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Database: PDB
Entry: 4COX
LinkDB: 4COX
Original site: 4COX 
HEADER    OXIDOREDUCTASE                          18-DEC-96   4COX              
TITLE     CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A NON-     
TITLE    2 SELECTIVE INHIBITOR, INDOMETHACIN                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLOOXYGENASE-2;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
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 4COX    1       VERSN                                    
REVDAT   3   24-FEB-09 4COX    1       VERSN                                    
REVDAT   2   01-APR-03 4COX    1       JRNL                                     
REVDAT   1   24-DEC-97 4COX    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.    2.90 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) : 2.90                           
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)   (%) : 68.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 41254                          
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) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.309                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4166                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 47.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3185                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640                       
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 362                          
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            : 17892                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 440                                     
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) : 12.00                          
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) : 1.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.69                            
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 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINED                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 300   ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : 1.0   ; NULL                 
REMARK   3   GROUP  2  POSITIONAL            (A) : 300   ; NULL                 
REMARK   3   GROUP  2  B-FACTOR           (A**2) : 1.0   ; NULL                 
REMARK   3   GROUP  3  POSITIONAL            (A) : 300   ; NULL                 
REMARK   3   GROUP  3  B-FACTOR           (A**2) : 1.0   ; NULL                 
REMARK   3   GROUP  4  POSITIONAL            (A) : 300   ; NULL                 
REMARK   3   GROUP  4  B-FACTOR           (A**2) : 1.0   ; NULL                 
REMARK   3   GROUP  5  POSITIONAL            (A) : 300   ; NULL                 
REMARK   3   GROUP  5  B-FACTOR           (A**2) : 1.0   ; NULL                 
REMARK   3   GROUP  6  POSITIONAL            (A) : 200   ; NULL                 
REMARK   3   GROUP  6  B-FACTOR           (A**2) : 2.0   ; NULL                 
REMARK   3   GROUP  7  POSITIONAL            (A) : 50    ; NULL                 
REMARK   3   GROUP  7  B-FACTOR           (A**2) : 5.0   ; NULL                 
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.INDOMETHACIN                             
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.INDOMETHACIN                               
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4COX 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        : AUG-95                             
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          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50058                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.500                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.13500                            
REMARK 200  R SYM                      (I) : 0.13500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.770                              
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: P 21 21 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+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       89.90000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.80000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       89.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.80000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 10550 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10510 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 465     ASP C   584                                                      
REMARK 465     PRO C   585                                                      
REMARK 465     GLN C   586                                                      
REMARK 465     PRO C   587                                                      
REMARK 465     THR C   588                                                      
REMARK 465     LYS C   589                                                      
REMARK 465     THR C   590                                                      
REMARK 465     ALA C   591                                                      
REMARK 465     THR C   592                                                      
REMARK 465     ILE C   593                                                      
REMARK 465     ASN C   594                                                      
REMARK 465     ALA C   595                                                      
REMARK 465     SER C   596                                                      
REMARK 465     ALA C   597                                                      
