HEADER PHOSPHOTRANSFERASE 15-MAY-98 1KI3
TITLE CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE I
TITLE 2 COMPLEXED WITH PENCICLOVIR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDINE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TK;
COMPND 5 EC: 2.7.1.21;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HERPES SIMPLEX VIRUS (TYPE 1 / STRAIN 17);
SOURCE 3 ORGANISM_TAXID: 10299;
SOURCE 4 STRAIN: 17;
SOURCE 5 GENE: TK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SY211;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT7\:HSVTK;
SOURCE 10 EXPRESSION_SYSTEM_GENE: TK
KEYWDS PHOSPHOTRANSFERASE, THYMIDINE KINASE, VIRIDAE, DS-DNA ENVELOPED
KEYWDS 2 VIRUSES, HERPESVIRIDAE, ALPHAHERPESVIRINAE, ANTIVIRAL DRUG
KEYWDS 3 PENCICLOVIR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.N.CHAMPNESS,M.S.BENNETT,F.WIEN,R.VISSE,R.L.JARVEST,W.C.SUMMERS,
AUTHOR 2 M.R.SANDERSON
REVDAT 4 14-FEB-24 1KI3 1 REMARK
REVDAT 3 24-FEB-09 1KI3 1 VERSN
REVDAT 2 01-APR-03 1KI3 1 JRNL
REVDAT 1 18-MAY-99 1KI3 0
JRNL AUTH J.N.CHAMPNESS,M.S.BENNETT,F.WIEN,R.VISSE,W.C.SUMMERS,
JRNL AUTH 2 P.HERDEWIJN,E.DE CLERQ,T.OSTROWSKI,R.L.JARVEST,M.R.SANDERSON
JRNL TITL EXPLORING THE ACTIVE SITE OF HERPES SIMPLEX VIRUS TYPE-1
JRNL TITL 2 THYMIDINE KINASE BY X-RAY CRYSTALLOGRAPHY OF COMPLEXES WITH
JRNL TITL 3 ACICLOVIR AND OTHER LIGANDS.
JRNL REF PROTEINS V. 32 350 1998
JRNL REFN ISSN 0887-3585
JRNL PMID 9715911
JRNL DOI 10.1002/(SICI)1097-0134(19980815)32:3<350::AID-PROT10>3.0.CO
JRNL DOI 2 ;2-8
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.P.TUNG,J.RESPASS,W.C.SUMMERS
REMARK 1 TITL 3'-AMINO THYMIDINE AFFINITY MATRIX FOR THE PURIFICATION OF
REMARK 1 TITL 2 HERPES SIMPLEX VIRUS THYMIDINE KINASE
REMARK 1 REF YALE J.BIOL.MED. V. 69 495 1996
REMARK 1 REFN ISSN 0044-0086
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.G.BROWN,R.VISSE,G.SANDHU,A.DAVIES,P.J.RIZKALLAH,C.MELITZ,
REMARK 1 AUTH 2 W.C.SUMMERS,M.R.SANDERSON
REMARK 1 TITL CRYSTAL STRUCTURES OF THE THYMIDINE KINASE FROM HERPES
REMARK 1 TITL 2 SIMPLEX VIRUS TYPE-1 IN COMPLEX WITH DEOXYTHYMIDINE AND
REMARK 1 TITL 3 GANCICLOVIR
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 876 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.J.MCGEOCH,M.A.DALRYMPLE,A.J.DAVISON,A.DOLAN,M.C.FRAME,
REMARK 1 AUTH 2 D.MCNAB,L.J.PERRY,J.E.SCOTT,P.TAYLOR
REMARK 1 TITL THE COMPLETE DNA SEQUENCE OF THE LONG UNIQUE REGION IN THE
REMARK 1 TITL 2 GENOME OF HERPES SIMPLEX VIRUS TYPE 1
REMARK 1 REF J.GEN.VIROL. V. 69 1531 1988
REMARK 1 REFN ISSN 0022-1317
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.R.SANDERSON,P.S.FREEMONT,H.M.MURTHY,J.F.KRANE,W.C.SUMMERS,
REMARK 1 AUTH 2 T.A.STEITZ
REMARK 1 TITL PURIFICATION AND CRYSTALLIZATION OF THYMIDINE KINASE FROM
REMARK 1 TITL 2 HERPES SIMPLEX VIRUS TYPE 1
REMARK 1 REF J.MOL.BIOL. V. 202 917 1988
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.J.WAGNER,J.A.SHARP,W.C.SUMMERS
REMARK 1 TITL NUCLEOTIDE SEQUENCE OF THE THYMIDINE KINASE GENE OF HERPES
REMARK 1 TITL 2 SIMPLEX VIRUS TYPE 1
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 78 1441 1981
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. 2.37 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) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.200
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 70.4
REMARK 3 NUMBER OF REFLECTIONS : 20953
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) : 0.200
REMARK 3 FREE R VALUE : 0.314
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2095
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.37
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.45
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1180
REMARK 3 BIN R VALUE (WORKING SET) : 0.2700
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 132
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 : 4691
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 132
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.20
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) : 0.35
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) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 2.075
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.06
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.696
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : INDIVIDUAL B-FACTOR REFT.
