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PDBsum entry 1e2h

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Top Page protein ligands Protein-protein interface(s) links
Transferase PDB id
1e2h
Jmol
Contents
Protein chains
306 a.a. *
Ligands
SO4 ×2
Waters ×276
* Residue conservation analysis
HEADER    TRANSFERASE                             23-MAY-00   1E2H
TITLE     THE NUCLEOSIDE BINDING SITE OF HERPES SIMPLEX TYPE 1
TITLE    2 THYMIDINE KINASE ANALYZED BY X-RAY CRYSTALLOGRAPHY
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    TRANSFERASE, ADENINE ANALOG, ENZYME-PRODRUG GENE THERAPY,
KEYWDS   2 NUCLEOSIDE- BINDING, THYMIDINE KINASE, X-RAY
KEYWDS   3 CRYSTALLOGRAPHY
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.VOGT,L.SCAPOZZA,G.E.SCHULZ
REVDAT   2   24-FEB-09 1E2H    1       VERSN
REVDAT   1   06-NOV-00 1E2H    0
JRNL        AUTH   J.VOGT,R.PEROZZO,A.PAUTSCH,A.PROTA,P.SCHELLING,
JRNL        AUTH 2 B.PILGER,G.FOLKERS,L.SCAPOZZA,G.E.SCHULZ
JRNL        TITL   NUCLEOSIDE BINDING SITE OF HERPES SIMPLEX TYPE 1
JRNL        TITL 2 THYMIDINE KINASE ANALYZED BY X-RAY CRYSTALLOGRAPHY
JRNL        REF    PROTEINS: STRUCT.,FUNCT.,     V.  41   545 2000
JRNL        REF  2 GENET.
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   11056041
JRNL        DOI    10.1002/1097-0134(20001201)41:4<545::AID-PROT
JRNL        DOI  2 110>3.0.CO;2-8
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   K.WILD,T.BOHNER,A.AUBRY,G.FOLKERS,G.E.SCHULZ
REMARK   1  TITL   THE THREE-DIMENSIONAL STRUCTURE OF THYMIDINE
REMARK   1  TITL 2 KINASE FROM HERPES SIMPLEX VIRUS TYPE 1
REMARK   1  REF    FEBS LETT.                    V. 368   289 1995
REMARK   1  REFN                   ISSN 0014-5793
REMARK   1  PMID   7628623
REMARK   1  DOI    10.1016/0014-5793(95)00680-8
REMARK   1 REFERENCE 2
REMARK   1  AUTH   D.G.BROWN,R.VISSE,G.SANDHU,A.DAVIES,P.J.RIZKALLAH,
REMARK   1  AUTH 2 C.MELITZ,W.C.SUMMERS,M.R.SANDERSON
REMARK   1  TITL   CRYSTAL STRUCTURES OF THE THYMIDINE KINASE FROM
REMARK   1  TITL 2 HERPES SIMPLEX VIRUS TYPE-1 IN COMPLEX WITH
REMARK   1  TITL 3 DEOXYTHYMIDINE AND GANCICLOVIR
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   2   876 1995
REMARK   1  REFN                   ISSN 1072-8368
REMARK   1  PMID   7552712
REMARK   1  DOI    10.1038/NSB1095-876
REMARK   2
REMARK   2 RESOLUTION.    1.9  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.9
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99
REMARK   3   NUMBER OF REFLECTIONS             : 56856
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.215
REMARK   3   FREE R VALUE                     : 0.249
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 2873
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4714
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 10
REMARK   3   SOLVENT ATOMS            : 276
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 25.8
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.0
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.16
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.15
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.05
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.9
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.008 ; NULL
REMARK   3    ANGLE DISTANCE                  (A) : 0.021 ; NULL
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1E2H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-00.
