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PDBsum entry 1diy

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Oxidoreductase PDB id
1diy
Jmol
Contents
Protein chain
553 a.a. *
Ligands
NAG-NDG
NAG-NAG-BMA-BMA-
MAN
NAG-NAG
BOG ×4
COH
ACD
Waters ×109
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          30-NOV-99   1DIY
TITLE     CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND IN THE CYCLOOXYGENASE
TITLE    2 ACTIVE SITE OF PGHS-1
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN H2 SYNTHASE-1;
COMPND   3 CHAIN: A;
COMPND   4 EC: 1.14.99.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE   3 ORGANISM_COMMON: SHEEP;
SOURCE   4 ORGANISM_TAXID: 9940;
SOURCE   5 ORGAN: SEMINAL VESSICLE
KEYWDS    ARACHIDONIC ACID, MEMBRANE PROTEIN, PEROXIDASE, DIOXYGENASE,
KEYWDS   2 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.G.MALKOWSKI,S.L.GINELL,W.L.SMITH,R.M.GARAVITO
REVDAT   3   13-JUL-11 1DIY    1       VERSN
REVDAT   2   24-FEB-09 1DIY    1       VERSN
REVDAT   1   22-SEP-00 1DIY    0
JRNL        AUTH   M.G.MALKOWSKI,S.L.GINELL,W.L.SMITH,R.M.GARAVITO
JRNL        TITL   THE PRODUCTIVE CONFORMATION OF ARACHIDONIC ACID BOUND TO
JRNL        TITL 2 PROSTAGLANDIN SYNTHASE.
JRNL        REF    SCIENCE                       V. 289  1933 2000
JRNL        REFN                   ISSN 0036-8075
JRNL        PMID   10988074
JRNL        DOI    10.1126/SCIENCE.289.5486.1933
REMARK   2
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.1
REMARK   3   NUMBER OF REFLECTIONS             : 18519
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5% OF THE TOTAL REFLECTIONS
REMARK   3                                      WERE SELECTED BY CNS USING THE
REMARK   3                                      SCRIPT MAKE_CV.INP
REMARK   3   R VALUE            (WORKING SET) : 0.215
REMARK   3   FREE R VALUE                     : 0.290
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 880
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.10
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1468
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3250
REMARK   3   BIN FREE R VALUE                    : 0.4150
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.70
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 72
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4409
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 262
REMARK   3   SOLVENT ATOMS            : 109
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38
REMARK   3   ESD FROM SIGMAA              (A) : 0.54
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 6.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.50
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.69
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.51
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.96
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.04
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  USED THE MLF TARGET IN CNS UTILIZING BULK SOLVENT AND OVERALL B-
REMARK   3  FACTOR
REMARK   3  CORRECTIONS
REMARK   4
REMARK   4 1DIY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-99.
