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PDBsum entry 2orv

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Top Page protein ligands metals Protein-protein interface(s) links
Transferase PDB id
2orv
Jmol
Contents
Protein chain
163 a.a.
Ligands
4TA ×2
Metals
_ZN ×2
Waters ×160
HEADER    TRANSFERASE                             04-FEB-07   2ORV
TITLE     HUMAN THYMIDINE KINASE 1 IN COMPLEX WITH TP4A
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: THYMIDINE KINASE;
COMPND   3 CHAIN: A, B;
COMPND   4 EC: 2.7.1.21;
COMPND   5 ENGINEERED: YES;
COMPND   6 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: TK1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(D3);
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS    TK-1 (THYMIDINE KINASE 1), TP4A (P1-(5'-ADENOSYL)P4-(5'-
KEYWDS   2 (2'DEOXYTHYMIDIL))TETRAPHOSPHATE, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.SEGURA-PENA,S.LUTZ,C.MONNERJAHN,M.KONRAD,A.LAVIE
REVDAT   4   13-JUL-11 2ORV    1       VERSN
REVDAT   3   24-FEB-09 2ORV    1       VERSN
REVDAT   2   22-MAY-07 2ORV    1       JRNL
REVDAT   1   27-MAR-07 2ORV    0
JRNL        AUTH   D.SEGURA-PENA,S.LUTZ,C.MONNERJAHN,M.KONRAD,A.LAVIE
JRNL        TITL   BINDING OF ATP TO TK1-LIKE ENZYMES IS ASSOCIATED WITH A
JRNL        TITL 2 CONFORMATIONAL CHANGE IN THE QUATERNARY STRUCTURE.
JRNL        REF    J.MOL.BIOL.                   V. 369   129 2007
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   17407781
JRNL        DOI    10.1016/J.JMB.2007.02.104
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.50
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7
REMARK   3   NUMBER OF REFLECTIONS             : 26191
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 + TEST SET) : 0.202
REMARK   3   R VALUE            (WORKING SET) : 0.197
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 2604
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) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1768
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840
REMARK   3   BIN FREE R VALUE SET COUNT          : 184
REMARK   3   BIN FREE R VALUE                    : 0.3430
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2479
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 68
REMARK   3   SOLVENT ATOMS            : 160
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 49.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.25
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 4.13000
REMARK   3    B22 (A**2) : 4.13000
REMARK   3    B33 (A**2) : -6.19000
REMARK   3    B12 (A**2) : 2.06000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.164
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.168
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2583 ; 0.016 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3493 ; 1.811 ; 2.008
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   319 ; 6.705 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;34.557 ;23.398
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   452 ;18.747 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;18.981 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   398 ; 0.122 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1865 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1207 ; 0.234 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1751 ; 0.312 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   148 ; 0.208 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    50 ; 0.309 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.225 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1640 ; 0.938 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2554 ; 1.632 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1060 ; 2.127 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   939 ; 3.357 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : B A
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B     18       B     191      4
REMARK   3           1     A     18       A     191      4
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1228 ; 0.210 ; 0.500
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1228 ; 0.740 ; 2.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2ORV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-07.
