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Database: PDB
Entry: 1DDX
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Original site: 1DDX 
HEADER    OXIDOREDUCTASE                          11-NOV-99   1DDX              
TITLE     CRYSTAL STRUCTURE OF A MIXTURE OF ARACHIDONIC ACID AND PROSTAGLANDIN  
TITLE    2 BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF COX-2: PROSTAGLANDIN      
TITLE    3 STRUCTURE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (PROSTAGLANDIN H2 SYNTHASE-2);                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: COX-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 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PVL1393                                   
KEYWDS    COX-2, CYCLOOXYGENASE, PROSTAGLANDIN, ARACHIDONATE, ENDOPEROXIDE,     
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.KIEFER,J.L.PAWLITZ,K.T.MORELAND,R.A.STEGEMAN,J.K.GIERSE,          
AUTHOR   2 A.M.STEVENS,D.C.GOODWIN,S.W.ROWLINSON,L.J.MARNETT,W.C.STALLINGS,     
AUTHOR   3 R.G.KURUMBAIL                                                        
REVDAT   4   13-JUL-11 1DDX    1       VERSN                                    
REVDAT   3   24-FEB-09 1DDX    1       VERSN                                    
REVDAT   2   01-APR-03 1DDX    1       JRNL                                     
REVDAT   1   16-MAY-00 1DDX    0                                                
JRNL        AUTH   J.R.KIEFER,J.L.PAWLITZ,K.T.MORELAND,R.A.STEGEMAN,W.F.HOOD,   
JRNL        AUTH 2 J.K.GIERSE,A.M.STEVENS,D.C.GOODWIN,S.W.ROWLINSON,            
JRNL        AUTH 3 L.J.MARNETT,W.C.STALLINGS,R.G.KURUMBAIL                      
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE STEREOCHEMISTRY OF THE          
JRNL        TITL 2 CYCLOOXYGENASE REACTION.                                     
JRNL        REF    NATURE                        V. 405    97 2000              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   10811226                                                     
JRNL        DOI    10.1038/35011103                                             
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   STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF                 
REMARK   1  TITL 2 CYCLOOXYGENASE-2 BY ANTI- INFLAMMATORY AGENTS                
REMARK   1  REF    NATURE                        V. 384   644 1996              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  DOI    10.1038/384644A0                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 76.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 45794                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.267                           
REMARK   3   FREE R VALUE                     : 0.324                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4324                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.19                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 57.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5106                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3560                       
REMARK   3   BIN FREE R VALUE                    : 0.4470                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 537                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17900                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 404                                     
REMARK   3   SOLVENT ATOMS            : 173                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.47                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.65                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.620 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.120 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.670 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.390 ; 2.500                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : PARAM19X_MOD.HEME                              
REMARK   3  PARAMETER FILE  4  : PARAM3_MOD.CHO                                 
REMARK   3  PARAMETER FILE  5  : B-OCTYLGLUCOPYRANOSIDE.PAR                     
REMARK   3  PARAMETER FILE  6  : GH2.PAR                                        
REMARK   3  PARAMETER FILE  7  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH19X_MOD.HEME                               
REMARK   3  TOPOLOGY FILE  4   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  5   : B-OCTYLGLUCOPYRANOSIDE.TOP                     
REMARK   3  TOPOLOGY FILE  6   : GH2.TOP                                        
REMARK   3  TOPOLOGY FILE  7   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1DDX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB010002.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-AUG-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 130.0                              
REMARK 200  PH                             : 8.00                               
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 RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.514                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : DOUBLE-MIRROR OPTICS               
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   : 45048                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.11200                            
REMARK 200  R SYM                      (I) : 0.11200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MONOMETHYL PEG 550, MAGNESIUM SULFATE,   
REMARK 280  ARACHIDNOIC ACID, EPPS, B-OG, PH 8.00, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 288K                                              
