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Database: PDB
Entry: 6COX
LinkDB: 6COX
Original site: 6COX 
HEADER    OXIDOREDUCTASE                          18-DEC-96   6COX              
TITLE     CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A SELECTIVE
TITLE    2 INHIBITOR, SC-558 IN I222 SPACE GROUP                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLOOXYGENASE-2;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PROSTAGLANDIN SYNTHASE-2;                                   
COMPND   5 EC: 1.14.99.1;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 CELL_LINE: CULTURED SF21;                                            
SOURCE   6 TISSUE: DERMAL;                                                      
SOURCE   7 CELL: FIBROBLAST;                                                    
SOURCE   8 CELLULAR_LOCATION: ENDOPLASMIC RETICULUM;                            
SOURCE   9 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  10 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  12 EXPRESSION_SYSTEM_CELL_LINE: CULTURED SF21;                          
SOURCE  13 EXPRESSION_SYSTEM_TISSUE: OVARIAN TISSUE;                            
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  15 EXPRESSION_SYSTEM_VECTOR: PVL1393                                    
KEYWDS    PEROXIDASE, DIOXYGENASE, CYCLOOXYGENASE, NONSTEROIDAL                 
KEYWDS   2 ANTIINFLAMMATORY DRUGS, INFLAMMATION, ARTHRITIS, PROSTAGLANDIN,      
KEYWDS   3 PROSTAGLANDIN SYNTHASE, OXIDOREDUCTASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.KURUMBAIL,W.STALLINGS                                               
REVDAT   4   13-JUL-11 6COX    1       VERSN                                    
REVDAT   3   24-FEB-09 6COX    1       VERSN                                    
REVDAT   2   01-APR-03 6COX    1       JRNL                                     
REVDAT   1   24-DEC-97 6COX    0                                                
JRNL        AUTH   R.G.KURUMBAIL,A.M.STEVENS,J.K.GIERSE,J.J.MCDONALD,           
JRNL        AUTH 2 R.A.STEGEMAN,J.Y.PAK,D.GILDEHAUS,J.M.MIYASHIRO,T.D.PENNING,  
JRNL        AUTH 3 K.SEIBERT,P.C.ISAKSON,W.C.STALLINGS                          
JRNL        TITL   STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF                 
JRNL        TITL 2 CYCLOOXYGENASE-2 BY ANTI-INFLAMMATORY AGENTS.                
JRNL        REF    NATURE                        V. 384   644 1996              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   8967954                                                      
JRNL        DOI    10.1038/384644A0                                             
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.G.KURUMBAIL,A.M.STEVENS,J.K.GIERSE,J.J.MCDONALD,           
REMARK   1  AUTH 2 R.A.STEGEMAN,J.Y.PAK,D.GILDEHAUS,J.M.MIYASHIRO,T.D.PENNING,  
REMARK   1  AUTH 3 K.SEIBERT,P.C.ISAKSON,W.C.STALLINGS                          
REMARK   1  TITL   ERRATUM. STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF        
REMARK   1  TITL 2 CYCLOOXYGENASE-2 BY ANTI-INFLAMMATORY AGENTS                 
REMARK   1  REF    NATURE                        V. 385   555 1997              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 31066                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.309                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3110                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2651                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE                    : 0.3460                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 301                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8946                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 222                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.60                          
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.83                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.67                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.500 ; 2.730                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; 3.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; 2.730                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; 3.000                
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINED                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 300   ; 0.049                
REMARK   3   GROUP  1  B-FACTOR           (A**2) : 1.0   ; 2.02                 
REMARK   3   GROUP  2  POSITIONAL            (A) : 300   ; 0.038                
REMARK   3   GROUP  2  B-FACTOR           (A**2) : 1.0   ; 1.94                 
REMARK   3   GROUP  3  POSITIONAL            (A) : 300   ; 0.047                
REMARK   3   GROUP  3  B-FACTOR           (A**2) : 1.0   ; 2.14                 
REMARK   3   GROUP  4  POSITIONAL            (A) : 300   ; 0.055                
REMARK   3   GROUP  4  B-FACTOR           (A**2) : 1.0   ; 2.55                 
REMARK   3   GROUP  5  POSITIONAL            (A) : 300   ; 0.042                
REMARK   3   GROUP  5  B-FACTOR           (A**2) : 1.0   ; 2.05                 
REMARK   3   GROUP  6  POSITIONAL            (A) : 300   ; 0.041                
REMARK   3   GROUP  6  B-FACTOR           (A**2) : 1.0   ; 1.55                 
REMARK   3   GROUP  7  POSITIONAL            (A) : 200   ; 0.058                
REMARK   3   GROUP  7  B-FACTOR           (A**2) : 2.0   ; 2.68                 
REMARK   3   GROUP  8  POSITIONAL            (A) : 50    ; 0.18                 
REMARK   3   GROUP  8  B-FACTOR           (A**2) : 5.0   ; 5.09                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARAM_ENGH.PRO                                 
REMARK   3  PARAMETER FILE  2  : PARAM19X_MOD.HEME                              
REMARK   3  PARAMETER FILE  3  : PARAM3_MOD.CHO                                 
REMARK   3  PARAMETER FILE  4  : PARAM.SC558                                    
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOP_ENGH.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19X_MOD.HEME                               
REMARK   3  TOPOLOGY FILE  3   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  4   : TOP.SC558                                      
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6COX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : APR-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : SUPPER MIRRORS                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35324                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 4.350                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.160                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MERLOT                                                
REMARK 200 STARTING MODEL: PROSTAGLANDIN SYNTHASE-1, PDB ENTRY 1PRH             
REMARK 200                                                                      
REMARK 200 REMARK: PGHS-1 DIMER WAS USED AS THE SEARCH MODEL.                   