REMARK 100 THE RCSB ID CODE IS RCSB041508.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-04
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.8
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-BM
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.072
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 225 MM
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34789
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.080
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.500
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4
REMARK 200  DATA REDUNDANCY                : 5.000
REMARK 200  R MERGE                    (I) : 0.07500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.18
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.35400
REMARK 200   FOR SHELL         : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 57.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.8 M NACL, 0.1M MES, 0.1M NAH2PO4,
REMARK 280  0.1M KH2PO4, PH 4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280  298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   Y,X,-Z
REMARK 290       5555   X-Y,-Y,-Z+2/3
REMARK 290       6555   -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.12000
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      104.24000
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      104.24000
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       52.12000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 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      104.24000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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     SER A     2
REMARK 465     CYS A     3
REMARK 465     ILE A     4
REMARK 465     ASN A     5
REMARK 465     LEU A     6
REMARK 465     PRO A     7
REMARK 465     THR A     8
REMARK 465     VAL A     9
REMARK 465     LEU A    10
REMARK 465     PRO A    11
REMARK 465     GLY A    12
REMARK 465     SER A    13
REMARK 465     PRO A    14
REMARK 465     SER A    15
REMARK 465     LYS A    16
REMARK 465     THR A    17
REMARK 465     SER A    62
REMARK 465     SER A    63
REMARK 465     SER A    64
REMARK 465     PHE A    65
REMARK 465     CYS A    66
REMARK 465     THR A    67
REMARK 465     HIS A    68
REMARK 465     ASP A    69
REMARK 465     ARG A    70
REMARK 465     ASN A    71
REMARK 465     THR A    72
REMARK 465     LYS A   192
REMARK 465     ALA A   193
REMARK 465     SER A   194
REMARK 465     GLY A   195
REMARK 465     GLN A   196
REMARK 465     PRO A   197
REMARK 465     ALA A   198
REMARK 465     GLY A   199
REMARK 465     PRO A   200
REMARK 465     ASP A   201
REMARK 465     ASN A   202
REMARK 465     ALA A   203
REMARK 465     ALA A   204
REMARK 465     ASN A   205
REMARK 465     CYS A   206
REMARK 465     PRO A   207
REMARK 465     VAL A   208
REMARK 465     PRO A   209
REMARK 465     GLY A   210
REMARK 465     LYS A   211
REMARK 465     PRO A   212
REMARK 465     GLY A   213
REMARK 465     GLU A   214
REMARK 465     ALA A   215
REMARK 465     VAL A   216
REMARK 465     ALA A   217
REMARK 465     ALA A   218
REMARK 465     ARG A   219
REMARK 465     LYS A   220
REMARK 465     LEU A   221
REMARK 465     PHE A   222
REMARK 465     ALA A   223
REMARK 465     PRO A   224
REMARK 465     GLN A   225
REMARK 465     GLN A   226
REMARK 465     ILE A   227
REMARK 465     LEU A   228
REMARK 465     GLN A   229
REMARK 465     CYS A   230
REMARK 465     SER A   231
REMARK 465     PRO A   232
REMARK 465     ALA A   233
REMARK 465     ASN A   234
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     CYS B     3
REMARK 465     ILE B     4
REMARK 465     ASN B     5
REMARK 465     LEU B     6
REMARK 465     PRO B     7
REMARK 465     THR B     8
REMARK 465     VAL B     9
REMARK 465     LEU B    10
REMARK 465     PRO B    11
