0.1631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1316 S12:  -0.3474 S13:  -0.0768                       
REMARK   3      S21:   0.1126 S22:   0.0269 S23:  -0.1048                       
REMARK   3      S31:   0.2857 S32:   0.0504 S33:  -0.0472                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resid 486 through 582 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.0353  49.9335  68.5386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1829 T22:   0.2704                                     
REMARK   3      T33:   0.2673 T12:  -0.0595                                     
REMARK   3      T13:  -0.1663 T23:  -0.3696                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4357 L22:   1.0241                                     
REMARK   3      L33:   1.3453 L12:   0.0166                                     
REMARK   3      L13:   0.3021 L23:  -0.5084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1610 S12:  -0.2524 S13:   1.0246                       
REMARK   3      S21:  -0.2498 S22:  -0.5706 S23:  -0.7479                       
REMARK   3      S31:   0.0809 S32:   0.3965 S33:  -0.6122                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4OTY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084944.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61543                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.700                              
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 3NT1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MCOX-2 PROTEIN RECONSTITUTED WITH A 2-   
REMARK 280  FOLD MOLAR EXCESS OF HEME IN PHOSPHTATE BUFFER, PH 6.7, 100 MM      
REMARK 280  NACL, 1.2% (W/V) -OG, AND 0.1% NAN3, AND 10-FOLD MOLAR EXCESS OF    
REMARK 280  INHIBITORS FROM 25 MM DMSO STOCKS WERE ADDED TO PROTEIN SAMPLES.    
REMARK 280  MIXING 3 UL OF THE PROTEIN-INHIBITOR COMPLEX WITH 3 UL              
REMARK 280  CRYSTALLIZATION SOLUTION CONTAINING 50 MM EPPS, PH 8.0, 120 MM      
REMARK 280  MGCL2, 22-26% PEG MME-550 AGAINST RESERVOIR SOLUTIONS COMPRISED     
REMARK 280  OF 50 MM EPPS PH 8.0, 120 MM MGCL2, 22-26% PEG MME-550, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       61.33150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.58650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.77300            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       61.33150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.58650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.77300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       61.33150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.58650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.77300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       61.33150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.58650            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.77300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 8170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 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     ASP A   584                                                      
REMARK 465     PRO A   585                                                      
REMARK 465     GLN A   586                                                      
REMARK 465     PRO A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     LYS A   589                                                      
REMARK 465     THR A   590                                                      
REMARK 465     ALA A   591                                                      
REMARK 465     THR A   592                                                      
REMARK 465     ILE A   593                                                      
REMARK 465     ASN A   594                                                      
REMARK 465     ALA A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     ALA A   597                                                      
REMARK 465     SER A   598                                                      
REMARK 465     HIS A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     ARG A   601                                                      
REMARK 465     LEU A   602                                                      
REMARK 465     ASP A   603                                                      
REMARK 465     ASP A   604                                                      
REMARK 465     ILE A   605                                                      
REMARK 465     ASN A   606                                                      
REMARK 465     PRO A   607                                                      
REMARK 465     THR A   608                                                      
REMARK 465     VAL A   609                                                      
REMARK 465     LEU A   610                                                      
REMARK 465     ILE A   611                                                      
REMARK 465     LYS A   612                                                      
REMARK 465     ARG A   613                                                      
REMARK 465     ARG A   614                                                      
REMARK 465     SER A   615                                                      
REMARK 465     THR A   616                                                      
REMARK 465     GLU A   617                                                      
REMARK 465     LEU A   618                                                      
REMARK 465     GLN B   583                                                      
REMARK 465     ASP B   584                                                      
REMARK 465     PRO B   585                                                      
REMARK 465     GLN B   586                                                      
REMARK 465     PRO B   587                                                      
REMARK 465     THR B   588                                                      
REMARK 465     LYS B   589                                                      
REMARK 465     THR B   590                                                      
REMARK 465     ALA B   591                                                      
REMARK 465     THR B   592                                                      
REMARK 465     ILE B   593                                                      
REMARK 465     ASN B   594                                                      
REMARK 465     ALA B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     ALA B   597                                                      
REMARK 465     SER B   598                                                      