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; 4.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.500 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.000 ; 4.000
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 : 1KIN_PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : 1KIN_PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : 1KIN_PARNAH1E.DNA
REMARK 3 PARAMETER FILE 4 : 1KIN_SO4.PAR
REMARK 3 PARAMETER FILE 5 : 1KIN_PEN.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : 1KIN_SO4.TOP
REMARK 3 TOPOLOGY FILE 2 : 1KIN_TOPH19.SOL
REMARK 3 TOPOLOGY FILE 3 : 1KIN_TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 4 : 1KIN_PEN.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 NCS RESTRAINTS NOT USED IN FINAL CYCLES.
REMARK 3
REMARK 3 IN C-TERMINAL PORTIONS OF MODELLED SEGMENTS, PEPTIDE
REMARK 3 HAS BECOME SIGNIFICANTLY NON-PLANAR.
REMARK 4
REMARK 4 1KI3 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_1000174428.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : AUG-96
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OTWINOWSKI MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28282
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11200
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) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR + NCS IMPROVEMENT AND
REMARK 200 SOLVENT FLATTENING FOR ORIGINAL NATIVE, 1KIN
REMARK 200 SOFTWARE USED: SOLOMON
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 54.30000
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 54.30000
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 56.90000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.85000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.90000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.85000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.30000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.90000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.85000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.30000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.90000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.85000
REMARK 290 SMTRY3 8 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: 4970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22210 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 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 GLY A 73
REMARK 465 SER A 74
REMARK 465 ARG A 75
REMARK 465 ASP A 76
REMARK 465 HIS A 151
REMARK 465 THR A 265
REMARK 465 ALA A 266
REMARK 465 VAL A 267
REMARK 465 PRO A 268
REMARK 465 PRO A 269
REMARK 465 GLN A 270
REMARK 465 GLY A 271
REMARK 465 ALA A 272
REMARK 465 GLU A 273
REMARK 465 PRO A 274
REMARK 465 GLN A 275
REMARK 465 SER A 276
REMARK 465 ASN A 277
REMARK 465 ALA A 278
REMARK 465 GLY A 279
REMARK 465 ALA A 375
REMARK 465 ASN A 376
REMARK 465 SER B 74
REMARK 465 ARG B 75
REMARK 465 ASP B 76
REMARK 465 HIS B 151
REMARK 465 GLY B 264
REMARK 465 THR B 265