REMARK 465     GLY B    12
REMARK 465     SER B    13
REMARK 465     PRO B    14
REMARK 465     SER B    15
REMARK 465     LYS B    16
REMARK 465     THR B    17
REMARK 465     THR B    59
REMARK 465     ARG B    60
REMARK 465     TYR B    61
REMARK 465     SER B    62
REMARK 465     SER B    63
REMARK 465     SER B    64
REMARK 465     PHE B    65
REMARK 465     CYS B    66
REMARK 465     THR B    67
REMARK 465     HIS B    68
REMARK 465     ASP B    69
REMARK 465     ARG B    70
REMARK 465     ASN B    71
REMARK 465     THR B    72
REMARK 465     LYS B   192
REMARK 465     ALA B   193
REMARK 465     SER B   194
REMARK 465     GLY B   195
REMARK 465     GLN B   196
REMARK 465     PRO B   197
REMARK 465     ALA B   198
REMARK 465     GLY B   199
REMARK 465     PRO B   200
REMARK 465     ASP B   201
REMARK 465     ASN B   202
REMARK 465     ALA B   203
REMARK 465     ALA B   204
REMARK 465     ASN B   205
REMARK 465     CYS B   206
REMARK 465     PRO B   207
REMARK 465     VAL B   208
REMARK 465     PRO B   209
REMARK 465     GLY B   210
REMARK 465     LYS B   211
REMARK 465     PRO B   212
REMARK 465     GLY B   213
REMARK 465     GLU B   214
REMARK 465     ALA B   215
REMARK 465     VAL B   216
REMARK 465     ALA B   217
REMARK 465     ALA B   218
REMARK 465     ARG B   219
REMARK 465     LYS B   220
REMARK 465     LEU B   221
REMARK 465     PHE B   222
REMARK 465     ALA B   223
REMARK 465     PRO B   224
REMARK 465     GLN B   225
REMARK 465     GLN B   226
REMARK 465     ILE B   227
REMARK 465     LEU B   228
REMARK 465     GLN B   229
REMARK 465     CYS B   230
REMARK 465     SER B   231
REMARK 465     PRO B   232
REMARK 465     ALA B   233
REMARK 465     ASN B   234
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     LYS A  54    CG   CD   CE   NZ
REMARK 470     TYR A  61    CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 470     ARG A  82    CG   CD   NE   CZ   NH1  NH2
REMARK 470     LYS B  54    CG   CD   CE   NZ
REMARK 470     ARG B  82    CG   CD   NE   CZ   NH1  NH2
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   CG1  ILE B   105     O    HOH B   865              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    CYS A 109   CB    CYS A 109   SG     -0.110
REMARK 500    ASP B 104   CB    ASP B 104   CG      0.150
REMARK 500
REMARK 500 REMARK: NULL
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    ASP B 104   CB  -  CG  -  OD2 ANGL. DEV. =   9.8 DEGREES
REMARK 500    LEU B 124   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES
REMARK 500    ARG B 130   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    GLN A  47       33.98     75.42
REMARK 500    THR A  59       70.77   -118.22
REMARK 500    GLU A  98       47.50     38.28
REMARK 500    ALA A 123      148.10   -170.99
REMARK 500    THR A 127     -173.71    -68.40
REMARK 500    ILE B  45       -5.31    -59.25
REMARK 500    GLN B  47       33.50     80.55
REMARK 500    CYS B 156       -6.14   -147.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 854        DISTANCE =  6.04 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610   M RES C SSEQI
REMARK 610     4TA A  801
REMARK 610     4TA B  802
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                              ZN A 235  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 188   SG
REMARK 620 2 CYS A 156   SG  114.5
REMARK 620 3 CYS A 153   SG   98.2 112.4
REMARK 620 4 CYS A 185   SG  106.1 110.8 114.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B 235  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 156   SG
REMARK 620 2 CYS B 185   SG  116.4
REMARK 620 3 CYS B 188   SG  115.6  96.0
REMARK 620 4 CYS B 153   SG  113.3 111.9 101.6
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4TA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4TA B 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ORW   RELATED DB: PDB