REMARK 465     HIS B   599                                                      
REMARK 465     SER B   600                                                      
REMARK 465     ARG B   601                                                      
REMARK 465     LEU B   602                                                      
REMARK 465     ASP B   603                                                      
REMARK 465     ASP B   604                                                      
REMARK 465     ILE B   605                                                      
REMARK 465     ASN B   606                                                      
REMARK 465     PRO B   607                                                      
REMARK 465     THR B   608                                                      
REMARK 465     VAL B   609                                                      
REMARK 465     LEU B   610                                                      
REMARK 465     ILE B   611                                                      
REMARK 465     LYS B   612                                                      
REMARK 465     ARG B   613                                                      
REMARK 465     ARG B   614                                                      
REMARK 465     SER B   615                                                      
REMARK 465     THR B   616                                                      
REMARK 465     GLU B   617                                                      
REMARK 465     LEU B   618                                                      
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    THR A 129      -87.54   -121.89                                   
REMARK 500    GLU A 398      -94.15     71.73                                   
REMARK 500    ASN A 439       17.14   -143.88                                   
REMARK 500    SER A 496      -52.47     76.58                                   
REMARK 500    THR B 129      -92.83   -110.03                                   
REMARK 500    GLU B 398     -101.91     57.69                                   
REMARK 500    ASN B 439       19.06   -146.70                                   
REMARK 500    SER B 496      -54.90     81.36                                   
REMARK 500    ASN B 571      -22.56   -152.61                                   
REMARK 500    CYS B 575       79.55     54.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 920        DISTANCE =  7.98 ANGSTROMS                       
REMARK 525    HOH A 923        DISTANCE =  7.80 ANGSTROMS                       
REMARK 525    HOH A 947        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH B 949        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH B 951        DISTANCE =  8.60 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUR A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LUR B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 704 BOUND   
REMARK 800  TO ASN A 68                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A   
REMARK 800  144 RESIDUES 701 TO 702                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG A 703 BOUND   
REMARK 800  TO ASN A 410                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 704 BOUND   
REMARK 800  TO ASN B 68                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B   
REMARK 800  144 RESIDUES 701 TO 702                                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE NAG B 703 BOUND   
REMARK 800  TO ASN B 410                                                        
DBREF  4OTY A   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
DBREF  4OTY B   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
SEQRES   1 A  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 A  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 A  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 A  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 A  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 A  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 A  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 A  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 A  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 A  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 A  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 A  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 A  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 A  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 A  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 A  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 A  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 A  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 A  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 A  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 A  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 A  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 A  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 A  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 A  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 A  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 A  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 A  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 A  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 A  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 A  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 A  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 A  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 A  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 A  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 A  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 A  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 A  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 A  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 A  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 A  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 A  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 A  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 A  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 A  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 A  587  GLU LEU                                                      
