HEADER OXIDOREDUCTASE 18-DEC-96 3PGH
TITLE CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A NON-
TITLE 2 SELECTIVE INHIBITOR, FLURBIPROFEN
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 3PGH 1 VERSN
REVDAT 3 24-FEB-09 3PGH 1 VERSN
REVDAT 2 01-APR-03 3PGH 1 JRNL
REVDAT 1 24-DEC-97 3PGH 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. 2.50 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) : 2.50
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) (%) : 63.1
REMARK 3 NUMBER OF REFLECTIONS : 59815
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : AS IMPLEMENTED IN X-PLOR
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.360
REMARK 3 FREE R VALUE TEST SET COUNT : 6027
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 38.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4058
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 486
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 : 412
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) : 15.00
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) : 1.86
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.FLURBIPROFEN
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.FLURBIPROFEN
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PGH 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 : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76325
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.8
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : 0.11100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : 0.42500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.320
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 89.75000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 66.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 89.75000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 66.90000
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: 10200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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: 10230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 92.5
REMARK 620 3 HEM A 682 NB 92.8 90.9
REMARK 620 4 HEM A 682 NC 85.2 177.6 89.9
REMARK 620 5 HEM A 682 ND 90.1 89.7 177.0 89.6
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 92.1
REMARK 620 3 HEM B 682 NB 97.2 90.1
REMARK 620 4 HEM B 682 NC 91.4 176.4 89.0
REMARK 620 5 HEM B 682 ND 90.6 90.5 172.1 89.9
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 93.9
REMARK 620 3 HEM C 682 NB 98.0 90.4
REMARK 620 4 HEM C 682 NC 88.1 178.1 89.2
REMARK 620 5 HEM C 682 ND 90.8 90.5 171.1 89.6
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 87.3
REMARK 620 3 HEM D 682 NB 96.7 89.9
REMARK 620 4 HEM D 682 NC 93.9 178.7 89.9
REMARK 620 5 HEM D 682 ND 89.8 90.7 173.5 89.4
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 FLP 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 FLP 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 FLP 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 FLP D 701
DBREF 3PGH A 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 3PGH B 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 3PGH C 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 3PGH D 33 618 UNP Q05769 PGH2_MOUSE 18 604
SEQADV 3PGH GLN A 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 3PGH LYS A 333 UNP Q05769 ARG 319 CONFLICT
SEQADV 3PGH GLN B 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 3PGH LYS B 333 UNP Q05769 ARG 319 CONFLICT
SEQADV 3PGH GLN C 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 3PGH LYS C 333 UNP Q05769 ARG 319 CONFLICT
SEQADV 3PGH GLN D 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 3PGH 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 3PGH ASN A 68 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN A 144 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN A 410 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN B 68 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN B 144 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN B 410 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN C 68 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN C 144 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN C 410 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN D 68 ASN GLYCOSYLATION SITE