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       90.12000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.12000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.40000            
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: 9700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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: 9710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 43300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 10.0 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO C2128   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  35       -8.40    -57.15                                   
REMARK 500    SER A  38       10.88    -67.23                                   
REMARK 500    SER A  49       95.95    -69.74                                   
REMARK 500    THR A  50       46.55    -87.64                                   
REMARK 500    TYR A  65     -142.22   -104.26                                   
REMARK 500    THR A  70      -60.96   -102.06                                   
REMARK 500    PHE A  74      -70.69    -54.96                                   
REMARK 500    LEU A  81       36.68    -81.17                                   
REMARK 500    LEU A  82       12.44   -163.58                                   
REMARK 500    HIS A  95     -157.90   -121.70                                   
REMARK 500    PHE A  96       26.78     37.32                                   
REMARK 500    LYS A  97      -39.71    -30.59                                   
REMARK 500    ASN A 104       -1.28    -54.98                                   
REMARK 500    PRO A 106      -71.38    -18.62                                   
REMARK 500    ARG A 120      -88.60    -66.27                                   
REMARK 500    SER A 121      -77.05     20.79                                   
REMARK 500    TYR A 122       12.45    -52.27                                   
REMARK 500    PRO A 128      153.80    -41.27                                   
REMARK 500    THR A 129     -104.21   -125.45                                   
REMARK 500    ALA A 141      -85.38    -61.72                                   
REMARK 500    PHE A 142      -25.50    -38.31                                   
REMARK 500    PRO A 154     -166.89    -71.22                                   
REMARK 500    VAL A 165      -43.51   -131.72                                   
REMARK 500    GLU A 176      -87.38    -52.83                                   
REMARK 500    VAL A 177      -52.99    -25.44                                   
REMARK 500    LYS A 180      -20.55    -33.38                                   
REMARK 500    VAL A 181       -1.29   -163.99                                   
REMARK 500    ARG A 185      -74.20    -95.79                                   
REMARK 500    SER A 194      103.31    -52.14                                   
REMARK 500    MET A 197      -70.48    -48.30                                   
REMARK 500    ALA A 199      -70.24    -42.68                                   
REMARK 500    PHE A 201      -78.54    -63.36                                   
REMARK 500    ALA A 202      -53.95    -27.84                                   
REMARK 500    THR A 206      -16.69    -49.92                                   
REMARK 500    LYS A 211       31.25   -164.12                                   
REMARK 500    THR A 212      126.12    -25.63                                   
REMARK 500    HIS A 226       49.87     37.11                                   
REMARK 500    VAL A 228       95.64    -63.72                                   
REMARK 500    GLN A 270        8.86     58.44                                   
REMARK 500    PRO A 277      -47.13    -25.17                                   
REMARK 500    ILE A 279      128.52    -38.19                                   
REMARK 500    GLN A 284       95.85    -64.78                                   
REMARK 500    PHE A 292       -8.60    -42.05                                   
REMARK 500    ALA A 302      -77.77    -46.07                                   
REMARK 500    THR A 303      -44.08    -28.60                                   
REMARK 500    ILE A 304      -71.04    -60.29                                   
REMARK 500    HIS A 309      -73.54    -45.01                                   
REMARK 500    LYS A 317      -18.46    -48.33                                   
REMARK 500    ASP A 347     -102.24   -106.61                                   
REMARK 500    TYR A 348      -91.07    -14.42                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     367 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PGX A  701                                                       
REMARK 610     PGX B 1701                                                       
REMARK 610     PGX C 2701                                                       
