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Database: PDB
Entry: 3Q7D
LinkDB: 3Q7D
Original site: 3Q7D 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-JAN-11   3Q7D              
TITLE     STRUCTURE OF (R)-NAPROXEN BOUND TO MCOX-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: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROSTAGLANDIN H2 SYNTHASE, CYCLOOXYGENASE-2, NAPROXEN,                
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.C.DUGGAN,D.J.HERMANSON,J.MUSEE,J.J.PRUSAKIEWICZ,J.SCHEIB,           
AUTHOR   2 B.D.CARTER,S.BANERJEE,L.J.MARNETT                                    
REVDAT   3   28-MAR-12 3Q7D    1       JRNL                                     
REVDAT   2   21-MAR-12 3Q7D    1       JRNL                                     
REVDAT   1   09-NOV-11 3Q7D    0                                                
JRNL        AUTH   K.C.DUGGAN,D.J.HERMANSON,J.MUSEE,J.J.PRUSAKIEWICZ,           
JRNL        AUTH 2 J.L.SCHEIB,B.D.CARTER,S.BANERJEE,J.A.OATES,L.J.MARNETT       
JRNL        TITL   (R)-PROFENS ARE SUBSTRATE-SELECTIVE INHIBITORS OF            
JRNL        TITL 2 ENDOCANNABINOID OXYGENATION BY COX-2.                        
JRNL        REF    NAT.CHEM.BIOL.                V.   7   803 2011              
JRNL        REFN                   ISSN 1552-4450                               
JRNL        PMID   22053353                                                     
JRNL        DOI    10.1038/NCHEMBIO.663                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 55701                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2799                            
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 29.5919 -  6.4928    0.99     2874   158  0.1962 0.2275        
REMARK   3     2  6.4928 -  5.1624    0.99     2818   139  0.1884 0.2202        
REMARK   3     3  5.1624 -  4.5125    0.99     2785   146  0.1332 0.1717        
REMARK   3     4  4.5125 -  4.1011    0.99     2767   126  0.1414 0.1902        
REMARK   3     5  4.1011 -  3.8078    0.99     2713   177  0.1417 0.1934        
REMARK   3     6  3.8078 -  3.5837    1.00     2741   149  0.1508 0.1900        
REMARK   3     7  3.5837 -  3.4045    0.99     2728   155  0.1755 0.2385        
REMARK   3     8  3.4045 -  3.2565    0.99     2731   127  0.1898 0.2425        
REMARK   3     9  3.2565 -  3.1312    0.98     2675   154  0.1956 0.2651        
REMARK   3    10  3.1312 -  3.0233    0.97     2660   140  0.2035 0.2618        
REMARK   3    11  3.0233 -  2.9288    0.96     2649   136  0.1991 0.2500        
REMARK   3    12  2.9288 -  2.8452    0.96     2577   154  0.1907 0.2625        
REMARK   3    13  2.8452 -  2.7704    0.95     2617   137  0.1992 0.2492        
REMARK   3    14  2.7704 -  2.7028    0.93     2568   133  0.1966 0.2841        
REMARK   3    15  2.7028 -  2.6414    0.93     2539   140  0.1998 0.3118        
REMARK   3    16  2.6414 -  2.5852    0.92     2524   122  0.2072 0.2478        
REMARK   3    17  2.5852 -  2.5335    0.92     2491   135  0.1923 0.2985        
REMARK   3    18  2.5335 -  2.4858    0.92     2528   133  0.1882 0.2827        
REMARK   3    19  2.4858 -  2.4414    0.90     2454   118  0.1925 0.2967        
REMARK   3    20  2.4414 -  2.4000    0.90     2463   120  0.1972 0.2860        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.30                                          
REMARK   3   B_SOL              : 25.02                                         
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) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.13600                                              
REMARK   3    B22 (A**2) : 3.23520                                              
REMARK   3    B33 (A**2) : -9.37120                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.008           9560                                  
REMARK   3   ANGLE     :  1.270          12969                                  
REMARK   3   CHIRALITY :  0.090           1381                                  
REMARK   3   PLANARITY :  0.005           1646                                  
REMARK   3   DIHEDRAL  : 19.941           3639                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3Q7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063286.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
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) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3NT1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