MODRES 3PGH ASN D 144 ASN GLYCOSYLATION SITE
MODRES 3PGH 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 FLP A 701 18
HET HEM B 682 43
HET FLP B 701 18
HET HEM C 682 43
HET FLP C 701 18
HET HEM D 682 43
HET FLP D 701 18
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM FLP FLURBIPROFEN
HETSYN HEM HEME
FORMUL 5 NAG 12(C8 H15 N O6)
FORMUL 17 HEM 4(C34 H32 FE N4 O4)
FORMUL 18 FLP 4(C15 H13 F O2)
HELIX 1 1 PHE A 74 LEU A 80 1 7
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 PHE A 209 1 14
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 THR A 383 1 5
HELIX 16 16 PHE A 404 PHE A 407 1 4
HELIX 17 17 ASN A 411 HIS A 417 1 7
HELIX 18 18 THR A 420 THR A 427 1 8
HELIX 19 19 ILE A 442 GLU A 457 5 16
HELIX 20 20 LEU A 463 ARG A 469 1 7
HELIX 21 21 PHE A 478 THR A 482 1 5
HELIX 22 22 GLU A 486 TYR A 495 1 10
HELIX 23 23 ILE A 498 VAL A 500 5 3
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 THR A 561 1 9
HELIX 29 29 ILE A 564 ASN A 571 1 8
HELIX 30 30 PHE B 74 LEU B 80 1 7
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 PHE B 209 1 14
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 PHE B 404 PHE B 407 1 4
HELIX 46 46 ASN B 411 HIS B 417 1 7
HELIX 47 47 THR B 420 THR B 427 1 8
HELIX 48 48 ILE B 442 GLU B 457 5 16
HELIX 49 49 LEU B 463 ARG B 469 1 7
HELIX 50 50 PHE B 478 THR B 482 1 5
HELIX 51 51 GLU B 486 TYR B 495 1 10
HELIX 52 52 ILE B 498 VAL B 500 5 3
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 THR B 561 1 9
HELIX 58 58 ILE B 564 ASN B 571 1 8
HELIX 59 59 PHE C 74 LEU C 80 1 7
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 PHE C 209 1 14
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 THR C 383 1 5
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 ASN C 411 HIS C 417 1 7
HELIX 77 77 THR C 420 THR C 427 1 8
HELIX 78 78 ILE C 442 GLU C 457 5 16
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 ILE C 498 VAL C 500 5 3
HELIX 83 83 LEU C 503 LEU C 508 1 6
HELIX 84 84 GLU C 520 MET C 535 1 16
HELIX 85 85 PRO C 538 CYS C 540 5 3
HELIX 86 86 PRO C 547 PHE C 550 5 4
HELIX 87 87 GLU C 553 THR C 561 1 9
HELIX 88 88 ILE C 564 ASN C 571 1 8
HELIX 89 89 PHE D 74 LEU D 80 1 7
HELIX 90 90 PRO D 86 THR D 94 1 9
HELIX 91 91 LYS D 97 ASN D 105 1 9
HELIX 92 92 PRO D 106 LEU D 123 1 18
HELIX 93 93 TRP D 139 SER D 143 1 5
HELIX 94 94 SER D 174 VAL D 181 1 8
HELIX 95 95 MET D 196 PHE D 209 1 14
HELIX 96 96 ASN D 231 TYR D 234 1 4
HELIX 97 97 LEU D 238 LEU D 244 1 7
HELIX 98 98 VAL D 266 THR D 269 1 4
HELIX 99 99 PRO D 296 GLU D 319 1 24
HELIX 100 100 ASP D 325 GLU D 346 1 22
HELIX 101 101 TYR D 348 SER D 353 1 6
HELIX 102 102 PRO D 363 LEU D 366 5 4
HELIX 103 103 SER D 379 LEU D 384 1 6
HELIX 104 104 PHE D 404 PHE D 407 1 4
HELIX 105 105 ASN D 411 HIS D 417 1 7
HELIX 106 106 THR D 420 THR D 427 1 8
HELIX 107 107 ILE D 442 GLU D 457 5 16
HELIX 108 108 LEU D 463 ARG D 469 1 7
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 ILE D 498 VAL D 500 5 3
HELIX 112 112 LEU D 503 LEU D 508 1 6
HELIX 113 113 GLU D 520 MET D 535 1 16
HELIX 114 114 PRO D 538 CYS D 540 5 3
HELIX 115 115 PRO D 547 PHE D 550 5 4
HELIX 116 116 GLU D 553 ASN D 560 1 8
HELIX 117 117 ILE D 564 ASN D 571 1 8
SHEET 1 A 2 GLU A 46 SER A 49 0
SHEET 2 A 2 TYR A 55 ASP A 58 -1 N ASP A 58 O GLU A 46
SHEET 1 B 2 GLN A 255 ILE A 257 0
SHEET 2 B 2 GLU A 260 TYR A 262 -1 N TYR A 262 O GLN A 255
SHEET 1 C 2 GLU B 46 SER B 49 0
SHEET 2 C 2 TYR B 55 ASP B 58 -1 N ASP B 58 O GLU B 46
SHEET 1 D 2 GLN B 255 ILE B 257 0
SHEET 2 D 2 GLU B 260 TYR B 262 -1 N TYR B 262 O GLN B 255
SHEET 1 E 2 GLU C 46 SER C 49 0
SHEET 2 E 2 TYR C 55 ASP C 58 -1 N ASP C 58 O GLU C 46
SHEET 1 F 2 GLN C 255 ILE C 257 0
SHEET 2 F 2 GLU C 260 TYR C 262 -1 N TYR C 262 O GLN C 255
SHEET 1 G 2 GLU D 46 SER D 49 0
SHEET 2 G 2 TYR D 55 ASP D 58 -1 N ASP D 58 O GLU D 46
SHEET 1 H 2 GLN D 255 ILE D 257 0
SHEET 2 H 2 GLU D 260 TYR D 262 -1 N TYR D 262 O GLN D 255