REMARK 610     PGX D 3701                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 662                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1661                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1662                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1671                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1681                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2661                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2662                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2671                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2681                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3661                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3662                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3671                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3681                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG B 1702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG C 2702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 3702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGX A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGX B 1701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGX C 2701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGX D 3701                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF ARACHIDONIC ACID BOUND TO COX-2                         
REMARK 900 RELATED ID: 1DCX   RELATED DB: PDB                                   
REMARK 900 MODEL OF ARACHIDONIC ACID BOUND TO COX-2                             
REMARK 900 RELATED ID: 1DD0   RELATED DB: PDB                                   
REMARK 900 MODEL OF PROSTAGLANDIN G2 BOUND TO COX-2                             
REMARK 900 RELATED ID: 6COX   RELATED DB: PDB                                   
REMARK 900 COX-2 COMPLEXED TO SELECTIVE INHIBITOR SC-558                        
REMARK 900 RELATED ID: 5COX   RELATED DB: PDB                                   
REMARK 900 COX-2 STRUCTURE WITHOUT INHIBITORS BOUND                             
REMARK 900 RELATED ID: 1CQE   RELATED DB: PDB                                   
REMARK 900 COX-1 STRUCTURE                                                      
DBREF  1DDX A   33   583  UNP    Q05769   PGH2_MOUSE      18    569             
DBREF  1DDX B 1033  1583  UNP    Q05769   PGH2_MOUSE      18    569             
DBREF  1DDX C 2033  2583  UNP    Q05769   PGH2_MOUSE      18    569             
DBREF  1DDX D 3033  3583  UNP    Q05769   PGH2_MOUSE      18    569             
SEQRES   1 A  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 A  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 A  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 A  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 A  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 A  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 A  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 A  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 A  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 A  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 A  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 A  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 A  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 A  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 A  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 A  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 A  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 A  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 A  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 A  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 A  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 A  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 A  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 A  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 A  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 A  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 A  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 A  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 A  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 A  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 A  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 A  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 A  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 A  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 A  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 A  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 A  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 A  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 A  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 A  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 A  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 A  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 A  552  THR SER PHE ASN VAL GLN                                      
SEQRES   1 B  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 B  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 B  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 B  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 B  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 B  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 B  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 B  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 B  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 B  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 B  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 B  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 B  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 B  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 B  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 B  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 B  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 B  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 B  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 B  