SEQRES   1 B  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 B  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 B  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 B  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 B  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 B  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 B  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 B  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 B  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 B  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 B  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 B  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 B  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 B  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 B  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 B  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 B  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 B  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 B  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 B  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 B  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 B  587  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 B  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 B  587  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 B  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 B  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 B  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 B  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 B  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 B  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 B  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 B  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 B  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 B  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 B  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 B  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 B  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 B  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 B  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 B  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 B  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 B  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 B  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 B  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 B  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 B  587  GLU LEU                                                      
MODRES 4OTY ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 4OTY ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4OTY ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 4OTY ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4OTY ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 4OTY ASN A   68  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 701      14                                                       
HET    NAG  A 702      14                                                       
HET    NAG  A 703      14                                                       
HET    NAG  A 704      14                                                       
HET    LUR  A 705      20                                                       
HET    NAG  B 701      14                                                       
HET    NAG  B 702      14                                                       
HET    NAG  B 703      14                                                       
HET    NAG  B 704      14                                                       
HET    LUR  B 705      20                                                       
HET    BOG  B 706      20                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     LUR {2-[(2-CHLORO-6-FLUOROPHENYL)AMINO]-5-                           
HETNAM   2 LUR  METHYLPHENYL}ACETIC ACID                                        
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETSYN     LUR LUMIRACOXIB                                                      
FORMUL   3  NAG    8(C8 H15 N O6)                                               
FORMUL   6  LUR    2(C15 H13 CL F N O2)                                         
FORMUL  11  BOG    C14 H28 O6                                                   
FORMUL  12  HOH   *307(H2 O)                                                    
HELIX    1   1 GLU A   73  LYS A   83  1                                  11    
HELIX    2   2 THR A   85  THR A   94  1                                  10    
HELIX    3   3 PHE A   96  ASN A  104  1                                   9    
HELIX    4   4 ILE A  105A TYR A  122  1                                  18    
HELIX    5   5 SER A  138  ASN A  144  1                                   7    
HELIX    6   6 ASP A  173  LEU A  182  1                                  10    
HELIX    7   7 ASN A  195  HIS A  207  1                                  13    
HELIX    8   8 LEU A  230  GLY A  235  1                                   6    
HELIX    9   9 THR A  237  ARG A  245  1                                   9    
HELIX   10  10 PRO A  280  GLN A  284  5                                   5    
HELIX   11  11 VAL A  295  HIS A  320  1                                  26    
HELIX   12  12 GLY A  324  ASP A  347  1                                  24    
HELIX   13  13 ASP A  347  GLY A  354  1                                   8    
HELIX   14  14 ASP A  362  PHE A  367  5                                   6    
HELIX   15  15 ALA A  378  TYR A  385  1                                   8    
HELIX   16  16 TRP A  387  LEU A  391  5                                   5    
HELIX   17  17 SER A  403  LEU A  408  1                                   6    
HELIX   18  18 ASN A  411  GLY A  418  1                                   8    
HELIX   19  19 LEU A  419  GLN A  429  1                                  11    
HELIX   20  20 PRO A  441  ALA A  443  5                                   3    
HELIX   21  21 VAL A  444  MET A  458  1                                  15    
HELIX   22  22 SER A  462  PHE A  470  1                                   9    
HELIX   23  23 SER A  477  GLY A  483  1                                   7    
HELIX   24  24 LYS A  485  SER A  496  1                                  12    
HELIX   25  25 ASP A  497  MET A  501  5                                   5    
HELIX   26  26 GLU A  502  GLU A  510  1                                   9    
HELIX   27  27 GLY A  519  GLY A  536  1                                  18    
HELIX   28  28 ASN A  537  SER A  541  5                                   5    
HELIX   29  29 LYS A  546  GLY A  551  5                                   6    
HELIX   30  30 GLY A  552  THR A  561  1                                  10    
HELIX   31  31 SER A  563  VAL A  572  1                                  10    
HELIX   32  32 GLU B   73  LYS B   83  1                                  11    
HELIX   33  33 THR B   85  THR B   94  1                                  10    
