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PDBsum entry 4cox

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
4cox
Jmol
Contents
Protein chains
552 a.a. *
Ligands
NAG ×12
HEM ×4
IMN ×4
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          18-DEC-96   4COX
TITLE     CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A NON-
TITLE    2 SELECTIVE INHIBITOR, INDOMETHACIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYCLOOXYGENASE-2;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: PROSTAGLANDIN SYNTHASE-2;
COMPND   5 EC: 1.14.99.1;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE   4 ORGANISM_TAXID: 10090;
SOURCE   5 CELL_LINE: CULTURED SF21;
SOURCE   6 TISSUE: DERMAL;
SOURCE   7 CELL: FIBROBLAST;
SOURCE   8 CELLULAR_LOCATION: ENDOPLASMIC RETICULUM;
SOURCE   9 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  10 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  12 EXPRESSION_SYSTEM_CELL_LINE: CULTURED SF21;
SOURCE  13 EXPRESSION_SYSTEM_TISSUE: OVARIAN TISSUE;
SOURCE  14 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  15 EXPRESSION_SYSTEM_VECTOR: PVL1393
KEYWDS    PEROXIDASE, DIOXYGENASE, CYCLOOXYGENASE, NONSTEROIDAL
KEYWDS   2 ANTIINFLAMMATORY DRUGS, INFLAMMATION, ARTHRITIS, PROSTAGLANDIN,
KEYWDS   3 PROSTAGLANDIN SYNTHASE, OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.KURUMBAIL,W.STALLINGS
REVDAT   4   13-JUL-11 4COX    1       VERSN
REVDAT   3   24-FEB-09 4COX    1       VERSN
REVDAT   2   01-APR-03 4COX    1       JRNL
REVDAT   1   24-DEC-97 4COX    0
JRNL        AUTH   R.G.KURUMBAIL,A.M.STEVENS,J.K.GIERSE,J.J.MCDONALD,
JRNL        AUTH 2 R.A.STEGEMAN,J.Y.PAK,D.GILDEHAUS,J.M.MIYASHIRO,T.D.PENNING,
JRNL        AUTH 3 K.SEIBERT,P.C.ISAKSON,W.C.STALLINGS
JRNL        TITL   STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF
JRNL        TITL 2 CYCLOOXYGENASE-2 BY ANTI-INFLAMMATORY AGENTS.
JRNL        REF    NATURE                        V. 384   644 1996
JRNL        REFN                   ISSN 0028-0836
JRNL        PMID   8967954
JRNL        DOI    10.1038/384644A0
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   R.G.KURUMBAIL,A.M.STEVENS,J.K.GIERSE,J.J.MCDONALD,
REMARK   1  AUTH 2 R.A.STEGEMAN,J.Y.PAK,D.GILDEHAUS,J.M.MIYASHIRO,T.D.PENNING,
REMARK   1  AUTH 3 K.SEIBERT,P.C.ISAKSON,W.C.STALLINGS
REMARK   1  TITL   ERRATUM. STRUCTURAL BASIS FOR SELECTIVE INHIBITION OF
REMARK   1  TITL 2 CYCLOOXYGENASE-2 BY ANTI-INFLAMMATORY AGENTS
REMARK   1  REF    NATURE                        V. 385   555 1997
REMARK   1  REFN                   ISSN 0028-0836
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 68.0
REMARK   3   NUMBER OF REFLECTIONS             : 41254
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.219
REMARK   3   FREE R VALUE                     : 0.309
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.870
REMARK   3   FREE R VALUE TEST SET COUNT      : 4166
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 47.20
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3185
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2640
REMARK   3   BIN FREE R VALUE                    : 0.3820
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 362
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 17892
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 440
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.00
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.014
REMARK   3   BOND ANGLES            (DEGREES) : 1.80
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.69
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.500 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.000 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.000 ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.500 ; NULL
REMARK   3
REMARK   3  NCS MODEL : RESTRAINED
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : 300   ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : 1.0   ; NULL
REMARK   3   GROUP  2  POSITIONAL            (A) : 300   ; NULL
REMARK   3   GROUP  2  B-FACTOR           (A**2) : 1.0   ; NULL
REMARK   3   GROUP  3  POSITIONAL            (A) : 300   ; NULL
REMARK   3   GROUP  3  B-FACTOR           (A**2) : 1.0   ; NULL
REMARK   3   GROUP  4  POSITIONAL            (A) : 300   ; NULL
REMARK   3   GROUP  4  B-FACTOR           (A**2) : 1.0   ; NULL
REMARK   3   GROUP  5  POSITIONAL            (A) : 300   ; NULL
REMARK   3   GROUP  5  B-FACTOR           (A**2) : 1.0   ; NULL
REMARK   3   GROUP  6  POSITIONAL            (A) : 200   ; NULL
REMARK   3   GROUP  6  B-FACTOR           (A**2) : 2.0   ; NULL
REMARK   3   GROUP  7  POSITIONAL            (A) : 50    ; NULL
REMARK   3   GROUP  7  B-FACTOR           (A**2) : 5.0   ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARAM_ENGH.PRO
REMARK   3  PARAMETER FILE  2  : PARAM19X_MOD.HEME
REMARK   3  PARAMETER FILE  3  : PARAM3_MOD.CHO
REMARK   3  PARAMETER FILE  4  : PARAM.INDOMETHACIN
REMARK   3  PARAMETER FILE  5  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOP_ENGH.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH19X_MOD.HEME
REMARK   3  TOPOLOGY FILE  3   : TOPH3.CHO
REMARK   3  TOPOLOGY FILE  4   : TOP.INDOMETHACIN
REMARK   3  TOPOLOGY FILE  5   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 4COX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : AUG-95
REMARK 200  TEMPERATURE           (KELVIN) : 113
