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Database: PDB
Entry: 2VCW
LinkDB: 2VCW
Original site: 2VCW 
HEADER    ISOMERASE                               27-SEP-07   2VCW              
TITLE     COMPLEX STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE AT 1.95A.              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE-REQUIRING PROSTAGLANDIN D SYNTHASE;            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: GLUTATHIONE-DEPENDENT PGD SYNTHETASE,                       
COMPND   5  PROSTAGLANDIN-H2 D-ISOMERASE, HEMATOPOIETIC PROSTAGLANDIN           
COMPND   6  D SYNTHASE, H-PGDS;                                                 
COMPND   7 EC: 5.3.99.2;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: THE PROTEIN CONTAIN A GLUTATHIONE CO-FACTOR.          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    PROSTAGLANDIN BIOSYNTHESIS, FATTY ACID BIOSYNTHESIS,                  
KEYWDS   2 PROSTAGLANDIN D2 SYNTHASE, PGDS, ASTHMA, CYTOPLASM,                  
KEYWDS   3 ISOMERASE, LIPID SYNTHESIS                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HOHWY,L.SPADOLA,B.LUNDQUIST,K.VON WACHENFELDT,                      
AUTHOR   2 S.PERSDOTTER,P.HAWTIN,J.DAHMEN,I.GROTH-CLAUSEN,                      
AUTHOR   3 R.H.A.FOLMER,K.EDMAN                                                 
REVDAT   2   24-FEB-09 2VCW    1       VERSN                                    
REVDAT   1   15-APR-08 2VCW    0                                                
JRNL        AUTH   M.HOHWY,L.SPADOLA,B.LUNDQUIST,P.HAWTIN,J.DAHMEN,             
JRNL        AUTH 2 I.GROTH-CLAUSEN,E.NILSSON,S.PERSDOTTER,                      
JRNL        AUTH 3 K.VON WACHENFELDT,R.H.A.FOLMER,K.EDMAN                       
JRNL        TITL   NOVEL PROSTAGLANDIN D SYNTHASE INHIBITORS                    
JRNL        TITL 2 GENERATED BY FRAGMENT-BASED DRUG DESIGN.                     
JRNL        REF    J.MED.CHEM.                   V.  51  2178 2008              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   18341273                                                     
JRNL        DOI    10.1021/JM701509K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 87.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 55544                          
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 + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2962                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4077                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 197                          
REMARK   3   BIN FREE R VALUE                    : 0.2970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6332                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 213                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.36000                                              
REMARK   3    B22 (A**2) : 0.36000                                              
REMARK   3    B33 (A**2) : -0.72000                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.194         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.171         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.885         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.904                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6570 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8934 ; 1.276 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   762 ; 2.773 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   318 ;29.245 ;24.057       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1117 ;10.866 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;12.917 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   983 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4994 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2988 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4521 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   324 ; 0.121 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    71 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.141 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3994 ; 0.773 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6253 ; 1.232 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3028 ; 1.628 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2681 ; 2.491 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2VCW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-SEP-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33992.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.939                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58526                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.95                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.3                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.7                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.50                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.37                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PD2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG6000, 1% DIOXANE, 5MM             
REMARK 280  DTT, 5MM GSH, 0.05 M TRISHCL PH8.4                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y,Z                                                 
REMARK 290       7555   -Y+1/2,X,Z+3/4                                          
REMARK 290       8555   Y,-X+1/2,Z+1/4                                          
