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PDBsum entry 1pxx

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1pxx
Jmol
Contents
Protein chains
552 a.a. *
Ligands
NAG ×8
NAG-NAG-NAG ×4
BOG ×2
HEM ×4
DIF ×4
Waters ×317
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          07-JUL-03   1PXX
TITLE     CRYSTAL STRUCTURE OF DICLOFENAC BOUND TO THE CYCLOOXYGENASE ACTIVE
TITLE    2 SITE OF COX-2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROSTAGLANDIN G/H SYNTHASE 2;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: CYCLOOXYGENASE-2, COX-2, PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE
COMPND   5 2, PROSTAGLANDIN H2 SYNTHASE 2, PGH SYNTHASE 2, PGHS-2, PHS II,
COMPND   6 GLUCOCORTICOID-REGULATED INFLAMMATORY CYCLOOXYGENASE, GRIPGHS, TIS10
COMPND   7 PROTEIN, MACROPHAGE ACTIVATION-ASSOCIATED MARKER PROTEIN P71/73, PES-
COMPND   8 2;
COMPND   9 EC: 1.14.99.1;
COMPND  10 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 GENE: PTGS2 OR COX2 OR COX-2 OR TIS10 OR PGHS-B;
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PVL1393
KEYWDS    COX-2, CYCLOOXYGENASE, PROSTAGLANDIN, DICLOFENAC, ENDOPEROXIDE,
KEYWDS   2 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.R.KIEFER,S.W.ROWLINSON,J.J.PRUSAKIEWICZ,J.L.PAWLITZ,K.R.KOZAK,
AUTHOR   2 A.S.KALGUTKAR,W.C.STALLINGS,L.J.MARNETT,R.G.KURUMBAIL
REVDAT   4   13-JUL-11 1PXX    1       VERSN
REVDAT   3   24-FEB-09 1PXX    1       VERSN
REVDAT   2   18-NOV-03 1PXX    1       JRNL   AUTHOR
REVDAT   1   09-SEP-03 1PXX    0
JRNL        AUTH   S.W.ROWLINSON,J.R.KIEFER,J.J.PRUSAKIEWICZ,J.L.PAWLITZ,
JRNL        AUTH 2 K.R.KOZAK,A.S.KALGUTKAR,W.C.STALLINGS,R.G.KURUMBAIL,
JRNL        AUTH 3 L.J.MARNETT
JRNL        TITL   A NOVEL MECHANISM OF CYCLOOXYGENASE-2 INHIBITION INVOLVING
JRNL        TITL 2 INTERACTIONS WITH SER-530 AND TYR-385.
JRNL        REF    J.BIOL.CHEM.                  V. 278 45763 2003
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   12925531
JRNL        DOI    10.1074/JBC.M305481200
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   1 REFERENCE 2
REMARK   1  AUTH   J.R.KIEFER,J.L.PAWLITZ,K.T.MORELAND,R.A.STEGEMAN,W.F.HOOD,
REMARK   1  AUTH 2 J.K.GIERSE,A.M.STEVENS,D.C.GOODWIN,S.W.ROWLINSON,
REMARK   1  AUTH 3 L.J.MARNETT,W.C.STALLINGS,R.G.KURUMBAIL
REMARK   1  TITL   STRUCTURAL INSIGHTS INTO THE STEREOCHEMISTRY OF THE
REMARK   1  TITL 2 CYCLOOXYGENASE REACTION
REMARK   1  REF    NATURE                        V.  45    97 2000
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1  DOI    10.1038/35011103
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 98.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 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)   (%) : 83.6
REMARK   3   NUMBER OF REFLECTIONS             : 56787
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) : 0.254
REMARK   3   FREE R VALUE                     : 0.302
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.600
REMARK   3   FREE R VALUE TEST SET COUNT      : 5471
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
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) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7496
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980
REMARK   3   BIN FREE R VALUE                    : 0.3500
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.60
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 795
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 17894
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 567
REMARK   3   SOLVENT ATOMS            : 317
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 38.90
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.40
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) : 0.36
REMARK   3   ESD FROM SIGMAA              (A) : 0.38
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.009
REMARK   3   BOND ANGLES            (DEGREES) : 1.40
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.20
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.81
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) : 1.900 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.030 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.060 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.680 ; 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  : PARAM.DICLOFENAC
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   : TOP.DICLOFENAC
REMARK   3  TOPOLOGY FILE  7   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK   4
REMARK   4 1PXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-03.
