HEADER TRANSFERASE 08-MAY-13 4KN6
TITLE CRYSTAL STRUCTURE OF HUMAN HYPOXANTHINE-GUANINE
TITLE 2 PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH 6-FLUORO-3-HYDROXY-2-
TITLE 3 PYRAZINECARBOXAMIDE (T-705) RIBOSE-5'-MONOPHOSPHATE
CAVEAT 4KN6 RESIDUES A GLY 57 AND A HIS 59 ARE LINKED TOGETHER (RESIDUE
CAVEAT 2 4KN6 A GLY 58 IS OMITTED). RESIDUES A ASP 89 AND A SER 90 ARE
CAVEAT 3 4KN6 LINKED TOGETHER (RESIDUE A ARG 90 IS OMITTED).
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HGPRT, HGPRTASE;
COMPND 5 EC: 2.4.2.8;
COMPND 6 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: HPRT1, HPRT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FAVIPIRAVIR, 6-OXOPURINE PHOSPHORIBOSYLTRANSFERASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.NAESENS,L.GUDDAT,D.KEOUGH,A.B.P.VAN KUILENBURG,J.MEIJER,J.VANDE
AUTHOR 2 VOORDE,J.BALZARINI
REVDAT 3 28-FEB-24 4KN6 1 REMARK
REVDAT 2 25-SEP-13 4KN6 1 JRNL
REVDAT 1 14-AUG-13 4KN6 0
JRNL AUTH L.NAESENS,L.W.GUDDAT,D.T.KEOUGH,A.B.VAN KUILENBURG,J.MEIJER,
JRNL AUTH 2 J.VANDE VOORDE,J.BALZARINI
JRNL TITL ROLE OF HUMAN HYPOXANTHINE GUANINE PHOSPHORIBOSYLTRANSFERASE
JRNL TITL 2 IN ACTIVATION OF THE ANTIVIRAL AGENT T-705 (FAVIPIRAVIR).
JRNL REF MOL.PHARMACOL. V. 84 615 2013
JRNL REFN ISSN 0026-895X
JRNL PMID 23907213
JRNL DOI 10.1124/MOL.113.087247
REMARK 2
REMARK 2 RESOLUTION. 2.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 5282
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.251
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.020
REMARK 3 FREE R VALUE TEST SET COUNT : 529
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.0623 - 4.3292 1.00 1243 138 0.2342 0.2267
REMARK 3 2 4.3292 - 3.4367 1.00 1188 133 0.2309 0.2650
REMARK 3 3 3.4367 - 3.0024 1.00 1163 130 0.2642 0.3289
REMARK 3 4 3.0024 - 2.7280 1.00 1159 128 0.3036 0.3935
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.030
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 1573
REMARK 3 ANGLE : 0.614 2136
REMARK 3 CHIRALITY : 0.038 241
REMARK 3 PLANARITY : 0.002 270
REMARK 3 DIHEDRAL : 14.493 602
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4941 -15.3217 -12.5730
REMARK 3 T TENSOR
REMARK 3 T11: 0.2466 T22: 0.2477
REMARK 3 T33: 0.2274 T12: 0.0082
REMARK 3 T13: -0.0462 T23: -0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 3.4368 L22: 3.2815
REMARK 3 L33: 1.5382 L12: 0.0681
REMARK 3 L13: -1.2033 L23: -0.3172
REMARK 3 S TENSOR
REMARK 3 S11: 0.0675 S12: 0.1483 S13: -0.3412
REMARK 3 S21: -0.1610 S22: -0.0122 S23: 0.2811
REMARK 3 S31: 0.1427 S32: -0.1566 S33: -0.0465
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4KN6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079547.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95369
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 5283
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.728
REMARK 200 RESOLUTION RANGE LOW (A) : 43.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
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) : 2.73
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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM CHLORIDE, 1 M
REMARK 280 SODIUM/POTASSIUM TARTRATE, 0.1 M IMIDAZOLE, PH 8.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
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 23.42900
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.70000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 54.56700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.42900
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.70000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.56700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.42900
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 36.70000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.56700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.42900
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 36.70000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 54.56700
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 413 LIES ON A SPECIAL POSITION.