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM SODIUM PHOSPHATE, 100 MM NACL,     
REMARK 280  0.6% BETA- OCTYLGLUCOSIDE, 10 MG/ML PROTEIN, 1MM INHIBITOR MIXED    
REMARK 280  WITH A RESERVOIR SOLUTION CONTAINING 20-34% MONOMETHYL PEG 550,     
REMARK 280  10-240 MGCL2, 50 MM EPPS PH 8.0 IN THE RATIO OF 1:1                 
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       90.58500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       66.40500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       61.37000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       90.58500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       66.40500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.37000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       90.58500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       66.40500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.37000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       90.58500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       66.40500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       61.37000            
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: 10420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS B 388   CG    HIS B 388   CD2     0.060                       
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    ARG A  44       16.22     85.69                                   
REMARK 500    PHE A  52      -55.62     77.37                                   
REMARK 500    TYR A  65     -157.89   -115.12                                   
REMARK 500    GLU A  67      -42.81    -28.79                                   
REMARK 500    LEU A  82      -35.25   -178.64                                   
REMARK 500    THR A  88       21.50    -69.49                                   
REMARK 500    VAL A  89      -42.30   -135.28                                   
REMARK 500    HIS A  95     -158.05    -89.59                                   
REMARK 500    PHE A  96       40.17     30.28                                   
REMARK 500    LYS A  97      -34.03    -38.12                                   
REMARK 500    ASN A 104       -8.16    -51.23                                   
REMARK 500    PRO A 128      158.95    -49.33                                   
REMARK 500    THR A 129      -99.90   -119.97                                   
REMARK 500    VAL A 132      -46.38    -28.89                                   
REMARK 500    SER A 138      157.55     48.06                                   
REMARK 500    ASN A 144      100.79    -54.14                                   
REMARK 500    PRO A 154     -172.19    -66.52                                   
REMARK 500    ASP A 157       -7.86    -56.56                                   
REMARK 500    PRO A 172      136.93    -31.39                                   
REMARK 500    ARG A 185      -78.18   -111.33                                   
REMARK 500    ASN A 195     -165.67    -76.36                                   
REMARK 500    PHE A 205      -72.55    -62.40                                   
REMARK 500    LYS A 211       35.47   -144.91                                   
REMARK 500    THR A 212      125.01    -15.15                                   
REMARK 500    HIS A 226       52.13     31.47                                   
REMARK 500    ASP A 249        2.30     56.58                                   
REMARK 500    HIS A 278       38.75    -80.15                                   
REMARK 500    GLN A 284       90.71    -69.38                                   
REMARK 500    VAL A 287      -54.04     57.65                                   
REMARK 500    GLU A 290       -8.47    -58.24                                   
REMARK 500    PHE A 292       -1.50    -58.55                                   
REMARK 500    HIS A 309      -72.54    -46.27                                   
REMARK 500    GLN A 318       32.38    -93.19                                   
REMARK 500    ASP A 325      -70.78    -52.58                                   
REMARK 500    PHE A 329      -78.96    -54.76                                   
REMARK 500    GLN A 330      -33.95    -39.60                                   
REMARK 500    VAL A 344      -29.78    -39.24                                   
REMARK 500    ASP A 347      -85.15   -108.71                                   
REMARK 500    TYR A 348      -86.73    -29.80                                   
REMARK 500    LEU A 352      -15.42    -46.11                                   
REMARK 500    LEU A 359      154.22    -49.35                                   
REMARK 500    GLU A 364       -4.38    -59.49                                   
REMARK 500    PHE A 371      139.77   -179.17                                   
REMARK 500    TRP A 387       49.99    -82.54                                   
REMARK 500    ILE A 397       66.75   -103.54                                   
REMARK 500    GLU A 398      109.15     20.78                                   
REMARK 500    ASP A 399       27.53     92.20                                   
REMARK 500    LYS A 405      -35.92    -39.82                                   
REMARK 500    TYR A 409       51.81     36.51                                   
REMARK 500    SER A 412      -72.03    -31.59                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     139 RAMACHANDRAN OUTLIERS.                        