REMARK 100 THE RCSB ID CODE IS RCSB019683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 17-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67852
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 5.300
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.16100
REMARK 200   FOR THE DATA SET  : 4.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.38100
REMARK 200   FOR SHELL         : 3.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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   (%): 55.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MONOMETHYL PEG 550, MAGNESIUM
REMARK 280  CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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       90.57250
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.54500
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       90.57250
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.54500
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 12000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 12000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET A    16
REMARK 465     LEU A    17
REMARK 465     PHE A    18
REMARK 465     ARG A    19
REMARK 465     ALA A    20
REMARK 465     VAL A    21
REMARK 465     LEU A    22
REMARK 465     LEU A    23
REMARK 465     CYS A    24
REMARK 465     ALA A    25
REMARK 465     ALA A    26
REMARK 465     LEU A    27
REMARK 465     GLY A    28
REMARK 465     LEU A    29
REMARK 465     SER A    30
REMARK 465     GLN A    31
REMARK 465     ALA A    32
REMARK 465     ASP A   584
REMARK 465     PRO A   585
REMARK 465     GLN A   586
REMARK 465     PRO A   587
REMARK 465     THR A   588
REMARK 465     LYS A   589
REMARK 465     THR A   590
REMARK 465     ALA A   591
REMARK 465     THR A   592
REMARK 465     ILE A   593
REMARK 465     ASN A   594
REMARK 465     ALA A   595
REMARK 465     SER A   596
REMARK 465     ALA A   597
REMARK 465     SER A   598
REMARK 465     HIS A   599
REMARK 465     SER A   600
REMARK 465     ARG A   601
REMARK 465     LEU A   602
REMARK 465     ASP A   603
REMARK 465     ASP A   604
REMARK 465     ILE A   605
REMARK 465     ASN A   606
REMARK 465     PRO A   607
REMARK 465     THR A   608
REMARK 465     VAL A   609
REMARK 465     LEU A   610
REMARK 465     ILE A   611
REMARK 465     LYS A   612
REMARK 465     ARG A   613
REMARK 465     ARG A   614
REMARK 465     SER A   615
REMARK 465     THR A   616
REMARK 465     GLU A   617
REMARK 465     LEU A   618
REMARK 465     MET B  1016
REMARK 465     LEU B  1017
REMARK 465     PHE B  1018
REMARK 465     ARG B  1019
REMARK 465     ALA B  1020
REMARK 465     VAL B  1021
REMARK 465     LEU B  1022
REMARK 465     LEU B  1023
REMARK 465     CYS B  1024
REMARK 465     ALA B  1025
REMARK 465     ALA B  1026
REMARK 465     LEU B  1027
REMARK 465     GLY B  1028
REMARK 465     LEU B  1029
REMARK 465     SER B  1030
REMARK 465     GLN B  1031
REMARK 465     ALA B  1032
REMARK 465     ASP B  1584
REMARK 465     PRO B  1585
REMARK 465     GLN B  1586
REMARK 465     PRO B  1587
REMARK 465     THR B  1588
REMARK 465     LYS B  1589
REMARK 465     THR B  1590
REMARK 465     ALA B  1591
REMARK 465     THR B  1592
REMARK 465     ILE B  1593
REMARK 465     ASN B  1594
REMARK 465     ALA B  1595
REMARK 465     SER B  1596
REMARK 465     ALA B  1597
REMARK 465     SER B  1598
REMARK 465     HIS B  1599
REMARK 465     SER B  1600
REMARK 465     ARG B  1601
REMARK 465     LEU B  1602
REMARK 465     ASP B  1603
REMARK 465     ASP B  1604
REMARK 465     ILE B  1605
REMARK 465     ASN B  1606
REMARK 465     PRO B  1607
REMARK 465     THR B  1608
REMARK 465     VAL B  1609
REMARK 465     LEU B  1610
REMARK 465     ILE B  1611
REMARK 465     LYS B  1612
REMARK 465     ARG B  1613
REMARK 465     ARG B  1614
REMARK 465     SER B  1615
REMARK 465     THR B  1616
REMARK 465     GLU B  1617
REMARK 465     LEU B  1618
REMARK 465     MET C  2016
REMARK 465     LEU C  2017
REMARK 465     PHE C  2018
REMARK 465     ARG C  2019
REMARK 465     ALA C  2020
REMARK 465     VAL C  2021
REMARK 465     LEU C  2022
REMARK 465     LEU C  2023
REMARK 465     CYS C  2024
REMARK 465     ALA C  2025
REMARK 465     ALA C  2026
REMARK 465     LEU C  2027
REMARK 465     GLY C  2028
REMARK 465     LEU C  2029
REMARK 465     SER C  2030
REMARK 465     GLN C  2031
REMARK 465     ALA C  2032
REMARK 465     ASP C  2584
REMARK 465     PRO C  2585
REMARK 465     GLN C  2586
REMARK 465     PRO C  2587
REMARK 465     THR C  2588
REMARK 465     LYS C  2589
REMARK 465     THR C  2590
REMARK 465     ALA C  2591
REMARK 465     THR C  2592
REMARK 465     ILE C  2593
REMARK 465     ASN C  2594
REMARK 465     ALA C  2595
REMARK 465     SER C  2596
REMARK 465     ALA C  2597
REMARK 465     SER C  2598
REMARK 465     HIS C  2599
REMARK 465     SER C  2600
REMARK 465     ARG C  2601
REMARK 465     LEU C  2602
REMARK 465     ASP C  2603
REMARK 465     ASP C  2604
REMARK 465     ILE C  2605
REMARK 465     ASN C  2606
REMARK 465     PRO C  2607
REMARK 465     THR C  2608
REMARK 465     VAL C  2609
REMARK 465     LEU C  2610
REMARK 465     ILE C  2611
REMARK 465     LYS C  2612
REMARK 465     ARG C  2613
REMARK 465     ARG C  2614
REMARK 465     SER C  2615
REMARK 465     THR C  2616
REMARK 465     GLU C  2617
REMARK 465     LEU C  2618
REMARK 465     MET D  3016
REMARK 465     LEU D  3017
REMARK 465     PHE D  3018
REMARK 465     ARG D  3019
REMARK 465     ALA D  3020
REMARK 465     VAL D  3021
REMARK 465     LEU D  3022
REMARK 465     LEU D  3023
REMARK 465     CYS D  3024
REMARK 465     ALA D  3025
REMARK 465     ALA D  3026
REMARK 465     LEU D  3027
REMARK 465     GLY D  3028
REMARK 465     LEU D  3029
REMARK 465     SER D  3030
REMARK 465     GLN D  3031
REMARK 465     ALA D  3032
REMARK 465     ASP D  3584
REMARK 465     PRO D  3585
REMARK 465     GLN D  3586
REMARK 465     PRO D  3587
REMARK 465     THR D  3588
REMARK 465     LYS D  3589
REMARK 465     THR D  3590
REMARK 465     ALA D  3591
REMARK 465     THR D  3592
REMARK 465     ILE D  3593
REMARK 465     ASN D  3594
REMARK 465     ALA D  3595
REMARK 465     SER D  3596
REMARK 465     ALA D  3597
REMARK 465     SER D  3598
REMARK 465     HIS D  3599
REMARK 465     SER D  3600
REMARK 465     ARG D  3601
REMARK 465     LEU D  3602
REMARK 465     ASP D  3603
REMARK 465     ASP D  3604
REMARK 465     ILE D  3605
REMARK 465     ASN D  3606
REMARK 465     PRO D  3607
REMARK 465     THR D  3608
REMARK 465     VAL D  3609
REMARK 465     LEU D  3610