REMARK 465     SER C   598                                                      
REMARK 465     HIS C   599                                                      
REMARK 465     SER C   600                                                      
REMARK 465     ARG C   601                                                      
REMARK 465     LEU C   602                                                      
REMARK 465     ASP C   603                                                      
REMARK 465     ASP C   604                                                      
REMARK 465     ILE C   605                                                      
REMARK 465     ASN C   606                                                      
REMARK 465     PRO C   607                                                      
REMARK 465     THR C   608                                                      
REMARK 465     VAL C   609                                                      
REMARK 465     LEU C   610                                                      
REMARK 465     ILE C   611                                                      
REMARK 465     LYS C   612                                                      
REMARK 465     ARG C   613                                                      
REMARK 465     ARG C   614                                                      
REMARK 465     SER C   615                                                      
REMARK 465     THR C   616                                                      
REMARK 465     GLU C   617                                                      
REMARK 465     LEU C   618                                                      
REMARK 465     ASP D   584                                                      
REMARK 465     PRO D   585                                                      
REMARK 465     GLN D   586                                                      
REMARK 465     PRO D   587                                                      
REMARK 465     THR D   588                                                      
REMARK 465     LYS D   589                                                      
REMARK 465     THR D   590                                                      
REMARK 465     ALA D   591                                                      
REMARK 465     THR D   592                                                      
REMARK 465     ILE D   593                                                      
REMARK 465     ASN D   594                                                      
REMARK 465     ALA D   595                                                      
REMARK 465     SER D   596                                                      
REMARK 465     ALA D   597                                                      
REMARK 465     SER D   598                                                      
REMARK 465     HIS D   599                                                      
REMARK 465     SER D   600                                                      
REMARK 465     ARG D   601                                                      
REMARK 465     LEU D   602                                                      
REMARK 465     ASP D   603                                                      
REMARK 465     ASP D   604                                                      
REMARK 465     ILE D   605                                                      
REMARK 465     ASN D   606                                                      
REMARK 465     PRO D   607                                                      
REMARK 465     THR D   608                                                      
REMARK 465     VAL D   609                                                      
REMARK 465     LEU D   610                                                      
REMARK 465     ILE D   611                                                      
REMARK 465     LYS D   612                                                      
REMARK 465     ARG D   613                                                      
REMARK 465     ARG D   614                                                      
REMARK 465     SER D   615                                                      
REMARK 465     THR D   616                                                      
REMARK 465     GLU D   617                                                      
REMARK 465     LEU D   618                                                      
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   89.1                                              
REMARK 620 3 HEM A 682   NB   90.6  90.7                                        
REMARK 620 4 HEM A 682   NC   82.9 172.0  89.2                                  
REMARK 620 5 HEM A 682   ND   89.2  89.4 179.7  90.7                            
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   87.1                                              
REMARK 620 3 HEM B 682   NB   95.3  89.3                                        
REMARK 620 4 HEM B 682   NC   89.1 175.8  89.4                                  
REMARK 620 5 HEM B 682   ND   85.7  90.4 178.9  91.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 388   NE2                                                    
REMARK 620 2 HEM C 682   NA   85.1                                              
REMARK 620 3 HEM C 682   NB   93.6  90.5                                        
REMARK 620 4 HEM C 682   NC   87.0 172.1  89.7                                  
