HEADER PHOSPHOTRANSFERASE 12-JUN-97 1TMK
TITLE YEAST THYMIDYLATE KINASE COMPLEXED WITH THYMIDINE MONOPHOSPHATE (DTMP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.4.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: CDC8;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE (PHOSPHOTRANSFERASE), KINASE, THYMIDINE ACTIVATION
KEYWDS 2 PATHWAY, ENZYME, PHOSPHOTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LAVIE,I.SCHLICHTING
REVDAT 3 14-FEB-24 1TMK 1 REMARK
REVDAT 2 24-FEB-09 1TMK 1 VERSN
REVDAT 1 17-JUN-98 1TMK 0
JRNL AUTH A.LAVIE,I.R.VETTER,M.KONRAD,R.S.GOODY,J.REINSTEIN,
JRNL AUTH 2 I.SCHLICHTING
JRNL TITL STRUCTURE OF THYMIDYLATE KINASE REVEALS THE CAUSE BEHIND THE
JRNL TITL 2 LIMITING STEP IN AZT ACTIVATION.
JRNL REF NAT.STRUCT.BIOL. V. 4 601 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9253404
JRNL DOI 10.1038/NSB0897-601
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.LAVIE,I.SCHLICHTING,I.R.VETTER,M.KONRAD,J.REINSTEIN,
REMARK 1 AUTH 2 R.S.GOODY
REMARK 1 TITL THE BOTTLENECK IN AZT ACTIVATION
REMARK 1 REF NAT.MED. (N.Y.) V. 3 922 1997
REMARK 1 REFN ISSN 1078-8956
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 23520
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1134
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.14
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 65.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 862
REMARK 3 BIN R VALUE (WORKING SET) : 0.2589
REMARK 3 BIN FREE R VALUE : 0.3238
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 38
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 : 3296
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 282
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.00
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.520
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.680
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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM11.DNA
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TMP.TOPH
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TMK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176732.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : APR-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : MACSCIENCE
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25398
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 12.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
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) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28100
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIR WITH NCS
REMARK 200 SOFTWARE USED: X-PLOR 3.8
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000 100 MM HEPES PH 7.5 25 MM
REMARK 280 MGAC
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 70.60000