REMARK 465 ALA B 266
REMARK 465 VAL B 267
REMARK 465 PRO B 268
REMARK 465 PRO B 269
REMARK 465 GLN B 270
REMARK 465 GLY B 271
REMARK 465 ALA B 272
REMARK 465 GLU B 273
REMARK 465 PRO B 274
REMARK 465 GLN B 275
REMARK 465 SER B 276
REMARK 465 ASN B 277
REMARK 465 ALA B 375
REMARK 465 ASN B 376
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 MET A 46 CG SD CE
REMARK 470 LEU A 72 CA C O CB CG CD1 CD2
REMARK 470 SER A 150 CA C O CB OG
REMARK 470 GLY A 264 CA C O
REMARK 470 PRO A 280 CG CD
REMARK 470 MET B 46 CG SD CE
REMARK 470 GLY B 73 CA C O
REMARK 470 SER B 150 CA C O CB OG
REMARK 470 SER B 263 CA C O CB OG
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 LEU A 69 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 PRO A 82 C - N - CA ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO A 280 N - CA - CB ANGL. DEV. = 7.7 DEGREES
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 ASP A 55 -159.34 -111.95
REMARK 500 PRO A 82 -170.53 -60.16
REMARK 500 VAL A 90 -71.95 -118.13
REMARK 500 GLU A 95 38.40 39.90
REMARK 500 GLN A 109 42.07 -80.90
REMARK 500 ALA A 140 -61.41 -15.80
REMARK 500 SER A 149 -169.17 -105.35
REMARK 500 ARG A 163 158.35 95.28
REMARK 500 LEU A 170 -67.24 -139.52
REMARK 500 CYS A 171 -71.13 -52.40
REMARK 500 LEU A 178 -7.96 -55.09
REMARK 500 ARG A 220 143.22 164.70
REMARK 500 ARG A 222 151.14 24.03
REMARK 500 TRP A 259 -24.79 -38.29
REMARK 500 PHE A 292 33.35 -88.41
REMARK 500 GLN A 331 130.39 179.55
REMARK 500 SER A 332 150.84 -49.38
REMARK 500 PRO A 333 161.26 -38.11
REMARK 500 ALA A 334 -46.59 67.86
REMARK 500 THR A 344 -23.48 -38.29
REMARK 500 VAL B 90 -81.28 -119.87
REMARK 500 ALA B 93 -109.41 -145.01
REMARK 500 SER B 94 104.60 178.74
REMARK 500 ALA B 140 -54.33 -29.95
REMARK 500 ALA B 147 -67.56 -122.66
REMARK 500 SER B 149 137.46 3.48
REMARK 500 ARG B 163 172.88 82.90
REMARK 500 LEU B 170 -83.47 -145.75
REMARK 500 ARG B 220 150.30 153.81
REMARK 500 GLN B 221 -124.08 -154.54
REMARK 500 PRO B 223 99.41 -64.22
REMARK 500 ARG B 247 -71.48 -53.49
REMARK 500 TRP B 255 -35.85 -39.15
REMARK 500 THR B 290 -34.98 -37.19
REMARK 500 ARG B 293 64.43 -115.81
REMARK 500 PRO B 295 -16.21 -49.64
REMARK 500 GLN B 331 -168.05 -160.60
REMARK 500 GLN B 342 2.03 -68.97
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 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE2 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE2 B 2
DBREF 1KI3 A 46 376 UNP P03176 KITH_HSV11 46 376
DBREF 1KI3 B 46 376 UNP P03176 KITH_HSV11 46 376
SEQRES 1 A 331 MET PRO THR LEU LEU ARG VAL TYR ILE ASP GLY PRO HIS
SEQRES 2 A 331 GLY MET GLY LYS THR THR THR THR GLN LEU LEU VAL ALA
SEQRES 3 A 331 LEU GLY SER ARG ASP ASP ILE VAL TYR VAL PRO GLU PRO
SEQRES 4 A 331 MET THR TYR TRP ARG VAL LEU GLY ALA SER GLU THR ILE
SEQRES 5 A 331 ALA ASN ILE TYR THR THR GLN HIS ARG LEU ASP GLN GLY
SEQRES 6 A 331 GLU ILE SER ALA GLY ASP ALA ALA VAL VAL MET THR SER
SEQRES 7 A 331 ALA GLN ILE THR MET GLY MET PRO TYR ALA VAL THR ASP
