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PDBsum entry 4ivq

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
4ivq
Jmol
Contents
Protein chains
313 a.a.
Ligands
I43 ×2
SO4 ×3
Waters ×203
HEADER    TRANSFERASE                             23-JAN-13   4IVQ
TITLE     CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE 1
TITLE    2 IN COMPLEX WITH IN43/5
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THYMIDINE KINASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 46-376;
COMPND   5 SYNONYM: HSV1-TK;
COMPND   6 EC: 2.7.1.21;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 1;
SOURCE   3 ORGANISM_COMMON: HHV-1;
SOURCE   4 ORGANISM_TAXID: 10299;
SOURCE   5 STRAIN: 17;
SOURCE   6 GENE: TK, TK (UL23), UL23;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-2
KEYWDS    DNA SYNTHESIS, PET IMAGING TRACER, ATP BINDING, NUCLEOTIDE BINDING,
KEYWDS   2 TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.PERNOT,I.NOVAKOVIC,Y.WESTERMAIER,R.PEROZZO,S.RAIC-MALIC,L.SCAPOZZA
REVDAT   2   02-OCT-13 4IVQ    1       AUTHOR SOURCE
REVDAT   1   06-FEB-13 4IVQ    0
JRNL        AUTH   L.PERNOT,I.NOVAKOVIC,R.PEROZZO,S.RAIC-MALIC,L.SCAPOZZA
JRNL        TITL   NEW THYMINE DERIVATIVES AS HSV1-TK LIGAND FOR THE
JRNL        TITL 2 DEVELOPMENT OF PET IMAGING TRACER
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   M.MARTIC,L.PERNOT,Y.WESTERMAIER,R.PEROZZO,T.G.KRALJEVIC,
REMARK   1  AUTH 2 S.KRISTAFOR,S.RAIC-MALIC,L.SCAPOZZA,S.AMETAMEY
REMARK   1  TITL   SYNTHESIS, CRYSTAL STRUCTURE, AND IN VITRO BIOLOGICAL
REMARK   1  TITL 2 EVALUATION OF C-6 PYRIMIDINE DERIVATIVES: NEW LEAD
REMARK   1  TITL 3 STRUCTURES FOR MONITORING GENE EXPRESSION IN VIVO.
REMARK   1  REF    NUCLEOSIDES NUCLEOTIDES       V.  30   293 2011
REMARK   1  REF  2 NUCLEIC ACIDS
REMARK   1  REFN                   ISSN 1525-7770
REMARK   1  PMID   21623543
REMARK   1  DOI    10.1080/15257770.2011.581258
REMARK   1 REFERENCE 2
REMARK   1  AUTH   S.KRISTAFOR,I.NOVAKOVIC,T.GAZIVODA KRALJEVIC,
REMARK   1  AUTH 2 S.KRALJEVIC PAVELIC,P.LUCIN,Y.WESTERMAIER,L.PERNOT,
REMARK   1  AUTH 3 L.SCAPOZZA,S.M.AMETAMEY,S.RAIC-MALIC
REMARK   1  TITL   A NEW N-METHYL THYMINE DERIVATIVE COMPRISING A
REMARK   1  TITL 2 DIHYDROXYISOBUTENYL UNIT AS LIGAND FOR THYMIDINE KINASE OF
REMARK   1  TITL 3 HERPES SIMPLEX VIRUS TYPE 1 (HSV-1 TK).