REMARK 620 5 HEM C 682   ND   84.7  89.7 178.3  89.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 682  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 388   NE2                                                    
REMARK 620 2 HEM D 682   NA   87.2                                              
REMARK 620 3 HEM D 682   NB   92.0  90.1                                        
REMARK 620 4 HEM D 682   NC   88.8 175.9  89.5                                  
REMARK 620 5 HEM D 682   ND   89.9  90.2 178.1  90.4                            
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 NAG C 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 682                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN D 701                 
DBREF  4COX A   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
DBREF  4COX B   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
DBREF  4COX C   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
DBREF  4COX D   33   618  UNP    Q05769   PGH2_MOUSE      18    604             
SEQADV 4COX GLN A  310  UNP  Q05769    ASN   296 CONFLICT                       
SEQADV 4COX LYS A  333  UNP  Q05769    ARG   319 CONFLICT                       
SEQADV 4COX GLN B  310  UNP  Q05769    ASN   296 CONFLICT                       
SEQADV 4COX LYS B  333  UNP  Q05769    ARG   319 CONFLICT                       
SEQADV 4COX GLN C  310  UNP  Q05769    ASN   296 CONFLICT                       
SEQADV 4COX LYS C  333  UNP  Q05769    ARG   319 CONFLICT                       
SEQADV 4COX GLN D  310  UNP  Q05769    ASN   296 CONFLICT                       
SEQADV 4COX LYS D  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                                                      
SEQRES   1 C  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 C  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 C  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 C  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 C  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 C  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 C  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 C  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 C  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 C  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 C  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 C  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 C  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 C  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 C  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 C  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 C  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 C  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 C  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 C  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 C  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 C  587  TRP LEU ARG GLU HIS GLN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 C  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 C  587  THR SER LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 C  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 C  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 C  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 C  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 C  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 C  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 C  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 C  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 C  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 C  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 C  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 C  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 C  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 C  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 C  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 C  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 C  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 C  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 C  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 C  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 C  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 C  587  GLU LEU                                                      
SEQRES   1 D  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 D  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 D  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 D  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 D  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 D  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 D  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 D  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 D  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 D  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 D  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 D  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 D  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 D  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 D  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 D  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 D  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 D  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 D  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 D  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 D  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 D  587  TRP LEU ARG GLU HIS GLN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 