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 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: 3170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 MET A 1
REMARK 465 MET A 2
REMARK 465 ASP A 136
REMARK 465 VAL A 137
REMARK 465 ASP A 138
REMARK 465 ASN A 139
REMARK 465 ASN A 140
REMARK 465 ALA A 141
REMARK 465 GLU A 142
REMARK 465 LYS A 143
REMARK 465 SER A 144
REMARK 465 GLY A 145
REMARK 465 MET B 1
REMARK 465 MET B 2
REMARK 465 ASP B 136
REMARK 465 VAL B 137
REMARK 465 ASP B 138
REMARK 465 ASN B 139
REMARK 465 ASN B 140
REMARK 465 ALA B 141
REMARK 465 GLU B 142
REMARK 465 LYS B 143
REMARK 465 SER B 144
REMARK 465 GLY B 145
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 ARG A 94 150.22 83.38
REMARK 500 TYR A 95 -139.74 -165.75
REMARK 500 ARG B 15 65.87 84.14
REMARK 500 PHE B 58 103.35 -54.21
REMARK 500 SER B 61 157.36 -49.56
REMARK 500 ARG B 94 144.42 80.44
REMARK 500 TYR B 95 -142.48 -162.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP A 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TMP B 217
DBREF 1TMK A 1 216 UNP P00572 KTHY_YEAST 1 216
DBREF 1TMK B 1 216 UNP P00572 KTHY_YEAST 1 216
SEQRES 1 A 216 MET MET GLY ARG GLY LYS LEU ILE LEU ILE GLU GLY LEU
SEQRES 2 A 216 ASP ARG THR GLY LYS THR THR GLN CYS ASN ILE LEU TYR
SEQRES 3 A 216 LYS LYS LEU GLN PRO ASN CYS LYS LEU LEU LYS PHE PRO
SEQRES 4 A 216 GLU ARG SER THR ARG ILE GLY GLY LEU ILE ASN GLU TYR
SEQRES 5 A 216 LEU THR ASP ASP SER PHE GLN LEU SER ASP GLN ALA ILE
SEQRES 6 A 216 HIS LEU LEU PHE SER ALA ASN ARG TRP GLU ILE VAL ASP
SEQRES 7 A 216 LYS ILE LYS LYS ASP LEU LEU GLU GLY LYS ASN ILE VAL
SEQRES 8 A 216 MET ASP ARG TYR VAL TYR SER GLY VAL ALA TYR SER ALA
SEQRES 9 A 216 ALA LYS GLY THR ASN GLY MET ASP LEU ASP TRP CYS LEU
SEQRES 10 A 216 GLN PRO ASP VAL GLY LEU LEU LYS PRO ASP LEU THR LEU
SEQRES 11 A 216 PHE LEU SER THR GLN ASP VAL ASP ASN ASN ALA GLU LYS
SEQRES 12 A 216 SER GLY PHE GLY ASP GLU ARG TYR GLU THR VAL LYS PHE
SEQRES 13 A 216 GLN GLU LYS VAL LYS GLN THR PHE MET LYS LEU LEU ASP
SEQRES 14 A 216 LYS GLU ILE ARG LYS GLY ASP GLU SER ILE THR ILE VAL
SEQRES 15 A 216 ASP VAL THR ASN LYS GLY ILE GLN GLU VAL GLU ALA LEU
SEQRES 16 A 216 ILE TRP GLN ILE VAL GLU PRO VAL LEU SER THR HIS ILE
SEQRES 17 A 216 ASP HIS ASP LYS PHE SER PHE PHE
SEQRES 1 B 216 MET MET GLY ARG GLY LYS LEU ILE LEU ILE GLU GLY LEU
SEQRES 2 B 216 ASP ARG THR GLY LYS THR THR GLN CYS ASN ILE LEU TYR
SEQRES 3 B 216 LYS LYS LEU GLN PRO ASN CYS LYS LEU LEU LYS PHE PRO
SEQRES 4 B 216 GLU ARG SER THR ARG ILE GLY GLY LEU ILE ASN GLU TYR
SEQRES 5 B 216 LEU THR ASP ASP SER PHE GLN LEU SER ASP GLN ALA ILE
SEQRES 6 B 216 HIS LEU LEU PHE SER ALA ASN ARG TRP GLU ILE VAL ASP
SEQRES 7 B 216 LYS ILE LYS LYS ASP LEU LEU GLU GLY LYS ASN ILE VAL
SEQRES 8 B 216 MET ASP ARG TYR VAL TYR SER GLY VAL ALA TYR SER ALA
SEQRES 9 B 216 ALA LYS GLY THR ASN GLY MET ASP LEU ASP TRP CYS LEU
SEQRES 10 B 216 GLN PRO ASP VAL GLY LEU LEU LYS PRO ASP LEU THR LEU