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 B  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 B  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 B  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 B  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 B  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 B  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 B  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 B  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 B  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 B  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 B  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 B  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 B  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 B  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 B  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 B  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 B  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 B  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 B  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 B  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 B  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 B  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 B  552  THR SER PHE ASN VAL GLN                                      
SEQRES   1 C  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 C  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 C  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 C  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 C  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 C  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 C  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 C  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 C  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 C  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 C  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 C  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 C  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 C  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 C  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 C  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 C  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 C  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 C  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 C  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 C  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 C  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 C  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 C  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 C  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 C  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 C  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 C  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 C  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 C  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 C  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 C  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 C  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 C  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 C  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 C  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 C  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 C  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 C  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 C  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 C  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 C  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 C  552  THR SER PHE ASN VAL GLN                                      
SEQRES   1 D  552  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY          
SEQRES   2 D  552  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP          
SEQRES   3 D  552  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR          
SEQRES   4 D  552  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO          
SEQRES   5 D  552  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS          
SEQRES   6 D  552  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG          
SEQRES   7 D  552  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR          
SEQRES   8 D  552  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY          
SEQRES   9 D  552  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR          
SEQRES  10 D  552  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR          
SEQRES  11 D  552  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER          
SEQRES  12 D  552  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE          
SEQRES  13 D  552  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE          
SEQRES  14 D  552  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP          
SEQRES  15 D  552  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS          
SEQRES  16 D  552  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP          
SEQRES  17 D  552  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU          
SEQRES  18 D  552  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR          
SEQRES  19 D  552  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS          
SEQRES  20 D  552  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL          
SEQRES  21 D  552  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE          