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       61.92900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       61.92900            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.31000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       61.92900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       26.65500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       61.92900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       79.96500            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       61.92900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.92900            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       53.31000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       61.92900            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       79.96500            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       61.92900            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       26.65500            
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 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.1 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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.2 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     MET A     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLU C   106                                                      
REMARK 465     LYS C   107                                                      
REMARK 465     LYS C   108                                                      
REMARK 465     GLN C   109                                                      
REMARK 465     ASP C   110                                                      
REMARK 465     VAL C   111                                                      
REMARK 465     LYS C   112                                                      
REMARK 465     GLU C   113                                                      
REMARK 465     GLN C   114                                                      
REMARK 465     MET D     1                                                      
REMARK 465     CYS D   101                                                      
REMARK 465     PHE D   102                                                      
REMARK 465     PRO D   103                                                      
REMARK 465     TRP D   104                                                      
REMARK 465     ALA D   105                                                      
REMARK 465     GLU D   106                                                      
REMARK 465     LYS D   107                                                      
REMARK 465     LYS D   108                                                      
REMARK 465     GLN D   109                                                      
REMARK 465     ASP D   110                                                      
REMARK 465     VAL D   111                                                      
REMARK 465     LYS D   112                                                      
REMARK 465     GLU D   113                                                      
REMARK 465     GLN D   114                                                      
REMARK 465     MET D   115                                                      
REMARK 465     PHE D   116                                                      
REMARK 465     ASN D   117                                                      
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 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    GLN A  63      104.99     72.70                                   
REMARK 500    TYR A 122      -62.37   -106.59                                   
REMARK 500    GLN B  63      104.54     73.73                                   
REMARK 500    GLN C  36       20.84    -62.70                                   
REMARK 500    GLN C  63      104.66     72.47                                   
REMARK 500    GLN D  63      100.10     71.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZZA B1201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH D1200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VCQ   RELATED DB: PDB                                   
REMARK 900  COMPLEX STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE                      
REMARK 900   AT 1.95A.                                                          
REMARK 900 RELATED ID: 2VCZ   RELATED DB: PDB                                   
REMARK 900  COMPLEX STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE                      
REMARK 900   AT 1.95A.                                                          
REMARK 900 RELATED ID: 2VCX   RELATED DB: PDB                                   
REMARK 900  COMPLEX STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE                      
REMARK 900   AT 2.1A.                                                           
REMARK 900 RELATED ID: 2VD0   RELATED DB: PDB                                   
REMARK 900  COMPLEX STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE                      
REMARK 900   AT 2.2A.                                                           
REMARK 900 RELATED ID: 2VD1   RELATED DB: PDB                                   
REMARK 900  COMPLEX STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE                      
REMARK 900   AT 2.25A.                                                          
REMARK 900 RELATED ID: 1IYI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN                    
REMARK 900   D SYNTHASE                                                         
REMARK 900 RELATED ID: 1V40   RELATED DB: PDB                                   
REMARK 900  FIRST INHIBITOR COMPLEX STRUCTURE OF HUMAN                          
REMARK 900  HEMATOPOIETICPROSTAGLANDIN D SYNTHASE                               
REMARK 900 RELATED ID: 1IYH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN                    
REMARK 900   D SYNTHASE                                                         
DBREF  2VCW A    1   199  UNP    O60760   PTGD2_HUMAN      1    199             
DBREF  2VCW B    1   199  UNP    O60760   PTGD2_HUMAN      1    199             
DBREF  2VCW C    1   199  UNP    O60760   PTGD2_HUMAN      1    199             
DBREF  2VCW D    1   199  UNP    O60760   PTGD2_HUMAN      1    199             