REMARK 900 THERMOTOGA MARITIMA THYMIDINE KINASE 1 LIKE ENZYME IN
REMARK 900 COMPLEX WITH TP4A
DBREF  2ORV A    1   234  UNP    P04183   KITH_HUMAN       1    234
DBREF  2ORV B    1   234  UNP    P04183   KITH_HUMAN       1    234
SEQADV 2ORV ALA A  203  UNP  P04183    LYS   203 ENGINEERED
SEQADV 2ORV ALA A  204  UNP  P04183    GLU   204 ENGINEERED
SEQADV 2ORV ALA B  203  UNP  P04183    LYS   203 ENGINEERED
SEQADV 2ORV ALA B  204  UNP  P04183    GLU   204 ENGINEERED
SEQRES   1 A  234  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER
SEQRES   2 A  234  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY
SEQRES   3 A  234  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG
SEQRES   4 A  234  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL
SEQRES   5 A  234  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE
SEQRES   6 A  234  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA
SEQRES   7 A  234  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL
SEQRES   8 A  234  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP
SEQRES   9 A  234  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS
SEQRES  10 A  234  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG
SEQRES  11 A  234  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA
SEQRES  12 A  234  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS
SEQRES  13 A  234  PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR GLU
SEQRES  14 A  234  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS
SEQRES  15 A  234  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER GLY
SEQRES  16 A  234  GLN PRO ALA GLY PRO ASP ASN ALA ALA ASN CYS PRO VAL
SEQRES  17 A  234  PRO GLY LYS PRO GLY GLU ALA VAL ALA ALA ARG LYS LEU
SEQRES  18 A  234  PHE ALA PRO GLN GLN ILE LEU GLN CYS SER PRO ALA ASN
SEQRES   1 B  234  MET SER CYS ILE ASN LEU PRO THR VAL LEU PRO GLY SER
SEQRES   2 B  234  PRO SER LYS THR ARG GLY GLN ILE GLN VAL ILE LEU GLY
SEQRES   3 B  234  PRO MET PHE SER GLY LYS SER THR GLU LEU MET ARG ARG
SEQRES   4 B  234  VAL ARG ARG PHE GLN ILE ALA GLN TYR LYS CYS LEU VAL
SEQRES   5 B  234  ILE LYS TYR ALA LYS ASP THR ARG TYR SER SER SER PHE
SEQRES   6 B  234  CYS THR HIS ASP ARG ASN THR MET GLU ALA LEU PRO ALA
SEQRES   7 B  234  CYS LEU LEU ARG ASP VAL ALA GLN GLU ALA LEU GLY VAL
SEQRES   8 B  234  ALA VAL ILE GLY ILE ASP GLU GLY GLN PHE PHE PRO ASP
SEQRES   9 B  234  ILE VAL GLU PHE CYS GLU ALA MET ALA ASN ALA GLY LYS
SEQRES  10 B  234  THR VAL ILE VAL ALA ALA LEU ASP GLY THR PHE GLN ARG
SEQRES  11 B  234  LYS PRO PHE GLY ALA ILE LEU ASN LEU VAL PRO LEU ALA
SEQRES  12 B  234  GLU SER VAL VAL LYS LEU THR ALA VAL CYS MET GLU CYS
SEQRES  13 B  234  PHE ARG GLU ALA ALA TYR THR LYS ARG LEU GLY THR GLU
SEQRES  14 B  234  LYS GLU VAL GLU VAL ILE GLY GLY ALA ASP LYS TYR HIS
SEQRES  15 B  234  SER VAL CYS ARG LEU CYS TYR PHE LYS LYS ALA SER GLY
SEQRES  16 B  234  GLN PRO ALA GLY PRO ASP ASN ALA ALA ASN CYS PRO VAL
SEQRES  17 B  234  PRO GLY LYS PRO GLY GLU ALA VAL ALA ALA ARG LYS LEU
SEQRES  18 B  234  PHE ALA PRO GLN GLN ILE LEU GLN CYS SER PRO ALA ASN
HET     ZN  A 235       1
HET     ZN  B 235       1
HET    4TA  A 801      33
HET    4TA  B 802      33
HETNAM      ZN ZINC ION
HETNAM     4TA P1-(5'-ADENOSYL)P4-(5'-(2'-DEOXY-THYMIDYL))
HETNAM   2 4TA  TETRAPHOSPHATE
FORMUL   3   ZN    2(ZN 2+)
FORMUL   5  4TA    2(C20 H25 N7 O20 P4 4-)
FORMUL   7  HOH   *160(H2 O)
HELIX    1   1 GLY A   31  ILE A   45  1                                  15
HELIX    2   2 LEU A   80  ASP A   83  5                                   4
HELIX    3   3 VAL A   84  LEU A   89  1                                   6
HELIX    4   4 GLU A   98  PHE A  102  5                                   5
HELIX    5   5 ASP A  104  ALA A  115  1                                  12
HELIX    6   6 ALA A  135  ALA A  143  5                                   9
