HEADER OXIDOREDUCTASE 18-DEC-96 5COX
TITLE UNINHIBITED MOUSE CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2)
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 TISSUE: DERMAL;
SOURCE 6 CELL: FIBROBLAST;
SOURCE 7 CELLULAR_LOCATION: ENDOPLASMIC RETICULUM;
SOURCE 8 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: CULTURED SF21;
SOURCE 12 EXPRESSION_SYSTEM_TISSUE: OVARIAN TISSUE;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 14 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 5COX 1 VERSN
REVDAT 3 24-FEB-09 5COX 1 VERSN
REVDAT 2 01-APR-03 5COX 1 JRNL
REVDAT 1 24-DEC-97 5COX 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. 3.00 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) : 3.00
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) (%) : 74.3
REMARK 3 NUMBER OF REFLECTIONS : 41397
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) : 0.321
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.470
REMARK 3 FREE R VALUE TEST SET COUNT : 4161
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 47.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2968
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 296
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 : 340
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) : 11.30
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) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.76
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 : 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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5COX 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 : MAR-96
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 : 52156
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
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 (%) : 89.2
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.8
REMARK 200 DATA REDUNDANCY IN SHELL : 1.95
REMARK 200 R MERGE FOR SHELL (I) : 0.28900
REMARK 200 R SYM FOR SHELL (I) : 0.28900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.760
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 MIXED WITH A RESERVOIR
REMARK 280 SOLUTION CONTAINING 20-34% MONOMETHYL PEG 550, 10-240 MGCL2, 50
REMARK 280 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 90.23000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 67.21000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 90.23000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 67.21000
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: 8980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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: 8970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 89.8
REMARK 620 3 HEM A 682 NB 95.3 90.3
REMARK 620 4 HEM A 682 NC 87.7 177.4 90.8
