HEADER OXIDOREDUCTASE(DIOXYGENASE, PEROXIDASE) 07-MAR-94 1PRH
TITLE THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2
TITLE 2 SYNTHASE-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROSTAGLANDIN H2 SYNTHASE-1;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.14.99.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE 3 ORGANISM_COMMON: SHEEP;
SOURCE 4 ORGANISM_TAXID: 9940
KEYWDS OXIDOREDUCTASE(DIOXYGENASE, PEROXIDASE)
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PICOT,P.J.LOLL,R.M.GARAVITO
REVDAT 3 23-MAR-11 1PRH 1 COMPND
REVDAT 2 24-FEB-09 1PRH 1 VERSN
REVDAT 1 31-MAR-95 1PRH 0
JRNL AUTH D.PICOT,P.J.LOLL,R.M.GARAVITO
JRNL TITL THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN
JRNL TITL 2 PROSTAGLANDIN H2 SYNTHASE-1.
JRNL REF NATURE V. 367 243 1994
JRNL REFN ISSN 0028-0836
JRNL PMID 8121489
JRNL DOI 10.1038/367243A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZENG,R.E.FENNA
REMARK 1 TITL X-RAY CRYSTAL STRUCTURE OF CANINE MYELOPEROXIDASE AT 3
REMARK 1 TITL 2 ANGSTROMS RESOLUTION
REMARK 1 REF J.MOL.BIOL. V. 226 185 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 32349
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.267
REMARK 3 FREE R VALUE : 0.316
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 9006
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
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) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 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) : 3.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 COORDINATES GIVEN HERE FOR RESIDUES 33 - 586 WHERE THE
REMARK 3 MAIN CHAIN ELECTRON DENSITY IS WELL DEFINED. ELECTRON
REMARK 3 DENSITY FOR THE EXTREME AMINO-TERMINUS (RESIDUES 25 - 33)
REMARK 3 AND THE EXTREME C-TERMINUS (RESIDUES 587 - 600) IS POORLY
REMARK 3 DEFINED.
REMARK 3
REMARK 3 RESOLUTION IS TOO LIMITED TO CLEARLY DEFINE TURN
REMARK 3 STEREOCHEMISTRY.
REMARK 3
REMARK 3 PHASED BY MIR (3 DERIVATIVES), SOLVENT FLATTENED AND
REMARK 3 TWO-FOLD AVERAGED ABOUT THE NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 3 AXIS.
REMARK 4
REMARK 4 1PRH 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 : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 49.70000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 105.15000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 116.55000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 49.70000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 105.15000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 116.55000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 49.70000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 105.15000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 116.55000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 49.70000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 105.15000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 116.55000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 300 REMARK: THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO
REMARK 300 CHAIN *A*.
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: 7140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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 400
REMARK 400 COMPOUND
REMARK 400 RESIDUES ASN 68, ASN 144 AND ASN 410 ARE GLYCOSYLATED AND
REMARK 400 THE FIRST 1 - 2 SUGARS ARE VISIBLE IN THE MAP(S).
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 95 CG HIS A 95 CD2 0.067
REMARK 500 HIS B 95 CG HIS B 95 CD2 0.062
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 49 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 TRP A 75 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 75 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 77 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP A 77 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 HIS A 95 CA - CB - CG ANGL. DEV. = 21.2 DEGREES
REMARK 500 TRP A 98 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP A 98 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES
REMARK 500 TRP A 100 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 100 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 100 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 120 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 120 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 SER A 143 CA - C - N ANGL. DEV. = 23.2 DEGREES
REMARK 500 SER A 143 O - C - N ANGL. DEV. = -25.1 DEGREES
