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PDBsum entry 1p7c

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
1p7c
Jmol
Contents
Protein chains
301 a.a. *
318 a.a. *
Ligands
T5A
SO4
THM
Waters ×340
* Residue conservation analysis
HEADER    TRANSFERASE                             01-MAY-03   1P7C
TITLE     CRYSTAL STRUCTURE OF HSV1-TK COMPLEXED WITH TP5A
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
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HERPES SIMPLEX VIRUS (TYPE 1 / STRAIN
SOURCE   3 17);
SOURCE   4 ORGANISM_TAXID: 10299;
SOURCE   5 STRAIN: 17;
SOURCE   6 GENE: TK OR UL23;
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-RB
KEYWDS    P-LOOP, LID, BISUBSTRATE INHIBITOR, TRANSFERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.GARDBERG,L.SHUVALOVA,C.MONNERJAHN,M.KONRAD,A.LAVIE
REVDAT   2   24-FEB-09 1P7C    1       VERSN
REVDAT   1   04-NOV-03 1P7C    0
JRNL        AUTH   A.GARDBERG,L.SHUVALOVA,C.MONNERJAHN,M.KONRAD,
JRNL        AUTH 2 A.LAVIE
JRNL        TITL   STRUCTURAL BASIS FOR THE DUAL THYMIDINE AND
JRNL        TITL 2 THYMIDYLATE KINASE ACTIVITY OF HERPES THYMIDINE
JRNL        TITL 3 KINASES.
JRNL        REF    STRUCTURE                     V.  11  1265 2003
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   14527394
JRNL        DOI    10.1016/J.STR.2003.09.003
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
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) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.94
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9
REMARK   3   NUMBER OF REFLECTIONS             : 37137
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) : 0.244
REMARK   3   R VALUE            (WORKING SET) : 0.239
REMARK   3   FREE R VALUE                     : 0.285
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4142
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2756
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790
REMARK   3   BIN FREE R VALUE SET COUNT          : 283
REMARK   3   BIN FREE R VALUE                    : 0.3420
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4654
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 77
REMARK   3   SOLVENT ATOMS            : 340
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.63
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.53000
REMARK   3    B22 (A**2) : 1.82000
REMARK   3    B33 (A**2) : -1.29000
REMARK   3    B12 (A**2) : 0.00000
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): 0.288
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.231
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.084
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.900
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4842 ; 0.011 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6629 ; 1.429 ; 1.990
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   612 ; 5.624 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   773 ; 0.090 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3638 ; 0.005 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2403 ; 0.213 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   339 ; 0.176 ; 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):    65 ; 0.244 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.338 ; 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):  3086 ; 0.703 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4951 ; 1.300 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1756 ; 1.837 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1678 ; 3.005 ; 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 : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : BABINET MODEL WITH MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1P7C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-03.