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       61.36750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.51400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       90.51950            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       61.36750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.51400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.51950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       61.36750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.51400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.51950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       61.36750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.51400            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       90.51950            
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: 12900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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     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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    SER B   138     O    HOH B   756              2.03            
REMARK 500   N    TYR B   130     O    HOH B   869              2.07            
REMARK 500   O    GLU B   281     N    LEU B   283              2.07            
REMARK 500   N    TYR A   130     O    HOH A   751              2.09            
REMARK 500   N    SER A   138     O    HOH A   908              2.10            
REMARK 500   ND2  ASN B   144     C1   NAG B   671              2.16            
REMARK 500   O    GLY B   418     O    GLN B   421              2.16            
REMARK 500   O    GLY B   574     O    HOH B   758              2.19            
REMARK 500   O4   NAG B   671     O5   NAG B     9              2.19            
REMARK 500   OE2  GLU B   322     O    HOH B   722              2.19            
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 376   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 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    TYR A 130      139.51     59.94                                   
REMARK 500    SER A 138      156.77    -28.51                                   
REMARK 500    ARG A 185      -83.20    -93.48                                   
REMARK 500    VAL A 287      -31.25     45.90                                   
REMARK 500    TRP A 387       43.32   -100.05                                   
REMARK 500    GLU A 398      103.61    -13.21                                   
REMARK 500    ASP A 399      -45.22    119.38                                   
REMARK 500    TYR A 409       60.32     35.71                                   
REMARK 500    PHE A 422      -63.75    101.36                                   
REMARK 500    ASN A 439       14.85   -140.72                                   
REMARK 500    GLU A 484     -168.84   -126.83                                   
REMARK 500    SER A 496      -40.07     78.59                                   
REMARK 500    ASP A 499        6.54    -68.38                                   
REMARK 500    PRO A 514      -77.05    -22.51                                   
REMARK 500    LYS A 573      -68.15    -22.29                                   
REMARK 500    LEU B  81       46.35    -91.92                                   
REMARK 500    LEU B  82        3.26   -162.37                                   
REMARK 500    TYR B 130      144.31     63.31                                   
REMARK 500    LYS B 137      -75.31    -49.90                                   
REMARK 500    SER B 138      140.68     56.80                                   
REMARK 500    ARG B 185      -80.14    -90.05                                   
REMARK 500    ASN B 195     -168.69   -115.57                                   
REMARK 500    PRO B 263      156.74    -48.61                                   
REMARK 500    GLU B 281     -147.36     40.05                                   
REMARK 500    ASN B 282      -36.08     38.52                                   
REMARK 500    VAL B 287      -23.00     51.41                                   
REMARK 500    GLU B 398      104.23    -25.66                                   
REMARK 500    ASP B 399      -36.15    113.76                                   
REMARK 500    TYR B 409       61.61     23.19                                   
REMARK 500    PHE B 422      -60.73    114.74                                   
REMARK 500    ASN B 439       18.26   -140.35                                   
REMARK 500    SER B 496      -34.92     75.35                                   
REMARK 500    PRO B 514      -87.88    -16.87                                   
REMARK 500    LYS B 573      -77.22    -21.64                                   
REMARK 500    CYS B 575       60.39    142.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B  288     GLN B  289                  144.60                    
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 A 287        21.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 287        21.9      L          L   OUTSIDE RANGE           