REMARK 500 THR A 149 CA - CB - CG2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 157 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 184 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 184 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 GLY A 219 N - CA - C ANGL. DEV. = -15.5 DEGREES
REMARK 500 TYR A 254 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 LEU A 294 C - N - CA ANGL. DEV. = 20.7 DEGREES
REMARK 500 TRP A 305 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 305 CB - CG - CD1 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TRP A 305 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 305 CG - CD2 - CE3 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 311 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 TRP A 323 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 LEU A 352 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG A 376 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 HIS A 386 CA - CB - CG ANGL. DEV. = -12.3 DEGREES
REMARK 500 TRP A 387 CA - CB - CG ANGL. DEV. = 13.5 DEGREES
REMARK 500 TRP A 387 CD1 - CG - CD2 ANGL. DEV. = 5.3 DEGREES
REMARK 500 TRP A 387 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 433 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 433 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU A 445 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG A 456 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 459 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 467 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 GLU A 486 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 LEU A 535 CA - CB - CG ANGL. DEV. = -14.9 DEGREES
REMARK 500 TYR A 544 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TRP A 545 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES
REMARK 500 CYS A 569 CA - CB - SG ANGL. DEV. = -14.4 DEGREES
REMARK 500 HIS A 581 CB - CG - CD2 ANGL. DEV. = -10.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 108 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 34 96.74 82.76
REMARK 500 HIS A 43 43.26 38.65
REMARK 500 PHE A 50 -166.90 -105.68
REMARK 500 LEU A 52 -88.16 58.69
REMARK 500 CYS A 59 31.28 -89.46
REMARK 500 ARG A 61 58.47 38.89
REMARK 500 HIS A 95 -166.38 -103.27
REMARK 500 THR A 129 -85.83 -107.00
REMARK 500 ASP A 135 48.95 -100.03
REMARK 500 SER A 146 54.32 -92.69
REMARK 500 TYR A 147 -31.40 -136.76
REMARK 500 TYR A 148 110.73 69.00
REMARK 500 ARG A 157 2.85 -58.33
REMARK 500 PRO A 162 -3.58 -58.63
REMARK 500 PHE A 220 98.75 57.29
REMARK 500 LEU A 230 45.75 -74.47
REMARK 500 ASP A 249 21.58 47.86
REMARK 500 ASN A 258 -126.51 54.19
REMARK 500 PRO A 263 153.49 -46.85
REMARK 500 VAL A 271 -51.76 33.37
REMARK 500 LEU A 272 -88.87 137.66
REMARK 500 MET A 273 132.96 66.03
REMARK 500 ARG A 277 126.79 -29.43
REMARK 500 PHE A 292 -2.39 -58.14
REMARK 500 HIS A 386 41.41 -74.37
REMARK 500 PRO A 389 -18.84 -49.32
REMARK 500 PRO A 399 34.18 -98.43
REMARK 500 PRO A 462 175.96 -57.68
REMARK 500 THR A 482 -72.62 -64.95
REMARK 500 PRO A 514 -90.37 15.62
REMARK 500 GLU A 520 -64.84 -22.96
REMARK 500 ASP A 584 6.74 40.24
REMARK 500 PRO A 585 100.34 20.32
REMARK 500 ASN B 34 96.45 82.42
REMARK 500 HIS B 43 43.46 38.41
REMARK 500 PHE B 50 -166.66 -105.63
REMARK 500 LEU B 52 -88.33 58.69
REMARK 500 CYS B 59 31.16 -89.19
REMARK 500 ARG B 61 58.77 38.39
REMARK 500 HIS B 95 -166.51 -103.26
REMARK 500 ARG B 97 -30.44 -39.96
REMARK 500 THR B 129 -86.04 -107.05
REMARK 500 ASP B 135 49.20 -99.98
REMARK 500 SER B 146 54.56 -93.08
REMARK 500 TYR B 147 -31.40 -136.70
REMARK 500 TYR B 148 110.40 69.37
REMARK 500 ARG B 157 2.92 -58.21
REMARK 500 PRO B 162 -4.11 -58.42
REMARK 500 PHE B 220 98.73 57.07
REMARK 500 LEU B 230 45.64 -74.24
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 584 PRO A 585 -119.46
REMARK 500 ASP B 584 PRO B 585 -119.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER A 143 11.80
REMARK 500 SER B 143 11.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 TYR A 147 24.4 L L OUTSIDE RANGE
REMARK 500 TYR B 147 24.3 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 COX -- THE CYCLOOXYGENASE ACTIVE SITE IS LOCATED
REMARK 600 WITHIN A LONG HYDROPHOBIC CHANNEL AT A REGION DEFINED BY
REMARK 600 RESIDUES ARG 120, SER 530 (SITE OF ASPIRIN ACETYLATION),
REMARK 600 TYR 385, AND GLU 524.
REMARK 600
REMARK 600 THE CRYSTALS CONTAIN A NON-STEROIDAL ANTI-INFLAMMATORY DRUG
REMARK 600 FLURBIPROFEN AND THE DRUG BINDING SITE HAS BEEN IDENTIFIED
REMARK 600 (SEE D. PICOT, P.J. LOLL AND R.M. GARAVITO, 1994), ALTHOUGH
REMARK 600 REGULARIZED AND REFINED COORDINATES FOR THE PROTEIN-BOUND
REMARK 600 DRUG ARE NOT YET AVAILABLE.