D  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 D  587  THR SER LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 D  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 D  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 D  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 D  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 D  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 D  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 D  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 D  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 D  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 D  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 D  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 D  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 D  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 D  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 D  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 D  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 D  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 D  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 D  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR          
SEQRES  44 D  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP          
SEQRES  45 D  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR          
SEQRES  46 D  587  GLU LEU                                                      
MODRES 4COX ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN B   68  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN B  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN B  410  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN C   68  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN C  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN C  410  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN D   68  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN D  144  ASN  GLYCOSYLATION SITE                                 
MODRES 4COX ASN D  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    NAG  C 661      14                                                       
HET    NAG  C 671      14                                                       
HET    NAG  C 681      14                                                       
HET    NAG  D 661      14                                                       
HET    NAG  D 671      14                                                       
HET    NAG  D 681      14                                                       
HET    HEM  A 682      43                                                       
HET    IMN  A 701      25                                                       
HET    HEM  B 682      43                                                       
HET    IMN  B 701      25                                                       
HET    HEM  C 682      43                                                       
HET    IMN  C 701      25                                                       
HET    HEM  D 682      43                                                       
HET    IMN  D 701      25                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     IMN INDOMETHACIN                                                     
HETSYN     HEM HEME                                                             
FORMUL   5  NAG    12(C8 H15 N O6)                                              
FORMUL  17  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  18  IMN    4(C19 H16 CL N O4)                                           
HELIX    1   1 PHE A   74  LEU A   82  1                                   9    
HELIX    2   2 PRO A   86  THR A   94  1                                   9    
HELIX    3   3 LYS A   97  ASN A  105  1                                   9    
HELIX    4   4 PRO A  106  LEU A  123  1                                  18    
HELIX    5   5 TRP A  139  SER A  143  1                                   5    
HELIX    6   6 SER A  174  VAL A  181  1                                   8    
HELIX    7   7 MET A  196  GLN A  208  1                                  13    
HELIX    8   8 ASN A  231  TYR A  234  1                                   4    
HELIX    9   9 LEU A  238  LEU A  244  1                                   7    
HELIX   10  10 VAL A  266  THR A  269  1                                   4    
HELIX   11  11 PRO A  296  GLU A  319  1                                  24    
HELIX   12  12 ASP A  325  GLU A  346  1                                  22    
HELIX   13  13 TYR A  348  SER A  353  1                                   6    
HELIX   14  14 PRO A  363  LEU A  366  5                                   4    
HELIX   15  15 SER A  379  LEU A  384  1                                   6    
HELIX   16  16 HIS A  388  LEU A  390  5                                   3    
HELIX   17  17 PHE A  404  PHE A  407  1                                   4    
HELIX   18  18 SER A  412  HIS A  417  1                                   6    
HELIX   19  19 THR A  420  THR A  427  1                                   8    
HELIX   20  20 ALA A  443  GLU A  457  5                                  15    
HELIX   21  21 LEU A  463  PHE A  470  1                                   8    
HELIX   22  22 PHE A  478  THR A  482  1                                   5    
HELIX   23  23 GLU A  486  TYR A  495  1                                  10    
HELIX   24  24 LEU A  503  LEU A  508  1                                   6    
HELIX   25  25 GLU A  520  MET A  535  1                                  16    