SEQRES   1 A  199  MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY          
SEQRES   2 A  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP          
SEQRES   3 A  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP          
SEQRES   4 A  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO          
SEQRES   5 A  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU          
SEQRES   6 A  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA          
SEQRES   7 A  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE          
SEQRES   8 A  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP          
SEQRES   9 A  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN          
SEQRES  10 A  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP          
SEQRES  11 A  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY          
SEQRES  12 A  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS          
SEQRES  13 A  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP          
SEQRES  14 A  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN          
SEQRES  15 A  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO          
SEQRES  16 A  199  GLN THR LYS LEU                                              
SEQRES   1 B  199  MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY          
SEQRES   2 B  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP          
SEQRES   3 B  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP          
SEQRES   4 B  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO          
SEQRES   5 B  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU          
SEQRES   6 B  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA          
SEQRES   7 B  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE          
SEQRES   8 B  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP          
SEQRES   9 B  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN          
SEQRES  10 B  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP          
SEQRES  11 B  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY          
SEQRES  12 B  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS          
SEQRES  13 B  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP          
SEQRES  14 B  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN          
SEQRES  15 B  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO          
SEQRES  16 B  199  GLN THR LYS LEU                                              
SEQRES   1 C  199  MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY          
SEQRES   2 C  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP          
SEQRES   3 C  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP          
SEQRES   4 C  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO          
SEQRES   5 C  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU          
SEQRES   6 C  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA          
SEQRES   7 C  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE          
SEQRES   8 C  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP          
SEQRES   9 C  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN          
SEQRES  10 C  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP          
SEQRES  11 C  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY          
SEQRES  12 C  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS          
SEQRES  13 C  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP          
SEQRES  14 C  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN          
SEQRES  15 C  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO          
SEQRES  16 C  199  GLN THR LYS LEU                                              
SEQRES   1 D  199  MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY          
SEQRES   2 D  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP          
SEQRES   3 D  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP          
SEQRES   4 D  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO          
SEQRES   5 D  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU          
SEQRES   6 D  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA          
SEQRES   7 D  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE          
SEQRES   8 D  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP          
SEQRES   9 D  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN          
SEQRES  10 D  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP          
SEQRES  11 D  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY          
SEQRES  12 D  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS          
SEQRES  13 D  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP          
SEQRES  14 D  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN          
SEQRES  15 D  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO          
SEQRES  16 D  199  GLN THR LYS LEU                                              
HET    GSH  A1200      20                                                       
HET    GSH  B1200      20                                                       
HET    ZZA  B1201      14                                                       
HET    GSH  D1200      20                                                       
HETNAM     ZZA 1-PHENYL-1H-PYRAZOLE-4-CARBOXYLIC ACID                           
HETNAM     GSH GLUTATHIONE                                                      
FORMUL   5  ZZA    C10 H8 N2 O2                                                 
FORMUL   6  GSH    3(C10 H17 N3 O6 S)                                           
FORMUL   7  HOH   *213(H2 O1)                                                   
HELIX    1   1 ALA A   15  LEU A   25  1                                  11    
HELIX    2   2 GLU A   35  ALA A   37  5                                   3    
HELIX    3   3 ASP A   38  SER A   44  1                                   7    