REMARK 100 THE RCSB ID CODE IS RCSB019098.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 2000
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.75
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 14-BM-C
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                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41672
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
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   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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1VTK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS, TP5A, PH
REMARK 280  6.75, VAPOR DIFFUSION, HANGING DROP
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       54.20000
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       54.20000
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       56.60950
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.92350
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.60950
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.92350
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.20000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.60950
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       58.92350
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.20000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.60950
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       58.92350
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: 5620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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 B 503  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B 668  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     GLN A    34
REMARK 465     GLN A    35
REMARK 465     GLU A    36
REMARK 465     ALA A    37
REMARK 465     THR A    38
REMARK 465     GLU A    39
REMARK 465     VAL A    40
REMARK 465     ARG A    41
REMARK 465     PRO A    42
REMARK 465     GLU A    43
REMARK 465     GLN A    44
REMARK 465     GLY A    73
REMARK 465     SER A    74
REMARK 465     ARG A    75
REMARK 465     ASP A    76
REMARK 465     MET A    85
REMARK 465     THR A    86
REMARK 465     TYR A    87
REMARK 465     TRP A    88
REMARK 465     SER A   149
REMARK 465     SER A   150
REMARK 465     HIS A   151
REMARK 465     ALA A   152
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     MET A   372
REMARK 465     GLY A   373
REMARK 465     GLU A   374
REMARK 465     ALA A   375
REMARK 465     ASN A   376
REMARK 465     GLN B    34
REMARK 465     GLN B    35
REMARK 465     GLU B    36
REMARK 465     ALA B    37
REMARK 465     THR B    38
REMARK 465     GLU B    39
REMARK 465     VAL B    40
REMARK 465     ARG B    41
REMARK 465     PRO B    42
REMARK 465     GLU B    43
REMARK 465     GLN B    44
REMARK 465     LYS B    45
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 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     LEU A  72    CG   CD1  CD2
REMARK 470     ARG A  89    CG   CD   NE   CZ   NH1  NH2
REMARK 470     VAL A  90    CG1  CG2
REMARK 470     LEU A  91    CG   CD1  CD2
REMARK 470     SER A  94    OG
REMARK 470     GLN A 221    CG   CD   OE1  NE2
REMARK 470     CYS A 251    SG
REMARK 470     ARG A 366    CG   CD   NE   CZ   NH1  NH2
REMARK 470     ARG A 370    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER B  74    OG
REMARK 470     ARG B  75    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER B 149    OG
REMARK 470     SER B 150    OG
REMARK 470     HIS B 151    CG   ND1  CD2  CE1  NE2
REMARK 470     GLN B 221    CG   CD   OE1  NE2
REMARK 470     ARG B 247    CG   CD   NE   CZ   NH1  NH2