HELIX   26  26 PRO A  538  CYS A  540  5                                   3    
HELIX   27  27 PRO A  547  PHE A  550  5                                   4    
HELIX   28  28 GLU A  553  ASN A  560  1                                   8    
HELIX   29  29 ILE A  564  CYS A  569  1                                   6    
HELIX   30  30 PHE B   74  LEU B   82  1                                   9    
HELIX   31  31 PRO B   86  THR B   94  1                                   9    
HELIX   32  32 LYS B   97  ASN B  105  1                                   9    
HELIX   33  33 PRO B  106  LEU B  123  1                                  18    
HELIX   34  34 TRP B  139  SER B  143  1                                   5    
HELIX   35  35 SER B  174  VAL B  181  1                                   8    
HELIX   36  36 MET B  196  GLN B  208  1                                  13    
HELIX   37  37 ASN B  231  TYR B  234  1                                   4    
HELIX   38  38 LEU B  238  LEU B  244  1                                   7    
HELIX   39  39 VAL B  266  THR B  269  1                                   4    
HELIX   40  40 PRO B  296  GLU B  319  1                                  24    
HELIX   41  41 ASP B  325  GLU B  346  1                                  22    
HELIX   42  42 TYR B  348  SER B  353  1                                   6    
HELIX   43  43 PRO B  363  LEU B  366  5                                   4    
HELIX   44  44 SER B  379  LEU B  384  1                                   6    
HELIX   45  45 HIS B  388  LEU B  390  5                                   3    
HELIX   46  46 PHE B  404  PHE B  407  1                                   4    
HELIX   47  47 SER B  412  HIS B  417  1                                   6    
HELIX   48  48 THR B  420  THR B  427  1                                   8    
HELIX   49  49 ALA B  443  GLU B  457  5                                  15    
HELIX   50  50 LEU B  463  ARG B  469  1                                   7    
HELIX   51  51 PHE B  478  THR B  482  1                                   5    
HELIX   52  52 GLU B  486  TYR B  495  1                                  10    
HELIX   53  53 LEU B  503  LEU B  508  1                                   6    
HELIX   54  54 GLU B  520  MET B  535  1                                  16    
HELIX   55  55 PRO B  538  CYS B  540  5                                   3    
HELIX   56  56 PRO B  547  PHE B  550  5                                   4    
HELIX   57  57 GLU B  553  ASN B  560  1                                   8    
HELIX   58  58 ILE B  564  CYS B  569  1                                   6    
HELIX   59  59 PHE C   74  LEU C   82  1                                   9    
HELIX   60  60 PRO C   86  THR C   94  1                                   9    
HELIX   61  61 LYS C   97  ASN C  105  1                                   9    
HELIX   62  62 PRO C  106  LEU C  123  1                                  18    
HELIX   63  63 TRP C  139  SER C  143  1                                   5    
HELIX   64  64 SER C  174  VAL C  181  1                                   8    
HELIX   65  65 MET C  196  GLN C  208  1                                  13    
HELIX   66  66 ASN C  231  TYR C  234  1                                   4    
HELIX   67  67 LEU C  238  LEU C  244  1                                   7    
HELIX   68  68 VAL C  266  THR C  269  1                                   4    
HELIX   69  69 PRO C  296  GLU C  319  1                                  24    
HELIX   70  70 ASP C  325  GLU C  346  1                                  22    
HELIX   71  71 TYR C  348  SER C  353  1                                   6    
HELIX   72  72 PRO C  363  LEU C  366  5                                   4    
HELIX   73  73 SER C  379  LEU C  384  1                                   6    
HELIX   74  74 HIS C  388  LEU C  390  5                                   3    
HELIX   75  75 PHE C  404  PHE C  407  1                                   4    
HELIX   76  76 SER C  412  HIS C  417  1                                   6    
HELIX   77  77 THR C  420  THR C  427  1                                   8    
HELIX   78  78 ALA C  443  GLU C  457  5                                  15    
HELIX   79  79 LEU C  463  ARG C  469  1                                   7    
HELIX   80  80 PHE C  478  THR C  482  1                                   5    
HELIX   81  81 GLU C  486  TYR C  495  1                                  10    
HELIX   82  82 LEU C  503  LEU C  508  1                                   6    
HELIX   83  83 GLU C  520  MET C  535  1                                  16    
HELIX   84  84 PRO C  538  CYS C  540  5                                   3    
HELIX   85  85 PRO C  547  PHE C  550  5                                   4    
HELIX   86  86 GLU C  553  ASN C  560  1                                   8    
HELIX   87  87 ILE C  564  CYS C  569  1                                   6    
HELIX   88  88 PHE D   74  LEU D   82  1                                   9    
HELIX   89  89 PRO D   86  THR D   94  1                                   9    
HELIX   90  90 LYS D   97  ASN D  105  1                                   9    
HELIX   91  91 PRO D  106  LEU D  123  1                                  18    
HELIX   92  92 TRP D  139  SER D  143  1                                   5    
HELIX   93  93 SER D  174  VAL D  181  1                                   8    
HELIX   94  94 MET D  196  GLN D  208  1                                  13    