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 THR A 2
REMARK 465 ARG A 3
REMARK 465 GLY A 58
REMARK 465 ARG A 89A
REMARK 465 SER A 103
REMARK 465 TYR A 104
REMARK 465 CYS A 105
REMARK 465 ASN A 106
REMARK 465 ASP A 107
REMARK 465 GLN A 108
REMARK 465 SER A 109
REMARK 465 THR A 110
REMARK 465 GLY A 111
REMARK 465 ASP A 112
REMARK 465 ILE A 113
REMARK 465 LYS A 114
REMARK 465 VAL A 115
REMARK 465 ILE A 116
REMARK 465 GLY A 117
REMARK 465 GLY A 118
REMARK 465 ASP A 119
REMARK 465 ASP A 120
REMARK 465 LEU A 121
REMARK 465 SER A 122
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 CYS A 22 SG
REMARK 470 SER A 90 OG
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 CYS A 205 SG
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 401 O HOH A 411 2.04
REMARK 500 OD2 ASP A 76 OH TYR A 190 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 420 O HOH A 420 3555 2.05
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 HIS A 60 117.10 -13.63
REMARK 500 LYS A 68 -102.64 -123.36
REMARK 500 TYR A 71 -15.43 -141.59
REMARK 500 ARG A 86 2.83 -68.13
REMARK 500 SER A 88 -97.55 151.14
REMARK 500 MET A 94 116.68 -164.32
REMARK 500 ASP A 137 -71.80 -103.26
REMARK 500 TYR A 190 -80.39 55.41
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 1RP A 301
DBREF 4KN6 A 2 217 UNP P00492 HPRT_HUMAN 3 218
SEQRES 1 A 216 THR ARG SER PRO GLY VAL VAL ILE SER ASP ASP GLU PRO
SEQRES 2 A 216 GLY TYR ASP LEU ASP LEU PHE CYS ILE PRO ASN HIS TYR
SEQRES 3 A 216 ALA GLU ASP LEU GLU ARG VAL PHE ILE PRO HIS GLY LEU
SEQRES 4 A 216 ILE MET ASP ARG THR GLU ARG LEU ALA ARG ASP VAL MET
SEQRES 5 A 216 LYS GLU MET GLY GLY HIS HIS ILE VAL ALA LEU CYS VAL
SEQRES 6 A 216 LEU LYS GLY GLY TYR LYS PHE PHE ALA ASP LEU LEU ASP
SEQRES 7 A 216 TYR ILE LYS ALA LEU ASN ARG ASN SER ASP ARG SER ILE
SEQRES 8 A 216 PRO MET THR VAL ASP PHE ILE ARG LEU LYS SER TYR CYS
SEQRES 9 A 216 ASN ASP GLN SER THR GLY ASP ILE LYS VAL ILE GLY GLY
SEQRES 10 A 216 ASP ASP LEU SER THR LEU THR GLY LYS ASN VAL LEU ILE
SEQRES 11 A 216 VAL GLU ASP ILE ILE ASP THR GLY LYS THR MET GLN THR
SEQRES 12 A 216 LEU LEU SER LEU VAL ARG GLN TYR ASN PRO LYS MET VAL
SEQRES 13 A 216 LYS VAL ALA SER LEU LEU VAL LYS ARG THR PRO ARG SER
SEQRES 14 A 216 VAL GLY TYR LYS PRO ASP PHE VAL GLY PHE GLU ILE PRO
SEQRES 15 A 216 ASP LYS PHE VAL VAL GLY TYR ALA LEU ASP TYR ASN GLU
SEQRES 16 A 216 TYR PHE ARG ASP LEU ASN HIS VAL CYS VAL ILE SER GLU
SEQRES 17 A 216 THR GLY LYS ALA LYS TYR LYS ALA
HET 1RP A 301 24
HETNAM 1RP 6-FLUORO-3-OXO-4-(5-O-PHOSPHONO-BETA-D-RIBOFURANOSYL)-
HETNAM 2 1RP 3,4-DIHYDROPYRAZINE-2-CARBOXAMIDE
FORMUL 2 1RP C10 H13 F N3 O9 P
FORMUL 3 HOH *31(H2 O)
HELIX 1 1 ASP A 17 PHE A 21 5 5
HELIX 2 2 PRO A 24 ALA A 28 5 5
HELIX 3 3 PRO A 37 LYS A 54 1 18
HELIX 4 4 TYR A 71 ARG A 86 1 16
HELIX 5 5 GLY A 139 GLN A 151 1 13
HELIX 6 6 SER A 208 TYR A 215 1 8
SHEET 1 A 6 VAL A 7 VAL A 8 0
SHEET 2 A 6 PHE A 177 ILE A 182 1 O GLU A 181 N VAL A 7
SHEET 3 A 6 MET A 156 LYS A 165 1 N LEU A 162 O PHE A 180
SHEET 4 A 6 ASN A 128 ILE A 136 1 N ILE A 131 O ALA A 160
SHEET 5 A 6 ILE A 61 LEU A 67 1 N VAL A 62 O ASN A 128
SHEET 6 A 6 THR A 95 ARG A 100 1 O ILE A 99 N LEU A 67
SHEET 1 B 3 LEU A 31 ILE A 36 0
SHEET 2 B 3 VAL A 204 ILE A 207 -1 O VAL A 206 N ARG A 33
SHEET 3 B 3 VAL A 187 VAL A 188 -1 N VAL A 188 O CYS A 205
CISPEP 1 ASP A 12 GLU A 13 0 -0.98
SITE 1 AC1 12 LYS A 68 ASP A 134 ILE A 135 ASP A 137
SITE 2 AC1 12 THR A 138 GLY A 139 THR A 141 LYS A 165
SITE 3 AC1 12 PHE A 186 VAL A 187 LEU A 192 ASP A 193
CRYST1 46.858 73.400 109.134 90.00 90.00 90.00 I 2 2 2 8
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 0.021341 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013624 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