REMARK 100 THE RCSB ID CODE IS RCSB010117.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-AUG-99
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03321
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : CUSTOM-MADE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19163
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000
REMARK 200  RESOLUTION RANGE LOW       (A) : 9.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : 0.06700
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.10
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.4
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.34700
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1PRH MOLECULE B, PROTEIN ONLY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM CHLORIDE, SODIUM AZIDE, SODIUM
REMARK 280  CITRATE, N-OCTYL GLUCOSIDE, PH 6.5, VAPOR DIFFUSION, SITTING
REMARK 280  DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
REMARK 290       7555   Y,X,-Z+2/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+1/3
REMARK 290      10555   -Y,-X,-Z+1/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.09333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       34.54667
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.82000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       17.27333
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       86.36667
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.09333
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       34.54667
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       17.27333
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       51.82000
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       86.36667
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 APPLY THE FOLLOWING TO CHAINS: A
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   BIOMT1   2  0.500000  0.866025  0.000000        0.00000
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       86.36667
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 18500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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   BIOMT1   2 -0.500000  0.866025  0.000000      273.15000
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000     -157.70323
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -34.54667
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A  83    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 169    CG   CD   CE   NZ
REMARK 470     GLN A 170    CG   CD   OE1  NE2
REMARK 470     ASP A 173    CG   OD1  OD2
REMARK 470     GLU A 175    CG   CD   OE1  OE2
REMARK 470     LYS A 186    CG   CD   CE   NZ
REMARK 470     LYS A 215    CG   CD   CE   NZ
REMARK 470     LYS A 248    CG   CD   CE   NZ
REMARK 470     GLU A 267    CG   CD   OE1  OE2
REMARK 470     GLU A 290    CG   CD   OE1  OE2
REMARK 470     LYS A 317    CG   CD   CE   NZ
REMARK 470     ARG A 396    CG   CD   NE   CZ   NH1  NH2
REMARK 470     GLN A 400    CG   CD   OE1  NE2
REMARK 470     GLU A 405    CG   CD   OE1  OE2
REMARK 470     ASP A 416    CG   OD1  OD2
REMARK 470     LYS A 473    CG   CD   CE   NZ
REMARK 470     GLN A 479    CG   CD   OE1  NE2
REMARK 470     LYS A 485    CG   CD   CE   NZ
REMARK 470     GLU A 486    CG   CD   OE1  OE2
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    ASN A  34      100.27    -48.41
REMARK 500    CYS A  36        3.36    -58.62
REMARK 500    CYS A  59        3.23    -63.40
REMARK 500    THR A  60      129.81    -38.53
REMARK 500    ARG A  61       27.63     48.94
REMARK 500    CYS A  69       61.33     63.40
REMARK 500    HIS A  95      -52.82   -139.64
REMARK 500    ARG A  97       27.54    -55.86
REMARK 500    TRP A  98      -50.41   -137.76
REMARK 500    ALA A 105       33.75    -95.52
REMARK 500    LEU A 117      -79.78    -47.51
REMARK 500    THR A 118      -74.04    -29.78
REMARK 500    THR A 129      -96.75   -102.25
REMARK 500    ASP A 135       41.99    -98.05
REMARK 500    VAL A 145      -11.90    -48.42
REMARK 500    PRO A 153     -171.78    -61.81
REMARK 500    ARG A 157       18.45    -66.59
REMARK 500    PRO A 160      -77.55    -41.06
REMARK 500    LYS A 169       -6.21    -56.78
REMARK 500    ARG A 185      -77.19   -101.27
REMARK 500    THR A 194      150.23    -46.76
REMARK 500    ALA A 223       83.81    -65.74
REMARK 500    HIS A 226       62.28     38.87