REMARK 465     ILE D  3611
REMARK 465     LYS D  3612
REMARK 465     ARG D  3613
REMARK 465     ARG D  3614
REMARK 465     SER D  3615
REMARK 465     THR D  3616
REMARK 465     GLU D  3617
REMARK 465     LEU D  3618
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     ALA A  33    N
REMARK 470     ASN A  34    N
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    LEU C  2123     NH2  ARG C  2469              2.14
REMARK 500   O    LEU D  3123     NH2  ARG D  3469              2.15
REMARK 500   O    LEU A   123     NH2  ARG A   469              2.15
REMARK 500   O    LEU B  1123     NH2  ARG B  1469              2.15
REMARK 500   OD1  ASP D  3058     OG1  THR D  3060              2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   OE1  GLU B  1490     O2   BOG A   703     4555     2.18
REMARK 500   OE1  GLU C  2490     O2   BOG D  3703     4456     2.18
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    THR A  50       61.93   -114.77
REMARK 500    PHE A  74      -71.49    -52.67
REMARK 500    PRO A 106      -63.85    -26.59
REMARK 500    SER A 121      -33.75    -38.48
REMARK 500    THR A 129      -91.61   -114.27
REMARK 500    ASN A 195     -163.37   -106.79
REMARK 500    LEU A 224        3.10    -67.32
REMARK 500    ASP A 347      -72.26   -115.11
REMARK 500    TRP A 387       39.03    -89.26
REMARK 500    GLU A 398     -116.67     69.27
REMARK 500    ARG A 438       58.54     27.01
REMARK 500    SER A 496      -60.48     83.38
REMARK 500    PRO A 514      107.97    -49.93
REMARK 500    ARG B1044        8.56     81.14
REMARK 500    THR B1050       75.08   -106.38
REMARK 500    ASP B1053       32.08   -147.76
REMARK 500    ARG B1061       18.38     52.53
REMARK 500    SER B1121      -32.21    -38.34
REMARK 500    THR B1129      -94.92   -113.88
REMARK 500    ASN B1195     -161.81   -104.77
REMARK 500    LEU B1224        4.37    -67.84
REMARK 500    PHE B1247       35.86     70.91
REMARK 500    ASP B1347      -72.89   -115.31
REMARK 500    TRP B1387       43.95    -88.06
REMARK 500    GLU B1398     -116.90     67.72
REMARK 500    ARG B1438       57.01     26.51
REMARK 500    SER B1496      -61.05     84.56
REMARK 500    PRO B1514      106.59    -48.61
REMARK 500    CYS B1575       73.00     35.26
REMARK 500    VAL B1582       99.03    -59.38
REMARK 500    ASN C2034      105.58    -57.62
REMARK 500    THR C2050       63.49   -102.21
REMARK 500    ASP C2053       29.99   -149.96
REMARK 500    GLU C2067      -38.98    -34.53
REMARK 500    PHE C2074      -73.57    -41.22
REMARK 500    PRO C2106      -66.19    -21.01
REMARK 500    SER C2121      -33.61    -37.64
REMARK 500    THR C2129      -92.48   -114.32
REMARK 500    ASN C2195     -163.12   -103.62
REMARK 500    LEU C2224        4.47    -67.00
REMARK 500    PHE C2247       35.42     71.17
REMARK 500    ASP C2347      -72.87   -116.02
REMARK 500    TRP C2387       42.31    -88.64
REMARK 500    GLU C2398     -117.65     67.38
REMARK 500    ARG C2438       60.78     24.44
REMARK 500    SER C2496      -58.54     82.79
REMARK 500    PRO C2514      106.68    -49.76
REMARK 500    ARG D3044       12.88     85.34
REMARK 500    SER D3121      -32.58    -37.48
REMARK 500    THR D3129      -91.82   -114.51
REMARK 500
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR B1348         0.07    SIDE CHAIN
REMARK 500    TYR D3348         0.06    SIDE CHAIN
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 B5238        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH D5255        DISTANCE =  5.26 ANGSTROMS
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     BOG D 3703
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 704  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 HEM A 704   NA   91.2
REMARK 620 3 HEM A 704   NB   93.0  89.7
REMARK 620 4 HEM A 704   NC   91.8 176.9  89.3
REMARK 620 5 HEM A 704   ND   91.3  89.8 175.7  90.9
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B1601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1388   NE2
REMARK 620 2 HEM B1601   NA   89.0
REMARK 620 3 HEM B1601   NB   91.7  90.4
REMARK 620 4 HEM B1601   NC   90.4 179.3  90.0
REMARK 620 5 HEM B1601   ND   92.4  90.6 175.8  89.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C2601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C2388   NE2
REMARK 620 2 HEM C2601   NA   89.0
REMARK 620 3 HEM C2601   NB   90.2  89.9
REMARK 620 4 HEM C2601   NC   92.3 178.7  90.2
REMARK 620 5 HEM C2601   ND   92.6  90.1 177.2  89.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D3601  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D3388   NE2
REMARK 620 2 HEM D3601   NA   89.6
REMARK 620 3 HEM D3601   NB   92.2  90.3
REMARK 620 4 HEM D3601   NC   92.6 177.7  89.6
REMARK 620 5 HEM D3601   ND   91.8  89.7 176.0  90.2
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 NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1661
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 1672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 1681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2672
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2673
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 2681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3672
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3673
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3681
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BOG D 3703
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 2601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 3601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIF A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIF B 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIF C 2701
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIF D 3701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6COX   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SC-558 BOUND TO COX-2
REMARK 900 RELATED ID: 1CVU   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ARACHIDONIC ACID BOUND TO COX-2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 17 RESIDUES ARE NOT OBSERVED IN
REMARK 999 THE ELECTRON DENSITY.  THE FULL SEQUENCE
REMARK 999 OF THE SEQUENCE DATABASE REFERENCE WAS
REMARK 999 INCLUDED IN THE SEQRES RECORD. THE C-TERMINAL
REMARK 999 ~3KDA OF THE PROTEIN ARE CLEAVED OFF BY
REMARK 999 TRYPSIN.  THE AUTHORS HAVE NOT DETERMINED
REMARK 999 THE FINAL C-TERMINAL AMINO ACID OF THE
REMARK 999 RESULTING PROTEIN AND DO NOT KNOW THE
REMARK 999 CLEAVAGE SITE.