SEQRES  22 D  552  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP ILE LEU LYS          
SEQRES  23 D  552  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN          
SEQRES  24 D  552  THR SER ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE          
SEQRES  25 D  552  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS          
SEQRES  26 D  552  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN          
SEQRES  27 D  552  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN          
SEQRES  28 D  552  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE          
SEQRES  29 D  552  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU          
SEQRES  30 D  552  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN          
SEQRES  31 D  552  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL          
SEQRES  32 D  552  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL          
SEQRES  33 D  552  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR          
SEQRES  34 D  552  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS          
SEQRES  35 D  552  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU          
SEQRES  36 D  552  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP          
SEQRES  37 D  552  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO          
SEQRES  38 D  552  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU          
SEQRES  39 D  552  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO          
SEQRES  40 D  552  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY          
SEQRES  41 D  552  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE          
SEQRES  42 D  552  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE          
SEQRES  43 D  552  THR SER PHE ASN VAL GLN                                      
MODRES 1DDX ASN A   68  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN A  144  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN A  410  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN B 1068  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN B 1144  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN B 1410  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN C 2068  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN C 2144  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN C 2410  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN D 3068  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN D 3144  ASN  GLYCOSYLATION SITE                                 
MODRES 1DDX ASN D 3410  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 661      14                                                       
HET    NAG  A 662      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 681      14                                                       
HET    NAG  B1661      14                                                       
HET    NAG  B1662      14                                                       
HET    NAG  B1671      14                                                       
HET    NAG  B1681      14                                                       
HET    NAG  C2661      14                                                       
HET    NAG  C2662      14                                                       
HET    NAG  C2671      14                                                       
HET    NAG  C2681      14                                                       
HET    NAG  D3661      14                                                       
HET    NAG  D3662      14                                                       
HET    NAG  D3671      14                                                       
HET    NAG  D3681      14                                                       
HET    BOG  A 702      20                                                       
HET    BOG  B1702      20                                                       
HET    BOG  C2702      20                                                       
HET    BOG  D3702      20                                                       
HET    PGX  A 701      25                                                       
HET    PGX  B1701      25                                                       
HET    PGX  C2701      25                                                       
HET    PGX  D3701      25                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     PGX 7-[6-(3-HYDROPEROXY-OCT-1-ENYL)-2,3-DIOXA-                       
HETNAM   2 PGX  BICYCLO[2.2.1]HEPT-5-YL]-HEPT-5-ENOIC ACID                      
HETSYN     PGX PROSTAGLANDIN G2                                                 
FORMUL   5  NAG    16(C8 H15 N O6)                                              
FORMUL  17  BOG    4(C14 H28 O6)                                                
FORMUL  21  PGX    4(C20 H32 O6)                                                
FORMUL  25  HOH   *173(H2 O)                                                    
HELIX    1   1 GLU A   73  LEU A   81  1                                   9    
HELIX    2   2 THR A   85  HIS A   95  1                                  11    
HELIX    3   3 PHE A   96  ASN A  104  1                                   9    
HELIX    4   4 ILE A  105A TYR A  122  1                                  18    
HELIX    5   5 SER A  138  ASN A  144  1                                   7    
HELIX    6   6 ASP A  173  LEU A  182  1                                  10    
HELIX    7   7 ASN A  195  HIS A  207  1                                  13    