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : SUPPER MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50058
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.9
REMARK 200  DATA REDUNDANCY                : 3.300
REMARK 200  R MERGE                    (I) : 0.13500
REMARK 200  R SYM                      (I) : 0.13500
REMARK 200   FOR THE DATA SET  : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800
REMARK 200  R SYM FOR SHELL            (I) : 0.48800
REMARK 200   FOR SHELL         : 1.770
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MERLOT
REMARK 200 STARTING MODEL: PROSTAGLANDIN SYNTHASE-1, PDB ENTRY 1PRH
REMARK 200
REMARK 200 REMARK: PGHS-1 DIMER WAS USED AS THE SEARCH MODEL.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM SODIUM PHOSPHATE, 100 MM NACL,
REMARK 280  0.6% BETA- OCTYLGLUCOSIDE, 10 MG/ML PROTEIN, 1MM INHIBITOR MIXED
REMARK 280  WITH A RESERVOIR SOLUTION CONTAINING 20-34% MONOMETHYL PEG 550,
REMARK 280  10-240 MGCL2, 50 MM EPPS PH 8.0 IN THE RATIO OF 1:1
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X+1/2,Y+1/2,-Z
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       89.90000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.80000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       89.90000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.80000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ASP A   584
REMARK 465     PRO A   585
REMARK 465     GLN A   586
REMARK 465     PRO A   587
REMARK 465     THR A   588
REMARK 465     LYS A   589
REMARK 465     THR A   590
REMARK 465     ALA A   591
REMARK 465     THR A   592
REMARK 465     ILE A   593
REMARK 465     ASN A   594
REMARK 465     ALA A   595
REMARK 465     SER A   596
REMARK 465     ALA A   597
REMARK 465     SER A   598
REMARK 465     HIS A   599
REMARK 465     SER A   600
REMARK 465     ARG A   601
REMARK 465     LEU A   602
REMARK 465     ASP A   603
REMARK 465     ASP A   604
REMARK 465     ILE A   605
REMARK 465     ASN A   606
REMARK 465     PRO A   607
REMARK 465     THR A   608
REMARK 465     VAL A   609
REMARK 465     LEU A   610
REMARK 465     ILE A   611
REMARK 465     LYS A   612
REMARK 465     ARG A   613
REMARK 465     ARG A   614
REMARK 465     SER A   615
REMARK 465     THR A   616
REMARK 465     GLU A   617
REMARK 465     LEU A   618
REMARK 465     ASP B   584
REMARK 465     PRO B   585
REMARK 465     GLN B   586
REMARK 465     PRO B   587
REMARK 465     THR B   588
REMARK 465     LYS B   589
REMARK 465     THR B   590
REMARK 465     ALA B   591
REMARK 465     THR B   592
REMARK 465     ILE B   593
REMARK 465     ASN B   594
REMARK 465     ALA B   595
REMARK 465     SER B   596
REMARK 465     ALA B   597
REMARK 465     SER B   598
REMARK 465     HIS B   599
REMARK 465     SER B   600
REMARK 465     ARG B   601
REMARK 465     LEU B   602
REMARK 465     ASP B   603
REMARK 465     ASP B   604
REMARK 465     ILE B   605
REMARK 465     ASN B   606
REMARK 465     PRO B   607
REMARK 465     THR B   608
REMARK 465     VAL B   609
REMARK 465     LEU B   610
REMARK 465     ILE B   611
REMARK 465     LYS B   612
REMARK 465     ARG B   613
REMARK 465     ARG B   614
REMARK 465     SER B   615
REMARK 465     THR B   616
REMARK 465     GLU B   617
REMARK 465     LEU B   618
REMARK 465     ASP C   584
REMARK 465     PRO C   585
REMARK 465     GLN C   586
REMARK 465     PRO C   587
REMARK 465     THR C   588
REMARK 465     LYS C   589
REMARK 465     THR C   590
REMARK 465     ALA C   591
REMARK 465     THR C   592
REMARK 465     ILE C   593
REMARK 465     ASN C   594
REMARK 465     ALA C   595
REMARK 465     SER C   596
REMARK 465     ALA C   597
REMARK 465     SER C   598
REMARK 465     HIS C   599
REMARK 465     SER C   600
REMARK 465     ARG C   601
REMARK 465     LEU C   602
REMARK 465     ASP C   603
REMARK 465     ASP C   604
REMARK 465     ILE C   605
REMARK 465     ASN C   606
REMARK 465     PRO C   607
REMARK 465     THR C   608
REMARK 465     VAL C   609
REMARK 465     LEU C   610
REMARK 465     ILE C   611
REMARK 465     LYS C   612
REMARK 465     ARG C   613
REMARK 465     ARG C   614
REMARK 465     SER C   615
REMARK 465     THR C   616
REMARK 465     GLU C   617
REMARK 465     LEU C   618
REMARK 465     ASP D   584
REMARK 465     PRO D   585
REMARK 465     GLN D   586
REMARK 465     PRO D   587
REMARK 465     THR D   588
REMARK 465     LYS D   589
REMARK 465     THR D   590
REMARK 465     ALA D   591
REMARK 465     THR D   592
REMARK 465     ILE D   593
REMARK 465     ASN D   594
REMARK 465     ALA D   595
REMARK 465     SER D   596
REMARK 465     ALA D   597
REMARK 465     SER D   598
REMARK 465     HIS D   599
REMARK 465     SER D   600
REMARK 465     ARG D   601
REMARK 465     LEU D   602
REMARK 465     ASP D   603
REMARK 465     ASP D   604
REMARK 465     ILE D   605
REMARK 465     ASN D   606
REMARK 465     PRO D   607
REMARK 465     THR D   608
REMARK 465     VAL D   609
REMARK 465     LEU D   610
REMARK 465     ILE D   611
REMARK 465     LYS D   612
REMARK 465     ARG D   613
REMARK 465     ARG D   614
REMARK 465     SER D   615
REMARK 465     THR D   616
REMARK 465     GLU D   617
REMARK 465     LEU D   618
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM A 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388   NE2
REMARK 620 2 HEM A 682   NA   89.1
REMARK 620 3 HEM A 682   NB   90.6  90.7
REMARK 620 4 HEM A 682   NC   82.9 172.0  89.2