REMARK 470     SER B 263    OG
REMARK 470     ASN B 376    CG   OD1  ND2
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   CB   SER B   149     O    MET B   347              2.14
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 B   653     O    HOH B   653     3555     1.59
REMARK 500   O    HOH A   615     O    HOH A   615     4566     1.84
REMARK 500   NH2  ARG A   320     NH2  ARG A   320     4566     1.92
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 A  55   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES
REMARK 500    ASP A 116   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 303   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ASP B 116   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ASP B 211   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP B 215   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP B 286   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP B 303   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES
REMARK 500    ARG B 318   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG B 318   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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     -154.54   -134.26
REMARK 500    VAL A  90      -55.53     64.81
REMARK 500    LEU A  91       40.61   -161.26
REMARK 500    SER A  94       53.74    -69.12
REMARK 500    GLU A  95       92.95     32.58
REMARK 500    ALA A 147      -89.48    -95.06
REMARK 500    ARG A 163      156.29     82.48
REMARK 500    LEU A 170      -58.55   -146.39
REMARK 500    ARG A 293       21.80    -79.70
REMARK 500    LEU B  72        1.22    -58.60
REMARK 500    SER B  74      -46.31    101.44
REMARK 500    ARG B  75      -43.01     53.76
REMARK 500    VAL B  90      -54.68   -134.06
REMARK 500    GLU B 146      126.56    -32.55
REMARK 500    SER B 149      -75.91     42.43
REMARK 500    SER B 150       97.24    -23.86
REMARK 500    PRO B 153     -163.71    -65.57
REMARK 500    ARG B 163      148.94     84.14
REMARK 500    LEU B 170      -60.44   -142.37
REMARK 500    SER B 263      -80.90   -133.53
REMARK 500    ARG B 293       75.20   -104.39
REMARK 500    PRO B 300       67.02    -62.99
REMARK 500    ASN B 301        5.45    178.88
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 A 662        DISTANCE =  5.55 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM B 501
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T5A A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P75   RELATED DB: PDB
REMARK 900 EHV4-TK COMPLEXED WITH SAME LIGAND
REMARK 900 RELATED ID: 1P72   RELATED DB: PDB
REMARK 900 EHV4-TK COMPLEXED WITH THY AND ADP
REMARK 900 RELATED ID: 1P6X   RELATED DB: PDB
REMARK 900 EHV4-TK COMPLEXED WITH THY AND SO4
REMARK 900 RELATED ID: 1P73   RELATED DB: PDB
REMARK 900 EHV4-TK COMPLEXED WITH TP4A
DBREF  1P7C A   34   376  UNP    P03176   KITH_HHV11      34    376
DBREF  1P7C B   34   376  UNP    P03176   KITH_HHV11      34    376
SEQRES   1 A  343  GLN GLN GLU ALA THR GLU VAL ARG PRO GLU GLN LYS MET
SEQRES   2 A  343  PRO THR LEU LEU ARG VAL TYR ILE ASP GLY PRO HIS GLY
SEQRES   3 A  343  MET GLY LYS THR THR THR THR GLN LEU LEU VAL ALA LEU
SEQRES   4 A  343  GLY SER ARG ASP ASP ILE VAL TYR VAL PRO GLU PRO MET
SEQRES   5 A  343  THR TYR TRP ARG VAL LEU GLY ALA SER GLU THR ILE ALA
SEQRES   6 A  343  ASN ILE TYR THR THR GLN HIS ARG LEU ASP GLN GLY GLU
SEQRES   7 A  343  ILE SER ALA GLY ASP ALA ALA VAL VAL MET THR SER ALA
SEQRES   8 A  343  GLN ILE THR MET GLY MET PRO TYR ALA VAL THR ASP ALA
SEQRES   9 A  343  VAL LEU ALA PRO HIS ILE GLY GLY GLU ALA GLY SER SER
SEQRES  10 A  343  HIS ALA PRO PRO PRO ALA LEU THR LEU ILE PHE ASP ARG