DBREF  1PXX A   16   618  UNP    Q05769   PGH2_MOUSE       1    604
DBREF  1PXX B 1016  1618  UNP    Q05769   PGH2_MOUSE       1    604
DBREF  1PXX C 2016  2618  UNP    Q05769   PGH2_MOUSE       1    604
DBREF  1PXX D 3016  3618  UNP    Q05769   PGH2_MOUSE       1    604
SEQRES   1 A  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 A  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS
SEQRES   3 A  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   4 A  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   5 A  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   6 A  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   7 A  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   8 A  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   9 A  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES  10 A  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  11 A  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  12 A  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  13 A  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  14 A  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  15 A  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  16 A  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  17 A  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  18 A  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  19 A  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  20 A  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  21 A  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  22 A  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  23 A  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  24 A  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  25 A  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  26 A  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  27 A  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  28 A  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  29 A  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  30 A  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  31 A  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  32 A  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  33 A  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  34 A  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  35 A  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  36 A  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  37 A  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  38 A  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  39 A  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  40 A  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  41 A  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  42 A  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  43 A  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  44 A  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  45 A  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS
SEQRES  46 A  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  47 A  604  ARG ARG SER THR GLU LEU
SEQRES   1 B  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 B  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS
SEQRES   3 B  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   4 B  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   5 B  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   6 B  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   7 B  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   8 B  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   9 B  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES  10 B  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  11 B  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  12 B  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  13 B  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  14 B  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  15 B  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  16 B  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  17 B  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  18 B  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  19 B  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  20 B  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  21 B  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  22 B  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  23 B  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  24 B  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  25 B  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  26 B  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  27 B  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  28 B  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  29 B  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  30 B  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  31 B  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  32 B  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  33 B  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  34 B  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  35 B  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  36 B  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  37 B  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  38 B  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  39 B  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  40 B  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  41 B  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  42 B  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  43 B  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  44 B  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  45 B  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS
SEQRES  46 B  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  47 B  604  ARG ARG SER THR GLU LEU
SEQRES   1 C  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 C  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS
SEQRES   3 C  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   4 C  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   5 C  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   6 C  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   7 C  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   8 C  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   9 C  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES  10 C  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  11 C  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  12 C  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  13 C  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  14 C  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  15 C  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  16 C  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  17 C  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  18 C  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  19 C  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  20 C  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  21 C  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  22 C  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  23 C  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  24 C  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  25 C  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  26 C  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  27 C  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  28 C  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  29 C  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  30 C  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  31 C  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  32 C  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  33 C  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  34 C  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  35 C  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  36 C  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  37 C  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  38 C  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  39 C  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  40 C  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  41 C  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  42 C  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  43 C  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  44 C  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  45 C  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS
SEQRES  46 C  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  47 C  604  ARG ARG SER THR GLU LEU
SEQRES   1 D  604  MET LEU PHE ARG ALA VAL LEU LEU CYS ALA ALA LEU GLY
SEQRES   2 D  604  LEU SER GLN ALA ALA ASN PRO CYS CYS SER ASN PRO CYS
SEQRES   3 D  604  GLN ASN ARG GLY GLU CYS MET SER THR GLY PHE ASP GLN
SEQRES   4 D  604  TYR LYS CYS ASP CYS THR ARG THR GLY PHE TYR GLY GLU
SEQRES   5 D  604  ASN CYS THR THR PRO GLU PHE LEU THR ARG ILE LYS LEU
SEQRES   6 D  604  LEU LEU LYS PRO THR PRO ASN THR VAL HIS TYR ILE LEU
SEQRES   7 D  604  THR HIS PHE LYS GLY VAL TRP ASN ILE VAL ASN ASN ILE
SEQRES   8 D  604  PRO PHE LEU ARG SER LEU ILE MET LYS TYR VAL LEU THR
SEQRES   9 D  604  SER ARG SER TYR LEU ILE ASP SER PRO PRO THR TYR ASN
SEQRES  10 D  604  VAL HIS TYR GLY TYR LYS SER TRP GLU ALA PHE SER ASN
SEQRES  11 D  604  LEU SER TYR TYR THR ARG ALA LEU PRO PRO VAL ALA ASP
SEQRES  12 D  604  ASP CYS PRO THR PRO MET GLY VAL LYS GLY ASN LYS GLU
SEQRES  13 D  604  LEU PRO ASP SER LYS GLU VAL LEU GLU LYS VAL LEU LEU
SEQRES  14 D  604  ARG ARG GLU PHE ILE PRO ASP PRO GLN GLY SER ASN MET
SEQRES  15 D  604  MET PHE ALA PHE PHE ALA GLN HIS PHE THR HIS GLN PHE
SEQRES  16 D  604  PHE LYS THR ASP HIS LYS ARG GLY PRO GLY PHE THR ARG
SEQRES  17 D  604  GLY LEU GLY HIS GLY VAL ASP LEU ASN HIS ILE TYR GLY
SEQRES  18 D  604  GLU THR LEU ASP ARG GLN HIS LYS LEU ARG LEU PHE LYS
SEQRES  19 D  604  ASP GLY LYS LEU LYS TYR GLN VAL ILE GLY GLY GLU VAL
SEQRES  20 D  604  TYR PRO PRO THR VAL LYS ASP THR GLN VAL GLU MET ILE
SEQRES  21 D  604  TYR PRO PRO HIS ILE PRO GLU ASN LEU GLN PHE ALA VAL
SEQRES  22 D  604  GLY GLN GLU VAL PHE GLY LEU VAL PRO GLY LEU MET MET
SEQRES  23 D  604  TYR ALA THR ILE TRP LEU ARG GLU HIS ASN ARG VAL CYS
SEQRES  24 D  604  ASP ILE LEU LYS GLN GLU HIS PRO GLU TRP GLY ASP GLU
SEQRES  25 D  604  GLN LEU PHE GLN THR SER ARG LEU ILE LEU ILE GLY GLU
SEQRES  26 D  604  THR ILE LYS ILE VAL ILE GLU ASP TYR VAL GLN HIS LEU
SEQRES  27 D  604  SER GLY TYR HIS PHE LYS LEU LYS PHE ASP PRO GLU LEU
SEQRES  28 D  604  LEU PHE ASN GLN GLN PHE GLN TYR GLN ASN ARG ILE ALA
SEQRES  29 D  604  SER GLU PHE ASN THR LEU TYR HIS TRP HIS PRO LEU LEU
SEQRES  30 D  604  PRO ASP THR PHE ASN ILE GLU ASP GLN GLU TYR SER PHE
SEQRES  31 D  604  LYS GLN PHE LEU TYR ASN ASN SER ILE LEU LEU GLU HIS
SEQRES  32 D  604  GLY LEU THR GLN PHE VAL GLU SER PHE THR ARG GLN ILE
SEQRES  33 D  604  ALA GLY ARG VAL ALA GLY GLY ARG ASN VAL PRO ILE ALA
SEQRES  34 D  604  VAL GLN ALA VAL ALA LYS ALA SER ILE ASP GLN SER ARG
SEQRES  35 D  604  GLU MET LYS TYR GLN SER LEU ASN GLU TYR ARG LYS ARG
SEQRES  36 D  604  PHE SER LEU LYS PRO TYR THR SER PHE GLU GLU LEU THR
SEQRES  37 D  604  GLY GLU LYS GLU MET ALA ALA GLU LEU LYS ALA LEU TYR
SEQRES  38 D  604  SER ASP ILE ASP VAL MET GLU LEU TYR PRO ALA LEU LEU
SEQRES  39 D  604  VAL GLU LYS PRO ARG PRO ASP ALA ILE PHE GLY GLU THR
SEQRES  40 D  604  MET VAL GLU LEU GLY ALA PRO PHE SER LEU LYS GLY LEU
SEQRES  41 D  604  MET GLY ASN PRO ILE CYS SER PRO GLN TYR TRP LYS PRO
SEQRES  42 D  604  SER THR PHE GLY GLY GLU VAL GLY PHE LYS ILE ILE ASN
SEQRES  43 D  604  THR ALA SER ILE GLN SER LEU ILE CYS ASN ASN VAL LYS
SEQRES  44 D  604  GLY CYS PRO PHE THR SER PHE ASN VAL GLN ASP PRO GLN
SEQRES  45 D  604  PRO THR LYS THR ALA THR ILE ASN ALA SER ALA SER HIS
SEQRES  46 D  604  SER ARG LEU ASP ASP ILE ASN PRO THR VAL LEU ILE LYS
SEQRES  47 D  604  ARG ARG SER THR GLU LEU
MODRES 1PXX ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN B 1068  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN B 1144  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN B 1410  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN C 2068  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN C 2144  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN C 2410  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN D 3068  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN D 3144  ASN  GLYCOSYLATION SITE