HELIX    7   7 CYS A  185  LYS A  191  1                                   7
HELIX    8   8 GLY B   31  ILE B   45  1                                  15
HELIX    9   9 LEU B   80  ASP B   83  5                                   4
HELIX   10  10 VAL B   84  LEU B   89  1                                   6
HELIX   11  11 GLU B   98  PHE B  102  5                                   5
HELIX   12  12 ASP B  104  ALA B  115  1                                  12
HELIX   13  13 ALA B  135  ALA B  143  5                                   9
HELIX   14  14 CYS B  185  PHE B  190  1                                   6
SHEET    1   A 6 GLU A  74  ALA A  78  0
SHEET    2   A 6 CYS A  50  TYR A  55  1  N  VAL A  52   O  GLU A  74
SHEET    3   A 6 VAL A  93  ILE A  96  1  O  GLY A  95   N  LEU A  51
SHEET    4   A 6 THR A 118  ALA A 122  1  O  ILE A 120   N  ILE A  96
SHEET    5   A 6 GLN A  20  LEU A  25  1  N  ILE A  24   O  VAL A 121
SHEET    6   A 6 SER A 145  LYS A 148  1  O  VAL A 147   N  LEU A  25
SHEET    1   B 2 ALA A 151  VAL A 152  0
SHEET    2   B 2 GLU A 159  ALA A 160 -1  O  ALA A 160   N  ALA A 151
SHEET    1   C 2 TYR A 162  ARG A 165  0
SHEET    2   C 2 TYR A 181  VAL A 184 -1  O  VAL A 184   N  TYR A 162
SHEET    1   D 6 GLU B  74  ALA B  78  0
SHEET    2   D 6 CYS B  50  TYR B  55  1  N  LYS B  54   O  LEU B  76
SHEET    3   D 6 VAL B  93  ILE B  96  1  O  GLY B  95   N  ILE B  53
SHEET    4   D 6 THR B 118  ALA B 122  1  O  ALA B 122   N  ILE B  96
SHEET    5   D 6 GLN B  20  LEU B  25  1  N  ILE B  24   O  VAL B 121
SHEET    6   D 6 SER B 145  LYS B 148  1  O  SER B 145   N  VAL B  23
SHEET    1   E 2 ALA B 151  VAL B 152  0
SHEET    2   E 2 GLU B 159  ALA B 160 -1  O  ALA B 160   N  ALA B 151
SHEET    1   F 2 TYR B 162  ARG B 165  0
SHEET    2   F 2 TYR B 181  VAL B 184 -1  O  HIS B 182   N  LYS B 164
LINK        ZN    ZN A 235                 SG  CYS A 188     1555   1555  2.30
LINK        ZN    ZN A 235                 SG  CYS A 156     1555   1555  2.01
LINK        ZN    ZN A 235                 SG  CYS A 153     1555   1555  2.45
LINK        ZN    ZN A 235                 SG  CYS A 185     1555   1555  2.49
LINK        ZN    ZN B 235                 SG  CYS B 156     1555   1555  2.26
LINK        ZN    ZN B 235                 SG  CYS B 185     1555   1555  2.48
LINK        ZN    ZN B 235                 SG  CYS B 188     1555   1555  2.43
LINK        ZN    ZN B 235                 SG  CYS B 153     1555   1555  2.39
SITE     1 AC1  4 CYS A 153  CYS A 156  CYS A 185  CYS A 188
SITE     1 AC2  4 CYS B 153  CYS B 156  CYS B 185  CYS B 188
SITE     1 AC3 30 MET A  28  PHE A  29  SER A  30  GLY A  31
SITE     2 AC3 30 LYS A  32  SER A  33  ASP A  58  ARG A  60
SITE     3 AC3 30 ASP A  97  GLU A  98  GLN A 100  PHE A 101
SITE     4 AC3 30 LEU A 124  THR A 127  PHE A 128  PHE A 133
SITE     5 AC3 30 VAL A 172  GLU A 173  VAL A 174  ILE A 175
SITE     6 AC3 30 GLY A 176  TYR A 181  HOH A 806  HOH A 810
SITE     7 AC3 30 HOH A 823  HOH A 831  HOH A 846  HOH A 863
SITE     8 AC3 30 HOH A 868  HOH A 880
SITE     1 AC4 27 MET B  28  PHE B  29  SER B  30  GLY B  31
SITE     2 AC4 27 LYS B  32  SER B  33  ASP B  58  ASP B  97
SITE     3 AC4 27 GLU B  98  GLN B 100  PHE B 101  LEU B 124
SITE     4 AC4 27 THR B 127  PHE B 128  PHE B 133  THR B 163
SITE     5 AC4 27 ARG B 165  VAL B 172  GLU B 173  VAL B 174
SITE     6 AC4 27 ILE B 175  GLY B 176  TYR B 181  HOH B 808
SITE     7 AC4 27 HOH B 821  HOH B 834  HOH B 872
CRYST1   80.980   80.980  156.360  90.00  90.00 120.00 P 31 2 1     12
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      0.012349  0.007130  0.000000        0.00000
SCALE2      0.000000  0.014259  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006395        0.00000
      
PROCHECK
Go to PROCHECK summary
 References