SEQRES  11 A  343  HIS PRO ILE ALA ALA LEU LEU CYS TYR PRO ALA ALA ARG
SEQRES  12 A  343  TYR LEU MET GLY SER MET THR PRO GLN ALA VAL LEU ALA
SEQRES  13 A  343  PHE VAL ALA LEU ILE PRO PRO THR LEU PRO GLY THR ASN
SEQRES  14 A  343  ILE VAL LEU GLY ALA LEU PRO GLU ASP ARG HIS ILE ASP
SEQRES  15 A  343  ARG LEU ALA LYS ARG GLN ARG PRO GLY GLU ARG LEU ASP
SEQRES  16 A  343  LEU ALA MET LEU ALA ALA ILE ARG ARG VAL TYR GLY LEU
SEQRES  17 A  343  LEU ALA ASN THR VAL ARG TYR LEU GLN CYS GLY GLY SER
SEQRES  18 A  343  TRP ARG GLU ASP TRP GLY GLN LEU SER GLY THR ALA VAL
SEQRES  19 A  343  PRO PRO GLN GLY ALA GLU PRO GLN SER ASN ALA GLY PRO
SEQRES  20 A  343  ARG PRO HIS ILE GLY ASP THR LEU PHE THR LEU PHE ARG
SEQRES  21 A  343  ALA PRO GLU LEU LEU ALA PRO ASN GLY ASP LEU TYR ASN
SEQRES  22 A  343  VAL PHE ALA TRP ALA LEU ASP VAL LEU ALA LYS ARG LEU
SEQRES  23 A  343  ARG SER MET HIS VAL PHE ILE LEU ASP TYR ASP GLN SER
SEQRES  24 A  343  PRO ALA GLY CYS ARG ASP ALA LEU LEU GLN LEU THR SER
SEQRES  25 A  343  GLY MET VAL GLN THR HIS VAL THR THR PRO GLY SER ILE
SEQRES  26 A  343  PRO THR ILE CYS ASP LEU ALA ARG THR PHE ALA ARG GLU
SEQRES  27 A  343  MET GLY GLU ALA ASN
SEQRES   1 B  343  GLN GLN GLU ALA THR GLU VAL ARG PRO GLU GLN LYS MET
SEQRES   2 B  343  PRO THR LEU LEU ARG VAL TYR ILE ASP GLY PRO HIS GLY
SEQRES   3 B  343  MET GLY LYS THR THR THR THR GLN LEU LEU VAL ALA LEU
SEQRES   4 B  343  GLY SER ARG ASP ASP ILE VAL TYR VAL PRO GLU PRO MET
SEQRES   5 B  343  THR TYR TRP ARG VAL LEU GLY ALA SER GLU THR ILE ALA
SEQRES   6 B  343  ASN ILE TYR THR THR GLN HIS ARG LEU ASP GLN GLY GLU
SEQRES   7 B  343  ILE SER ALA GLY ASP ALA ALA VAL VAL MET THR SER ALA
SEQRES   8 B  343  GLN ILE THR MET GLY MET PRO TYR ALA VAL THR ASP ALA
SEQRES   9 B  343  VAL LEU ALA PRO HIS ILE GLY GLY GLU ALA GLY SER SER
SEQRES  10 B  343  HIS ALA PRO PRO PRO ALA LEU THR LEU ILE PHE ASP ARG
SEQRES  11 B  343  HIS PRO ILE ALA ALA LEU LEU CYS TYR PRO ALA ALA ARG
SEQRES  12 B  343  TYR LEU MET GLY SER MET THR PRO GLN ALA VAL LEU ALA
SEQRES  13 B  343  PHE VAL ALA LEU ILE PRO PRO THR LEU PRO GLY THR ASN
SEQRES  14 B  343  ILE VAL LEU GLY ALA LEU PRO GLU ASP ARG HIS ILE ASP
SEQRES  15 B  343  ARG LEU ALA LYS ARG GLN ARG PRO GLY GLU ARG LEU ASP
SEQRES  16 B  343  LEU ALA MET LEU ALA ALA ILE ARG ARG VAL TYR GLY LEU
SEQRES  17 B  343  LEU ALA ASN THR VAL ARG TYR LEU GLN CYS GLY GLY SER
SEQRES  18 B  343  TRP ARG GLU ASP TRP GLY GLN LEU SER GLY THR ALA VAL
SEQRES  19 B  343  PRO PRO GLN GLY ALA GLU PRO GLN SER ASN ALA GLY PRO
SEQRES  20 B  343  ARG PRO HIS ILE GLY ASP THR LEU PHE THR LEU PHE ARG
SEQRES  21 B  343  ALA PRO GLU LEU LEU ALA PRO ASN GLY ASP LEU TYR ASN
SEQRES  22 B  343  VAL PHE ALA TRP ALA LEU ASP VAL LEU ALA LYS ARG LEU
SEQRES  23 B  343  ARG SER MET HIS VAL PHE ILE LEU ASP TYR ASP GLN SER
SEQRES  24 B  343  PRO ALA GLY CYS ARG ASP ALA LEU LEU GLN LEU THR SER
SEQRES  25 B  343  GLY MET VAL GLN THR HIS VAL THR THR PRO GLY SER ILE
SEQRES  26 B  343  PRO THR ILE CYS ASP LEU ALA ARG THR PHE ALA ARG GLU
SEQRES  27 B  343  MET GLY GLU ALA ASN
HET    SO4  B 502       5
HET    THM  B 501      17
HET    T5A  A 503      55
HETNAM     SO4 SULFATE ION
HETNAM     THM THYMIDINE
HETNAM     T5A P1-(5'-ADENOSYL)P5-(5'-THYMIDYL)PENTAPHOSPHATE
HETSYN     THM DEOXYTHYMIDINE; 2'-DEOXYTHYMIDINE
FORMUL   3  SO4    O4 S 2-
FORMUL   4  THM    C10 H14 N2 O5
FORMUL   5  T5A    C20 H30 N7 O23 P5
FORMUL   6  HOH   *340(H2 O)
HELIX    1   1 GLY A   61  ALA A   71  1                                  11
HELIX    2   2 GLU A   95  GLN A  109  1                                  15
HELIX    3   3 SER A  113  ALA A  140  1                                  28
HELIX    4   4 PRO A  165  LEU A  170  1                                   6