HELIX    8   8 LEU A  230  GLY A  235  1                                   6    
HELIX    9   9 THR A  237  LEU A  244  1                                   8    
HELIX   10  10 THR A  265  GLN A  270  1                                   6    
HELIX   11  11 VAL A  291  LEU A  294  5                                   4    
HELIX   12  12 VAL A  295  HIS A  320  1                                  26    
HELIX   13  13 GLY A  324  ASP A  347  1                                  24    
HELIX   14  14 ASP A  347  GLY A  354  1                                   8    
HELIX   15  15 ASP A  362  LEU A  366  5                                   5    
HELIX   16  16 ALA A  378  HIS A  386  1                                   9    
HELIX   17  17 TRP A  387  LEU A  391  5                                   5    
HELIX   18  18 SER A  403  LEU A  408  1                                   6    
HELIX   19  19 ASN A  410  GLY A  418  1                                   9    
HELIX   20  20 GLY A  418  THR A  427  1                                  10    
HELIX   21  21 VAL A  444  MET A  458  1                                  15    
HELIX   22  22 SER A  462  PHE A  470  1                                   9    
HELIX   23  23 SER A  477  GLY A  483  1                                   7    
HELIX   24  24 LYS A  485  SER A  496  1                                  12    
HELIX   25  25 GLU A  502  GLU A  510  1                                   9    
HELIX   26  26 GLY A  519  GLY A  536  1                                  18    
HELIX   27  27 ASN A  537  SER A  541  5                                   5    
HELIX   28  28 LYS A  546  GLY A  551  5                                   6    
HELIX   29  29 GLY A  552  THR A  561  1                                  10    
HELIX   30  30 SER A  563  VAL A  572  1                                  10    
HELIX   31  31 GLU B 1073  LEU B 1081  1                                   9    
HELIX   32  32 THR B 1085  HIS B 1095  1                                  11    
HELIX   33  33 PHE B 1096  ASN B 1104  1                                   9    
HELIX   34  34 ILE B 1105B TYR B 1122  1                                  18    
HELIX   35  35 SER B 1138  ASN B 1144  1                                   7    
HELIX   36  36 ASP B 1173  LEU B 1182  1                                  10    
HELIX   37  37 ASN B 1195  HIS B 1207  1                                  13    
HELIX   38  38 LEU B 1230  GLY B 1235  1                                   6    
HELIX   39  39 THR B 1237  LEU B 1244  1                                   8    
HELIX   40  40 THR B 1265  GLN B 1270  1                                   6    
HELIX   41  41 VAL B 1291  LEU B 1294  5                                   4    
HELIX   42  42 VAL B 1295  HIS B 1320  1                                  26    
HELIX   43  43 GLY B 1324  ASP B 1347  1                                  24    
HELIX   44  44 ASP B 1347  GLY B 1354  1                                   8    
HELIX   45  45 ASP B 1362  LEU B 1366  5                                   5    
HELIX   46  46 ALA B 1378  HIS B 1386  1                                   9    
HELIX   47  47 TRP B 1387  LEU B 1391  5                                   5    
HELIX   48  48 SER B 1403  LEU B 1408  1                                   6    
HELIX   49  49 ASN B 1410  GLY B 1418  1                                   9    
HELIX   50  50 GLY B 1418  THR B 1427  1                                  10    
HELIX   51  51 VAL B 1444  MET B 1458  1                                  15    
HELIX   52  52 SER B 1462  PHE B 1470  1                                   9    
HELIX   53  53 SER B 1477  GLY B 1483  1                                   7    
HELIX   54  54 LYS B 1485  SER B 1496  1                                  12    
HELIX   55  55 GLU B 1502  GLU B 1510  1                                   9    
HELIX   56  56 GLY B 1519  GLY B 1536  1                                  18    
HELIX   57  57 ASN B 1537  SER B 1541  5                                   5    
HELIX   58  58 LYS B 1546  GLY B 1551  5                                   6    
HELIX   59  59 GLY B 1552  THR B 1561  1                                  10    
HELIX   60  60 SER B 1563  VAL B 1572  1                                  10    
HELIX   61  61 GLU C 2073  LEU C 2081  1                                   9    
HELIX   62  62 THR C 2085  HIS C 2095  1                                  11    
HELIX   63  63 PHE C 2096  ASN C 2104  1                                   9    
HELIX   64  64 ILE C 2105C TYR C 2122  1                                  18    
HELIX   65  65 SER C 2138  ASN C 2144  1                                   7    
HELIX   66  66 ASP C 2173  LEU C 2182  1                                  10    
HELIX   67  67 ASN C 2195  HIS C 2207  1                                  13    
HELIX   68  68 LEU C 2230  GLY C 2235  1                                   6    
HELIX   69  69 THR C 2237  LEU C 2244  1                                   8    
HELIX   70  70 THR C 2265  GLN C 2270  1                                   6    
HELIX   71  71 VAL C 2291  LEU C 2294  5                                   4    
HELIX   72  72 VAL C 2295  HIS C 2320  1                                  26    
HELIX   73  73 GLY C 2324  ASP C 2347  1                                  24    
HELIX   74  74 ASP C 2347  GLY C 2354  1                                   8    
HELIX   75  75 ASP C 2362  LEU C 2366  5                                   5    
HELIX   76  76 ALA C 2378  HIS C 2386  1                                   9    
HELIX   77  77 TRP C 2387  LEU C 2391  5                                   5    