REMARK 620 5 HEM A 682 ND 90.1 88.5 174.4 90.6
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 84.7
REMARK 620 3 HEM B 682 NB 91.1 91.1
REMARK 620 4 HEM B 682 NC 94.3 178.2 90.4
REMARK 620 5 HEM B 682 ND 94.2 88.3 174.6 90.3
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 86.7
REMARK 620 3 HEM C 682 NB 96.5 89.7
REMARK 620 4 HEM C 682 NC 91.5 178.2 90.0
REMARK 620 5 HEM C 682 ND 88.7 90.0 174.8 90.5
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 92.9
REMARK 620 3 HEM D 682 NB 93.0 91.3
REMARK 620 4 HEM D 682 NC 88.5 177.7 90.4
REMARK 620 5 HEM D 682 ND 93.4 88.5 173.6 89.7
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 HEM B 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 682
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 682
DBREF 5COX A 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 5COX B 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 5COX C 33 618 UNP Q05769 PGH2_MOUSE 18 604
DBREF 5COX D 33 618 UNP Q05769 PGH2_MOUSE 18 604
SEQADV 5COX GLN A 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 5COX LYS A 333 UNP Q05769 ARG 319 CONFLICT
SEQADV 5COX GLN B 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 5COX LYS B 333 UNP Q05769 ARG 319 CONFLICT
SEQADV 5COX GLN C 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 5COX LYS C 333 UNP Q05769 ARG 319 CONFLICT
SEQADV 5COX GLN D 310 UNP Q05769 ASN 296 CONFLICT
SEQADV 5COX 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 5COX ASN A 68 ASN GLYCOSYLATION SITE
MODRES 5COX ASN A 144 ASN GLYCOSYLATION SITE
MODRES 5COX ASN A 410 ASN GLYCOSYLATION SITE
MODRES 5COX ASN B 68 ASN GLYCOSYLATION SITE
MODRES 5COX ASN B 144 ASN GLYCOSYLATION SITE
MODRES 5COX ASN B 410 ASN GLYCOSYLATION SITE
MODRES 5COX ASN C 68 ASN GLYCOSYLATION SITE
MODRES 5COX ASN C 144 ASN GLYCOSYLATION SITE
MODRES 5COX ASN C 410 ASN GLYCOSYLATION SITE
MODRES 5COX ASN D 68 ASN GLYCOSYLATION SITE
MODRES 5COX ASN D 144 ASN GLYCOSYLATION SITE
MODRES 5COX 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 HEM B 682 43
HET HEM C 682 43
HET HEM D 682 43
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 5 NAG 12(C8 H15 N O6)
FORMUL 17 HEM 4(C34 H32 FE N4 O4)
HELIX 1 1 PRO A 35 SER A 38 5 4
HELIX 2 2 PHE A 74 LEU A 82 1 9
HELIX 3 3 PRO A 86 THR A 94 1 9
HELIX 4 4 LYS A 97 ASN A 105 1 9
HELIX 5 5 PRO A 106 LEU A 123 1 18
HELIX 6 6 TRP A 139 SER A 143 1 5
HELIX 7 7 SER A 174 VAL A 181 1 8
HELIX 8 8 MET A 196 PHE A 209 1 14
HELIX 9 9 ASN A 231 TYR A 234 1 4
HELIX 10 10 LEU A 238 LEU A 244 1 7
HELIX 11 11 VAL A 266 THR A 269 1 4
HELIX 12 12 GLU A 290 GLY A 293 5 4
HELIX 13 13 PRO A 296 GLU A 319 1 24
HELIX 14 14 ASP A 325 GLU A 346 1 22
HELIX 15 15 TYR A 348 SER A 353 1 6
HELIX 16 16 PRO A 363 LEU A 366 5 4
HELIX 17 17 SER A 379 LEU A 384 1 6