REMARK 620 5 HEM A 682   ND   89.2  89.4 179.7  90.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM B 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388   NE2
REMARK 620 2 HEM B 682   NA   87.1
REMARK 620 3 HEM B 682   NB   95.3  89.3
REMARK 620 4 HEM B 682   NC   89.1 175.8  89.4
REMARK 620 5 HEM B 682   ND   85.7  90.4 178.9  91.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 388   NE2
REMARK 620 2 HEM C 682   NA   85.1
REMARK 620 3 HEM C 682   NB   93.6  90.5
REMARK 620 4 HEM C 682   NC   87.0 172.1  89.7
REMARK 620 5 HEM C 682   ND   84.7  89.7 178.3  89.8
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 682  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 388   NE2
REMARK 620 2 HEM D 682   NA   87.2
REMARK 620 3 HEM D 682   NB   92.0  90.1
REMARK 620 4 HEM D 682   NC   88.8 175.9  89.5
REMARK 620 5 HEM D 682   ND   89.9  90.2 178.1  90.4
REMARK 620 N                    1     2     3     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CAT
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: TYR 385 IS BELIEVED TO BE THE AMINO ACID THAT
REMARK 800  ABSTRACTS A HYDROGEN ATOM FROM THE SUBSTRATE. IT IS LOCATED CLOSE
REMARK 800  TO THE HEME. A TYROSINE RADICAL IS FORMED DURING THE COURSE OF
REMARK 800  THE REACTION.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ACE
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SER 530 IS ACETYLATED BY ASPIRIN (AN ACETYL
REMARK 800  GROUP IS COVALENTLY ATTACHED TO THE PROTEIN WHEN INHIBITED WITH
REMARK 800  ASPIRIN). THE ACETYLATED SER PREVENTS THE PROPER BINDING OF THE
REMARK 800  SUBSTRATE IN THE CYCLOOXYGENASE ACTIVE SITE. IT HAS BEEN RECENTLY
REMARK 800  SHOWN, HOWEVER, THAT ACETYLATION OF CYCLOOXYGENASE-2 RESULTS IN
REMARK 800  THE FORMATION OF A DIFFERENT PRODUCT (15-HETE).
REMARK 800
REMARK 800 SITE_IDENTIFIER: HEM
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HIS 388 IS THE AXIAL LIGAND TO THE HEME.
REMARK 800
REMARK 800 SITE_IDENTIFIER: SUB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ARGININE 120 IS BELIEVED TO ANCHOR THE
REMARK 800  CARBOXYLATE OF THE SUBSTRATE BY FORMING AN ION-PAIR.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 661
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 671
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 681
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMN D 701
DBREF  4COX A   33   618  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  4COX B   33   618  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  4COX C   33   618  UNP    Q05769   PGH2_MOUSE      18    604
DBREF  4COX D   33   618  UNP    Q05769   PGH2_MOUSE      18    604
SEQADV 4COX GLN A  310  UNP  Q05769    ASN   296 CONFLICT
SEQADV 4COX LYS A  333  UNP  Q05769    ARG   319 CONFLICT
SEQADV 4COX GLN B  310  UNP  Q05769    ASN   296 CONFLICT
SEQADV 4COX LYS B  333  UNP  Q05769    ARG   319 CONFLICT
SEQADV 4COX GLN C  310  UNP  Q05769    ASN   296 CONFLICT
SEQADV 4COX LYS C  333  UNP  Q05769    ARG   319 CONFLICT
SEQADV 4COX GLN D  310  UNP  Q05769    ASN   296 CONFLICT
SEQADV 4COX LYS D  333  UNP  Q05769    ARG   319 CONFLICT
SEQRES   1 A  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 A  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 A  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 A  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 A  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 A  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 A  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 A  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 A  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 A  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 A  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 A  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 A  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 A  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 A  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 A  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 A  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 A  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 A  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 A  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 A  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 A  587  TRP LEU ARG GLU HIS GLN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 A  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 A  587  THR SER LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 A  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 A  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 A  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 A  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 A  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 A  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 A  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 A  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 A  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 A  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 A  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 A  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 A  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 A  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 A  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 A  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 A  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 A  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 A  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 A  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 A  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 A  587  GLU LEU