SEQRES 8 A 331 ALA VAL LEU ALA PRO HIS ILE GLY GLY GLU ALA GLY SER
SEQRES 9 A 331 SER HIS ALA PRO PRO PRO ALA LEU THR LEU ILE PHE ASP
SEQRES 10 A 331 ARG HIS PRO ILE ALA ALA LEU LEU CYS TYR PRO ALA ALA
SEQRES 11 A 331 ARG TYR LEU MET GLY SER MET THR PRO GLN ALA VAL LEU
SEQRES 12 A 331 ALA PHE VAL ALA LEU ILE PRO PRO THR LEU PRO GLY THR
SEQRES 13 A 331 ASN ILE VAL LEU GLY ALA LEU PRO GLU ASP ARG HIS ILE
SEQRES 14 A 331 ASP ARG LEU ALA LYS ARG GLN ARG PRO GLY GLU ARG LEU
SEQRES 15 A 331 ASP LEU ALA MET LEU ALA ALA ILE ARG ARG VAL TYR GLY
SEQRES 16 A 331 LEU LEU ALA ASN THR VAL ARG TYR LEU GLN CYS GLY GLY
SEQRES 17 A 331 SER TRP ARG GLU ASP TRP GLY GLN LEU SER GLY THR ALA
SEQRES 18 A 331 VAL PRO PRO GLN GLY ALA GLU PRO GLN SER ASN ALA GLY
SEQRES 19 A 331 PRO ARG PRO HIS ILE GLY ASP THR LEU PHE THR LEU PHE
SEQRES 20 A 331 ARG ALA PRO GLU LEU LEU ALA PRO ASN GLY ASP LEU TYR
SEQRES 21 A 331 ASN VAL PHE ALA TRP ALA LEU ASP VAL LEU ALA LYS ARG
SEQRES 22 A 331 LEU ARG SER MET HIS VAL PHE ILE LEU ASP TYR ASP GLN
SEQRES 23 A 331 SER PRO ALA GLY CYS ARG ASP ALA LEU LEU GLN LEU THR
SEQRES 24 A 331 SER GLY MET VAL GLN THR HIS VAL THR THR PRO GLY SER
SEQRES 25 A 331 ILE PRO THR ILE CYS ASP LEU ALA ARG THR PHE ALA ARG
SEQRES 26 A 331 GLU MET GLY GLU ALA ASN
SEQRES 1 B 331 MET PRO THR LEU LEU ARG VAL TYR ILE ASP GLY PRO HIS
SEQRES 2 B 331 GLY MET GLY LYS THR THR THR THR GLN LEU LEU VAL ALA
SEQRES 3 B 331 LEU GLY SER ARG ASP ASP ILE VAL TYR VAL PRO GLU PRO
SEQRES 4 B 331 MET THR TYR TRP ARG VAL LEU GLY ALA SER GLU THR ILE
SEQRES 5 B 331 ALA ASN ILE TYR THR THR GLN HIS ARG LEU ASP GLN GLY
SEQRES 6 B 331 GLU ILE SER ALA GLY ASP ALA ALA VAL VAL MET THR SER
SEQRES 7 B 331 ALA GLN ILE THR MET GLY MET PRO TYR ALA VAL THR ASP
SEQRES 8 B 331 ALA VAL LEU ALA PRO HIS ILE GLY GLY GLU ALA GLY SER
SEQRES 9 B 331 SER HIS ALA PRO PRO PRO ALA LEU THR LEU ILE PHE ASP
SEQRES 10 B 331 ARG HIS PRO ILE ALA ALA LEU LEU CYS TYR PRO ALA ALA
SEQRES 11 B 331 ARG TYR LEU MET GLY SER MET THR PRO GLN ALA VAL LEU
SEQRES 12 B 331 ALA PHE VAL ALA LEU ILE PRO PRO THR LEU PRO GLY THR
SEQRES 13 B 331 ASN ILE VAL LEU GLY ALA LEU PRO GLU ASP ARG HIS ILE
SEQRES 14 B 331 ASP ARG LEU ALA LYS ARG GLN ARG PRO GLY GLU ARG LEU
SEQRES 15 B 331 ASP LEU ALA MET LEU ALA ALA ILE ARG ARG VAL TYR GLY
SEQRES 16 B 331 LEU LEU ALA ASN THR VAL ARG TYR LEU GLN CYS GLY GLY
SEQRES 17 B 331 SER TRP ARG GLU ASP TRP GLY GLN LEU SER GLY THR ALA
SEQRES 18 B 331 VAL PRO PRO GLN GLY ALA GLU PRO GLN SER ASN ALA GLY
SEQRES 19 B 331 PRO ARG PRO HIS ILE GLY ASP THR LEU PHE THR LEU PHE
SEQRES 20 B 331 ARG ALA PRO GLU LEU LEU ALA PRO ASN GLY ASP LEU TYR
SEQRES 21 B 331 ASN VAL PHE ALA TRP ALA LEU ASP VAL LEU ALA LYS ARG
SEQRES 22 B 331 LEU ARG SER MET HIS VAL PHE ILE LEU ASP TYR ASP GLN
SEQRES 23 B 331 SER PRO ALA GLY CYS ARG ASP ALA LEU LEU GLN LEU THR
SEQRES 24 B 331 SER GLY MET VAL GLN THR HIS VAL THR THR PRO GLY SER
SEQRES 25 B 331 ILE PRO THR ILE CYS ASP LEU ALA ARG THR PHE ALA ARG
SEQRES 26 B 331 GLU MET GLY GLU ALA ASN