REMARK 500    ILE A 233      -56.42   -124.25
REMARK 500    PHE A 247       55.15     14.10
REMARK 500    GLU A 268      -36.10    147.19
REMARK 500    ALA A 269       65.87   -113.80
REMARK 500    PRO A 270       58.00    -58.29
REMARK 500    MET A 273     -148.74   -128.64
REMARK 500    HIS A 274       15.52   -155.50
REMARK 500    ARG A 277       97.93    -53.89
REMARK 500    PRO A 280        2.57    -58.20
REMARK 500    PRO A 281      -91.43    -92.58
REMARK 500    SER A 283       15.13     58.38
REMARK 500    GLN A 284       77.20   -117.51
REMARK 500    VAL A 287      -46.07   -134.83
REMARK 500    GLU A 290      -42.87    -25.34
REMARK 500    THR A 322       19.99    -62.77
REMARK 500    GLN A 327      -71.89    -55.47
REMARK 500    PHE A 329      -70.58    -64.34
REMARK 500    GLU A 347      -46.89   -137.02
REMARK 500    GLN A 350      -71.19    -60.74
REMARK 500    LEU A 359      146.80    -38.50
REMARK 500    ARG A 374      125.49   -174.02
REMARK 500    ARG A 376      103.33   -162.09
REMARK 500    TRP A 387       51.07    -90.64
REMARK 500    PRO A 392     -162.15    -71.87
REMARK 500    TYR A 402      155.08    -45.14
REMARK 500    PHE A 409       -2.50     50.22
REMARK 500    ASN A 410      160.87    -48.67
REMARK 500
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A 823        DISTANCE =  6.52 ANGSTROMS
REMARK 525    HOH A 844        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH A 848        DISTANCE =  6.13 ANGSTROMS
REMARK 525    HOH A 854        DISTANCE =  5.63 ANGSTROMS
REMARK 525    HOH A 861        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH A 868        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH A 875        DISTANCE =  7.21 ANGSTROMS
REMARK 525    HOH A 876        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH A 879        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH A 889        DISTANCE =  5.46 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             COH A 601  CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 COH A 601   NA  106.8
REMARK 620 3 COH A 601   NB   88.8  86.0
REMARK 620 4 COH A 601   NC   73.3 178.9  92.9
REMARK 620 5 COH A 601   ND   91.8  95.9 177.8  85.3
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG 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 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 675
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 750
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 753
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COH A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACD A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO THE
REMARK 900 CYCLOOXYGENASE ACTIVE SITE OF COX-2
REMARK 900 RELATED ID: 1DDX   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MIXTURE OF ARACHIDONIC ACID AND
REMARK 900 PROSTAGLANDIN BOUND TO THE CYCLOOXYGENASE ACTIVE SITE OF
REMARK 900 COX-2: PROSTAGLANDIN STRUCTURE
REMARK 900 RELATED ID: 1PRH   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2
REMARK 900 SYNTHASE-1
REMARK 900 RELATED ID: 1PTH   RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF ASPIRIN ACTIVITY INFERRED FROM THE
REMARK 900 CRYSTAL STRUCTURE OF INACTIVATED PROSTAGLANDIN H2 SYNTHASE-1
REMARK 900 RELATED ID: 1PGE   RELATED DB: PDB
REMARK 900 SYNTHESIS AND USE OF IODINATED NONSTEROIDAL
REMARK 900 ANTIINFLAMMATORY DRUG ANALOGS AS CRYSTALLOGRAPHIC PROBES OF
REMARK 900 THE PROSTAGLANDIN H2 SYNTHASE-1 CYCLOOXYGENASE ACTIVE SITE
DBREF  1DIY A   32   584  GB     165844   AAA31511        31    583
SEQRES   1 A  553  PRO VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN
SEQRES   2 A  553  GLY ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS
SEQRES   3 A  553  ASP CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR
SEQRES   4 A  553  ILE PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG
SEQRES   5 A  553  PRO SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY
SEQRES   6 A  553  ARG TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG
SEQRES   7 A  553  ASP THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN
SEQRES   8 A  553  LEU ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP
SEQRES   9 A  553  TYR ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR
SEQRES  10 A  553  THR ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR
SEQRES  11 A  553  PRO MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA
SEQRES  12 A  553  GLU PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE
SEQRES  13 A  553  ILE PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE
SEQRES  14 A  553  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER
SEQRES  15 A  553  GLY LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS
SEQRES  16 A  553  GLY VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU
SEQRES  17 A  553  ARG GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  553  LYS TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER
SEQRES  19 A  553  VAL GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY
SEQRES  20 A  553  ILE PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL
SEQRES  21 A  553  PHE GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE
SEQRES  22 A  553  TRP LEU ARG GLU HIS ASN ARG VAL CYS ASP LEU LEU LYS
SEQRES  23 A  553  ALA GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  553  THR ALA ARG LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  553  VAL ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE
SEQRES  26 A  553  LEU GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA
SEQRES  27 A  553  GLN PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN
SEQRES  28 A  553  GLN LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE
SEQRES  29 A  553  ARG VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU
SEQRES  30 A  553  PHE ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA
SEQRES  31 A  553  LEU VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE
SEQRES  32 A  553  GLY GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL
SEQRES  33 A  553  ALA VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU
SEQRES  34 A  553  GLN PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS
SEQRES  35 A  553  PRO TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  553  MET ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP
SEQRES  37 A  553  ALA LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS
SEQRES  38 A  553  HIS PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET
SEQRES  39 A  553  GLY ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO
SEQRES  40 A  553  ILE CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY
SEQRES  41 A  553  GLY GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU
SEQRES  42 A  553  LYS LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR
SEQRES  43 A  553  VAL SER PHE HIS VAL PRO ASP
MODRES 1DIY ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 1DIY ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 1DIY ASN A  410  ASN  GLYCOSYLATION SITE
HET    NAG  A 661      14
HET    NDG  A 662      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    BMA  A 673      11
HET    BMA  A 674      11
HET    MAN  A 675      11
HET    NAG  A 681      14
HET    NAG  A 682      14
HET    BOG  A 750      20
HET    BOG  A 751      20
HET    BOG  A 752      20
HET    BOG  A 753      20
HET    COH  A 601      43
HET    ACD  A 700      22
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE
HETNAM     BMA BETA-D-MANNOSE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     COH PROTOPORPHYRIN IX CONTAINING CO
HETNAM     ACD ARACHIDONIC ACID
FORMUL   2  NAG    5(C8 H15 N O6)
FORMUL   2  NDG    C8 H15 N O6
FORMUL   3  BMA    2(C6 H12 O6)
FORMUL   3  MAN    C6 H12 O6
FORMUL   5  BOG    4(C14 H28 O6)
FORMUL   9  COH    C34 H32 CO N4 O4
FORMUL  10  ACD    C20 H32 O2
FORMUL  11  HOH   *109(H2 O)
HELIX    1   1 ASN A   34  TYR A   38  5                                   5
HELIX    2   2 GLU A   73  ARG A   83  1                                  11
HELIX    3   3 SER A   85  THR A   94  1                                  10
HELIX    4   4 TRP A   98  ALA A  105  1                                   8
HELIX    5   5 PHE A  107  ASN A  122  1                                  16
HELIX    6   6 SER A  138  ASN A  144  1                                   7
HELIX    7   7 ASP A  173  LEU A  182  1                                  10
HELIX    8   8 ASN A  195  HIS A  207  1                                  13
HELIX    9   9 ASN A  237  ARG A  245  1                                   9
HELIX   10  10 LEU A  295  HIS A  320  1                                  26
HELIX   11  11 GLY A  324  GLU A  347  1                                  24
HELIX   12  12 GLU A  347  GLY A  354  1                                   8
HELIX   13  13 ASP A  362  PHE A  367  5                                   6