SEQRES   1 B  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 B  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 B  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 B  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 B  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 B  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 B  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 B  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 B  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 B  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 B  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 B  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 B  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 B  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 B  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 B  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 B  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 B  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 B  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 B  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 B  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 B  587  TRP LEU ARG GLU HIS GLN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 B  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 B  587  THR SER LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 B  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 B  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 B  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 B  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 B  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 B  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 B  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 B  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 B  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 B  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 B  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 B  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 B  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 B  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 B  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 B  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 B  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 B  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 B  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 B  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 B  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 B  587  GLU LEU
SEQRES   1 C  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 C  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 C  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 C  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 C  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 C  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 C  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 C  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 C  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 C  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 C  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 C  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 C  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 C  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 C  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 C  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 C  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 C  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 C  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 C  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 C  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 C  587  TRP LEU ARG GLU HIS GLN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 C  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 C  587  THR SER LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 C  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 C  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 C  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 C  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 C  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 C  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 C  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 C  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 C  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 C  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 C  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 C  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 C  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 C  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 C  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 C  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 C  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 C  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 C  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 C  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 C  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 C  587  GLU LEU
SEQRES   1 D  587  ALA ASN PRO CYS CYS SER ASN PRO CYS GLN ASN ARG GLY
SEQRES   2 D  587  GLU CYS MET SER THR GLY PHE ASP GLN TYR LYS CYS ASP
SEQRES   3 D  587  CYS THR ARG THR GLY PHE TYR GLY GLU ASN CYS THR THR
SEQRES   4 D  587  PRO GLU PHE LEU THR ARG ILE LYS LEU LEU LEU LYS PRO
SEQRES   5 D  587  THR PRO ASN THR VAL HIS TYR ILE LEU THR HIS PHE LYS
SEQRES   6 D  587  GLY VAL TRP ASN ILE VAL ASN ASN ILE PRO PHE LEU ARG
SEQRES   7 D  587  SER LEU ILE MET LYS TYR VAL LEU THR SER ARG SER TYR
SEQRES   8 D  587  LEU ILE ASP SER PRO PRO THR TYR ASN VAL HIS TYR GLY
SEQRES   9 D  587  TYR LYS SER TRP GLU ALA PHE SER ASN LEU SER TYR TYR
SEQRES  10 D  587  THR ARG ALA LEU PRO PRO VAL ALA ASP ASP CYS PRO THR
SEQRES  11 D  587  PRO MET GLY VAL LYS GLY ASN LYS GLU LEU PRO ASP SER
SEQRES  12 D  587  LYS GLU VAL LEU GLU LYS VAL LEU LEU ARG ARG GLU PHE
SEQRES  13 D  587  ILE PRO ASP PRO GLN GLY SER ASN MET MET PHE ALA PHE
SEQRES  14 D  587  PHE ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR ASP
SEQRES  15 D  587  HIS LYS ARG GLY PRO GLY PHE THR ARG GLY LEU GLY HIS
SEQRES  16 D  587  GLY VAL ASP LEU ASN HIS ILE TYR GLY GLU THR LEU ASP
SEQRES  17 D  587  ARG GLN HIS LYS LEU ARG LEU PHE LYS ASP GLY LYS LEU
SEQRES  18 D  587  LYS TYR GLN VAL ILE GLY GLY GLU VAL TYR PRO PRO THR
SEQRES  19 D  587  VAL LYS ASP THR GLN VAL GLU MET ILE TYR PRO PRO HIS
SEQRES  20 D  587  ILE PRO GLU ASN LEU GLN PHE ALA VAL GLY GLN GLU VAL
SEQRES  21 D  587  PHE GLY LEU VAL PRO GLY LEU MET MET TYR ALA THR ILE
SEQRES  22 D  587  TRP LEU ARG GLU HIS GLN ARG VAL CYS ASP ILE LEU LYS
SEQRES  23 D  587  GLN GLU HIS PRO GLU TRP GLY ASP GLU GLN LEU PHE GLN
SEQRES  24 D  587  THR SER LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE
SEQRES  25 D  587  VAL ILE GLU ASP TYR VAL GLN HIS LEU SER GLY TYR HIS
SEQRES  26 D  587  PHE LYS LEU LYS PHE ASP PRO GLU LEU LEU PHE ASN GLN
SEQRES  27 D  587  GLN PHE GLN TYR GLN ASN ARG ILE ALA SER GLU PHE ASN
SEQRES  28 D  587  THR LEU TYR HIS TRP HIS PRO LEU LEU PRO ASP THR PHE
SEQRES  29 D  587  ASN ILE GLU ASP GLN GLU TYR SER PHE LYS GLN PHE LEU
SEQRES  30 D  587  TYR ASN ASN SER ILE LEU LEU GLU HIS GLY LEU THR GLN
SEQRES  31 D  587  PHE VAL GLU SER PHE THR ARG GLN ILE ALA GLY ARG VAL
SEQRES  32 D  587  ALA GLY GLY ARG ASN VAL PRO ILE ALA VAL GLN ALA VAL
SEQRES  33 D  587  ALA LYS ALA SER ILE ASP GLN SER ARG GLU MET LYS TYR
SEQRES  34 D  587  GLN SER LEU ASN GLU TYR ARG LYS ARG PHE SER LEU LYS
SEQRES  35 D  587  PRO TYR THR SER PHE GLU GLU LEU THR GLY GLU LYS GLU
SEQRES  36 D  587  MET ALA ALA GLU LEU LYS ALA LEU TYR SER ASP ILE ASP
SEQRES  37 D  587  VAL MET GLU LEU TYR PRO ALA LEU LEU VAL GLU LYS PRO
SEQRES  38 D  587  ARG PRO ASP ALA ILE PHE GLY GLU THR MET VAL GLU LEU
SEQRES  39 D  587  GLY ALA PRO PHE SER LEU LYS GLY LEU MET GLY ASN PRO
SEQRES  40 D  587  ILE CYS SER PRO GLN TYR TRP LYS PRO SER THR PHE GLY
SEQRES  41 D  587  GLY GLU VAL GLY PHE LYS ILE ILE ASN THR ALA SER ILE
SEQRES  42 D  587  GLN SER LEU ILE CYS ASN ASN VAL LYS GLY CYS PRO PHE
SEQRES  43 D  587  THR SER PHE ASN VAL GLN ASP PRO GLN PRO THR LYS THR
SEQRES  44 D  587  ALA THR ILE ASN ALA SER ALA SER HIS SER ARG LEU ASP
SEQRES  45 D  587  ASP ILE ASN PRO THR VAL LEU ILE LYS ARG ARG SER THR
SEQRES  46 D  587  GLU LEU
MODRES 4COX ASN A   68  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN A  144  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN A  410  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN B   68  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN B  144  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN B  410  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN C   68  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN C  144  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN C  410  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN D   68  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN D  144  ASN  GLYCOSYLATION SITE
MODRES 4COX ASN D  410  ASN  GLYCOSYLATION SITE
HET    NAG  A 661      14
HET    NAG  A 671      14
HET    NAG  A 681      14
HET    NAG  B 661      14
HET    NAG  B 671      14
HET    NAG  B 681      14
HET    NAG  C 661      14
HET    NAG  C 671      14
HET    NAG  C 681      14
HET    NAG  D 661      14
HET    NAG  D 671      14
HET    NAG  D 681      14
HET    HEM  A 682      43
HET    IMN  A 701      25
HET    HEM  B 682      43
HET    IMN  B 701      25
HET    HEM  C 682      43
HET    IMN  C 701      25
HET    HEM  D 682      43
HET    IMN  D 701      25
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     IMN INDOMETHACIN
HETSYN     HEM HEME
FORMUL   5  NAG    12(C8 H15 N O6)
FORMUL  17  HEM    4(C34 H32 FE N4 O4)
FORMUL  18  IMN    4(C19 H16 CL N O4)
HELIX    1   1 PHE A   74  LEU A   82  1                                   9
HELIX    2   2 PRO A   86  THR A   94  1                                   9
HELIX    3   3 LYS A   97  ASN A  105  1                                   9
HELIX    4   4 PRO A  106  LEU A  123  1                                  18
HELIX    5   5 TRP A  139  SER A  143  1                                   5
HELIX    6   6 SER A  174  VAL A  181  1                                   8
HELIX    7   7 MET A  196  GLN A  208  1                                  13