HELIX    4   4 GLN A   63  LYS A   73  1                                  11    
HELIX    5   5 THR A   75  GLY A   79  5                                   5    
HELIX    6   6 THR A   81  SER A  100  1                                  20    
HELIX    7   7 LYS A  108  TYR A  122  1                                  15    
HELIX    8   8 TYR A  122  GLY A  136  1                                  15    
HELIX    9   9 THR A  147  LYS A  164  1                                  18    
HELIX   10  10 HIS A  171  ILE A  184  1                                  14    
HELIX   11  11 ILE A  184  ARG A  194  1                                  11    
HELIX   12  12 ARG B   12  ARG B   14  5                                   3    
HELIX   13  13 ALA B   15  ASP B   26  1                                  12    
HELIX   14  14 GLU B   35  ALA B   37  5                                   3    
HELIX   15  15 ASP B   38  SER B   44  1                                   7    
HELIX   16  16 GLN B   63  LYS B   73  1                                  11    
HELIX   17  17 THR B   81  SER B  100  1                                  20    
HELIX   18  18 LYS B  108  ASN B  123  1                                  16    
HELIX   19  19 ASN B  123  GLY B  136  1                                  14    
HELIX   20  20 THR B  147  LYS B  164  1                                  18    
HELIX   21  21 HIS B  171  ILE B  184  1                                  14    
HELIX   22  22 ILE B  184  ARG B  194  1                                  11    
HELIX   23  23 ALA C   15  LEU C   25  1                                  11    
HELIX   24  24 ASP C   38  SER C   44  1                                   7    
HELIX   25  25 GLN C   63  LYS C   73  1                                  11    
HELIX   26  26 THR C   81  CYS C  101  1                                  21    
HELIX   27  27 MET C  115  ASN C  123  1                                   9    
HELIX   28  28 ASN C  123  GLY C  136  1                                  14    
HELIX   29  29 THR C  147  LYS C  164  1                                  18    
HELIX   30  30 HIS C  171  ILE C  184  1                                  14    
HELIX   31  31 ILE C  184  ARG C  194  1                                  11    
HELIX   32  32 ARG D   12  ARG D   14  5                                   3    
HELIX   33  33 ALA D   15  LEU D   25  1                                  11    
HELIX   34  34 GLU D   35  ALA D   37  5                                   3    
HELIX   35  35 ASP D   38  SER D   44  1                                   7    
HELIX   36  36 GLN D   63  LYS D   73  1                                  11    
HELIX   37  37 THR D   81  SER D  100  1                                  20    
HELIX   38  38 GLU D  118  GLY D  136  1                                  19    
HELIX   39  39 THR D  147  LYS D  164  1                                  18    
HELIX   40  40 HIS D  171  ALA D  183  1                                  13    
HELIX   41  41 ILE D  184  ARG D  194  1                                  11    
SHEET    1  AA 4 GLU A  30  ILE A  34  0                                        
SHEET    2  AA 4 TYR A   4  PHE A   9  1  O  TYR A   4   N  GLU A  30           
SHEET    3  AA 4 ILE A  53  VAL A  56 -1  O  ILE A  53   N  THR A   7           
SHEET    4  AA 4 LEU A  59  HIS A  62 -1  O  LEU A  59   N  VAL A  56           
SHEET    1  BA 4 GLU B  30  ILE B  34  0                                        
SHEET    2  BA 4 TYR B   4  PHE B   9  1  O  TYR B   4   N  GLU B  30           
SHEET    3  BA 4 ILE B  53  VAL B  56 -1  O  ILE B  53   N  THR B   7           
SHEET    4  BA 4 LEU B  59  HIS B  62 -1  O  LEU B  59   N  VAL B  56           
SHEET    1  CA 4 TYR C  29  ILE C  34  0                                        
SHEET    2  CA 4 TYR C   4  PHE C   9  1  O  TYR C   4   N  GLU C  30           
SHEET    3  CA 4 ILE C  53  VAL C  56 -1  O  ILE C  53   N  THR C   7           
SHEET    4  CA 4 LEU C  59  HIS C  62 -1  O  LEU C  59   N  VAL C  56           
SHEET    1  DA 4 GLU D  30  ILE D  34  0                                        
SHEET    2  DA 4 TYR D   4  PHE D   9  1  O  TYR D   4   N  GLU D  30           
SHEET    3  DA 4 ILE D  53  VAL D  56 -1  O  ILE D  53   N  THR D   7           
SHEET    4  DA 4 LEU D  59  HIS D  62 -1  O  LEU D  59   N  VAL D  56           
CISPEP   1 ILE A   51    PRO A   52          0         5.59                     
CISPEP   2 ILE B   51    PRO B   52          0         6.29                     
CISPEP   3 ILE C   51    PRO C   52          0         4.61                     
CISPEP   4 ILE D   51    PRO D   52          0         3.92                     
SITE     1 AC1 12 TYR A   8  ARG A  14  TRP A  39  LYS A  43                    
SITE     2 AC1 12 LYS A  50  ILE A  51  GLN A  63  SER A  64                    
SITE     3 AC1 12 HOH A2006  HOH A2021  HOH A2069  ASP B  97                    
SITE     1 AC2 12 ASP A  97  TYR B   8  ARG B  14  TRP B  39                    
SITE     2 AC2 12 LYS B  43  LYS B  50  ILE B  51  PRO B  52                    
SITE     3 AC2 12 GLN B  63  SER B  64  ZZA B1201  HOH B2024                    
SITE     1 AC3  7 GLY B  13  ARG B  14  MET B  99  TRP B 104                    
SITE     2 AC3  7 TYR B 152  GSH B1200  HOH B2049                               
SITE     1 AC4 11 ASP C  97  TYR D   8  ARG D  14  TRP D  39                    
SITE     2 AC4 11 LYS D  43  LYS D  50  ILE D  51  PRO D  52                    
SITE     3 AC4 11 GLN D  63  SER D  64  HOH D2015                               
CRYST1  123.858  123.858  106.620  90.00  90.00  90.00 I 41         32          
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      0.008074  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008074  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009379        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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