HELIX   34  34 PHE B   96  ASN B  105  1                                  10    
HELIX   35  35 ILE B  105A TYR B  122  1                                  18    
HELIX   36  36 SER B  138  ASN B  144  1                                   7    
HELIX   37  37 ASP B  173  LEU B  182  1                                  10    
HELIX   38  38 ASN B  195  HIS B  207  1                                  13    
HELIX   39  39 LEU B  230  GLY B  235  1                                   6    
HELIX   40  40 THR B  237  ARG B  245  1                                   9    
HELIX   41  41 THR B  265  GLN B  270  1                                   6    
HELIX   42  42 PRO B  280  GLN B  284  5                                   5    
HELIX   43  43 VAL B  295  HIS B  320  1                                  26    
HELIX   44  44 GLY B  324  ASP B  347  1                                  24    
HELIX   45  45 ASP B  347  GLY B  354  1                                   8    
HELIX   46  46 ASP B  362  PHE B  367  5                                   6    
HELIX   47  47 ALA B  378  TYR B  385  1                                   8    
HELIX   48  48 TRP B  387  LEU B  391  5                                   5    
HELIX   49  49 SER B  403  LEU B  408  1                                   6    
HELIX   50  50 ASN B  411  GLN B  429  1                                  19    
HELIX   51  51 PRO B  441  ALA B  443  5                                   3    
HELIX   52  52 VAL B  444  MET B  458  1                                  15    
HELIX   53  53 SER B  462  PHE B  470  1                                   9    
HELIX   54  54 SER B  477  GLY B  483  1                                   7    
HELIX   55  55 LYS B  485  SER B  496  1                                  12    
HELIX   56  56 ASP B  497  MET B  501  5                                   5    
HELIX   57  57 GLU B  502  GLU B  510  1                                   9    
HELIX   58  58 GLY B  519  GLY B  536  1                                  18    
HELIX   59  59 ASN B  537  SER B  541  5                                   5    
HELIX   60  60 LYS B  546  GLY B  551  5                                   6    
HELIX   61  61 GLY B  552  THR B  561  1                                  10    
HELIX   62  62 SER B  563  ASN B  570  1                                   8    
SHEET    1   A 2 GLU A  46  SER A  49  0                                        
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46           
SHEET    1   B 2 PHE A  64  TYR A  65  0                                        
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65           
SHEET    1   C 2 GLN A 255  ILE A 257  0                                        
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257           
SHEET    1   D 2 PHE A 395  ILE A 397  0                                        
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  TYR A 402   N  PHE A 395           
SHEET    1   E 2 GLU B  46  SER B  49  0                                        
SHEET    2   E 2 TYR B  55  ASP B  58 -1  O  ASP B  58   N  GLU B  46           
SHEET    1   F 2 PHE B  64  TYR B  65  0                                        
SHEET    2   F 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   G 2 TYR B 130  ASN B 131  0                                        
SHEET    2   G 2 THR B 149  ARG B 150 -1  O  ARG B 150   N  TYR B 130           
SHEET    1   H 2 GLN B 255  ILE B 257  0                                        
SHEET    2   H 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   I 2 PHE B 395  ILE B 397  0                                        
SHEET    2   I 2 GLN B 400  TYR B 402 -1  O  TYR B 402   N  PHE B 395           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  1.98  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.02  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.04  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.03  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.03  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.01  
LINK         ND2 ASN B  68                 C1  NAG B 704     1555   1555  1.34  
LINK         ND2 ASN A 144                 C1  NAG A 701     1555   1555  1.43  
LINK         ND2 ASN A 410                 C1  NAG A 703     1555   1555  1.44  
LINK         ND2 ASN B 144                 C1  NAG B 701     1555   1555  1.44  
LINK         ND2 ASN B 410                 C1  NAG B 703     1555   1555  1.44  
LINK         O4  NAG A 701                 C1  NAG A 702     1555   1555  1.44  
LINK         ND2 ASN A  68                 C1  NAG A 704     1555   1555  1.44  
LINK         O4  NAG B 701                 C1  NAG B 702     1555   1555  1.44  
CISPEP   1 SER A  126    PRO A  127          0        -1.04                     
CISPEP   2 SER B  126    PRO B  127          0         6.20                     
SITE     1 AC1 12 TYR A 348  VAL A 349  LEU A 352  SER A 353                    
SITE     2 AC1 12 TYR A 385  TRP A 387  MET A 522  VAL A 523                    
SITE     3 AC1 12 GLY A 526  ALA A 527  SER A 530  HOH A 904                    
SITE     1 AC2 11 TYR B 348  VAL B 349  LEU B 352  TYR B 385                    
SITE     2 AC2 11 TRP B 387  MET B 522  GLY B 526  ALA B 527                    
SITE     3 AC2 11 SER B 530  LEU B 531  HOH B 869                               
SITE     1 AC3  9 GLU A 179  LEU A 183  ARG A 185  ILE A 442                    
SITE     2 AC3  9 GLN A 445  ARG B 185  ARG B 438  GLU B 486                    
SITE     3 AC3  9 GLU B 490                                                     
SITE     1 AC4  3 TYR A  55  GLU A  67  ASN A  68                               
SITE     1 AC5  6 GLU A 140  ASN A 144  TYR A 147  ARG A 216                    
SITE     2 AC5  6 HOH A 804  HOH A 863                                          
SITE     1 AC6  6 GLN A 406  ASN A 410  ILE A 413  GLU A 416                    
SITE     2 AC6  6 HOH A 912  HOH A 951                                          
SITE     1 AC7  3 TYR B  55  GLU B  67  ASN B  68                               
SITE     1 AC8  6 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     2 AC8  6 HOH B 841  HOH B 842                                          
SITE     1 AC9  6 GLN B 406  ASN B 410  SER B 412  ILE B 413                    
SITE     2 AC9  6 GLU B 416  HOH B 945                                          
CRYST1  122.663  133.173  181.546  90.00  90.00  90.00 I 2 2 2      16          
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      0.008152  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007509  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005508        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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