HELIX    8   8 ASN A  231  TYR A  234  1                                   4
HELIX    9   9 LEU A  238  LEU A  244  1                                   7
HELIX   10  10 VAL A  266  THR A  269  1                                   4
HELIX   11  11 PRO A  296  GLU A  319  1                                  24
HELIX   12  12 ASP A  325  GLU A  346  1                                  22
HELIX   13  13 TYR A  348  SER A  353  1                                   6
HELIX   14  14 PRO A  363  LEU A  366  5                                   4
HELIX   15  15 SER A  379  LEU A  384  1                                   6
HELIX   16  16 HIS A  388  LEU A  390  5                                   3
HELIX   17  17 PHE A  404  PHE A  407  1                                   4
HELIX   18  18 SER A  412  HIS A  417  1                                   6
HELIX   19  19 THR A  420  THR A  427  1                                   8
HELIX   20  20 ALA A  443  GLU A  457  5                                  15
HELIX   21  21 LEU A  463  PHE A  470  1                                   8
HELIX   22  22 PHE A  478  THR A  482  1                                   5
HELIX   23  23 GLU A  486  TYR A  495  1                                  10
HELIX   24  24 LEU A  503  LEU A  508  1                                   6
HELIX   25  25 GLU A  520  MET A  535  1                                  16
HELIX   26  26 PRO A  538  CYS A  540  5                                   3
HELIX   27  27 PRO A  547  PHE A  550  5                                   4
HELIX   28  28 GLU A  553  ASN A  560  1                                   8
HELIX   29  29 ILE A  564  CYS A  569  1                                   6
HELIX   30  30 PHE B   74  LEU B   82  1                                   9
HELIX   31  31 PRO B   86  THR B   94  1                                   9
HELIX   32  32 LYS B   97  ASN B  105  1                                   9
HELIX   33  33 PRO B  106  LEU B  123  1                                  18
HELIX   34  34 TRP B  139  SER B  143  1                                   5
HELIX   35  35 SER B  174  VAL B  181  1                                   8
HELIX   36  36 MET B  196  GLN B  208  1                                  13
HELIX   37  37 ASN B  231  TYR B  234  1                                   4
HELIX   38  38 LEU B  238  LEU B  244  1                                   7
HELIX   39  39 VAL B  266  THR B  269  1                                   4
HELIX   40  40 PRO B  296  GLU B  319  1                                  24
HELIX   41  41 ASP B  325  GLU B  346  1                                  22
HELIX   42  42 TYR B  348  SER B  353  1                                   6
HELIX   43  43 PRO B  363  LEU B  366  5                                   4
HELIX   44  44 SER B  379  LEU B  384  1                                   6
HELIX   45  45 HIS B  388  LEU B  390  5                                   3
HELIX   46  46 PHE B  404  PHE B  407  1                                   4
HELIX   47  47 SER B  412  HIS B  417  1                                   6
HELIX   48  48 THR B  420  THR B  427  1                                   8
HELIX   49  49 ALA B  443  GLU B  457  5                                  15
HELIX   50  50 LEU B  463  ARG B  469  1                                   7
HELIX   51  51 PHE B  478  THR B  482  1                                   5
HELIX   52  52 GLU B  486  TYR B  495  1                                  10
HELIX   53  53 LEU B  503  LEU B  508  1                                   6
HELIX   54  54 GLU B  520  MET B  535  1                                  16
HELIX   55  55 PRO B  538  CYS B  540  5                                   3
HELIX   56  56 PRO B  547  PHE B  550  5                                   4
HELIX   57  57 GLU B  553  ASN B  560  1                                   8
HELIX   58  58 ILE B  564  CYS B  569  1                                   6
HELIX   59  59 PHE C   74  LEU C   82  1                                   9
HELIX   60  60 PRO C   86  THR C   94  1                                   9
HELIX   61  61 LYS C   97  ASN C  105  1                                   9
HELIX   62  62 PRO C  106  LEU C  123  1                                  18
HELIX   63  63 TRP C  139  SER C  143  1                                   5
HELIX   64  64 SER C  174  VAL C  181  1                                   8
HELIX   65  65 MET C  196  GLN C  208  1                                  13
HELIX   66  66 ASN C  231  TYR C  234  1                                   4
HELIX   67  67 LEU C  238  LEU C  244  1                                   7
HELIX   68  68 VAL C  266  THR C  269  1                                   4
HELIX   69  69 PRO C  296  GLU C  319  1                                  24
HELIX   70  70 ASP C  325  GLU C  346  1                                  22
HELIX   71  71 TYR C  348  SER C  353  1                                   6
HELIX   72  72 PRO C  363  LEU C  366  5                                   4
HELIX   73  73 SER C  379  LEU C  384  1                                   6
HELIX   74  74 HIS C  388  LEU C  390  5                                   3
HELIX   75  75 PHE C  404  PHE C  407  1                                   4
HELIX   76  76 SER C  412  HIS C  417  1                                   6
HELIX   77  77 THR C  420  THR C  427  1                                   8