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.03
SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.03
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.00
SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.05
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.01
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.01
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.02
SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.05
SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.02
SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.02
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 2.02
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 2.02
LINK FE HEM A 682 NE2 HIS A 388 1555 1555 2.19
LINK C1 NAG A 661 ND2 ASN A 68 1555 1555 1.45
LINK C1 NAG A 671 ND2 ASN A 144 1555 1555 1.45
LINK C1 NAG A 681 ND2 ASN A 410 1555 1555 1.46
LINK FE HEM B 682 NE2 HIS B 388 1555 1555 2.21
LINK C1 NAG B 661 ND2 ASN B 68 1555 1555 1.46
LINK C1 NAG B 671 ND2 ASN B 144 1555 1555 1.44
LINK C1 NAG B 681 ND2 ASN B 410 1555 1555 1.45
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 1.47
LINK C1 NAG C 681 ND2 ASN C 410 1555 1555 1.44
LINK FE HEM D 682 NE2 HIS D 388 1555 1555 2.22
LINK C1 NAG D 661 ND2 ASN D 68 1555 1555 1.47
LINK C1 NAG D 671 ND2 ASN D 144 1555 1555 1.44
LINK C1 NAG D 681 ND2 ASN D 410 1555 1555 1.43
CISPEP 1 SER A 126 PRO A 127 0 0.97
CISPEP 2 SER B 126 PRO B 127 0 0.10
CISPEP 3 SER C 126 PRO C 127 0 0.70
CISPEP 4 SER D 126 PRO D 127 0 0.23
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 3 TYR A 55 GLU A 67 ASN A 68
SITE 1 AC2 4 GLU A 140 ASN A 144 TYR A 147 LEU B 238
SITE 1 AC3 4 TYR A 402 GLN A 406 ASN A 410 ILE A 413
SITE 1 AC4 4 PRO B 40 TYR B 55 GLU B 67 ASN B 68
SITE 1 AC5 4 GLU B 140 ASN B 144 TYR B 147 ARG B 216
SITE 1 AC6 3 TYR B 402 ASN B 410 ILE B 413
SITE 1 AC7 3 TYR C 55 GLU C 67 ASN C 68
SITE 1 AC8 5 GLU C 140 ASN C 144 TYR C 147 ARG C 216
SITE 2 AC8 5 LEU D 238
SITE 1 AC9 4 TYR C 402 GLN C 406 ASN C 410 ILE C 413
SITE 1 BC1 4 SER D 38 TYR D 55 GLU D 67 ASN D 68
SITE 1 BC2 5 LEU C 238 GLU D 140 ASN D 144 TYR D 147
SITE 2 BC2 5 ARG D 216
SITE 1 BC3 4 TYR D 402 GLN D 406 ASN D 410 ILE D 413
SITE 1 BC4 13 TYR A 148 ALA A 199 GLN A 203 HIS A 207
SITE 2 BC4 13 THR A 212 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 10 ARG A 120 VAL A 349 TYR A 355 LEU A 359
SITE 2 BC5 10 TYR A 385 TRP A 387 GLY A 526 ALA A 527
SITE 3 BC5 10 SER A 530 LEU A 531
SITE 1 BC6 13 TYR B 148 ALA B 199 ALA B 202 GLN B 203
SITE 2 BC6 13 HIS B 207 PHE B 210 THR B 212 ASN B 382
SITE 3 BC6 13 TYR B 385 HIS B 386 HIS B 388 VAL B 447
SITE 4 BC6 13 GLN B 454
SITE 1 BC7 8 ARG B 120 VAL B 349 TYR B 355 TYR B 385
SITE 2 BC7 8 TRP B 387 MET B 522 VAL B 523 ALA B 527
SITE 1 BC8 12 TYR C 148 ALA C 199 GLN C 203 HIS C 207
SITE 2 BC8 12 THR C 212 ASN C 382 TYR C 385 HIS C 386
SITE 3 BC8 12 HIS C 388 LEU C 391 VAL C 447 GLN C 454
SITE 1 BC9 10 ARG C 120 VAL C 349 TYR C 355 LEU C 359
SITE 2 BC9 10 TYR C 385 TRP C 387 GLY C 526 ALA C 527
SITE 3 BC9 10 SER C 530 LEU C 531
SITE 1 CC1 14 TYR D 148 ALA D 199 ALA D 202 GLN D 203
SITE 2 CC1 14 THR D 206 HIS D 207 PHE D 210 THR D 212
SITE 3 CC1 14 ASN D 382 TYR D 385 HIS D 386 HIS D 388
SITE 4 CC1 14 VAL D 447 GLN D 454
SITE 1 CC2 10 ARG D 120 VAL D 349 TYR D 355 TYR D 385
SITE 2 CC2 10 TRP D 387 MET D 522 VAL D 523 GLY D 526
SITE 3 CC2 10 ALA D 527 SER D 530
CRYST1 179.500 133.800 117.100 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 0.005571 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007474 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008540 0.00000
MTRIX1 1 -0.997500 0.050400 -0.049500 93.37000 1
MTRIX2 1 0.049400 -0.003800 -0.998800 28.99910 1
MTRIX3 1 -0.050500 -0.998700 0.001300 33.58290 1
MTRIX1 2 -0.999300 -0.031900 0.016900 84.61660 1
MTRIX2 2 0.032300 -0.999200 0.023800 65.41520 1
MTRIX3 2 0.016100 0.024400 0.999600 57.14170 1
MTRIX1 3 0.995000 -0.061900 0.078600 -9.25440 1
MTRIX2 3 -0.079800 -0.017100 0.996700 40.03670 1
MTRIX3 3 -0.060400 -0.997900 -0.022000 92.72010 1
(ATOM LINES ARE NOT SHOWN.)
END