HELIX    5   5 LEU A  170  MET A  179  1                                  10
HELIX    6   6 THR A  183  LEU A  193  1                                  11
HELIX    7   7 PRO A  209  ARG A  220  1                                  12
HELIX    8   8 ASP A  228  CYS A  251  1                                  24
HELIX    9   9 SER A  254  TRP A  259  1                                   6
HELIX   10  10 GLY A  260  SER A  263  5                                   4
HELIX   11  11 HIS A  283  ARG A  293  5                                  11
HELIX   12  12 ALA A  294  LEU A  298  5                                   5
HELIX   13  13 TYR A  305  ARG A  320  1                                  16
HELIX   14  14 SER A  332  THR A  344  1                                  13
HELIX   15  15 SER A  345  MET A  347  5                                   3
HELIX   16  16 GLY A  356  GLU A  371  1                                  16
HELIX   17  17 GLY B   61  LEU B   72  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 PRO B  165  LEU B  170  1                                   6
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  LEU B  262  5                                   3
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  ARG B  320  1                                  16
HELIX   31  31 SER B  332  GLY B  346  1                                  15
HELIX   32  32 GLY B  356  GLY B  373  1                                  18
SHEET    1   A 5 HIS A 323  ASP A 328  0
SHEET    2   A 5 ASN A 202  ALA A 207  1  N  LEU A 205   O  LEU A 327
SHEET    3   A 5 THR A  48  ILE A  54  1  N  TYR A  53   O  ASN A 202
SHEET    4   A 5 LEU A 157  ASP A 162  1  O  PHE A 161   N  VAL A  52
SHEET    5   A 5 ILE A  78  VAL A  81  1  N  VAL A  81   O  ILE A 160
SHEET    1   B 4 HIS A 323  ASP A 328  0
SHEET    2   B 4 ASN A 202  ALA A 207  1  N  LEU A 205   O  LEU A 327
SHEET    3   B 4 THR A  48  ILE A  54  1  N  TYR A  53   O  ASN A 202
SHEET    4   B 4 THR A 350  VAL A 352 -1  O  THR A 350   N  LEU A  49
SHEET    1   C 5 HIS B 323  ASP B 328  0
SHEET    2   C 5 ASN B 202  ALA B 207  1  N  LEU B 205   O  PHE B 325
SHEET    3   C 5 THR B  48  ASP B  55  1  N  TYR B  53   O  VAL B 204
SHEET    4   C 5 LEU B 157  ASP B 162  1  O  PHE B 161   N  VAL B  52
SHEET    5   C 5 ILE B  78  VAL B  81  1  N  VAL B  81   O  ASP B 162
SHEET    1   D 4 HIS B 323  ASP B 328  0
SHEET    2   D 4 ASN B 202  ALA B 207  1  N  LEU B 205   O  PHE B 325
SHEET    3   D 4 THR B  48  ASP B  55  1  N  TYR B  53   O  VAL B 204
SHEET    4   D 4 THR B 350  VAL B 352 -1  O  THR B 350   N  LEU B  49
SITE     1 AC1  9 HIS B  58  GLY B  59  MET B  60  GLY B  61
SITE     2 AC1  9 LYS B  62  THR B  63  ARG B 220  HOH B 519
SITE     3 AC1  9 HOH B 540
SITE     1 AC2 13 HIS B  58  GLU B  83  TRP B  88  TYR B 101
SITE     2 AC2 13 GLN B 125  MET B 128  ARG B 163  ALA B 168
SITE     3 AC2 13 TYR B 172  GLU B 225  HOH B 532  HOH B 575
SITE     4 AC2 13 HOH B 590
SITE     1 AC3 33 HIS A  58  GLY A  59  MET A  60  GLY A  61
SITE     2 AC3 33 LYS A  62  THR A  63  THR A  64  GLU A  83
SITE     3 AC3 33 ILE A  97  ILE A 100  TYR A 101  GLN A 125
SITE     4 AC3 33 MET A 128  TYR A 132  ARG A 163  ALA A 168
SITE     5 AC3 33 TYR A 172  ARG A 216  LYS A 219  ARG A 220
SITE     6 AC3 33 ARG A 222  GLU A 225  GLN A 331  SER A 332
SITE     7 AC3 33 PRO A 333  CYS A 336  HOH A 593  HOH A 608
SITE     8 AC3 33 HOH A 637  HOH A 642  HOH A 660  GLN B 221
SITE     9 AC3 33 ASN B 376
CRYST1  113.219  117.847  108.400  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      0.008832  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008486  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009225        0.00000
      
PROCHECK
Go to PROCHECK summary
 References