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 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 388 NE2
REMARK 620 2 HEM A 601 NA 91.5
REMARK 620 3 HEM A 601 NB 88.8 89.3
REMARK 620 4 HEM A 601 NC 92.8 175.3 88.9
REMARK 620 5 HEM A 601 ND 90.9 90.0 179.3 91.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 388 NE2
REMARK 620 2 HEM B 601 NA 91.5
REMARK 620 3 HEM B 601 NB 88.4 89.5
REMARK 620 4 HEM B 601 NC 92.6 175.5 88.8
REMARK 620 5 HEM B 601 ND 90.9 90.1 179.3 91.7
REMARK 620 N 1 2 3 4
REMARK 650
REMARK 650 HELIX
REMARK 650 HELIX -- THE NOMENCLATURE FOR THE HELICES 1 - 19 IS BASED
REMARK 650 ON THE TOPOLOGICAL AND SPATIAL EQUIVALENCE OF SECONDARY
REMARK 650 STRUCTURE BETWEEN PROSTAGLANDIN H SYNTHASE AND
REMARK 650 MYELO-PEROXIDASE (ZENG AND FENNA, 1992). HELICES
REMARK 650 IDENTIFIED WITH A LETTER A - E HAVE NO EQUIVALENT IN
REMARK 650 MYELOPEROXIDASE.
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEET -- ONLY A SMALL REGION OF BETA-SHEET IS OBSERVED IN
REMARK 700 THE EGF-LIKE MODULE (RESIDUES 33 - 72) ALTHOUGH THE EXACT
REMARK 700 HYDROGEN BONDING SCHEME IS NOT UNEQUIVOCAL AT THE PRESENT
REMARK 700 RESOLUTION.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: COX
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CYCLOOXYGENASE ACTIVE SITE IS LOCATED WITHIN A
REMARK 800 LONG HYDROPHOBIC CHANNEL
REMARK 800
REMARK 800 SITE_IDENTIFIER: PER
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: PEROXIDASE ACTIVE SITE IS AT THE HEME (HEM 601)
REMARK 800 SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
DBREF 1PRH A 33 586 UNP P05979 PGH1_SHEEP 33 586
DBREF 1PRH B 33 586 UNP P05979 PGH1_SHEEP 33 586
SEQADV 1PRH LEU A 92 UNP P05979 MET 92 CONFLICT
SEQADV 1PRH GLN A 310 UNP P05979 ASN 310 CONFLICT
SEQADV 1PRH LYS A 333 UNP P05979 ARG 333 CONFLICT
SEQADV 1PRH LEU B 92 UNP P05979 MET 92 CONFLICT
SEQADV 1PRH GLN B 310 UNP P05979 ASN 310 CONFLICT
SEQADV 1PRH LYS B 333 UNP P05979 ARG 333 CONFLICT
SEQRES 1 A 554 VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN GLY
SEQRES 2 A 554 ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS ASP
SEQRES 3 A 554 CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR ILE
SEQRES 4 A 554 PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG PRO
SEQRES 5 A 554 SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY ARG
SEQRES 6 A 554 TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG ASP
SEQRES 7 A 554 THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN LEU
SEQRES 8 A 554 ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP TYR
SEQRES 9 A 554 ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR THR
SEQRES 10 A 554 ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR PRO
SEQRES 11 A 554 MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA GLU
SEQRES 12 A 554 PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE ILE
SEQRES 13 A 554 PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE PHE
SEQRES 14 A 554 ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER GLY
SEQRES 15 A 554 LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS GLY