MODRES 1PXX ASN D 3410  ASN  GLYCOSYLATION SITE
HET    NAG  A 661      14
HET    NAG  A 671      14
HET    NAG  A 672      14
HET    NAG  A 673      14
HET    NAG  A 681      14
HET    NAG  B1661      14
HET    NAG  B1671      14
HET    NAG  B1672      14
HET    NAG  B1673      14
HET    NAG  B1681      14
HET    NAG  C2661      14
HET    NAG  C2671      14
HET    NAG  C2672      14
HET    NAG  C2673      14
HET    NAG  C2681      14
HET    NAG  D3661      14
HET    NAG  D3671      14
HET    NAG  D3672      14
HET    NAG  D3673      14
HET    NAG  D3681      14
HET    BOG  A 703      20
HET    BOG  D3703      19
HET    HEM  A 704      43
HET    HEM  B1601      43
HET    HEM  C2601      43
HET    HEM  D3601      43
HET    DIF  A 701      19
HET    DIF  B1701      19
HET    DIF  C2701      19
HET    DIF  D3701      19
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     BOG B-OCTYLGLUCOSIDE
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     DIF 2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID
HETSYN     HEM HEME
HETSYN     DIF DICLOFENAC
FORMUL   5  NAG    20(C8 H15 N O6)
FORMUL  17  BOG    2(C14 H28 O6)
FORMUL  19  HEM    4(C34 H32 FE N4 O4)
FORMUL  23  DIF    4(C14 H11 CL2 N O2)
FORMUL  27  HOH   *317(H2 O)
HELIX    1   1 GLU A   73  LEU A   82  1                                  10
HELIX    2   2 THR A   85  THR A   94  1                                  10
HELIX    3   3 GLY A   98  ASN A  104  1                                   7
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  ARG A  245  1                                   9
HELIX   10  10 THR A  265  GLN A  270  1                                   6
HELIX   11  11 VAL A  295  HIS A  320  1                                  26
HELIX   12  12 GLY A  324  ASP A  347  1                                  24
HELIX   13  13 ASP A  347  GLY A  354  1                                   8
HELIX   14  14 ASP A  362  PHE A  367  5                                   6
HELIX   15  15 ALA A  378  TYR A  385  1                                   8
HELIX   16  16 HIS A  386  HIS A  386  5                                   1
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  GLN A  429  1                                  20
HELIX   20  20 PRO A  441  ALA A  443  5                                   3
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 ASP A  497  MET A  501  5                                   5
HELIX   26  26 GLU A  502  GLU A  510  1                                   9
HELIX   27  27 GLY A  519  GLY A  536  1                                  18
HELIX   28  28 ASN A  537  SER A  541  5                                   5
HELIX   29  29 LYS A  546  GLY A  551  5                                   6
HELIX   30  30 GLY A  552  THR A  561  1                                  10
HELIX   31  31 SER A  563  VAL A  572  1                                  10
HELIX   32  32 GLU B 1073  LEU B 1082  1                                  10
HELIX   33  33 THR B 1085  HIS B 1095  1                                  11
HELIX   34  34 PHE B 1096  ASN B 1104  1                                   9
HELIX   35  35 ILE B 1105B TYR B 1122  1                                  18
HELIX   36  36 SER B 1138  ASN B 1144  1                                   7
HELIX   37  37 ASP B 1173  LEU B 1182  1                                  10
HELIX   38  38 ASN B 1195  HIS B 1207  1                                  13
HELIX   39  39 LEU B 1230  GLY B 1235  1                                   6
HELIX   40  40 THR B 1237  ARG B 1245  1                                   9
HELIX   41  41 THR B 1265  GLN B 1270  1                                   6
HELIX   42  42 PRO B 1280  GLN B 1284  5                                   5
HELIX   43  43 VAL B 1295  HIS B 1320  1                                  26
HELIX   44  44 GLY B 1324  ASP B 1347  1                                  24
HELIX   45  45 ASP B 1347  GLY B 1354  1                                   8
HELIX   46  46 ASP B 1362  PHE B 1367  5                                   6
HELIX   47  47 ALA B 1378  TYR B 1385  1                                   8
HELIX   48  48 HIS B 1386  HIS B 1386  5                                   1
HELIX   49  49 TRP B 1387  LEU B 1391  5                                   5
HELIX   50  50 SER B 1403  LEU B 1408  1                                   6
HELIX   51  51 ASN B 1410  GLN B 1429  1                                  20
HELIX   52  52 PRO B 1441  ALA B 1443  5                                   3
HELIX   53  53 VAL B 1444  MET B 1458  1                                  15
HELIX   54  54 SER B 1462  PHE B 1470  1                                   9
HELIX   55  55 SER B 1477  GLY B 1483  1                                   7
HELIX   56  56 LYS B 1485  SER B 1496  1                                  12
HELIX   57  57 ASP B 1497  MET B 1501  5                                   5
HELIX   58  58 GLU B 1502  GLU B 1510  1                                   9
HELIX   59  59 GLY B 1519  GLY B 1536  1                                  18
HELIX   60  60 ASN B 1537  SER B 1541  5                                   5
HELIX   61  61 LYS B 1546  GLY B 1551  5                                   6
HELIX   62  62 GLY B 1552  THR B 1561  1                                  10
HELIX   63  63 SER B 1563  VAL B 1572  1                                  10
HELIX   64  64 GLU C 2073  LEU C 2082  1                                  10
HELIX   65  65 THR C 2085  HIS C 2095  1                                  11
HELIX   66  66 PHE C 2096  ASN C 2104  1                                   9
HELIX   67  67 ILE C 2105C TYR C 2122  1                                  18
HELIX   68  68 SER C 2138  ASN C 2144  1                                   7
HELIX   69  69 ASP C 2173  LEU C 2182  1                                  10
HELIX   70  70 ASN C 2195  HIS C 2207  1                                  13
HELIX   71  71 LEU C 2230  GLY C 2235  1                                   6
HELIX   72  72 THR C 2237  ARG C 2245  1                                   9
HELIX   73  73 THR C 2265  GLN C 2270  1                                   6
HELIX   74  74 PRO C 2280  GLN C 2284  5                                   5