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    LYS A 137        24.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 287        21.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 453        24.1      L          L   OUTSIDE RANGE           
REMARK 500    LYS A 459        24.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS B 137        24.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 287        22.3      L          L   OUTSIDE RANGE           
REMARK 500    ASP B 453        22.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 388   NE2                                                    
REMARK 620 2 HEM A 682   NA   91.1                                              
REMARK 620 3 HEM A 682   NB   88.0  91.1                                        
REMARK 620 4 HEM A 682   NC   90.3 178.5  89.7                                  
REMARK 620 5 HEM A 682   ND   97.3  89.6 174.6  89.5                            
REMARK 620 N                    1     2     3     4                             
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   92.8                                              
REMARK 620 3 HEM B 682   NB   90.7  90.5                                        
REMARK 620 4 HEM B 682   NC   88.6 178.6  89.4                                  
REMARK 620 5 HEM B 682   ND   94.0  90.2 175.2  89.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: TYR 385 IS BELIEVED TO BE THE AMINO ACID THAT      
REMARK 800  ABSTRACTS A HYDROGEN ATOM FROM THE SUBSTRATE. IT IS LOCATED CLOSE   
REMARK 800  TO THE HEME. A TYROSINE RADICAL IS FORMED DURING THE COURSE OF      
REMARK 800  THE REACTION.                                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ACE                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: SER 530 IS ACETYLATED BY ASPIRIN (AN ACETYL        
REMARK 800  GROUP IS COVALENTLY ATTACHED TO THE PROTEIN WHEN INHIBITED WITH     
REMARK 800  ASPIRIN). THE ACETYLATED SER PREVENTS THE PROPER BINDING OF THE     
REMARK 800  SUBSTRATE IN THE CYCLOOXYGENASE ACTIVE SITE. IT HAS BEEN RECENTLY   
REMARK 800  SHOWN, HOWEVER, THAT ACETYLATION OF CYCLOOXYGENASE-2 RESULTS IN     
REMARK 800  THE FORMATION OF A DIFFERENT PRODUCT (15-HETE).                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HEM                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: HIS 388 IS THE AXIAL LIGAND TO THE HEME.           
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: SUB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ARGININE 120 IS BELIEVED TO ANCHOR THE             
REMARK 800  CARBOXYLATE OF THE SUBSTRATE BY FORMING AN ION-PAIR.                
REMARK 800                                                                      
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 NAG B 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S58 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S58 B 701                 
DBREF  6COX A   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
DBREF  6COX B   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
SEQADV 6COX GLN A  310  UNP  Q05769    ASN   296 CONFLICT                       
SEQADV 6COX LYS A  333  UNP  Q05769    ARG   319 CONFLICT                       
SEQADV 6COX GLN B  310  UNP  Q05769    ASN   296 CONFLICT                       
SEQADV 6COX LYS B  333  UNP  Q05769    ARG   319 CONFLICT                       
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 GLN 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 LYS 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 GLN 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 LYS 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 6COX ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 6COX ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 6COX ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 6COX ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 6COX ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 6COX ASN B  410  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 661      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 681      14                                                       
HET    NAG  B 661      14                                                       
HET    NAG  B 671      14                                                       
HET    NAG  B 681      14                                                       
HET    HEM  A 682      43                                                       
HET    S58  A 701      26                                                       
HET    HEM  B 682      43                                                       
HET    S58  B 701      26                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     S58 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-                         
HETNAM   2 S58  PARABROMOPHENYLPYRAZOLE                                         
HETSYN     HEM HEME                                                             
FORMUL   3  NAG    6(C8 H15 N O6)                                               