HELIX   95  95 ASN D  231  TYR D  234  1                                   4    
HELIX   96  96 LEU D  238  LEU D  244  1                                   7    
HELIX   97  97 VAL D  266  THR D  269  1                                   4    
HELIX   98  98 PRO D  296  GLU D  319  1                                  24    
HELIX   99  99 ASP D  325  GLU D  346  1                                  22    
HELIX  100 100 TYR D  348  SER D  353  1                                   6    
HELIX  101 101 PRO D  363  LEU D  366  5                                   4    
HELIX  102 102 SER D  379  LEU D  384  1                                   6    
HELIX  103 103 HIS D  388  LEU D  390  5                                   3    
HELIX  104 104 PHE D  404  PHE D  407  1                                   4    
HELIX  105 105 SER D  412  HIS D  417  1                                   6    
HELIX  106 106 THR D  420  THR D  427  1                                   8    
HELIX  107 107 ALA D  443  GLU D  457  5                                  15    
HELIX  108 108 LEU D  463  PHE D  470  1                                   8    
HELIX  109 109 PHE D  478  THR D  482  1                                   5    
HELIX  110 110 GLU D  486  TYR D  495  1                                  10    
HELIX  111 111 LEU D  503  LEU D  508  1                                   6    
HELIX  112 112 GLU D  520  MET D  535  1                                  16    
HELIX  113 113 PRO D  538  CYS D  540  5                                   3    
HELIX  114 114 PRO D  547  PHE D  550  5                                   4    
HELIX  115 115 GLU D  553  ASN D  560  1                                   8    
HELIX  116 116 ILE D  564  CYS D  569  1                                   6    
SHEET    1   A 2 GLU A  46  MET A  48  0                                        
SHEET    2   A 2 LYS A  56  ASP A  58 -1  N  ASP A  58   O  GLU A  46           
SHEET    1   B 2 TYR A 254  ILE A 257  0                                        
SHEET    2   B 2 GLU A 260  PRO A 263 -1  N  TYR A 262   O  GLN A 255           
SHEET    1   C 2 THR A 394  ILE A 397  0                                        
SHEET    2   C 2 GLN A 400  SER A 403 -1  N  TYR A 402   O  PHE A 395           
SHEET    1   D 2 GLU B  46  MET B  48  0                                        
SHEET    2   D 2 LYS B  56  ASP B  58 -1  N  ASP B  58   O  GLU B  46           
SHEET    1   E 2 GLN B 255  ILE B 257  0                                        
SHEET    2   E 2 GLU B 260  TYR B 262 -1  N  TYR B 262   O  GLN B 255           
SHEET    1   F 2 PHE B 395  ILE B 397  0                                        
SHEET    2   F 2 GLN B 400  TYR B 402 -1  N  TYR B 402   O  PHE B 395           
SHEET    1   G 2 GLU C  46  MET C  48  0                                        
SHEET    2   G 2 LYS C  56  ASP C  58 -1  N  ASP C  58   O  GLU C  46           
SHEET    1   H 2 GLN C 255  ILE C 257  0                                        
SHEET    2   H 2 GLU C 260  TYR C 262 -1  N  TYR C 262   O  GLN C 255           
SHEET    1   I 2 THR C 394  ILE C 397  0                                        
SHEET    2   I 2 GLN C 400  SER C 403 -1  N  TYR C 402   O  PHE C 395           
SHEET    1   J 2 GLU D  46  MET D  48  0                                        
SHEET    2   J 2 LYS D  56  ASP D  58 -1  N  ASP D  58   O  GLU D  46           
SHEET    1   K 2 GLN D 255  ILE D 257  0                                        
SHEET    2   K 2 GLU D 260  TYR D 262 -1  N  TYR D 262   O  GLN D 255           
SHEET    1   L 2 THR D 394  ILE D 397  0                                        
SHEET    2   L 2 GLN D 400  SER D 403 -1  N  TYR D 402   O  PHE D 395           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.06  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.01  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03  
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04  
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03  
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.05  
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.04  
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03  
SSBOND  11 CYS C   36    CYS C   47                          1555   1555  2.02  
SSBOND  12 CYS C   37    CYS C  159                          1555   1555  2.01  
SSBOND  13 CYS C   41    CYS C   57                          1555   1555  2.01  
SSBOND  14 CYS C   59    CYS C   69                          1555   1555  2.04  
SSBOND  15 CYS C  569    CYS C  575                          1555   1555  2.04  
SSBOND  16 CYS D   36    CYS D   47                          1555   1555  2.03  
SSBOND  17 CYS D   37    CYS D  159                          1555   1555  2.02  
SSBOND  18 CYS D   41    CYS D   57                          1555   1555  2.04  
SSBOND  19 CYS D   59    CYS D   69                          1555   1555  2.03  
SSBOND  20 CYS D  569    CYS D  575                          1555   1555  2.04  
LINK        FE   HEM A 682                 NE2 HIS A 388     1555   1555  2.20  
LINK         C1  NAG A 661                 ND2 ASN A  68     1555   1555  1.45  
LINK         C1  NAG A 671                 ND2 ASN A 144     1555   1555  1.47  
LINK         C1  NAG A 681                 ND2 ASN A 410     1555   1555  1.45  
LINK        FE   HEM B 682                 NE2 HIS B 388     1555   1555  2.25  
LINK         C1  NAG B 661                 ND2 ASN B  68     1555   1555  1.45  
LINK         C1  NAG B 671                 ND2 ASN B 144     1555   1555  1.44  
LINK         C1  NAG B 681                 ND2 ASN B 410     1555   1555  1.46  