HELIX   14  14 ALA A  378  TYR A  385  1                                   8
HELIX   15  15 HIS A  386  HIS A  386  5                                   1
HELIX   16  16 TRP A  387  MET A  391  5                                   5
HELIX   17  17 SER A  403  LEU A  408  1                                   6
HELIX   18  18 SER A  412  GLY A  418  1                                   7
HELIX   19  19 GLY A  418  GLN A  429  1                                  12
HELIX   20  20 ILE A  444  ARG A  459  1                                  16
HELIX   21  21 PRO A  462  PHE A  470  1                                   9
HELIX   22  22 SER A  477  THR A  482  1                                   6
HELIX   23  23 LYS A  485  GLY A  496  1                                  12
HELIX   24  24 ASP A  497  LEU A  501  5                                   5
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  PHE A  550  5                                   5
HELIX   29  29 GLY A  552  THR A  561  1                                  10
HELIX   30  30 THR A  563  LEU A  570  1                                   8
SHEET    1   A 2 ILE A  46  PHE A  50  0
SHEET    2   A 2 ARG A  54  ASP A  58 -1  O  ARG A  54   N  PHE A  50
SHEET    1   B 2 TYR A  64  SER A  65  0
SHEET    2   B 2 ILE A  71  PRO A  72 -1  N  ILE A  71   O  SER A  65
SHEET    1   C 2 GLN A 255  LEU A 257  0
SHEET    2   C 2 GLU A 260  TYR A 262 -1  O  GLU A 260   N  LEU A 257
SHEET    1   D 2 PHE A 395  VAL A 397  0
SHEET    2   D 2 GLN A 400  TYR A 402 -1  O  GLN A 400   N  VAL A 397
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.05
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.03
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03
LINK         O4  NAG A 661                 C1  NDG A 662     1555   1555  1.41
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.40
LINK         O4  NAG A 681                 C1  NAG A 682     1555   1555  1.39
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.46
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.45
LINK         O4  NAG A 672                 C1  BMA A 673     1555   1555  1.40
LINK         C1  BMA A 674                 O6  BMA A 673     1555   1555  1.41
LINK         C1  MAN A 675                 O3  BMA A 674     1555   1555  1.41
LINK        CO   COH A 601                 NE2 HIS A 388     1555   1555  2.16
CISPEP   1 SER A  126    PRO A  127          0         0.19
SITE     1 AC1  4 PRO A  40  TYR A  55  ASN A  68  NDG A 662
SITE     1 AC2  3 TYR A  38  ASP A 584  NAG A 661
SITE     1 AC3  5 ASN A 144  TYR A 147  PHE A 220  LEU A 238
SITE     2 AC3  5 NAG A 672
SITE     1 AC4  6 MET A 216  LEU A 238  GLU A 239  TYR A 242
SITE     2 AC4  6 NAG A 671  BMA A 673
SITE     1 AC5  3 NAG A 672  BMA A 674  HOH A 833
SITE     1 AC6  3 BMA A 673  MAN A 675  HOH A 833
SITE     1 AC7  3 GLN A 243  PRO A 270  BMA A 674
SITE     1 AC8 10 GLY A 278  ILE A 279  PRO A 280  PRO A 281
SITE     2 AC8 10 TYR A 402  GLN A 406  ASN A 410  ASP A 416
SITE     3 AC8 10 NAG A 682  HOH A 872
SITE     1 AC9  5 TYR A 402  GLN A 406  NAG A 681  HOH A 862
SITE     2 AC9  5 HOH A 872
SITE     1 BC1  3 SER A  87  PHE A  88  PHE A  91
SITE     1 BC2 10 PRO A  86  LEU A 115  VAL A 119  ARG A 120
SITE     2 BC2 10 LEU A 123  GLY A 471  GLU A 524  BOG A 752
SITE     3 BC2 10 HOH A 835  HOH A 855
SITE     1 BC3  4 ILE A  89  LEU A 115  BOG A 751  HOH A 900
SITE     1 BC4  5 PHE A  91  LEU A  92  GLY A  96  LEU A  99
SITE     2 BC4  5 VAL A 103
SITE     1 BC5 14 GLN A 203  HIS A 207  PHE A 210  THR A 212
SITE     2 BC5 14 LEU A 295  ASN A 382  TYR A 385  HIS A 386
SITE     3 BC5 14 HIS A 388  ILE A 444  HIS A 446  VAL A 447
SITE     4 BC5 14 ASP A 450  HOH A 908
SITE     1 BC6 21 VAL A 116  ARG A 120  PHE A 205  PHE A 209
SITE     2 BC6 21 TYR A 348  VAL A 349  LEU A 352  TYR A 355
SITE     3 BC6 21 ASN A 375  ILE A 377  PHE A 381  TYR A 385
SITE     4 BC6 21 TRP A 387  MET A 522  ILE A 523  GLY A 526
SITE     5 BC6 21 ALA A 527  SER A 530  LEU A 531  GLY A 533
SITE     6 BC6 21 LEU A 534
CRYST1  182.100  182.100  103.640  90.00  90.00 120.00 P 65 2 2     12
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      0.005491  0.003171  0.000000        0.00000
SCALE2      0.000000  0.006341  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009649        0.00000
      
PROCHECK
Go to PROCHECK summary
 References