SEQRES 16 A 554 VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU ARG
SEQRES 17 A 554 GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS
SEQRES 18 A 554 TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER VAL
SEQRES 19 A 554 GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY ILE
SEQRES 20 A 554 PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL PHE
SEQRES 21 A 554 GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE TRP
SEQRES 22 A 554 LEU ARG GLU HIS GLN ARG VAL CYS ASP LEU LEU LYS ALA
SEQRES 23 A 554 GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN THR
SEQRES 24 A 554 ALA LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL
SEQRES 25 A 554 ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE LEU
SEQRES 26 A 554 GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA GLN
SEQRES 27 A 554 PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN GLN
SEQRES 28 A 554 LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE ARG
SEQRES 29 A 554 VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU PHE
SEQRES 30 A 554 ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA LEU
SEQRES 31 A 554 VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE GLY
SEQRES 32 A 554 GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL ALA
SEQRES 33 A 554 VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU GLN
SEQRES 34 A 554 PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS PRO
SEQRES 35 A 554 TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU MET
SEQRES 36 A 554 ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP ALA
SEQRES 37 A 554 LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS HIS
SEQRES 38 A 554 PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET GLY
SEQRES 39 A 554 ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO ILE
SEQRES 40 A 554 CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY GLY
SEQRES 41 A 554 GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU LYS
SEQRES 42 A 554 LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR VAL
SEQRES 43 A 554 SER PHE HIS VAL PRO ASP PRO ARG
SEQRES 1 B 554 VAL ASN PRO CYS CYS TYR TYR PRO CYS GLN HIS GLN GLY
SEQRES 2 B 554 ILE CYS VAL ARG PHE GLY LEU ASP ARG TYR GLN CYS ASP
SEQRES 3 B 554 CYS THR ARG THR GLY TYR SER GLY PRO ASN CYS THR ILE
SEQRES 4 B 554 PRO GLU ILE TRP THR TRP LEU ARG THR THR LEU ARG PRO
SEQRES 5 B 554 SER PRO SER PHE ILE HIS PHE LEU LEU THR HIS GLY ARG
SEQRES 6 B 554 TRP LEU TRP ASP PHE VAL ASN ALA THR PHE ILE ARG ASP
SEQRES 7 B 554 THR LEU MET ARG LEU VAL LEU THR VAL ARG SER ASN LEU
SEQRES 8 B 554 ILE PRO SER PRO PRO THR TYR ASN ILE ALA HIS ASP TYR
SEQRES 9 B 554 ILE SER TRP GLU SER PHE SER ASN VAL SER TYR TYR THR
SEQRES 10 B 554 ARG ILE LEU PRO SER VAL PRO ARG ASP CYS PRO THR PRO
SEQRES 11 B 554 MET GLY THR LYS GLY LYS LYS GLN LEU PRO ASP ALA GLU
SEQRES 12 B 554 PHE LEU SER ARG ARG PHE LEU LEU ARG ARG LYS PHE ILE
SEQRES 13 B 554 PRO ASP PRO GLN GLY THR ASN LEU MET PHE ALA PHE PHE
SEQRES 14 B 554 ALA GLN HIS PHE THR HIS GLN PHE PHE LYS THR SER GLY