HELIX   75  75 VAL C 2295  HIS C 2320  1                                  26
HELIX   76  76 GLY C 2324  ASP C 2347  1                                  24
HELIX   77  77 ASP C 2347  GLY C 2354  1                                   8
HELIX   78  78 ASP C 2362  PHE C 2367  5                                   6
HELIX   79  79 ALA C 2378  TYR C 2385  1                                   8
HELIX   80  80 HIS C 2386  HIS C 2386  5                                   1
HELIX   81  81 TRP C 2387  LEU C 2391  5                                   5
HELIX   82  82 SER C 2403  LEU C 2408  1                                   6
HELIX   83  83 ASN C 2411  GLN C 2429  1                                  19
HELIX   84  84 PRO C 2441  ALA C 2443  5                                   3
HELIX   85  85 VAL C 2444  MET C 2458  1                                  15
HELIX   86  86 SER C 2462  PHE C 2470  1                                   9
HELIX   87  87 SER C 2477  GLY C 2483  1                                   7
HELIX   88  88 LYS C 2485  SER C 2496  1                                  12
HELIX   89  89 ASP C 2497  MET C 2501  5                                   5
HELIX   90  90 GLU C 2502  GLU C 2510  1                                   9
HELIX   91  91 GLY C 2519  GLY C 2536  1                                  18
HELIX   92  92 ASN C 2537  SER C 2541  5                                   5
HELIX   93  93 LYS C 2546  GLY C 2551  5                                   6
HELIX   94  94 GLY C 2552  THR C 2561  1                                  10
HELIX   95  95 SER C 2563  VAL C 2572  1                                  10
HELIX   96  96 GLU D 3073  LEU D 3082  1                                  10
HELIX   97  97 THR D 3085  THR D 3094  1                                  10
HELIX   98  98 PHE D 3096  ASN D 3104  1                                   9
HELIX   99  99 ILE D 3105D TYR D 3122  1                                  18
HELIX  100 100 SER D 3138  ASN D 3144  1                                   7
HELIX  101 101 ASP D 3173  LEU D 3182  1                                  10
HELIX  102 102 ASN D 3195  HIS D 3207  1                                  13
HELIX  103 103 LEU D 3230  GLY D 3235  1                                   6
HELIX  104 104 THR D 3237  ARG D 3245  1                                   9
HELIX  105 105 THR D 3265  GLN D 3270  1                                   6
HELIX  106 106 VAL D 3295  HIS D 3320  1                                  26
HELIX  107 107 GLY D 3324  ASP D 3347  1                                  24
HELIX  108 108 ASP D 3347  GLY D 3354  1                                   8
HELIX  109 109 ASP D 3362  PHE D 3367  5                                   6
HELIX  110 110 ALA D 3378  TYR D 3385  1                                   8
HELIX  111 111 HIS D 3386  HIS D 3386  5                                   1
HELIX  112 112 TRP D 3387  LEU D 3391  5                                   5
HELIX  113 113 SER D 3403  LEU D 3408  1                                   6
HELIX  114 114 ASN D 3410  GLN D 3429  1                                  20
HELIX  115 115 PRO D 3441  ALA D 3443  5                                   3
HELIX  116 116 VAL D 3444  MET D 3458  1                                  15
HELIX  117 117 SER D 3462  PHE D 3470  1                                   9
HELIX  118 118 SER D 3477  GLY D 3483  1                                   7
HELIX  119 119 LYS D 3485  SER D 3496  1                                  12
HELIX  120 120 ASP D 3497  MET D 3501  5                                   5
HELIX  121 121 GLU D 3502  GLU D 3510  1                                   9
HELIX  122 122 GLY D 3519  GLY D 3536  1                                  18
HELIX  123 123 ASN D 3537  SER D 3541  5                                   5
HELIX  124 124 LYS D 3546  GLY D 3551  5                                   6
HELIX  125 125 GLY D 3552  THR D 3561  1                                  10
HELIX  126 126 SER D 3563  VAL D 3572  1                                  10
SHEET    1   A 2 GLU A  46  SER A  49  0
SHEET    2   A 2 TYR A  55  ASP A  58 -1  O  ASP A  58   N  GLU A  46
SHEET    1   B 2 PHE A  64  TYR A  65  0
SHEET    2   B 2 THR A  71  PRO A  72 -1  O  THR A  71   N  TYR A  65
SHEET    1   C 2 TYR A 130  ASN A 131  0
SHEET    2   C 2 THR A 149  ARG A 150 -1  O  ARG A 150   N  TYR A 130
SHEET    1   D 2 GLN A 255  ILE A 257  0
SHEET    2   D 2 GLU A 260  TYR A 262 -1  O  TYR A 262   N  GLN A 255
SHEET    1   E 2 GLU B1046  SER B1049  0
SHEET    2   E 2 TYR B1055  ASP B1058 -1  O  ASP B1058   N  GLU B1046
SHEET    1   F 2 PHE B1064  TYR B1065  0
SHEET    2   F 2 THR B1071  PRO B1072 -1  O  THR B1071   N  TYR B1065
SHEET    1   G 2 TYR B1130  ASN B1131  0
SHEET    2   G 2 THR B1149  ARG B1150 -1  O  ARG B1150   N  TYR B1130
SHEET    1   H 2 GLN B1255  ILE B1257  0
SHEET    2   H 2 GLU B1260  TYR B1262 -1  O  TYR B1262   N  GLN B1255
SHEET    1   I 2 GLU C2046  MET C2048  0
SHEET    2   I 2 LYS C2056  ASP C2058 -1  O  ASP C2058   N  GLU C2046
SHEET    1   J 2 PHE C2064  TYR C2065  0
SHEET    2   J 2 THR C2071  PRO C2072 -1  O  THR C2071   N  TYR C2065
SHEET    1   K 2 TYR C2130  ASN C2131  0
SHEET    2   K 2 THR C2149  ARG C2150 -1  O  ARG C2150   N  TYR C2130
SHEET    1   L 2 GLN C2255  ILE C2257  0
SHEET    2   L 2 GLU C2260  TYR C2262 -1  O  TYR C2262   N  GLN C2255
SHEET    1   M 2 GLU D3046  MET D3048  0
SHEET    2   M 2 LYS D3056  ASP D3058 -1  O  ASP D3058   N  GLU D3046
SHEET    1   N 2 PHE D3064  TYR D3065  0
SHEET    2   N 2 THR D3071  PRO D3072 -1  O  THR D3071   N  TYR D3065
SHEET    1   O 2 TYR D3130  ASN D3131  0
SHEET    2   O 2 THR D3149  ARG D3150 -1  O  ARG D3150   N  TYR D3130
SHEET    1   P 2 GLN D3255  ILE D3257  0
SHEET    2   P 2 GLU D3260  TYR D3262 -1  O  TYR D3262   N  GLN D3255
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  2.03
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.06
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.04
SSBOND   6 CYS B 1036    CYS B 1047                          1555   1555  2.04
SSBOND   7 CYS B 1037    CYS B 1159                          1555   1555  2.04
SSBOND   8 CYS B 1041    CYS B 1057                          1555   1555  2.04
SSBOND   9 CYS B 1059    CYS B 1069                          1555   1555  2.04