HELIX 18 18 HIS A 388 LEU A 390 5 3
HELIX 19 19 PHE A 404 PHE A 407 1 4
HELIX 20 20 ASN A 411 HIS A 417 1 7
HELIX 21 21 THR A 420 THR A 427 1 8
HELIX 22 22 GLN A 445 GLU A 457 1 13
HELIX 23 23 LEU A 463 ARG A 469 1 7
HELIX 24 24 PHE A 478 THR A 482 1 5
HELIX 25 25 GLU A 486 TYR A 495 1 10
HELIX 26 26 ILE A 498 VAL A 500 5 3
HELIX 27 27 TYR A 504 LEU A 508 1 5
HELIX 28 28 GLU A 520 MET A 535 1 16
HELIX 29 29 PRO A 538 CYS A 540 5 3
HELIX 30 30 PRO A 547 PHE A 550 5 4
HELIX 31 31 VAL A 554 THR A 561 1 8
HELIX 32 32 ILE A 564 ASN A 571 1 8
HELIX 33 33 PRO B 35 SER B 38 5 4
HELIX 34 34 PHE B 74 LEU B 82 1 9
HELIX 35 35 PRO B 86 THR B 94 1 9
HELIX 36 36 LYS B 97 ASN B 105 1 9
HELIX 37 37 PRO B 106 LEU B 123 1 18
HELIX 38 38 TRP B 139 SER B 143 1 5
HELIX 39 39 SER B 174 VAL B 181 1 8
HELIX 40 40 MET B 196 PHE B 209 1 14
HELIX 41 41 ASN B 231 TYR B 234 1 4
HELIX 42 42 LEU B 238 LEU B 244 1 7
HELIX 43 43 VAL B 266 THR B 269 1 4
HELIX 44 44 GLU B 290 GLY B 293 5 4
HELIX 45 45 PRO B 296 GLU B 319 1 24
HELIX 46 46 ASP B 325 GLU B 346 1 22
HELIX 47 47 TYR B 348 SER B 353 1 6
HELIX 48 48 PRO B 363 LEU B 366 5 4
HELIX 49 49 SER B 379 LEU B 384 1 6
HELIX 50 50 HIS B 388 LEU B 390 5 3
HELIX 51 51 PHE B 404 PHE B 407 1 4
HELIX 52 52 ASN B 411 HIS B 417 1 7
HELIX 53 53 THR B 420 THR B 427 1 8
HELIX 54 54 GLN B 445 GLU B 457 1 13
HELIX 55 55 LEU B 463 ARG B 469 1 7
HELIX 56 56 PHE B 478 THR B 482 1 5
HELIX 57 57 GLU B 486 TYR B 495 1 10
HELIX 58 58 ILE B 498 VAL B 500 5 3
HELIX 59 59 TYR B 504 LEU B 508 1 5
HELIX 60 60 GLU B 520 MET B 535 1 16
HELIX 61 61 PRO B 538 CYS B 540 5 3
HELIX 62 62 PRO B 547 PHE B 550 5 4
HELIX 63 63 VAL B 554 THR B 561 1 8
HELIX 64 64 ILE B 564 ASN B 571 1 8
HELIX 65 65 PRO C 35 SER C 38 5 4
HELIX 66 66 PHE C 74 LEU C 82 1 9
HELIX 67 67 PRO C 86 THR C 94 1 9
HELIX 68 68 LYS C 97 ASN C 105 1 9
HELIX 69 69 PRO C 106 LEU C 123 1 18
HELIX 70 70 TRP C 139 SER C 143 1 5
HELIX 71 71 SER C 174 VAL C 181 1 8
HELIX 72 72 MET C 196 PHE C 209 1 14
HELIX 73 73 ASN C 231 TYR C 234 1 4
HELIX 74 74 LEU C 238 LEU C 244 1 7
HELIX 75 75 VAL C 266 THR C 269 1 4
HELIX 76 76 GLU C 290 GLY C 293 5 4
HELIX 77 77 PRO C 296 GLU C 319 1 24
HELIX 78 78 ASP C 325 GLU C 346 1 22
HELIX 79 79 TYR C 348 SER C 353 1 6
HELIX 80 80 PRO C 363 LEU C 366 5 4
HELIX 81 81 SER C 379 LEU C 384 1 6
HELIX 82 82 HIS C 388 LEU C 390 5 3
HELIX 83 83 PHE C 404 PHE C 407 1 4
HELIX 84 84 ASN C 411 HIS C 417 1 7
HELIX 85 85 THR C 420 THR C 427 1 8
HELIX 86 86 GLN C 445 GLU C 457 1 13
HELIX 87 87 LEU C 463 ARG C 469 1 7
HELIX 88 88 PHE C 478 THR C 482 1 5
HELIX 89 89 GLU C 486 TYR C 495 1 10
HELIX 90 90 ILE C 498 VAL C 500 5 3
HELIX 91 91 TYR C 504 LEU C 508 1 5
HELIX 92 92 GLU C 520 MET C 535 1 16
HELIX 93 93 PRO C 538 CYS C 540 5 3
HELIX 94 94 PRO C 547 PHE C 550 5 4