SEQRES 15 B 554 LYS MET GLY PRO GLY PHE THR LYS ALA LEU GLY HIS GLY
SEQRES 16 B 554 VAL ASP LEU GLY HIS ILE TYR GLY ASP ASN LEU GLU ARG
SEQRES 17 B 554 GLN TYR GLN LEU ARG LEU PHE LYS ASP GLY LYS LEU LYS
SEQRES 18 B 554 TYR GLN MET LEU ASN GLY GLU VAL TYR PRO PRO SER VAL
SEQRES 19 B 554 GLU GLU ALA PRO VAL LEU MET HIS TYR PRO ARG GLY ILE
SEQRES 20 B 554 PRO PRO GLN SER GLN MET ALA VAL GLY GLN GLU VAL PHE
SEQRES 21 B 554 GLY LEU LEU PRO GLY LEU MET LEU TYR ALA THR ILE TRP
SEQRES 22 B 554 LEU ARG GLU HIS GLN ARG VAL CYS ASP LEU LEU LYS ALA
SEQRES 23 B 554 GLU HIS PRO THR TRP GLY ASP GLU GLN LEU PHE GLN THR
SEQRES 24 B 554 ALA LYS LEU ILE LEU ILE GLY GLU THR ILE LYS ILE VAL
SEQRES 25 B 554 ILE GLU GLU TYR VAL GLN GLN LEU SER GLY TYR PHE LEU
SEQRES 26 B 554 GLN LEU LYS PHE ASP PRO GLU LEU LEU PHE GLY ALA GLN
SEQRES 27 B 554 PHE GLN TYR ARG ASN ARG ILE ALA MET GLU PHE ASN GLN
SEQRES 28 B 554 LEU TYR HIS TRP HIS PRO LEU MET PRO ASP SER PHE ARG
SEQRES 29 B 554 VAL GLY PRO GLN ASP TYR SER TYR GLU GLN PHE LEU PHE
SEQRES 30 B 554 ASN THR SER MET LEU VAL ASP TYR GLY VAL GLU ALA LEU
SEQRES 31 B 554 VAL ASP ALA PHE SER ARG GLN PRO ALA GLY ARG ILE GLY
SEQRES 32 B 554 GLY GLY ARG ASN ILE ASP HIS HIS ILE LEU HIS VAL ALA
SEQRES 33 B 554 VAL ASP VAL ILE LYS GLU SER ARG VAL LEU ARG LEU GLN
SEQRES 34 B 554 PRO PHE ASN GLU TYR ARG LYS ARG PHE GLY MET LYS PRO
SEQRES 35 B 554 TYR THR SER PHE GLN GLU LEU THR GLY GLU LYS GLU MET
SEQRES 36 B 554 ALA ALA GLU LEU GLU GLU LEU TYR GLY ASP ILE ASP ALA
SEQRES 37 B 554 LEU GLU PHE TYR PRO GLY LEU LEU LEU GLU LYS CYS HIS
SEQRES 38 B 554 PRO ASN SER ILE PHE GLY GLU SER MET ILE GLU MET GLY
SEQRES 39 B 554 ALA PRO PHE SER LEU LYS GLY LEU LEU GLY ASN PRO ILE
SEQRES 40 B 554 CYS SER PRO GLU TYR TRP LYS ALA SER THR PHE GLY GLY
SEQRES 41 B 554 GLU VAL GLY PHE ASN LEU VAL LYS THR ALA THR LEU LYS
SEQRES 42 B 554 LYS LEU VAL CYS LEU ASN THR LYS THR CYS PRO TYR VAL
SEQRES 43 B 554 SER PHE HIS VAL PRO ASP PRO ARG
HET HEM A 601 43
HET HEM B 601 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
HELIX 1 AA ILE A 74 LEU A 82 1 9
HELIX 2 BA PRO A 86 LEU A 92 1 7
HELIX 3 CA ARG A 97 ALA A 105 1 9
HELIX 4 DA ILE A 108 ASN A 122 1 15
HELIX 5 EA TRP A 139 SER A 143 1 5
HELIX 6 1A ALA A 174 PHE A 181 1 8
HELIX 7 2A LEU A 196 HIS A 207 1 12
HELIX 8 3A LEU A 238 LEU A 244 1 7
HELIX 9 5A PRO A 296 GLU A 319 1 24
HELIX 10 6A ASP A 325 SER A 353 1 29
HELIX 11 8A MET A 379 TYR A 385 1 7
HELIX 12 9A MET A 413 TYR A 417 1 5
HELIX 13 10A VAL A 419 ARG A 428 1 10
HELIX 14 11A LEU A 445 VAL A 457 111/12 13
HELIX 15 13A PHE A 463 ARG A 469 1 7
HELIX 16 14A PHE A 478 THR A 482 1 5
HELIX 17 15A GLU A 486 TYR A 495 1 10
HELIX 18 16A PHE A 503 LEU A 509 1 7
HELIX 19 17A GLU A 520 LEU A 535 1 16
HELIX 20 18A GLU A 553 THR A 561 1 9
HELIX 21 19A LEU A 564 CYS A 569 1 6
HELIX 22 AB ILE B 74 LEU B 82 1 9
HELIX 23 BB PRO B 86 LEU B 92 1 7
HELIX 24 CB ARG B 97 ALA B 105 1 9
HELIX 25 DB ILE B 108 ASN B 122 1 15
HELIX 26 EB TRP B 139 SER B 143 1 5
HELIX 27 1B ALA B 174 PHE B 181 1 8
HELIX 28 2B LEU B 196 HIS B 207 1 12