FORMUL   9  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL  10  S58    2(C16 H11 BR F3 N3 O2 S)                                     
HELIX    1   1 PRO A   35  SER A   38  5                                   4    
HELIX    2   2 GLN A   42  ARG A   44  5                                   3    
HELIX    3   3 PHE A   74  LEU A   80  1                                   7    
HELIX    4   4 ASN A   87  THR A   94  1                                   8    
HELIX    5   5 LYS A   97  ASN A  105  1                                   9    
HELIX    6   6 PRO A  106  LEU A  123  1                                  18    
HELIX    7   7 TRP A  139  SER A  143  1                                   5    
HELIX    8   8 SER A  174  VAL A  181  1                                   8    
HELIX    9   9 MET A  196  PHE A  205  1                                  10    
HELIX   10  10 ASN A  231  TYR A  234  1                                   4    
HELIX   11  11 LEU A  238  LYS A  243  1                                   6    
HELIX   12  12 GLU A  281  LEU A  283  5                                   3    
HELIX   13  13 PHE A  292  LEU A  294  5                                   3    
HELIX   14  14 PRO A  296  GLU A  319  1                                  24    
HELIX   15  15 ASP A  325  GLU A  346  1                                  22    
HELIX   16  16 TYR A  348  SER A  353  1                                   6    
HELIX   17  17 PRO A  363  LEU A  365  5                                   3    
HELIX   18  18 SER A  379  TYR A  385  1                                   7    
HELIX   19  19 HIS A  388  LEU A  390  5                                   3    
HELIX   20  20 PHE A  404  PHE A  407  1                                   4    
HELIX   21  21 ASN A  411  HIS A  417  1                                   7    
HELIX   22  22 THR A  420  THR A  427  1                                   8    
HELIX   23  23 ALA A  443  GLN A  454  5                                  12    
HELIX   24  24 LEU A  463  ARG A  469  1                                   7    
HELIX   25  25 PHE A  478  THR A  482  1                                   5    
HELIX   26  26 GLU A  486  LEU A  494  1                                   9    
HELIX   27  27 ILE A  498  VAL A  500  5                                   3    
HELIX   28  28 LEU A  503  VAL A  509  1                                   7    
HELIX   29  29 GLU A  520  MET A  535  1                                  16    
HELIX   30  30 PRO A  538  CYS A  540  5                                   3    
HELIX   31  31 VAL A  554  ASN A  560  1                                   7    
HELIX   32  32 ILE A  564  ASN A  571  1                                   8    
HELIX   33  33 PRO B   35  SER B   38  5                                   4    
HELIX   34  34 PHE B   74  LEU B   80  1                                   7    
HELIX   35  35 ASN B   87  THR B   94  1                                   8    
HELIX   36  36 LYS B   97  ASN B  105  1                                   9    
HELIX   37  37 PRO B  106  LEU B  123  1                                  18    
HELIX   38  38 TRP B  139  SER B  143  1                                   5    
HELIX   39  39 SER B  174  VAL B  181  1                                   8    
HELIX   40  40 MET B  196  PHE B  205  1                                  10    
HELIX   41  41 ASN B  231  TYR B  234  1                                   4    
HELIX   42  42 LEU B  238  LYS B  243  1                                   6    
HELIX   43  43 GLU B  281  LEU B  283  5                                   3    
HELIX   44  44 PHE B  292  LEU B  294  5                                   3    
HELIX   45  45 PRO B  296  GLU B  319  1                                  24    
HELIX   46  46 ASP B  325  GLU B  346  1                                  22    
HELIX   47  47 TYR B  348  SER B  353  1                                   6    
HELIX   48  48 PRO B  363  LEU B  365  5                                   3    
HELIX   49  49 SER B  379  TYR B  385  1                                   7    
HELIX   50  50 HIS B  388  LEU B  390  5                                   3    
HELIX   51  51 PHE B  404  PHE B  407  1                                   4    
HELIX   52  52 ASN B  411  HIS B  417  1                                   7    
HELIX   53  53 THR B  420  THR B  427  1                                   8    
HELIX   54  54 ALA B  443  GLN B  454  5                                  12    
HELIX   55  55 LEU B  463  PHE B  470  1                                   8    
HELIX   56  56 PHE B  478  THR B  482  1                                   5    
HELIX   57  57 GLU B  486  LEU B  494  1                                   9    
HELIX   58  58 ILE B  498  VAL B  500  5                                   3    
HELIX   59  59 LEU B  503  VAL B  509  1                                   7    
HELIX   60  60 GLU B  520  MET B  535  1                                  16    
HELIX   61  61 PRO B  538  CYS B  540  5                                   3    