HELIX   78  78 SER C 2403  LEU C 2408  1                                   6    
HELIX   79  79 ASN C 2410  GLY C 2418  1                                   9    
HELIX   80  80 GLY C 2418  GLN C 2429  1                                  12    
HELIX   81  81 VAL C 2444  MET C 2458  1                                  15    
HELIX   82  82 SER C 2462  PHE C 2470  1                                   9    
HELIX   83  83 SER C 2477  GLY C 2483  1                                   7    
HELIX   84  84 LYS C 2485  SER C 2496  1                                  12    
HELIX   85  85 GLU C 2502  GLU C 2510  1                                   9    
HELIX   86  86 GLY C 2519  GLY C 2536  1                                  18    
HELIX   87  87 ASN C 2537  SER C 2541  5                                   5    
HELIX   88  88 LYS C 2546  PHE C 2550  5                                   5    
HELIX   89  89 GLY C 2551  THR C 2561  1                                  11    
HELIX   90  90 SER C 2563  VAL C 2572  1                                  10    
HELIX   91  91 GLU D 3073  LEU D 3081  1                                   9    
HELIX   92  92 THR D 3085  HIS D 3095  1                                  11    
HELIX   93  93 PHE D 3096  ASN D 3104  1                                   9    
HELIX   94  94 ILE D 3105D TYR D 3122  1                                  18    
HELIX   95  95 SER D 3138  ASN D 3144  1                                   7    
HELIX   96  96 ASP D 3173  LEU D 3182  1                                  10    
HELIX   97  97 ASN D 3195  HIS D 3207  1                                  13    
HELIX   98  98 LEU D 3230  GLY D 3235  1                                   6    
HELIX   99  99 THR D 3237  LEU D 3244  1                                   8    
HELIX  100 100 THR D 3265  GLN D 3270  1                                   6    
HELIX  101 101 VAL D 3291  LEU D 3294  5                                   4    
HELIX  102 102 VAL D 3295  HIS D 3320  1                                  26    
HELIX  103 103 GLY D 3324  ASP D 3347  1                                  24    
HELIX  104 104 ASP D 3347  GLY D 3354  1                                   8    
HELIX  105 105 ASP D 3362  LEU D 3366  5                                   5    
HELIX  106 106 ALA D 3378  HIS D 3386  1                                   9    
HELIX  107 107 TRP D 3387  LEU D 3391  5                                   5    
HELIX  108 108 SER D 3403  LEU D 3408  1                                   6    
HELIX  109 109 ASN D 3410  GLY D 3418  1                                   9    
HELIX  110 110 GLY D 3418  THR D 3427  1                                  10    
HELIX  111 111 VAL D 3444  MET D 3458  1                                  15    
HELIX  112 112 SER D 3462  PHE D 3470  1                                   9    
HELIX  113 113 SER D 3477  GLY D 3483  1                                   7    
HELIX  114 114 LYS D 3485  SER D 3496  1                                  12    
HELIX  115 115 GLU D 3502  GLU D 3510  1                                   9    
HELIX  116 116 GLY D 3519  GLY D 3536  1                                  18    
HELIX  117 117 ASN D 3537  SER D 3541  5                                   5    
HELIX  118 118 LYS D 3546  GLY D 3551  5                                   6    
HELIX  119 119 GLY D 3552  THR D 3561  1                                  10    
HELIX  120 120 SER D 3563  VAL D 3572  1                                  10    
SHEET    1   A 2 CYS A  47  MET A  48  0                                        
SHEET    2   A 2 LYS A  56  CYS A  57 -1  O  LYS A  56   N  MET A  48           
SHEET    1   B 2 GLN A 255  ILE A 257  0                                        
SHEET    2   B 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  ILE A 257           
SHEET    1   C 2 CYS B1047  MET B1048  0                                        
SHEET    2   C 2 LYS B1056  CYS B1057 -1  O  LYS B1056   N  MET B1048           
SHEET    1   D 2 GLN B1255  ILE B1257  0                                        
SHEET    2   D 2 GLU B1260  TYR B1262 -1  O  GLU B1260   N  ILE B1257           
SHEET    1   E 2 CYS C2047  MET C2048  0                                        
SHEET    2   E 2 LYS C2056  CYS C2057 -1  O  LYS C2056   N  MET C2048           
SHEET    1   F 2 GLN C2255  ILE C2257  0                                        
SHEET    2   F 2 GLU C2260  TYR C2262 -1  O  GLU C2260   N  ILE C2257           
SHEET    1   G 2 CYS D3047  MET D3048  0                                        
SHEET    2   G 2 LYS D3056  CYS D3057 -1  O  LYS D3056   N  MET D3048           
SHEET    1   H 2 GLN D3255  ILE D3257  0                                        
SHEET    2   H 2 GLU D3260  TYR D3262 -1  O  GLU D3260   N  ILE D3257           
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.04  
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.03  
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.04  
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03  
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.02  
SSBOND   6 CYS B 1036    CYS B 1047                          1555   1555  2.03  
SSBOND   7 CYS B 1037    CYS B 1159                          1555   1555  2.03  
SSBOND   8 CYS B 1041    CYS B 1057                          1555   1555  2.03  
SSBOND   9 CYS B 1059    CYS B 1069                          1555   1555  2.04  
SSBOND  10 CYS B 1569    CYS B 1575                          1555   1555  2.02  
SSBOND  11 CYS C 2036    CYS C 2047                          1555   1555  2.03  
SSBOND  12 CYS C 2037    CYS C 2159                          1555   1555  2.02  