HELIX 29 3B LEU B 238 LEU B 244 1 7
HELIX 30 5B PRO B 296 GLU B 319 1 24
HELIX 31 6B ASP B 325 SER B 353 1 29
HELIX 32 8B MET B 379 TYR B 385 1 7
HELIX 33 9B MET B 413 TYR B 417 1 5
HELIX 34 10B VAL B 419 ARG B 428 1 10
HELIX 35 11B LEU B 445 VAL B 457 111/12 13
HELIX 36 13B PHE B 463 ARG B 469 1 7
HELIX 37 14B PHE B 478 THR B 482 1 5
HELIX 38 15B GLU B 486 TYR B 495 1 10
HELIX 39 16B PHE B 503 LEU B 509 1 7
HELIX 40 17B GLU B 520 LEU B 535 1 16
HELIX 41 18B GLU B 553 THR B 561 1 9
HELIX 42 19B LEU B 564 CYS B 569 1 6
SHEET 1 A 2 ILE A 46 ARG A 49 0
SHEET 2 A 2 TYR A 55 ASP A 58 -1 O GLN A 56 N VAL A 48
SHEET 1 B 2 TYR A 64 SER A 65 0
SHEET 2 B 2 ILE A 71 PRO A 72 -1 N ILE A 71 O SER A 65
SHEET 1 C 2 THR A 212 GLY A 214 0
SHEET 2 C 2 GLY A 217 THR A 221 -1 O GLY A 217 N GLY A 214
SHEET 1 D 2 GLN A 255 LEU A 257 0
SHEET 2 D 2 GLU A 260 TYR A 262 -1 O GLU A 260 N LEU A 257
SHEET 1 E 2 PHE A 395 VAL A 397 0
SHEET 2 E 2 GLN A 400 TYR A 402 -1 N GLN A 400 O VAL A 397
SHEET 1 F 2 ILE B 46 ARG B 49 0
SHEET 2 F 2 TYR B 55 ASP B 58 -1 O GLN B 56 N VAL B 48
SHEET 1 G 2 TYR B 64 SER B 65 0
SHEET 2 G 2 ILE B 71 PRO B 72 -1 N ILE B 71 O SER B 65
SHEET 1 H 2 THR B 212 GLY B 214 0
SHEET 2 H 2 GLY B 217 THR B 221 -1 O GLY B 217 N GLY B 214
SHEET 1 I 2 GLN B 255 LEU B 257 0
SHEET 2 I 2 GLU B 260 TYR B 262 -1 O GLU B 260 N LEU B 257
SHEET 1 J 2 PHE B 395 VAL B 397 0
SHEET 2 J 2 GLN B 400 TYR B 402 -1 N GLN B 400 O VAL B 397
SSBOND 1 CYS A 36 CYS A 47 1555 1555 2.01
SSBOND 2 CYS A 37 CYS A 159 1555 1555 2.03
SSBOND 3 CYS A 41 CYS A 57 1555 1555 2.01
SSBOND 4 CYS A 59 CYS A 69 1555 1555 2.01
SSBOND 5 CYS A 569 CYS A 575 1555 1555 2.03
SSBOND 6 CYS B 36 CYS B 47 1555 1555 2.02
SSBOND 7 CYS B 37 CYS B 159 1555 1555 2.03
SSBOND 8 CYS B 41 CYS B 57 1555 1555 2.00
SSBOND 9 CYS B 59 CYS B 69 1555 1555 2.01
SSBOND 10 CYS B 569 CYS B 575 1555 1555 2.04
LINK FE HEM A 601 NE2 HIS A 388 1555 1555 2.14
LINK FE HEM B 601 NE2 HIS B 388 1555 1555 2.15
CISPEP 1 SER A 126 PRO A 127 0 -9.23
CISPEP 2 SER B 126 PRO B 127 0 -9.21
SITE 1 COX 4 ARG A 120 SER A 530 TYR A 385 GLU A 524
SITE 1 PER 4 GLN A 203 HIS A 207 HIS A 388 HEM A 601
SITE 1 AC1 17 TYR A 148 ALA A 199 GLN A 203 THR A 206
SITE 2 AC1 17 HIS A 207 PHE A 210 THR A 212 LEU A 295
SITE 3 AC1 17 ASN A 382 TYR A 385 HIS A 386 HIS A 388
SITE 4 AC1 17 LEU A 390 MET A 391 LEU A 408 ILE A 444
SITE 5 AC1 17 ASP A 450
SITE 1 AC2 17 TYR B 148 ALA B 199 GLN B 203 THR B 206
SITE 2 AC2 17 HIS B 207 PHE B 210 THR B 212 LEU B 295
SITE 3 AC2 17 ASN B 382 TYR B 385 HIS B 386 HIS B 388
SITE 4 AC2 17 LEU B 390 MET B 391 LEU B 408 ILE B 444
SITE 5 AC2 17 ASP B 450
CRYST1 99.400 210.300 233.100 90.00 90.00 90.00 I 2 2 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 0.010060 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004755 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004290 0.00000
MTRIX1 1 -0.995340 -0.059900 0.075620 81.43000 1
MTRIX2 1 -0.059260 -0.238880 -0.969240 234.50500 1
MTRIX3 1 0.076120 -0.969200 0.234220 179.08299 1
(ATOM LINES ARE NOT SHOWN.)
END