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 819        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A 881        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH A 886        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH A 887        DISTANCE =  8.99 ANGSTROMS                       
REMARK 525    HOH A 902        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A 903        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH A 910        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH A 911        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH A 917        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH A 918        DISTANCE = 11.66 ANGSTROMS                       
REMARK 525    HOH B 873        DISTANCE =  8.26 ANGSTROMS                       
REMARK 525    HOH B 880        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH B 883        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH B 885        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH B 892        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH B 895        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH B 917        DISTANCE =  9.14 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  661                                                       
REMARK 610     NAG A  671                                                       
REMARK 610     NAG A  681                                                       
REMARK 610     NAG A    9                                                       
REMARK 610     NAG B  661                                                       
REMARK 610     NAG B  671                                                       
REMARK 610     NAG B  681                                                       
REMARK 610     NAG B    9                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 HEM A 682   NA   95.7                                              
REMARK 620 3 HEM A 682   NB   92.5  89.2                                        
REMARK 620 4 HEM A 682   NC   91.9 172.3  91.9                                  
REMARK 620 5 HEM A 682   ND   92.2  91.0 175.3  87.3                            
REMARK 620 6 HOH A 645   O   175.4  79.8  87.8  92.7  87.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 388   NE2                                                    
REMARK 620 2 HEM B 682   NA   94.3                                              
REMARK 620 3 HEM B 682   NB   90.8  90.6                                        
REMARK 620 4 HEM B 682   NC   91.4 174.3  88.6                                  
REMARK 620 5 HEM B 682   ND   91.2  91.4 177.1  89.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPX A 1591                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPX B 1591                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1                    
DBREF  3Q7D A   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
DBREF  3Q7D 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                                                      
HET    NAG  A 661      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 681      14                                                       
HET    HEM  A 682      43                                                       
HET    NPX  A1591      17                                                       
HET    BOG  A   3      20                                                       
HET    BOG  A   6      20                                                       
HET    BOG  A 620      20                                                       
HET    NAG  A   9      14                                                       
HET     CL  A   1       1                                                       
HET    NAG  B 661      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 681      14                                                       
HET    HEM  B 682      43                                                       
HET    NPX  B1591      17                                                       
HET    BOG  B   3      20                                                       
HET    BOG  B 620      20                                                       
HET    NAG  B   9      14                                                       
HET     CL  B   1       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     NPX (2R)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC ACID                  
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM      CL CHLORIDE ION                                                     
HETSYN     HEM HEME                                                             
HETSYN     NPX (R)-NAPROXEN                                                     
FORMUL   3  NAG    8(C8 H15 N O6)                                               
FORMUL   6  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   7  NPX    2(C14 H14 O3)                                                