SSBOND  10 CYS B 1569    CYS B 1575                          1555   1555  2.05
SSBOND  11 CYS C 2036    CYS C 2047                          1555   1555  2.04
SSBOND  12 CYS C 2037    CYS C 2159                          1555   1555  2.04
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  2.04
SSBOND  16 CYS D 3036    CYS D 3047                          1555   1555  2.04
SSBOND  17 CYS D 3037    CYS D 3159                          1555   1555  2.04
SSBOND  18 CYS D 3041    CYS D 3057                          1555   1555  2.03
SSBOND  19 CYS D 3059    CYS D 3069                          1555   1555  2.05
SSBOND  20 CYS D 3569    CYS D 3575                          1555   1555  2.04
LINK         ND2 ASN A  68                 C1  NAG A 661     1555   1555  1.45
LINK         ND2 ASN A 144                 C1  NAG A 671     1555   1555  1.44
LINK         NE2 HIS A 388                FE   HEM A 704     1555   1555  2.22
LINK         ND2 ASN A 410                 C1  NAG A 681     1555   1555  1.45
LINK         ND2 ASN B1068                 C1  NAG B1661     1555   1555  1.45
LINK         ND2 ASN B1144                 C1  NAG B1671     1555   1555  1.45
LINK         NE2 HIS B1388                FE   HEM B1601     1555   1555  2.22
LINK         ND2 ASN B1410                 C1  NAG B1681     1555   1555  1.46
LINK         ND2 ASN C2068                 C1  NAG C2661     1555   1555  1.45
LINK         ND2 ASN C2144                 C1  NAG C2671     1555   1555  1.45
LINK         NE2 HIS C2388                FE   HEM C2601     1555   1555  2.21
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         NE2 HIS D3388                FE   HEM D3601     1555   1555  2.20
LINK         ND2 ASN D3410                 C1  NAG D3681     1555   1555  1.45
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.39
LINK         O4  NAG A 672                 C1  NAG A 673     1555   1555  1.41
LINK         O4  NAG B1671                 C1  NAG B1672     1555   1555  1.39
LINK         O4  NAG B1672                 C1  NAG B1673     1555   1555  1.41
LINK         O4  NAG C2671                 C1  NAG C2672     1555   1555  1.39
LINK         O4  NAG C2672                 C1  NAG C2673     1555   1555  1.41
LINK         O4  NAG D3671                 C1  NAG D3672     1555   1555  1.39
LINK         O4  NAG D3672                 C1  NAG D3673     1555   1555  1.41
CISPEP   1 SER A  126    PRO A  127          0         0.35
CISPEP   2 SER B 1126    PRO B 1127          0         0.10
CISPEP   3 SER C 2126    PRO C 2127          0         0.19
CISPEP   4 SER D 3126    PRO D 3127          0         0.21
SITE     1 AC1  5 SER A  38  PRO A  40  TYR A  55  GLU A  67
SITE     2 AC1  5 ASN A  68
SITE     1 AC2  6 GLU A 140  ASN A 144  TYR A 147  ARG A 216
SITE     2 AC2  6 NAG A 672  HOH A5048
SITE     1 AC3  4 ARG A 216  NAG A 671  NAG A 673  ASP B1239
SITE     1 AC4  1 NAG A 672
SITE     1 AC5  3 GLN A 406  ASN A 410  ILE A 413
SITE     1 AC6  6 SER B1038  PRO B1040  TYR B1055  GLU B1067
SITE     2 AC6  6 ASN B1068  HOH B5128
SITE     1 AC7  5 ASN B1144  TYR B1147  ARG B1216  PHE B1220
SITE     2 AC7  5 NAG B1672
SITE     1 AC8  5 ARG B1216  NAG B1671  NAG B1673  HOH B5102
SITE     2 AC8  5 HOH B5168
SITE     1 AC9  2 NAG B1672  HOH B5279
SITE     1 BC1  3 GLN B1406  ASN B1410  ILE B1413
SITE     1 BC2  6 SER C2038  PRO C2040  TYR C2055  GLU C2067
SITE     2 BC2  6 ASN C2068  HOH C5190
SITE     1 BC3  7 GLU C2140  ASN C2144  TYR C2147  ARG C2216
SITE     2 BC3  7 PHE C2220  NAG C2672  HOH C5155
SITE     1 BC4  4 ARG C2216  NAG C2671  NAG C2673  ASP D3239
SITE     1 BC5  1 NAG C2672
SITE     1 BC6  3 GLN C2406  ASN C2410  ILE C2413
SITE     1 BC7  5 SER D3038  PRO D3040  TYR D3055  GLU D3067
SITE     2 BC7  5 ASN D3068
SITE     1 BC8  7 GLU D3140  ASN D3144  TYR D3147  ARG D3216
SITE     2 BC8  7 PHE D3220  NAG D3672  HOH D5108
SITE     1 BC9  4 ASP C2239  ARG D3216  NAG D3671  NAG D3673
SITE     1 CC1  1 NAG D3672
SITE     1 CC2  3 GLN D3406  ASN D3410  ILE D3413
SITE     1 CC3 12 GLU A 179  LEU A 183  ARG A 185  ILE A 442
SITE     2 CC3 12 GLN A 445  LEU B1183  ARG B1184  ARG B1185
SITE     3 CC3 12 ARG B1438  ILE B1442  GLU B1486  GLU B1490
SITE     1 CC4 12 LEU C2183  ARG C2184  ARG C2185  ARG C2438
SITE     2 CC4 12 ILE C2442  GLU C2486  GLU C2490  GLU D3179
SITE     3 CC4 12 LEU D3183  ARG D3185  ILE D3442  GLN D3445
SITE     1 CC5 16 ALA A 199  PHE A 200  GLN A 203  HIS A 207
SITE     2 CC5 16 PHE A 210  LYS A 211  THR A 212  VAL A 295
SITE     3 CC5 16 ASN A 382  TYR A 385  HIS A 386  TRP A 387
SITE     4 CC5 16 HIS A 388  LEU A 391  VAL A 447  GLN A 454
SITE     1 CC6 17 TYR B1148  ALA B1199  PHE B1200  ALA B1202
SITE     2 CC6 17 GLN B1203  HIS B1207  PHE B1210  THR B1212
SITE     3 CC6 17 VAL B1295  ASN B1382  TYR B1385  HIS B1386
SITE     4 CC6 17 TRP B1387  HIS B1388  LEU B1391  VAL B1447
SITE     5 CC6 17 GLN B1454
SITE     1 CC7 17 ALA C2199  PHE C2200  ALA C2202  GLN C2203
SITE     2 CC7 17 THR C2206  HIS C2207  PHE C2210  LYS C2211
SITE     3 CC7 17 THR C2212  VAL C2295  ASN C2382  TYR C2385
SITE     4 CC7 17 HIS C2386  HIS C2388  LEU C2391  VAL C2447
SITE     5 CC7 17 GLN C2454
SITE     1 CC8 17 TYR D3148  ALA D3199  PHE D3200  GLN D3203
SITE     2 CC8 17 HIS D3207  PHE D3210  THR D3212  VAL D3295
SITE     3 CC8 17 ASN D3382  TYR D3385  HIS D3386  TRP D3387
SITE     4 CC8 17 HIS D3388  LEU D3391  VAL D3447  GLN D3454
SITE     5 CC8 17 HOH D5235
SITE     1 CC9 10 TYR A 348  VAL A 349  LEU A 352  TYR A 385
SITE     2 CC9 10 TRP A 387  MET A 522  GLY A 526  ALA A 527
SITE     3 CC9 10 SER A 530  HOH A5210
SITE     1 DC1  9 TYR B1348  VAL B1349  LEU B1352  TYR B1385
SITE     2 DC1  9 TRP B1387  MET B1522  GLY B1526  ALA B1527
SITE     3 DC1  9 SER B1530
SITE     1 DC2  9 TYR C2348  VAL C2349  LEU C2352  TYR C2385
SITE     2 DC2  9 TRP C2387  MET C2522  GLY C2526  ALA C2527
SITE     3 DC2  9 SER C2530
SITE     1 DC3 10 TYR D3348  VAL D3349  LEU D3352  TYR D3385
SITE     2 DC3 10 TRP D3387  MET D3522  VAL D3523  GLY D3526
SITE     3 DC3 10 ALA D3527  SER D3530
CRYST1  181.145  135.090  124.165  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      0.005520  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007402  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008054        0.00000
      
PROCHECK
Go to PROCHECK summary
 References