HELIX 95 95 VAL C 554 THR C 561 1 8
HELIX 96 96 ILE C 564 ASN C 571 1 8
HELIX 97 97 PRO D 35 SER D 38 5 4
HELIX 98 98 PHE D 74 LEU D 82 1 9
HELIX 99 99 PRO D 86 THR D 94 1 9
HELIX 100 100 LYS D 97 ASN D 105 1 9
HELIX 101 101 PRO D 106 LEU D 123 1 18
HELIX 102 102 TRP D 139 SER D 143 1 5
HELIX 103 103 SER D 174 VAL D 181 1 8
HELIX 104 104 MET D 196 PHE D 209 1 14
HELIX 105 105 ASN D 231 TYR D 234 1 4
HELIX 106 106 LEU D 238 LEU D 244 1 7
HELIX 107 107 VAL D 266 THR D 269 1 4
HELIX 108 108 GLU D 290 GLY D 293 5 4
HELIX 109 109 PRO D 296 GLU D 319 1 24
HELIX 110 110 ASP D 325 GLU D 346 1 22
HELIX 111 111 TYR D 348 SER D 353 1 6
HELIX 112 112 PRO D 363 LEU D 366 5 4
HELIX 113 113 SER D 379 LEU D 384 1 6
HELIX 114 114 HIS D 388 LEU D 390 5 3
HELIX 115 115 PHE D 404 PHE D 407 1 4
HELIX 116 116 ASN D 411 HIS D 417 1 7
HELIX 117 117 THR D 420 THR D 427 1 8
HELIX 118 118 ALA D 443 GLU D 457 5 15
HELIX 119 119 LEU D 463 ARG D 469 1 7
HELIX 120 120 PHE D 478 THR D 482 1 5
HELIX 121 121 GLU D 486 TYR D 495 1 10
HELIX 122 122 ILE D 498 VAL D 500 5 3
HELIX 123 123 TYR D 504 LEU D 508 1 5
HELIX 124 124 GLU D 520 MET D 535 1 16
HELIX 125 125 PRO D 538 CYS D 540 5 3
HELIX 126 126 PRO D 547 PHE D 550 5 4
HELIX 127 127 VAL D 554 THR D 561 1 8
HELIX 128 128 ILE D 564 ASN D 571 1 8
SHEET 1 A 2 CYS A 47 SER A 49 0
SHEET 2 A 2 TYR A 55 CYS A 57 -1 N LYS A 56 O MET A 48
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 CYS B 47 SER B 49 0
SHEET 2 C 2 TYR B 55 CYS B 57 -1 N LYS B 56 O MET B 48
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 PHE B 395 ILE B 397 0
SHEET 2 E 2 GLN B 400 TYR B 402 -1 N TYR B 402 O PHE B 395
SHEET 1 F 2 CYS C 47 SER C 49 0
SHEET 2 F 2 TYR C 55 CYS C 57 -1 N LYS C 56 O MET C 48
SHEET 1 G 2 GLN C 255 ILE C 257 0
SHEET 2 G 2 GLU C 260 TYR C 262 -1 N TYR C 262 O GLN C 255
SHEET 1 H 2 CYS D 47 SER D 49 0
SHEET 2 H 2 TYR D 55 CYS D 57 -1 N LYS D 56 O MET D 48
SHEET 1 I 2 GLN D 255 ILE D 257 0
SHEET 2 I 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 2.05
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.04
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 2.03
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 2.03
SSBOND 13 CYS C 41 CYS C 57 1555 1555 2.04
SSBOND 14 CYS C 59 CYS C 69 1555 1555 2.03
SSBOND 15 CYS C 569 CYS C 575 1555 1555 2.03
SSBOND 16 CYS D 36 CYS D 47 1555 1555 2.04
SSBOND 17 CYS D 37 CYS D 159 1555 1555 2.02
SSBOND 18 CYS D 41 CYS D 57 1555 1555 2.03
SSBOND 19 CYS D 59 CYS D 69 1555 1555 2.05
SSBOND 20 CYS D 569 CYS D 575 1555 1555 2.03
LINK FE HEM A 682 NE2 HIS A 388 1555 1555 2.18
LINK C1 NAG A 661 ND2 ASN A 68 1555 1555 1.46
LINK C1 NAG A 671 ND2 ASN A 144 1555 1555 1.44
LINK C1 NAG A 681 ND2 ASN A 410 1555 1555 1.47
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 1.47