FORMUL   8  BOG    5(C14 H28 O6)                                                
FORMUL  12   CL    2(CL 1-)                                                     
FORMUL  22  HOH   *598(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  105  1                                  10    
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 THR A  265  GLN A  270  1                                   6    
HELIX   11  11 PRO A  280  GLN A  284  5                                   5    
HELIX   12  12 VAL A  291  LEU A  294  5                                   4    
HELIX   13  13 VAL A  295  HIS A  320  1                                  26    
HELIX   14  14 GLY A  324  ASP A  347  1                                  24    
HELIX   15  15 ASP A  347  GLY A  354  1                                   8    
HELIX   16  16 ASP A  362  PHE A  367  5                                   6    
HELIX   17  17 ALA A  378  TYR A  385  1                                   8    
HELIX   18  18 TRP A  387  LEU A  391  5                                   5    
HELIX   19  19 SER A  403  LEU A  408  1                                   6    
HELIX   20  20 ASN A  411  GLY A  418  1                                   8    
HELIX   21  21 LEU A  419  GLN A  429  1                                  11    
HELIX   22  22 PRO A  441  ALA A  443  5                                   3    
HELIX   23  23 VAL A  444  MET A  458  1                                  15    
HELIX   24  24 SER A  462  PHE A  470  1                                   9    
HELIX   25  25 SER A  477  GLY A  483  1                                   7    
HELIX   26  26 LYS A  485  SER A  496  1                                  12    
HELIX   27  27 ASP A  497  MET A  501  5                                   5    
HELIX   28  28 GLU A  502  GLU A  510  1                                   9    
HELIX   29  29 GLY A  519  ASN A  537  1                                  19    
HELIX   30  30 PRO A  538  SER A  541  5                                   4    
HELIX   31  31 LYS A  546  GLY A  551  5                                   6    
HELIX   32  32 GLY A  552  THR A  561  1                                  10    
HELIX   33  33 SER A  563  VAL A  572  1                                  10    
HELIX   34  34 GLU B   73  LEU B   81  1                                   9    
HELIX   35  35 THR B   85  THR B   94  1                                  10    
HELIX   36  36 PHE B   96  ASN B  104  1                                   9    
HELIX   37  37 ILE B  105A TYR B  122  1                                  18    
HELIX   38  38 SER B  138  ASN B  144  1                                   7    
HELIX   39  39 ASP B  173  LEU B  182  1                                  10    
HELIX   40  40 ASN B  195  HIS B  207  1                                  13    
HELIX   41  41 LEU B  230  GLY B  235  1                                   6    
HELIX   42  42 THR B  237  ARG B  245  1                                   9    
HELIX   43  43 THR B  265  GLN B  270  1                                   6    
HELIX   44  44 VAL B  291  LEU B  294  5                                   4    
HELIX   45  45 VAL B  295  HIS B  320  1                                  26    
HELIX   46  46 GLY B  324  ASP B  347  1                                  24    
HELIX   47  47 ASP B  347  GLY B  354  1                                   8    
HELIX   48  48 ASP B  362  PHE B  367  5                                   6    
HELIX   49  49 ALA B  378  TYR B  385  1                                   8    
HELIX   50  50 HIS B  386  LEU B  391  5                                   6    
HELIX   51  51 SER B  403  LEU B  408  1                                   6    
HELIX   52  52 ASN B  411  GLY B  418  1                                   8    
HELIX   53  53 LEU B  419  GLN B  429  1                                  11    
HELIX   54  54 PRO B  441  ALA B  443  5                                   3    
HELIX   55  55 VAL B  444  MET B  458  1                                  15    
HELIX   56  56 SER B  462  PHE B  470  1                                   9    
HELIX   57  57 SER B  477  GLY B  483  1                                   7    
HELIX   58  58 LYS B  485  SER B  496  1                                  12    
HELIX   59  59 ASP B  497  MET B  501  5                                   5    
HELIX   60  60 GLU B  502  GLU B  510  1                                   9    
HELIX   61  61 GLY B  519  GLY B  536  1                                  18    
HELIX   62  62 ASN B  537  SER B  541  5                                   5    
HELIX   63  63 LYS B  546  GLY B  551  5                                   6    
HELIX   64  64 GLY B  552  ALA B  562  1                                  11    
HELIX   65  65 SER B  563  VAL B  572  1                                  10    
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  TYR A 262   N  GLN A 255           