SEQRES 11 B 216 PHE LEU SER THR GLN ASP VAL ASP ASN ASN ALA GLU LYS
SEQRES 12 B 216 SER GLY PHE GLY ASP GLU ARG TYR GLU THR VAL LYS PHE
SEQRES 13 B 216 GLN GLU LYS VAL LYS GLN THR PHE MET LYS LEU LEU ASP
SEQRES 14 B 216 LYS GLU ILE ARG LYS GLY ASP GLU SER ILE THR ILE VAL
SEQRES 15 B 216 ASP VAL THR ASN LYS GLY ILE GLN GLU VAL GLU ALA LEU
SEQRES 16 B 216 ILE TRP GLN ILE VAL GLU PRO VAL LEU SER THR HIS ILE
SEQRES 17 B 216 ASP HIS ASP LYS PHE SER PHE PHE
HET TMP A 217 21
HET SO4 B 218 5
HET TMP B 217 21
HETNAM TMP THYMIDINE-5'-PHOSPHATE
HETNAM SO4 SULFATE ION
FORMUL 3 TMP 2(C10 H15 N2 O8 P)
FORMUL 4 SO4 O4 S 2-
FORMUL 6 HOH *282(H2 O)
HELIX 1 1 LYS A 18 LYS A 28 1 11
HELIX 2 2 ARG A 44 THR A 54 1 11
HELIX 3 3 ASP A 62 TRP A 74 1 13
HELIX 4 4 VAL A 77 LEU A 85 1 9
HELIX 5 5 VAL A 96 LYS A 106 1 11
HELIX 6 6 LEU A 113 ASP A 120 1 8
HELIX 7 7 VAL A 154 ARG A 173 1 20
HELIX 8 8 ILE A 189 SER A 205 1 17
HELIX 9 9 LYS B 18 LYS B 28 1 11
HELIX 10 10 ARG B 44 THR B 54 1 11
HELIX 11 11 ASP B 62 TRP B 74 1 13
HELIX 12 12 VAL B 77 LEU B 85 1 9
HELIX 13 13 VAL B 96 LYS B 106 1 11
HELIX 14 14 LEU B 113 ASP B 120 1 8
HELIX 15 15 VAL B 154 ARG B 173 1 20
HELIX 16 16 ILE B 189 LEU B 204 1 16
SHEET 1 A 5 ILE A 179 ASP A 183 0
SHEET 2 A 5 LEU A 128 SER A 133 1 N THR A 129 O THR A 180
SHEET 3 A 5 LEU A 7 GLY A 12 1 N LEU A 9 O LEU A 128
SHEET 4 A 5 ASN A 89 ASP A 93 1 N ILE A 90 O ILE A 8
SHEET 5 A 5 CYS A 33 LYS A 37 1 N LYS A 34 O ASN A 89
SHEET 1 B 5 ILE B 179 ASP B 183 0
SHEET 2 B 5 LEU B 128 SER B 133 1 N THR B 129 O THR B 180
SHEET 3 B 5 LEU B 7 GLY B 12 1 N LEU B 9 O LEU B 128
SHEET 4 B 5 ASN B 89 ASP B 93 1 N ILE B 90 O ILE B 8
SHEET 5 B 5 CYS B 33 LYS B 37 1 N LYS B 34 O ASN B 89
CISPEP 1 GLN A 30 PRO A 31 0 16.01
CISPEP 2 PHE A 38 PRO A 39 0 -0.15
CISPEP 3 GLN B 30 PRO B 31 0 -3.27
CISPEP 4 PHE B 38 PRO B 39 0 1.43
SITE 1 AC1 10 ASP B 14 ARG B 15 THR B 16 GLY B 17
SITE 2 AC1 10 LYS B 18 THR B 19 HOH B1035 HOH B1036
SITE 3 AC1 10 HOH B1203 HOH B1352
SITE 1 AC2 19 ASP A 14 LYS A 37 PHE A 38 ARG A 41
SITE 2 AC2 19 LEU A 53 PHE A 69 ARG A 73 ARG A 94
SITE 3 AC2 19 SER A 98 GLY A 99 TYR A 102 TYR A 151
SITE 4 AC2 19 HOH A1235 HOH A1236 HOH A1241 HOH A1301
SITE 5 AC2 19 HOH A1302 HOH A1303 HOH A1304
SITE 1 AC3 18 ASP B 14 LYS B 37 PHE B 38 PRO B 39
SITE 2 AC3 18 ARG B 41 LEU B 53 PHE B 69 ARG B 73
SITE 3 AC3 18 ARG B 94 GLY B 99 TYR B 102 GLU B 149
SITE 4 AC3 18 TYR B 151 HOH B1029 HOH B1030 HOH B1036
SITE 5 AC3 18 HOH B1037 HOH B1038
CRYST1 36.450 141.200 48.750 90.00 109.35 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 0.027435 0.000000 0.009634 0.00000
SCALE2 0.000000 0.007082 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021741 0.00000
MTRIX1 1 0.983800 -0.162700 -0.075800 3.49690 1
MTRIX2 1 -0.162900 -0.986600 0.003000 38.29280 1
MTRIX3 1 -0.075300 0.009400 -0.997100 8.71750 1
(ATOM LINES ARE NOT SHOWN.)
END