LINK        FE   HEM C 682                 NE2 HIS C 388     1555   1555  2.17  
LINK         C1  NAG C 661                 ND2 ASN C  68     1555   1555  1.44  
LINK         C1  NAG C 671                 ND2 ASN C 144     1555   1555  1.46  
LINK         C1  NAG C 681                 ND2 ASN C 410     1555   1555  1.44  
LINK        FE   HEM D 682                 NE2 HIS D 388     1555   1555  2.24  
LINK         C1  NAG D 661                 ND2 ASN D  68     1555   1555  1.49  
LINK         C1  NAG D 671                 ND2 ASN D 144     1555   1555  1.46  
LINK         C1  NAG D 681                 ND2 ASN D 410     1555   1555  1.46  
CISPEP   1 SER A  126    PRO A  127          0        -0.09                     
CISPEP   2 SER B  126    PRO B  127          0         0.19                     
CISPEP   3 SER C  126    PRO C  127          0         0.14                     
CISPEP   4 SER D  126    PRO D  127          0         0.50                     
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 TYR A  55  GLU A  67  ASN A  68  THR A  70                    
SITE     1 AC2  3 GLU A 140  ASN A 144  TYR A 147                               
SITE     1 AC3  3 ASN A 410  SER A 412  ILE A 413                               
SITE     1 AC4  4 TYR B  55  GLU B  67  ASN B  68  THR B  70                    
SITE     1 AC5  5 GLU B 140  ASN B 144  SER B 146  TYR B 147                    
SITE     2 AC5  5 ARG B 216                                                     
SITE     1 AC6  4 TYR B 402  ASN B 410  SER B 412  ILE B 413                    
SITE     1 AC7  4 PRO C  40  TYR C  55  GLU C  67  ASN C  68                    
SITE     1 AC8  6 GLU C 140  ASN C 144  SER C 146  TYR C 147                    
SITE     2 AC8  6 ARG C 216  LEU D 238                                          
SITE     1 AC9  4 TYR C 402  GLN C 406  ASN C 410  ILE C 413                    
SITE     1 BC1  4 PRO D  40  TYR D  55  GLU D  67  ASN D  68                    
SITE     1 BC2  4 LEU C 238  ASN D 144  TYR D 147  ARG D 216                    
SITE     1 BC3  5 GLN D 406  ASN D 410  SER D 412  ILE D 413                    
SITE     2 BC3  5 GLU D 416                                                     
SITE     1 BC4 13 ALA A 199  GLN A 203  HIS A 207  THR A 212                    
SITE     2 BC4 13 VAL A 295  ASN A 382  TYR A 385  HIS A 386                    
SITE     3 BC4 13 TRP A 387  HIS A 388  LEU A 391  VAL A 447                    
SITE     4 BC4 13 GLN A 454                                                     
SITE     1 BC5 14 ARG A 120  VAL A 349  LEU A 352  SER A 353                    
SITE     2 BC5 14 TYR A 355  LEU A 384  TYR A 385  TRP A 387                    
SITE     3 BC5 14 MET A 522  VAL A 523  GLY A 526  ALA A 527                    
SITE     4 BC5 14 SER A 530  LEU A 531                                          
SITE     1 BC6 13 ALA B 199  GLN B 203  HIS B 207  THR B 212                    
SITE     2 BC6 13 VAL B 295  ASN B 382  TYR B 385  HIS B 386                    
SITE     3 BC6 13 HIS B 388  LEU B 391  LEU B 408  VAL B 447                    
SITE     4 BC6 13 ALA B 450                                                     
SITE     1 BC7 12 ARG B 120  VAL B 349  LEU B 352  SER B 353                    
SITE     2 BC7 12 TYR B 355  TYR B 385  MET B 522  VAL B 523                    
SITE     3 BC7 12 GLY B 526  ALA B 527  SER B 530  LEU B 531                    
SITE     1 BC8 12 ALA C 199  GLN C 203  THR C 212  VAL C 295                    
SITE     2 BC8 12 ASN C 382  TYR C 385  HIS C 386  TRP C 387                    
SITE     3 BC8 12 HIS C 388  LEU C 391  VAL C 447  ALA C 450                    
SITE     1 BC9 14 ARG C 120  VAL C 349  LEU C 352  SER C 353                    
SITE     2 BC9 14 TYR C 355  LEU C 384  TYR C 385  TRP C 387                    
SITE     3 BC9 14 MET C 522  VAL C 523  GLY C 526  ALA C 527                    
SITE     4 BC9 14 SER C 530  LEU C 531                                          
SITE     1 CC1 12 ALA D 199  ALA D 202  GLN D 203  HIS D 207                    
SITE     2 CC1 12 THR D 212  VAL D 295  ASN D 382  TYR D 385                    
SITE     3 CC1 12 HIS D 386  HIS D 388  LEU D 391  VAL D 447                    
SITE     1 CC2 14 ARG D 120  VAL D 349  LEU D 352  SER D 353                    
SITE     2 CC2 14 TYR D 355  LEU D 384  TYR D 385  TRP D 387                    
SITE     3 CC2 14 MET D 522  VAL D 523  GLY D 526  ALA D 527                    
SITE     4 CC2 14 SER D 530  LEU D 531                                          
CRYST1  179.800  133.600  118.400  90.00  90.00  90.00 P 21 21 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      0.005562  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007485  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008446        0.00000                         
MTRIX1   1 -0.999300  0.028200 -0.025200       94.17520    1                    
MTRIX2   1  0.024700 -0.016900 -0.999600       30.43300    1                    
MTRIX3   1 -0.028700 -0.999500  0.016200       32.51540    1                    
MTRIX1   2 -0.998400 -0.047500  0.029800       85.09360    1                    
MTRIX2   2  0.048600 -0.998100  0.037100       64.57020    1                    
MTRIX3   2  0.028000  0.038500  0.998900       56.85230    1                    
MTRIX1   3  0.996400 -0.049300  0.068800       -9.72720    1                    
MTRIX2   3 -0.070000 -0.023300  0.997300       39.85570    1                    
MTRIX3   3 -0.047500 -0.998500 -0.026700       92.85020    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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