HET SO4 A 3 5
HET PE2 A 1 18
HET SO4 B 4 5
HET PE2 B 2 18
HETNAM SO4 SULFATE ION
HETNAM PE2 9-(4-HYDROXY-3-(HYDROXYMETHYL)BUT-1-YL)GUANINE
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 PE2 2(C10 H15 N5 O3)
FORMUL 7 HOH *132(H2 O)
HELIX 1 1 LYS A 62 VAL A 70 1 9
HELIX 2 2 MET A 85 ARG A 89 1 5
HELIX 3 3 THR A 96 ASP A 108 1 13
HELIX 4 4 ALA A 114 HIS A 142 1 29
HELIX 5 5 PRO A 165 LEU A 169 1 5
HELIX 6 6 CYS A 171 MET A 179 1 9
HELIX 7 7 PRO A 184 LEU A 193 1 10
HELIX 8 8 GLU A 210 LEU A 217 1 8
HELIX 9 9 LEU A 229 CYS A 251 1 23
HELIX 10 10 TRP A 255 ASP A 258 1 4
HELIX 11 11 ILE A 284 ASP A 286 5 3
HELIX 12 12 THR A 290 PHE A 292 5 3
HELIX 13 13 PRO A 295 LEU A 297 5 3
HELIX 14 14 ASN A 306 ARG A 320 1 15
HELIX 15 15 GLY A 335 SER A 345 1 11
HELIX 16 16 SER A 357 MET A 372 1 16
HELIX 17 17 LYS B 62 VAL B 70 1 9
HELIX 18 18 MET B 85 ARG B 89 1 5
HELIX 19 19 THR B 96 GLN B 109 1 14
HELIX 20 20 ALA B 114 MET B 128 1 15
HELIX 21 21 MET B 130 HIS B 142 1 13
HELIX 22 22 PRO B 165 LEU B 169 1 5
HELIX 23 23 CYS B 171 LEU B 178 1 8
HELIX 24 24 PRO B 184 VAL B 191 1 8
HELIX 25 25 GLU B 210 LYS B 219 1 10
HELIX 26 26 LEU B 229 CYS B 251 1 23
HELIX 27 27 TRP B 255 GLN B 261 1 7
HELIX 28 28 ILE B 284 ASP B 286 5 3
HELIX 29 29 PHE B 289 PHE B 292 5 4
HELIX 30 30 ASN B 306 SER B 321 1 16
HELIX 31 31 PRO B 333 GLY B 346 1 14
HELIX 32 32 PRO B 355 MET B 372 5 18
SHEET 1 A 4 GLN A 349 HIS A 351 0
SHEET 2 A 4 THR A 48 TYR A 53 -1 N LEU A 49 O THR A 350
SHEET 3 A 4 LEU A 157 PHE A 161 1 N LEU A 157 O LEU A 50
SHEET 4 A 4 ILE A 78 VAL A 81 1 N VAL A 79 O THR A 158
SHEET 1 B 3 VAL A 52 ILE A 54 0
SHEET 2 B 3 ASN A 202 ALA A 207 1 N ASN A 202 O TYR A 53
SHEET 3 B 3 HIS A 323 ASP A 328 1 N HIS A 323 O ILE A 203
SHEET 1 C 3 LEU B 49 ILE B 54 0
SHEET 2 C 3 LEU B 157 ASP B 162 1 N LEU B 157 O LEU B 50
SHEET 3 C 3 ILE B 78 VAL B 81 1 N VAL B 79 O THR B 158
SHEET 1 D 2 ASN B 202 ALA B 207 0
SHEET 2 D 2 HIS B 323 ASP B 328 1 N HIS B 323 O ILE B 203
CISPEP 1 PRO A 153 PRO A 154 0 -0.46
CISPEP 2 PRO B 153 PRO B 154 0 0.00
SITE 1 AC1 8 HIS A 58 GLY A 59 MET A 60 GLY A 61
SITE 2 AC1 8 LYS A 62 THR A 63 GLN A 221 ARG A 222
SITE 1 AC2 7 GLY B 59 MET B 60 GLY B 61 LYS B 62
SITE 2 AC2 7 THR B 63 GLN B 221 HOH B 510
SITE 1 AC3 12 HIS A 58 GLU A 83 ILE A 97 ILE A 100
SITE 2 AC3 12 TYR A 101 GLN A 125 MET A 128 ARG A 163
SITE 3 AC3 12 TYR A 172 ARG A 176 ARG A 222 GLU A 225
SITE 1 AC4 12 HIS B 58 GLU B 83 TRP B 88 ILE B 100
SITE 2 AC4 12 TYR B 101 MET B 121 GLN B 125 MET B 128
SITE 3 AC4 12 TYR B 172 ARG B 176 GLU B 225 HOH B 527
CRYST1 113.800 117.700 108.600 90.00 90.00 90.00 C 2 2 21 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 0.008787 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008496 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009208 0.00000
MTRIX1 1 -0.926960 0.323960 0.189190 26.46062 1
MTRIX2 1 0.321520 0.426170 0.845580 -0.85954 1
MTRIX3 1 0.193300 0.844650 -0.499200 -8.64933 1
(ATOM LINES ARE NOT SHOWN.)
END