HELIX   62  62 PRO B  547  PHE B  550  5                                   4    
HELIX   63  63 VAL B  554  ASN B  560  1                                   7    
HELIX   64  64 ILE B  564  ASN B  571  1                                   8    
SHEET    1   A 2 GLU A  46  SER A  49  0                                        
SHEET    2   A 2 TYR A  55  ASP A  58 -1  N  ASP A  58   O  GLU A  46           
SHEET    1   B 2 GLN A 255  ILE A 257  0                                        
SHEET    2   B 2 GLU A 260  TYR A 262 -1  N  TYR A 262   O  GLN A 255           
SHEET    1   C 2 GLU B  46  SER B  49  0                                        
SHEET    2   C 2 TYR B  55  ASP B  58 -1  N  ASP B  58   O  GLU B  46           
SHEET    1   D 2 GLN B 255  ILE B 257  0                                        
SHEET    2   D 2 GLU B 260  TYR B 262 -1  N  TYR B 262   O  GLN B 255           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.03  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.02  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.04  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.02  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.02  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.02  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.02  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.04  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.03  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.02  
LINK        FE   HEM A 682                 NE2 HIS A 388     1555   1555  2.23  
LINK         C1  NAG A 661                 ND2 ASN A  68     1555   1555  1.45  
LINK         C1  NAG A 671                 ND2 ASN A 144     1555   1555  1.45  
LINK         C1  NAG A 681                 ND2 ASN A 410     1555   1555  1.45  
LINK        FE   HEM B 682                 NE2 HIS B 388     1555   1555  2.21  
LINK         C1  NAG B 661                 ND2 ASN B  68     1555   1555  1.44  
LINK         C1  NAG B 671                 ND2 ASN B 144     1555   1555  1.43  
LINK         C1  NAG B 681                 ND2 ASN B 410     1555   1555  1.47  
CISPEP   1 SER A  126    PRO A  127          0         0.37                     
CISPEP   2 SER B  126    PRO B  127          0         0.33                     
SITE     1 CAT  1 TYR A 385                                                     
SITE     1 ACE  1 SER A 530                                                     
SITE     1 HEM  1 HIS A 388                                                     
SITE     1 SUB  1 ARG A 120                                                     
SITE     1 AC1  4 PRO A  40  TYR A  55  GLU A  67  ASN A  68                    
SITE     1 AC2  3 ASN A 144  TYR A 147  ARG A 216                               
SITE     1 AC3  4 TYR A 402  ASN A 410  SER A 412  ILE A 413                    
SITE     1 AC4  4 PRO B  40  TYR B  55  GLU B  67  ASN B  68                    
SITE     1 AC5  4 GLU B 140  ASN B 144  TYR B 147  ARG B 216                    
SITE     1 AC6  4 TYR B 402  ASN B 410  SER B 412  ILE B 413                    
SITE     1 AC7 15 ALA A 199  GLN A 203  HIS A 207  PHE A 210                    
SITE     2 AC7 15 LYS A 211  THR A 212  HIS A 214  VAL A 295                    
SITE     3 AC7 15 ASN A 382  TYR A 385  HIS A 386  HIS A 388                    
SITE     4 AC7 15 LEU A 391  VAL A 447  GLN A 454                               
SITE     1 AC8 16 HIS A  90  ARG A 120  GLN A 192  VAL A 349                    
SITE     2 AC8 16 LEU A 352  SER A 353  TYR A 355  LEU A 359                    
SITE     3 AC8 16 TYR A 385  TRP A 387  ALA A 516  PHE A 518                    
SITE     4 AC8 16 VAL A 523  GLY A 526  ALA A 527  LEU A 531                    
SITE     1 AC9 14 ALA B 199  GLN B 203  HIS B 207  PHE B 210                    
SITE     2 AC9 14 LYS B 211  THR B 212  HIS B 214  VAL B 295                    
SITE     3 AC9 14 ASN B 382  TYR B 385  HIS B 386  HIS B 388                    
SITE     4 AC9 14 VAL B 447  GLN B 454                                          
SITE     1 BC1 17 HIS B  90  ARG B 120  GLN B 192  VAL B 349                    
SITE     2 BC1 17 LEU B 352  SER B 353  TYR B 355  LEU B 359                    
SITE     3 BC1 17 TYR B 385  TRP B 387  ARG B 513  ALA B 516                    
SITE     4 BC1 17 PHE B 518  VAL B 523  GLY B 526  ALA B 527                    
SITE     5 BC1 17 LEU B 531                                                     
CRYST1  181.170  132.810  122.740  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      0.005520  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007530  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008147        0.00000                         
MTRIX1   1 -0.999600  0.019600 -0.021200       94.38400    1                    
MTRIX2   1  0.018900 -0.109200 -0.993800       64.06400    1                    
MTRIX3   1 -0.021800 -0.993800  0.108800       59.22200    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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