HEADER ISOMERASE/ISOMERASE INHIBITOR 26-MAR-12 4EC0
TITLE CRYSTAL STRUCTURE OF HH-PGDS WITH WATER DISPLACING INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: H-PGDS, GST CLASS-SIGMA, GLUTATHIONE S-TRANSFERASE,
COMPND 5 GLUTATHIONE-DEPENDENT PGD SYNTHASE, GLUTATHIONE-REQUIRING
COMPND 6 PROSTAGLANDIN D SYNTHASE, PROSTAGLANDIN-H2 D-ISOMERASE;
COMPND 7 EC: 5.3.99.2, 2.5.1.18;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GSTS, HPGDS, PGDS, PTGDS2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, SOLVENT REPLACEMENT, ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.DAY,A.THORARENSEN,J.I.TRUJILLO
REVDAT 4 28-FEB-24 4EC0 1 REMARK SEQADV LINK
REVDAT 3 15-NOV-17 4EC0 1 REMARK
REVDAT 2 02-JAN-13 4EC0 1 JRNL
REVDAT 1 16-MAY-12 4EC0 0
JRNL AUTH J.I.TRUJILLO,J.R.KIEFER,W.HUANG,J.E.DAY,J.MOON,G.M.JEROME,
JRNL AUTH 2 C.P.BONO,C.M.KORNMEIER,M.L.WILLIAMS,C.KUHN,G.R.RENNIE,
JRNL AUTH 3 T.A.WYNN,C.P.CARRON,A.THORARENSEN
JRNL TITL INVESTIGATION OF THE BINDING POCKET OF HUMAN HEMATOPOIETIC
JRNL TITL 2 PROSTAGLANDIN (PG) D2 SYNTHASE (HH-PGDS): A TALE OF TWO
JRNL TITL 3 WATERS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 3795 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 22546671
JRNL DOI 10.1016/J.BMCL.2012.04.004
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
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 : 32124
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) : 0.186
REMARK 3 FREE R VALUE : 0.252
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 : 3302
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 761
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.48
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) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
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: NULL
REMARK 4
REMARK 4 4EC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071427.
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 : 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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32926
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
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 (%): 41.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 38.85300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 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 HIS A 0
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 GLN A 36 -18.35 -49.56
REMARK 500 SER A 44 5.61 -63.10
REMARK 500 GLN A 63 106.09 76.63
REMARK 500 GLN B1063 104.88 72.57
REMARK 500 GLU B1106 127.35 -12.77
REMARK 500 GLU B1113 0.71 -68.90
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 412 O
REMARK 620 2 HOH A 423 O 83.5
REMARK 620 3 HOH A 459 O 90.7 88.2
REMARK 620 4 HOH B1372 O 91.9 173.4 87.1
REMARK 620 5 HOH B1384 O 167.9 85.9 94.9 99.1
REMARK 620 6 HOH B1437 O 89.2 92.4 179.4 92.3 85.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7PQ A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH B 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EE0 RELATED DB: PDB
REMARK 900 RELATED ID: 4EDY RELATED DB: PDB
REMARK 900 RELATED ID: 4EDZ RELATED DB: PDB
DBREF 4EC0 A 1 199 UNP O60760 HPGDS_HUMAN 1 199
DBREF 4EC0 B 1001 1199 UNP O60760 HPGDS_HUMAN 1 199
SEQADV 4EC0 HIS A 0 UNP O60760 EXPRESSION TAG
SEQADV 4EC0 HIS B 1000 UNP O60760 EXPRESSION TAG
SEQRES 1 A 200 HIS MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG
SEQRES 2 A 200 GLY ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU
SEQRES 3 A 200 ASP ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP
SEQRES 4 A 200 TRP PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE
SEQRES 5 A 200 PRO ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER
SEQRES 6 A 200 LEU ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU
SEQRES 7 A 200 ALA GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA
SEQRES 8 A 200 ILE VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO
SEQRES 9 A 200 TRP ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE
SEQRES 10 A 200 ASN GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN
SEQRES 11 A 200 ASP LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE
SEQRES 12 A 200 GLY ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE
SEQRES 13 A 200 CYS SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU
SEQRES 14 A 200 ASP ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL
SEQRES 15 A 200 GLN ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG
SEQRES 16 A 200 PRO GLN THR LYS LEU
SEQRES 1 B 200 HIS MET PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG
SEQRES 2 B 200 GLY ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU
SEQRES 3 B 200 ASP ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP
SEQRES 4 B 200 TRP PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE
SEQRES 5 B 200 PRO ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER
SEQRES 6 B 200 LEU ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU
SEQRES 7 B 200 ALA GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA
SEQRES 8 B 200 ILE VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO
SEQRES 9 B 200 TRP ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE
SEQRES 10 B 200 ASN GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN
SEQRES 11 B 200 ASP LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE
SEQRES 12 B 200 GLY ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE
SEQRES 13 B 200 CYS SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU
SEQRES 14 B 200 ASP ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL
SEQRES 15 B 200 GLN ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG
SEQRES 16 B 200 PRO GLN THR LYS LEU
HET GSH A 201 20
HET MG A 202 1
HET 7PQ A 203 29
HET GSH B1201 20
HETNAM GSH GLUTATHIONE
HETNAM MG MAGNESIUM ION
HETNAM 7PQ 4-[2-(AMINOMETHYL)NAPHTHALEN-1-YL]-N-[2-(MORPHOLIN-4-
HETNAM 2 7PQ YL)ETHYL]BENZAMIDE
FORMUL 3 GSH 2(C10 H17 N3 O6 S)
FORMUL 4 MG MG 2+
FORMUL 5 7PQ C24 H27 N3 O2
FORMUL 7 HOH *761(H2 O)
HELIX 1 1 ALA A 15 ASP A 26 1 12
HELIX 2 2 ASP A 38 LYS A 43 1 6
HELIX 3 3 SER A 44 LEU A 46 5 3
HELIX 4 4 GLN A 63 LYS A 73 1 11
HELIX 5 5 THR A 81 CYS A 101 1 21
HELIX 6 6 LYS A 108 TYR A 122 1 15
HELIX 7 7 TYR A 122 GLY A 136 1 15
HELIX 8 8 THR A 147 LYS A 164 1 18
HELIX 9 9 HIS A 171 ALA A 183 1 13
HELIX 10 10 ILE A 184 ARG A 194 1 11
HELIX 11 11 ALA B 1015 LEU B 1025 1 11
HELIX 12 12 GLU B 1035 ALA B 1037 5 3
HELIX 13 13 ASP B 1038 THR B 1045 1 8
HELIX 14 14 GLN B 1063 LYS B 1073 1 11
HELIX 15 15 THR B 1081 SER B 1100 1 20
HELIX 16 16 LYS B 1108 ASN B 1123 1 16
HELIX 17 17 ASN B 1123 GLY B 1136 1 14
HELIX 18 18 THR B 1147 LYS B 1164 1 18
HELIX 19 19 HIS B 1171 ILE B 1184 1 14
HELIX 20 20 ILE B 1184 ARG B 1194 1 11
SHEET 1 A 4 GLU A 30 ARG A 33 0
SHEET 2 A 4 TYR A 4 TYR A 8 1 N TYR A 4 O GLU A 30
SHEET 3 A 4 ILE A 53 VAL A 56 -1 O GLU A 55 N LYS A 5
SHEET 4 A 4 LEU A 59 HIS A 62 -1 O LEU A 59 N VAL A 56
SHEET 1 B 4 GLU B1030 ILE B1034 0
SHEET 2 B 4 TYR B1004 PHE B1009 1 N LEU B1006 O GLU B1030
SHEET 3 B 4 ILE B1053 VAL B1056 -1 O GLU B1055 N LYS B1005
SHEET 4 B 4 LEU B1059 HIS B1062 -1 O LEU B1059 N VAL B1056
LINK MG MG A 202 O HOH A 412 1555 1555 2.30
LINK MG MG A 202 O HOH A 423 1555 1555 2.36
LINK MG MG A 202 O HOH A 459 1555 1555 2.28
LINK MG MG A 202 O HOH B1372 1555 1555 2.34
LINK MG MG A 202 O HOH B1384 1555 1555 2.39
LINK MG MG A 202 O HOH B1437 1555 1555 2.26
CISPEP 1 ILE A 51 PRO A 52 0 0.80
CISPEP 2 ILE B 1051 PRO B 1052 0 0.76
SITE 1 AC1 17 TYR A 8 ARG A 14 TRP A 39 LYS A 43
SITE 2 AC1 17 LYS A 50 ILE A 51 PRO A 52 GLN A 63
SITE 3 AC1 17 SER A 64 7PQ A 203 HOH A 301 HOH A 402
SITE 4 AC1 17 HOH A 464 HOH A 472 HOH A 652 HOH A 684
SITE 5 AC1 17 ASP B1097
SITE 1 AC2 6 HOH A 412 HOH A 423 HOH A 459 HOH B1372
SITE 2 AC2 6 HOH B1384 HOH B1437
SITE 1 AC3 11 TYR A 8 GLY A 13 ARG A 14 ASP A 96
SITE 2 AC3 11 MET A 99 TRP A 104 TYR A 152 THR A 159
SITE 3 AC3 11 LEU A 199 GSH A 201 HOH A 461
SITE 1 AC4 15 ASP A 97 TYR B1008 ARG B1014 TRP B1039
SITE 2 AC4 15 LYS B1043 LYS B1050 ILE B1051 GLN B1063
SITE 3 AC4 15 SER B1064 HOH B1309 HOH B1353 HOH B1404
SITE 4 AC4 15 HOH B1430 HOH B1438 HOH B1649
CRYST1 48.740 77.706 52.449 90.00 91.56 90.00 P 1 21 1 4
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 0.020517 0.000000 0.000559 0.00000
SCALE2 0.000000 0.012869 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