REMARK   1  REF    BIOORG.MED.CHEM.LETT.         V.  21  6161 2011
REMARK   1  REFN                   ISSN 0960-894X
REMARK   1  PMID   21911293
REMARK   1  DOI    10.1016/J.BMCL.2011.07.115
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.16
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5
REMARK   3   NUMBER OF REFLECTIONS             : 55816
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193
REMARK   3   R VALUE            (WORKING SET) : 0.192
REMARK   3   FREE R VALUE                     : 0.222
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.580
REMARK   3   FREE R VALUE TEST SET COUNT      : 1999
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 27.1577 -  4.5725    0.97     3986   148  0.1947 0.1993
REMARK   3     2  4.5725 -  3.6321    1.00     3953   147  0.1652 0.1922
REMARK   3     3  3.6321 -  3.1738    1.00     3926   146  0.1858 0.2029
REMARK   3     4  3.1738 -  2.8840    1.00     3881   144  0.1997 0.2619
REMARK   3     5  2.8840 -  2.6774    0.96     3737   139  0.1988 0.2156
REMARK   3     6  2.6774 -  2.5197    0.99     3880   144  0.2027 0.2228
REMARK   3     7  2.5197 -  2.3936    0.99     3839   142  0.2003 0.2438
REMARK   3     8  2.3936 -  2.2895    0.99     3854   144  0.2024 0.2561
REMARK   3     9  2.2895 -  2.2014    0.99     3805   141  0.1972 0.2349
REMARK   3    10  2.2014 -  2.1254    0.99     3848   143  0.1985 0.2411
REMARK   3    11  2.1254 -  2.0590    0.99     3821   143  0.2089 0.2533
REMARK   3    12  2.0590 -  2.0002    0.99     3816   142  0.2059 0.2611
REMARK   3    13  2.0002 -  1.9475    0.99     3819   141  0.2189 0.2833
REMARK   3    14  1.9475 -  1.9000    0.95     3652   135  0.2321 0.3005
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)     : 0.220
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.310
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 28.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.82
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      :  0.007           4908
REMARK   3   ANGLE     :  1.097           6713
REMARK   3   CHIRALITY :  0.073            783
REMARK   3   PLANARITY :  0.005            852
REMARK   3   DIHEDRAL  : 12.561           1792
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
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 4IVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB077269.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-12
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06DA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55929
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.155
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8
REMARK 200  DATA REDUNDANCY                : 10.900
REMARK 200  R MERGE                    (I) : 0.05700
REMARK 200  R SYM                      (I) : 0.05400
REMARK 200   FOR THE DATA SET  : 24.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.32900
REMARK 200  R SYM FOR SHELL            (I) : 0.31200
REMARK 200   FOR SHELL         : 6.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3F0T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 50.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9-1.2 M LITHIUM SULFATE, 1 MM DTT,
REMARK 280  0.1 M HEPES, PH 7.5-8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 296K
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       53.88750
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       53.88750
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       56.71750
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.53450
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.71750
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.53450
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.88750
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.71750
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       58.53450
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.88750
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.71750
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       58.53450