SHEET    1   D 2 GLU B  46  SER B  49  0                                        
SHEET    2   D 2 TYR B  55  ASP B  58 -1  O  LYS B  56   N  MET B  48           
SHEET    1   E 2 PHE B  64  TYR B  65  0                                        
SHEET    2   E 2 THR B  71  PRO B  72 -1  O  THR B  71   N  TYR B  65           
SHEET    1   F 2 GLN B 255  ILE B 257  0                                        
SHEET    2   F 2 GLU B 260  TYR B 262 -1  O  TYR B 262   N  GLN B 255           
SHEET    1   G 2 PHE B 395  ILE B 397  0                                        
SHEET    2   G 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  2.07  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.05  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.05  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.05  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.04  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.05  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.05  
LINK         NE2 HIS A 388                FE   HEM A 682     1555   1555  2.19  
LINK         NE2 HIS B 388                FE   HEM B 682     1555   1555  2.23  
LINK        FE   HEM A 682                 O   HOH A 645     1555   1555  2.78  
CISPEP   1 SER A  126    PRO A  127          0        -1.33                     
CISPEP   2 SER B  126    PRO B  127          0         0.75                     
SITE     1 AC1  4 TYR A  55  GLU A  67  ASN A  68  HOH A 885                    
SITE     1 AC2  8 NAG A   9  GLU A 140  ASN A 144  TYR A 147                    
SITE     2 AC2  8 ARG A 216  HOH A 676  HOH A 678  HOH A 824                    
SITE     1 AC3  7 GLN A 406  ASN A 410  SER A 412  ILE A 413                    
SITE     2 AC3  7 GLU A 416  HOH A 855  HOH A 867                               
SITE     1 AC4 15 ALA A 199  GLN A 203  HIS A 207  PHE A 210                    
SITE     2 AC4 15 LYS A 211  THR A 212  HIS A 214  VAL A 295                    
SITE     3 AC4 15 ASN A 382  TYR A 385  HIS A 386  HIS A 388                    
SITE     4 AC4 15 LEU A 391  LEU A 408  HOH A 645                               
SITE     1 AC5 10 VAL A 116  ARG A 120  VAL A 349  LEU A 352                    
SITE     2 AC5 10 SER A 353  TYR A 355  TYR A 385  TRP A 387                    
SITE     3 AC5 10 ALA A 527  SER A 530                                          
SITE     1 AC6 11 LYS A 180  ARG A 184  ARG A 185  ARG A 438                    
SITE     2 AC6 11 GLU A 486  GLU A 490  GLU B 179  ARG B 184                    
SITE     3 AC6 11 ARG B 185  ILE B 442  GLN B 445                               
SITE     1 AC7  7 PRO A  84  PRO A  86  TYR A 115  SER A 119                    
SITE     2 AC7  7 ARG A 120  GLU A 524  HOH A 664                               
SITE     1 AC8  2 ASN A  87  HOH A 900                                          
SITE     1 AC9  3 ARG A 216  NAG A 671  HOH A 893                               
SITE     1 BC1  3 PHE A 205  TYR A 385  SER A 530                               
SITE     1 BC2  4 TYR B  55  GLU B  67  ASN B  68  HOH B 890                    
SITE     1 BC3  6 NAG B   9  HOH B  26  ASN B 144  ARG B 216                    
SITE     2 BC3  6 HOH B 667  HOH B 819                                          
SITE     1 BC4  9 TYR B 402  GLN B 406  ASN B 410  SER B 412                    
SITE     2 BC4  9 ILE B 413  GLU B 416  HOH B 727  HOH B 775                    
SITE     3 BC4  9 HOH B 889                                                     
SITE     1 BC5 15 ALA B 199  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 BC5 15 LYS B 211  THR B 212  HIS B 214  VAL B 295                    
SITE     3 BC5 15 ASN B 382  TYR B 385  HIS B 386  HIS B 388                    
SITE     4 BC5 15 LEU B 408  HOH B 788  HOH B 811                               
SITE     1 BC6 10 ARG B 120  VAL B 349  LEU B 352  SER B 353                    
SITE     2 BC6 10 TYR B 355  TYR B 385  TRP B 387  ALA B 527                    
SITE     3 BC6 10 SER B 530  LEU B 531                                          
SITE     1 BC7  6 PRO B  84  VAL B  89  TYR B 115  SER B 119                    
SITE     2 BC7  6 ARG B 120  LEU B 123                                          
SITE     1 BC8  2 ASN B  87  TYR B  91                                          
SITE     1 BC9  5 HOH A 904  ARG B 216  NAG B 671  HOH B 882                    
SITE     2 BC9  5 HOH B 886                                                     
SITE     1 CC1  4 PHE B 205  TYR B 385  SER B 530  HOH B 686                    
CRYST1  122.735  133.028  181.039  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      0.008148  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007517  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005524        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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