LINK C1 NAG B 681 ND2 ASN B 410 1555 1555 1.43
LINK FE HEM C 682 NE2 HIS C 388 1555 1555 2.18
LINK C1 NAG C 661 ND2 ASN C 68 1555 1555 1.45
LINK C1 NAG C 671 ND2 ASN C 144 1555 1555 1.45
LINK C1 NAG C 681 ND2 ASN C 410 1555 1555 1.47
LINK FE HEM D 682 NE2 HIS D 388 1555 1555 2.21
LINK C1 NAG D 661 ND2 ASN D 68 1555 1555 1.46
LINK C1 NAG D 671 ND2 ASN D 144 1555 1555 1.45
LINK C1 NAG D 681 ND2 ASN D 410 1555 1555 1.45
CISPEP 1 SER A 126 PRO A 127 0 0.10
CISPEP 2 SER B 126 PRO B 127 0 -0.14
CISPEP 3 SER C 126 PRO C 127 0 0.05
CISPEP 4 SER D 126 PRO D 127 0 0.09
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 ASN A 68 THR A 70
SITE 1 AC2 4 GLU A 140 ASN A 144 SER A 146 TYR A 147
SITE 1 AC3 4 TYR A 402 GLN A 406 ASN A 410 ILE A 413
SITE 1 AC4 5 SER B 38 TYR B 55 GLU B 67 ASN B 68
SITE 2 AC4 5 THR B 70
SITE 1 AC5 4 GLU B 140 ASN B 144 TYR B 147 ARG B 216
SITE 1 AC6 5 TYR B 402 LYS B 405 GLN B 406 ASN B 410
SITE 2 AC6 5 ILE B 413
SITE 1 AC7 5 SER C 38 TYR C 55 GLU C 67 ASN C 68
SITE 2 AC7 5 THR C 70
SITE 1 AC8 6 TYR C 134 GLU C 140 ASN C 144 SER C 146
SITE 2 AC8 6 TYR C 147 ARG C 216
SITE 1 AC9 4 TYR C 402 GLN C 406 ASN C 410 ILE C 413
SITE 1 BC1 5 SER D 38 PRO D 40 TYR D 55 GLU D 67
SITE 2 BC1 5 ASN D 68
SITE 1 BC2 4 GLU D 140 ASN D 144 TYR D 147 ARG D 216
SITE 1 BC3 6 LYS D 405 GLN D 406 ASN D 410 SER D 412
SITE 2 BC3 6 ILE D 413 GLU D 416
SITE 1 BC4 12 ALA A 199 PHE A 200 GLN A 203 HIS A 207
SITE 2 BC4 12 THR A 212 ASN A 382 TYR A 385 HIS A 386
SITE 3 BC4 12 TRP A 387 HIS A 388 LEU A 391 GLN A 454
SITE 1 BC5 13 ALA B 199 PHE B 200 GLN B 203 HIS B 207
SITE 2 BC5 13 PHE B 210 THR B 212 VAL B 295 ASN B 382
SITE 3 BC5 13 TYR B 385 HIS B 386 HIS B 388 LEU B 391
SITE 4 BC5 13 GLN B 454
SITE 1 BC6 14 ALA C 199 PHE C 200 GLN C 203 HIS C 207
SITE 2 BC6 14 THR C 212 VAL C 295 ASN C 382 TYR C 385
SITE 3 BC6 14 HIS C 386 TRP C 387 HIS C 388 LEU C 391
SITE 4 BC6 14 LEU C 408 GLN C 454
SITE 1 BC7 12 ALA D 199 GLN D 203 HIS D 207 THR D 212
SITE 2 BC7 12 VAL D 295 ASN D 382 TYR D 385 HIS D 386
SITE 3 BC7 12 TRP D 387 HIS D 388 LEU D 391 GLN D 454
CRYST1 180.460 134.420 119.900 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 0.005541 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007439 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008340 0.00000
MTRIX1 1 -0.999800 0.017200 -0.013700 94.84790 1
MTRIX2 1 0.013500 -0.011600 -0.999800 31.08800 1
MTRIX3 1 -0.017300 -0.999800 0.011300 32.21280 1
MTRIX1 2 -0.998500 -0.047000 0.027900 85.26010 1
MTRIX2 2 0.048000 -0.998200 0.034600 65.02600 1
MTRIX3 2 0.026200 0.035900 0.999000 57.74280 1
MTRIX1 3 0.997400 -0.039900 0.060100 -10.21210 1
MTRIX2 3 -0.061100 -0.023800 0.997900 39.60550 1
MTRIX3 3 -0.038400 -0.998900 -0.026200 93.41290 1
(ATOM LINES ARE NOT SHOWN.)
END