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: 3930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 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 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 693  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     GLY A   148
REMARK 465     SER A   149
REMARK 465     SER A   150
REMARK 465     HIS A   151
REMARK 465     ALA A   152
REMARK 465     GLN A   221
REMARK 465     ARG A   222
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     ALA A   375
REMARK 465     ASN A   376
REMARK 465     GLY B   148
REMARK 465     SER B   149
REMARK 465     SER B   150
REMARK 465     HIS B   151
REMARK 465     ALA B   152
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   278
REMARK 465     GLY B   279
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     ARG A  75    NE   CZ   NH1  NH2
REMARK 470     ARG A  89    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 106    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS A 219    CG   CD   CE   NZ
REMARK 470     LEU A 364    CG   CD1  CD2
REMARK 470     ARG A 370    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B  62    CG   CD   CE   NZ
REMARK 470     THR B  63    OG1  CG2
REMARK 470     THR B  64    OG1  CG2
REMARK 470     THR B  65    OG1  CG2
REMARK 470     GLN B  67    CG   CD   OE1  NE2
REMARK 470     LEU B  68    CG   CD1  CD2
REMARK 470     LEU B  72    CG   CD1  CD2
REMARK 470     ASP B  76    CG   OD1  OD2
REMARK 470     ARG B 366    CG   CD   NE   CZ   NH1  NH2
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    SER A  74     -164.07    -69.38
REMARK 500    PRO A  84       46.61    -81.33
REMARK 500    VAL A  90      -61.67   -130.00
REMARK 500    ARG A 163      154.77     80.38
REMARK 500    LEU A 170      -58.55   -148.70
REMARK 500    LYS A 219      -92.60    -79.71
REMARK 500    SER A 263      -81.55   -169.51
REMARK 500    GLN A 275      146.42   -170.36
REMARK 500    ASN A 277       -2.12     73.82
REMARK 500    ASP B  55     -159.76   -138.46
REMARK 500    VAL B  90      -57.38   -130.73
REMARK 500    ARG B 163      156.06     81.22
REMARK 500    LEU B 170      -58.96   -146.62
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 I43 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I43 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F0T   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX
REMARK 900 VIRUS TYPE 1 IN COMPLEX WITH N-METHYL-DHBT
REMARK 900 RELATED ID: 3RDP   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX
REMARK 900 VIRUS TYPE 1 IN COMPLEX WITH N-METHYL-FHBT
REMARK 900 RELATED ID: 1E2P   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX
REMARK 900 VIRUS TYPE 1 IN COMPLEX WITH DHBT
REMARK 900 RELATED ID: 4IVP   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX
REMARK 900 VIRUS TYPE 1 IN COMPLEX WITH IN51/20
REMARK 900 RELATED ID: 4IVR   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THYMIDINE KINASE FROM HERPES SIMPLEX
REMARK 900 VIRUS TYPE 1 IN COMPLEX WITH IN52/10
DBREF  4IVQ A   46   376  UNP    P03176   KITH_HHV11      46    376
DBREF  4IVQ B   46   376  UNP    P03176   KITH_HHV11      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    I43  A 501      17
HET    SO4  A 502       5
HET    SO4  A 503       5
HET    I43  B 401      17
HET    SO4  B 402       5
HETNAM     I43 6-[3-HYDROXY-2-(HYDROXYMETHYL)PROP-1-EN-1-YL]-4-
HETNAM   2 I43  METHOXY-1,5-DIMETHYLPYRIMIDIN-2(1H)-ONE
HETNAM     SO4 SULFATE ION
FORMUL   3  I43    2(C11 H16 N2 O4)
FORMUL   4  SO4    3(O4 S 2-)
FORMUL   8  HOH   *203(H2 O)
HELIX    1   1 GLY A   61  ALA A   71  1                                  11
HELIX    2   2 PRO A   84  VAL A   90  1                                   7
HELIX    3   3 GLU A   95  GLN A  109  1                                  15
HELIX    4   4 SER A  113  ALA A  140  1                                  28
HELIX    5   5 HIS A  164  LEU A  170  1                                   7
HELIX    6   6 LEU A  170  MET A  179  1                                  10
HELIX    7   7 THR A  183  ILE A  194  1                                  12
HELIX    8   8 PRO A  209  ARG A  220  1                                  12
HELIX    9   9 ASP A  228  CYS A  251  1                                  24