SSBOND  13 CYS C 2041    CYS C 2057                          1555   1555  2.03  
SSBOND  14 CYS C 2059    CYS C 2069                          1555   1555  2.04  
SSBOND  15 CYS C 2569    CYS C 2575                          1555   1555  2.03  
SSBOND  16 CYS D 3036    CYS D 3047                          1555   1555  2.04  
SSBOND  17 CYS D 3037    CYS D 3159                          1555   1555  2.03  
SSBOND  18 CYS D 3041    CYS D 3057                          1555   1555  2.04  
SSBOND  19 CYS D 3059    CYS D 3069                          1555   1555  2.03  
SSBOND  20 CYS D 3569    CYS D 3575                          1555   1555  2.03  
LINK         O4  NAG A 661                 C1  NAG A 662     1555   1555  1.40  
LINK         O4  NAG B1661                 C1  NAG B1662     1555   1555  1.40  
LINK         O4  NAG C2661                 C1  NAG C2662     1555   1555  1.39  
LINK         O4  NAG D3661                 C1  NAG D3662     1555   1555  1.40  
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.44  
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.47  
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.45  
LINK         ND2 ASN B1068                 C1  NAG B1661     1555   1555  1.46  
LINK         ND2 ASN B1144                 C1  NAG B1671     1555   1555  1.45  
LINK         ND2 ASN B1410                 C1  NAG B1681     1555   1555  1.46  
LINK         ND2 ASN C2068                 C1  NAG C2661     1555   1555  1.46  
LINK         ND2 ASN C2144                 C1  NAG C2671     1555   1555  1.46  
LINK         ND2 ASN C2410                 C1  NAG C2681     1555   1555  1.46  
LINK         ND2 ASN D3068                 C1  NAG D3661     1555   1555  1.45  
LINK         ND2 ASN D3144                 C1  NAG D3671     1555   1555  1.46  
LINK         ND2 ASN D3410                 C1  NAG D3681     1555   1555  1.44  
CISPEP   1 SER A  126    PRO A  127          0         0.36                     
CISPEP   2 SER B 1126    PRO B 1127          0         0.51                     
CISPEP   3 SER C 2126    PRO C 2127          0         0.05                     
CISPEP   4 SER D 3126    PRO D 3127          0        -0.19                     
SITE     1 AC1  4 PRO A  40  TYR A  55  ASN A  68  NAG A 662                    
SITE     1 AC2  1 NAG A 661                                                     
SITE     1 AC3  4 ASN A 144  SER A 146  TYR A 147  ARG A 216                    
SITE     1 AC4  3 GLN A 406  ASN A 410  GLU A 416                               
SITE     1 AC5  4 PRO B1040  TYR B1055  ASN B1068  NAG B1662                    
SITE     1 AC6  1 NAG B1661                                                     
SITE     1 AC7  4 ASN B1144  SER B1146  TYR B1147  ARG B1216                    
SITE     1 AC8  3 GLN B1406  ASN B1410  GLU B1416                               
SITE     1 AC9  3 PRO C2040  ASN C2068  NAG C2662                               
SITE     1 BC1  1 NAG C2661                                                     
SITE     1 BC2  5 GLU C2140  ASN C2144  SER C2146  TYR C2147                    
SITE     2 BC2  5 ARG C2216                                                     
SITE     1 BC3  3 GLN C2406  ASN C2410  GLU C2416                               
SITE     1 BC4  4 PRO D3040  GLU D3067  ASN D3068  NAG D3662                    
SITE     1 BC5  1 NAG D3661                                                     
SITE     1 BC6  4 ASN D3144  SER D3146  TYR D3147  ARG D3216                    
SITE     1 BC7  3 GLN D3406  ASN D3410  GLU D3416                               
SITE     1 BC8  2 THR A  88  TYR A  91                                          
SITE     1 BC9  2 THR B1088  PHE B1096                                          
SITE     1 CC1  2 TYR C2091  PRO C2514                                          
SITE     1 CC2  4 THR D3085  ASN D3087  THR D3088  TYR D3091                    
SITE     1 CC3 14 PHE A 205  PHE A 209  TYR A 348  VAL A 349                    
SITE     2 CC3 14 LEU A 352  SER A 353  PHE A 381  LEU A 384                    
SITE     3 CC3 14 TYR A 385  TRP A 387  GLY A 526  SER A 530                    
SITE     4 CC3 14 GLY A 533  LEU A 534                                          
SITE     1 CC4 18 PHE B1205  THR B1206  PHE B1209  PHE B1210                    
SITE     2 CC4 18 VAL B1228  TYR B1348  VAL B1349  LEU B1352                    
SITE     3 CC4 18 LEU B1384  TYR B1385  TRP B1387  VAL B1523                    
SITE     4 CC4 18 GLY B1526  ALA B1527  SER B1530  GLY B1533                    
SITE     5 CC4 18 LEU B1534  HOH B4074                                          
SITE     1 CC5 16 PHE C2205  THR C2206  PHE C2209  PHE C2210                    
SITE     2 CC5 16 TYR C2348  VAL C2349  LEU C2352  LEU C2384                    
SITE     3 CC5 16 TYR C2385  TRP C2387  VAL C2523  GLY C2526                    
SITE     4 CC5 16 ALA C2527  SER C2530  GLY C2533  LEU C2534                    
SITE     1 CC6 14 PHE D3205  PHE D3209  TYR D3348  VAL D3349                    
SITE     2 CC6 14 LEU D3352  SER D3353  PHE D3381  LEU D3384                    
SITE     3 CC6 14 TYR D3385  TRP D3387  GLY D3526  SER D3530                    
SITE     4 CC6 14 GLY D3533  LEU D3534                                          
CRYST1  180.240  134.800  122.510  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      0.005548  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007418  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008163        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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