HELIX   78  78 ALA C  443  GLU C  457  5                                  15
HELIX   79  79 LEU C  463  ARG C  469  1                                   7
HELIX   80  80 PHE C  478  THR C  482  1                                   5
HELIX   81  81 GLU C  486  TYR C  495  1                                  10
HELIX   82  82 LEU C  503  LEU C  508  1                                   6
HELIX   83  83 GLU C  520  MET C  535  1                                  16
HELIX   84  84 PRO C  538  CYS C  540  5                                   3
HELIX   85  85 PRO C  547  PHE C  550  5                                   4
HELIX   86  86 GLU C  553  ASN C  560  1                                   8
HELIX   87  87 ILE C  564  CYS C  569  1                                   6
HELIX   88  88 PHE D   74  LEU D   82  1                                   9
HELIX   89  89 PRO D   86  THR D   94  1                                   9
HELIX   90  90 LYS D   97  ASN D  105  1                                   9
HELIX   91  91 PRO D  106  LEU D  123  1                                  18
HELIX   92  92 TRP D  139  SER D  143  1                                   5
HELIX   93  93 SER D  174  VAL D  181  1                                   8
HELIX   94  94 MET D  196  GLN D  208  1                                  13
HELIX   95  95 ASN D  231  TYR D  234  1                                   4
HELIX   96  96 LEU D  238  LEU D  244  1                                   7
HELIX   97  97 VAL D  266  THR D  269  1                                   4
HELIX   98  98 PRO D  296  GLU D  319  1                                  24
HELIX   99  99 ASP D  325  GLU D  346  1                                  22
HELIX  100 100 TYR D  348  SER D  353  1                                   6
HELIX  101 101 PRO D  363  LEU D  366  5                                   4
HELIX  102 102 SER D  379  LEU D  384  1                                   6
HELIX  103 103 HIS D  388  LEU D  390  5                                   3
HELIX  104 104 PHE D  404  PHE D  407  1                                   4
HELIX  105 105 SER D  412  HIS D  417  1                                   6
HELIX  106 106 THR D  420  THR D  427  1                                   8
HELIX  107 107 ALA D  443  GLU D  457  5                                  15
HELIX  108 108 LEU D  463  PHE D  470  1                                   8
HELIX  109 109 PHE D  478  THR D  482  1                                   5
HELIX  110 110 GLU D  486  TYR D  495  1                                  10
HELIX  111 111 LEU D  503  LEU D  508  1                                   6
HELIX  112 112 GLU D  520  MET D  535  1                                  16
HELIX  113 113 PRO D  538  CYS D  540  5                                   3
HELIX  114 114 PRO D  547  PHE D  550  5                                   4
HELIX  115 115 GLU D  553  ASN D  560  1                                   8
HELIX  116 116 ILE D  564  CYS D  569  1                                   6
SHEET    1   A 2 GLU A  46  MET A  48  0
SHEET    2   A 2 LYS A  56  ASP A  58 -1  N  ASP A  58   O  GLU A  46
SHEET    1   B 2 TYR A 254  ILE A 257  0
SHEET    2   B 2 GLU A 260  PRO A 263 -1  N  TYR A 262   O  GLN A 255
SHEET    1   C 2 THR A 394  ILE A 397  0
SHEET    2   C 2 GLN A 400  SER A 403 -1  N  TYR A 402   O  PHE A 395
SHEET    1   D 2 GLU B  46  MET B  48  0
SHEET    2   D 2 LYS B  56  ASP B  58 -1  N  ASP B  58   O  GLU B  46
SHEET    1   E 2 GLN B 255  ILE B 257  0
SHEET    2   E 2 GLU B 260  TYR B 262 -1  N  TYR B 262   O  GLN B 255
SHEET    1   F 2 PHE B 395  ILE B 397  0
SHEET    2   F 2 GLN B 400  TYR B 402 -1  N  TYR B 402   O  PHE B 395
SHEET    1   G 2 GLU C  46  MET C  48  0
SHEET    2   G 2 LYS C  56  ASP C  58 -1  N  ASP C  58   O  GLU C  46
SHEET    1   H 2 GLN C 255  ILE C 257  0
SHEET    2   H 2 GLU C 260  TYR C 262 -1  N  TYR C 262   O  GLN C 255
SHEET    1   I 2 THR C 394  ILE C 397  0
SHEET    2   I 2 GLN C 400  SER C 403 -1  N  TYR C 402   O  PHE C 395
SHEET    1   J 2 GLU D  46  MET D  48  0
SHEET    2   J 2 LYS D  56  ASP D  58 -1  N  ASP D  58   O  GLU D  46
SHEET    1   K 2 GLN D 255  ILE D 257  0
SHEET    2   K 2 GLU D 260  TYR D 262 -1  N  TYR D 262   O  GLN D 255
SHEET    1   L 2 THR D 394  ILE D 397  0
SHEET    2   L 2 GLN D 400  SER D 403 -1  N  TYR D 402   O  PHE D 395
SSBOND   1 CYS A   36    CYS A   47                          1555   1555  2.06
SSBOND   2 CYS A   37    CYS A  159                          1555   1555  2.04
SSBOND   3 CYS A   41    CYS A   57                          1555   1555  2.01
SSBOND   4 CYS A   59    CYS A   69                          1555   1555  2.03
SSBOND   5 CYS A  569    CYS A  575                          1555   1555  2.03
SSBOND   6 CYS B   36    CYS B   47                          1555   1555  2.04
SSBOND   7 CYS B   37    CYS B  159                          1555   1555  2.03
SSBOND   8 CYS B   41    CYS B   57                          1555   1555  2.05
SSBOND   9 CYS B   59    CYS B   69                          1555   1555  2.04
SSBOND  10 CYS B  569    CYS B  575                          1555   1555  2.03
SSBOND  11 CYS C   36    CYS C   47                          1555   1555  2.02
SSBOND  12 CYS C   37    CYS C  159                          1555   1555  2.01
SSBOND  13 CYS C   41    CYS C   57                          1555   1555  2.01
SSBOND  14 CYS C   59    CYS C   69                          1555   1555  2.04