HELIX   10  10 SER A  254  TRP A  259  1                                   6
HELIX   11  11 GLY A  260  LEU A  262  5                                   3
HELIX   12  12 HIS A  283  ARG A  293  5                                  11
HELIX   13  13 ALA A  294  LEU A  298  5                                   5
HELIX   14  14 TYR A  305  SER A  321  1                                  17
HELIX   15  15 SER A  332  SER A  345  1                                  14
HELIX   16  16 GLY A  356  GLY A  373  1                                  18
HELIX   17  17 LYS B   62  GLY B   73  1                                  12
HELIX   18  18 PRO B   84  VAL B   90  1                                   7
HELIX   19  19 GLU B   95  GLN B  109  1                                  15
HELIX   20  20 SER B  113  ALA B  140  1                                  28
HELIX   21  21 HIS B  164  LEU B  170  1                                   7
HELIX   22  22 LEU B  170  MET B  179  1                                  10
HELIX   23  23 THR B  183  LEU B  193  1                                  11
HELIX   24  24 PRO B  209  ARG B  220  1                                  12
HELIX   25  25 ASP B  228  CYS B  251  1                                  24
HELIX   26  26 SER B  254  TRP B  259  1                                   6
HELIX   27  27 GLY B  260  SER B  263  5                                   4
HELIX   28  28 HIS B  283  ARG B  293  5                                  11
HELIX   29  29 ALA B  294  LEU B  298  5                                   5
HELIX   30  30 TYR B  305  SER B  321  1                                  17
HELIX   31  31 SER B  332  THR B  344  1                                  13
HELIX   32  32 SER B  345  MET B  347  5                                   3
HELIX   33  33 GLY B  356  GLY B  373  1                                  18
SHEET    1   A 5 ILE A  78  VAL A  81  0
SHEET    2   A 5 LEU A 157  ASP A 162  1  O  ILE A 160   N  VAL A  81
SHEET    3   A 5 THR A  48  ILE A  54  1  N  LEU A  50   O  LEU A 159
SHEET    4   A 5 THR A 350  VAL A 352 -1  O  THR A 350   N  LEU A  49
SHEET    5   A 5 ILE A 143  GLU A 146 -1  N  GLY A 144   O  HIS A 351
SHEET    1   B 5 ILE A  78  VAL A  81  0
SHEET    2   B 5 LEU A 157  ASP A 162  1  O  ILE A 160   N  VAL A  81
SHEET    3   B 5 THR A  48  ILE A  54  1  N  LEU A  50   O  LEU A 159
SHEET    4   B 5 ASN A 202  ALA A 207  1  O  ASN A 202   N  TYR A  53
SHEET    5   B 5 HIS A 323  ASP A 328  1  O  LEU A 327   N  LEU A 205
SHEET    1   C 5 ILE B  78  VAL B  81  0
SHEET    2   C 5 LEU B 157  ASP B 162  1  O  ILE B 160   N  VAL B  81
SHEET    3   C 5 THR B  48  ILE B  54  1  N  LEU B  50   O  LEU B 159
SHEET    4   C 5 THR B 350  VAL B 352 -1  O  THR B 350   N  LEU B  49
SHEET    5   C 5 ILE B 143  GLU B 146 -1  N  GLY B 144   O  HIS B 351
SHEET    1   D 5 ILE B  78  VAL B  81  0
SHEET    2   D 5 LEU B 157  ASP B 162  1  O  ILE B 160   N  VAL B  81
SHEET    3   D 5 THR B  48  ILE B  54  1  N  LEU B  50   O  LEU B 159
SHEET    4   D 5 ASN B 202  ALA B 207  1  O  VAL B 204   N  TYR B  53
SHEET    5   D 5 HIS B 323  ASP B 328  1  O  LEU B 327   N  LEU B 205
SITE     1 AC1 13 HIS A  58  GLU A  83  TRP A  88  ILE A  97
SITE     2 AC1 13 TYR A 101  GLN A 125  MET A 128  ARG A 163
SITE     3 AC1 13 TYR A 172  ARG A 176  MET A 231  HOH A 673
SITE     4 AC1 13 HOH A 674
SITE     1 AC2  8 HIS A  58  GLY A  59  MET A  60  GLY A  61
SITE     2 AC2  8 LYS A  62  THR A  63  ARG A 216  HOH A 669
SITE     1 AC3  4 LYS A 317  ARG A 320  HOH A 608  HOH A 692
SITE     1 AC4 14 HIS B  58  GLU B  83  TRP B  88  ILE B  97
SITE     2 AC4 14 TYR B 101  GLN B 125  MET B 128  ARG B 163
SITE     3 AC4 14 TYR B 172  ARG B 176  ARG B 222  MET B 231
SITE     4 AC4 14 HOH B 556  HOH B 589
SITE     1 AC5  6 HIS B  58  GLY B  59  GLY B  61  ARG B 220
SITE     2 AC5  6 ARG B 222  HOH B 583
CRYST1  113.435  117.069  107.775  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      0.008816  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008542  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009279        0.00000
      
PROCHECK
Go to PROCHECK summary
 References