SSBOND  15 CYS C  569    CYS C  575                          1555   1555  2.04
SSBOND  16 CYS D   36    CYS D   47                          1555   1555  2.03
SSBOND  17 CYS D   37    CYS D  159                          1555   1555  2.02
SSBOND  18 CYS D   41    CYS D   57                          1555   1555  2.04
SSBOND  19 CYS D   59    CYS D   69                          1555   1555  2.03
SSBOND  20 CYS D  569    CYS D  575                          1555   1555  2.04
LINK        FE   HEM A 682                 NE2 HIS A 388     1555   1555  2.20
LINK         C1  NAG A 661                 ND2 ASN A  68     1555   1555  1.45
LINK         C1  NAG A 671                 ND2 ASN A 144     1555   1555  1.47
LINK         C1  NAG A 681                 ND2 ASN A 410     1555   1555  1.45
LINK        FE   HEM B 682                 NE2 HIS B 388     1555   1555  2.25
LINK         C1  NAG B 661                 ND2 ASN B  68     1555   1555  1.45
LINK         C1  NAG B 671                 ND2 ASN B 144     1555   1555  1.44
LINK         C1  NAG B 681                 ND2 ASN B 410     1555   1555  1.46
LINK        FE   HEM C 682                 NE2 HIS C 388     1555   1555  2.17
LINK         C1  NAG C 661                 ND2 ASN C  68     1555   1555  1.44
LINK         C1  NAG C 671                 ND2 ASN C 144     1555   1555  1.46
LINK         C1  NAG C 681                 ND2 ASN C 410     1555   1555  1.44
LINK        FE   HEM D 682                 NE2 HIS D 388     1555   1555  2.24
LINK         C1  NAG D 661                 ND2 ASN D  68     1555   1555  1.49
LINK         C1  NAG D 671                 ND2 ASN D 144     1555   1555  1.46
LINK         C1  NAG D 681                 ND2 ASN D 410     1555   1555  1.46
CISPEP   1 SER A  126    PRO A  127          0        -0.09
CISPEP   2 SER B  126    PRO B  127          0         0.19
CISPEP   3 SER C  126    PRO C  127          0         0.14
CISPEP   4 SER D  126    PRO D  127          0         0.50
SITE     1 CAT  1 TYR A 385
SITE     1 ACE  1 SER A 530
SITE     1 HEM  1 HIS A 388
SITE     1 SUB  1 ARG A 120
SITE     1 AC1  4 TYR A  55  GLU A  67  ASN A  68  THR A  70
SITE     1 AC2  3 GLU A 140  ASN A 144  TYR A 147
SITE     1 AC3  3 ASN A 410  SER A 412  ILE A 413
SITE     1 AC4  4 TYR B  55  GLU B  67  ASN B  68  THR B  70
SITE     1 AC5  5 GLU B 140  ASN B 144  SER B 146  TYR B 147
SITE     2 AC5  5 ARG B 216
SITE     1 AC6  4 TYR B 402  ASN B 410  SER B 412  ILE B 413
SITE     1 AC7  4 PRO C  40  TYR C  55  GLU C  67  ASN C  68
SITE     1 AC8  6 GLU C 140  ASN C 144  SER C 146  TYR C 147
SITE     2 AC8  6 ARG C 216  LEU D 238
SITE     1 AC9  4 TYR C 402  GLN C 406  ASN C 410  ILE C 413
SITE     1 BC1  4 PRO D  40  TYR D  55  GLU D  67  ASN D  68
SITE     1 BC2  4 LEU C 238  ASN D 144  TYR D 147  ARG D 216
SITE     1 BC3  5 GLN D 406  ASN D 410  SER D 412  ILE D 413
SITE     2 BC3  5 GLU D 416
SITE     1 BC4 13 ALA A 199  GLN A 203  HIS A 207  THR A 212
SITE     2 BC4 13 VAL A 295  ASN A 382  TYR A 385  HIS A 386
SITE     3 BC4 13 TRP A 387  HIS A 388  LEU A 391  VAL A 447
SITE     4 BC4 13 GLN A 454
SITE     1 BC5 14 ARG A 120  VAL A 349  LEU A 352  SER A 353
SITE     2 BC5 14 TYR A 355  LEU A 384  TYR A 385  TRP A 387
SITE     3 BC5 14 MET A 522  VAL A 523  GLY A 526  ALA A 527
SITE     4 BC5 14 SER A 530  LEU A 531
SITE     1 BC6 13 ALA B 199  GLN B 203  HIS B 207  THR B 212
SITE     2 BC6 13 VAL B 295  ASN B 382  TYR B 385  HIS B 386
SITE     3 BC6 13 HIS B 388  LEU B 391  LEU B 408  VAL B 447
SITE     4 BC6 13 ALA B 450
SITE     1 BC7 12 ARG B 120  VAL B 349  LEU B 352  SER B 353
SITE     2 BC7 12 TYR B 355  TYR B 385  MET B 522  VAL B 523
SITE     3 BC7 12 GLY B 526  ALA B 527  SER B 530  LEU B 531
SITE     1 BC8 12 ALA C 199  GLN C 203  THR C 212  VAL C 295
SITE     2 BC8 12 ASN C 382  TYR C 385  HIS C 386  TRP C 387
SITE     3 BC8 12 HIS C 388  LEU C 391  VAL C 447  ALA C 450
SITE     1 BC9 14 ARG C 120  VAL C 349  LEU C 352  SER C 353
SITE     2 BC9 14 TYR C 355  LEU C 384  TYR C 385  TRP C 387
SITE     3 BC9 14 MET C 522  VAL C 523  GLY C 526  ALA C 527
SITE     4 BC9 14 SER C 530  LEU C 531
SITE     1 CC1 12 ALA D 199  ALA D 202  GLN D 203  HIS D 207
SITE     2 CC1 12 THR D 212  VAL D 295  ASN D 382  TYR D 385
SITE     3 CC1 12 HIS D 386  HIS D 388  LEU D 391  VAL D 447
SITE     1 CC2 14 ARG D 120  VAL D 349  LEU D 352  SER D 353
SITE     2 CC2 14 TYR D 355  LEU D 384  TYR D 385  TRP D 387
SITE     3 CC2 14 MET D 522  VAL D 523  GLY D 526  ALA D 527
SITE     4 CC2 14 SER D 530  LEU D 531
CRYST1  179.800  133.600  118.400  90.00  90.00  90.00 P 21 21 2    16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.005562  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007485  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008446        0.00000
MTRIX1   1 -0.999300  0.028200 -0.025200       94.17520    1
MTRIX2   1  0.024700 -0.016900 -0.999600       30.43300    1
MTRIX3   1 -0.028700 -0.999500  0.016200       32.51540    1
MTRIX1   2 -0.998400 -0.047500  0.029800       85.09360    1
MTRIX2   2  0.048600 -0.998100  0.037100       64.57020    1
MTRIX3   2  0.028000  0.038500  0.998900       56.85230    1
MTRIX1   3  0.996400 -0.049300  0.068800       -9.72720    1
MTRIX2   3 -0.070000 -0.023300  0.997300       39.85570    1
MTRIX3   3 -0.047500 -0.998500 -0.026700       92.85020    1
      
PROCHECK
Go to PROCHECK summary
 References