REMARK 100 THE PDBE ID CODE IS EBI-4054.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 24-APR-98
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 7.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG
REMARK 200  BEAMLINE                       : X11
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9057
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56856
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.04900
REMARK 200  R SYM                      (I) : 0.04900
REMARK 200   FOR THE DATA SET  : 26.0000
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     (%) : 99.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40
REMARK 200  R MERGE FOR SHELL          (I) : 0.23100
REMARK 200  R SYM FOR SHELL            (I) : 0.23100
REMARK 200   FOR SHELL         : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1VTK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS:
REMARK 280 LITHIUM SULPHATE, HEPES, DTT
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       53.95000
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       53.95000
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       56.95000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       58.65000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.95000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       58.65000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.95000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.95000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       58.65000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.95000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.95000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       58.65000
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 300
REMARK 300 DETAILS:THE STRONG CRYSTAL PACKING GENERATED USING X
REMARK 300 , 1-Y, -Z GIVESCHAIN A TO CHAIN A (SYMMETRY
REMARK 300 RELATED) CONTACTS.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375      HOH B2124  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     VAL A    70
REMARK 465     ALA A    71
REMARK 465     LEU A    72
REMARK 465     GLY A    73
REMARK 465     SER A    74
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     GLY A   279
REMARK 465     ALA A   375
REMARK 465     ASN A   376
REMARK 465     SER B   150
REMARK 465     HIS B   151
REMARK 465     ALA B   152
REMARK 465     ARG B   220
REMARK 465     GLN B   221
REMARK 465     ARG B   222
REMARK 465     PRO B   223
REMARK 465     GLY B   224
REMARK 465     GLU B   225
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     ALA B   375
REMARK 465     ASN B   376
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    ASP B   328  -  NE2  GLN B   331              2.20
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    THR B  96   N     THR B  96   CA      0.271
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    ARG A  51   CD  -  NE  -  CZ  ANGL. DEV. =  12.2 DEGREES
REMARK 500    PRO A 154   C   -  N   -  CA  ANGL. DEV. = -17.2 DEGREES
REMARK 500    ARG A 222   CD  -  NE  -  CZ  ANGL. DEV. =   8.9 DEGREES
REMARK 500    ARG A 226   CD  -  NE  -  CZ  ANGL. DEV. =   9.1 DEGREES
REMARK 500    ARG A 320   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG B  51   CD  -  NE  -  CZ  ANGL. DEV. =  10.0 DEGREES
REMARK 500    THR B  96   C   -  N   -  CA  ANGL. DEV. = -25.0 DEGREES
REMARK 500    ARG B 237   CD  -  NE  -  CZ  ANGL. DEV. =  11.8 DEGREES
REMARK 500    VAL B 307   CB  -  CA  -  C   ANGL. DEV. = -11.4 DEGREES
REMARK 500    GLN B 331   CG  -  CD  -  OE1 ANGL. DEV. =  23.2 DEGREES
REMARK 500    GLN B 331   OE1 -  CD  -  NE2 ANGL. DEV. = -25.0 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 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    VAL A  90      -55.96   -132.28
REMARK 500    ARG A 163      156.69     83.11
REMARK 500    LEU A 170      -57.83   -145.57
REMARK 500    LEU A 208      127.88   -173.98
REMARK 500    ARG A 220       48.21   -156.28
REMARK 500    ARG A 293       58.05    -93.30
REMARK 500    VAL B  90      -69.56   -124.00
REMARK 500    ALA B  93     -179.20   -171.29
REMARK 500    ARG B 163      156.95     82.20
REMARK 500    LEU B 170      -61.75   -146.46
REMARK 500    LEU B 208      119.07   -174.75
REMARK 500    ALA B 218        7.65    -56.10
REMARK 500    LEU B 227       64.23     65.60
REMARK 500    PHE B 292       30.16    -97.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PRO A 154        23.6      L          L   OUTSIDE RANGE
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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KIM   RELATED DB: PDB
REMARK 900 RELATED ID: 1VTK   RELATED DB: PDB
REMARK 900 RELATED ID: 2VTK   RELATED DB: PDB
REMARK 900 RELATED ID: 3VTK   RELATED DB: PDB
REMARK 900 RELATED ID: 1KI2   RELATED DB: PDB
REMARK 900 RELATED ID: 1KI4   RELATED DB: PDB
REMARK 900 RELATED ID: 1KI5   RELATED DB: PDB
REMARK 900 RELATED ID: 1KI6   RELATED DB: PDB
REMARK 900 RELATED ID: 1KI7   RELATED DB: PDB
REMARK 900 RELATED ID: 1KI8   RELATED DB: PDB
REMARK 900 RELATED ID: 1E2I   RELATED DB: PDB
REMARK 900 RELATED ID: 1E2J   RELATED DB: PDB
REMARK 900 RELATED ID: 1E2K   RELATED DB: PDB
REMARK 900 RELATED ID: 1E2L   RELATED DB: PDB
REMARK 900 RELATED ID: 1E2M   RELATED DB: PDB
REMARK 900 RELATED ID: 1E2N   RELATED DB: PDB
REMARK 900 RELATED ID: 1E2P   RELATED DB: PDB
DBREF  1E2H A   46   376  UNP    P03176   KITH_HSV11      46    376
DBREF  1E2H B   46   376  UNP    P03176   KITH_HSV11      46    376
SEQRES   1 A  331  MET PRO THR LEU LEU ARG VAL TYR ILE ASP GLY PRO HIS
SEQRES   2 A  331  GLY MET GLY LYS THR THR THR THR GLN LEU LEU VAL ALA
SEQRES   3 A  331  LEU GLY SER ARG ASP ASP ILE VAL TYR VAL PRO GLU PRO
SEQRES   4 A  331  MET THR TYR TRP ARG VAL LEU GLY ALA SER GLU THR ILE
SEQRES   5 A  331  ALA ASN ILE TYR THR THR GLN HIS ARG LEU ASP GLN GLY
SEQRES   6 A  331  GLU ILE SER ALA GLY ASP ALA ALA VAL VAL MET THR SER
SEQRES   7 A  331  ALA GLN ILE THR MET GLY MET PRO TYR ALA VAL THR ASP
SEQRES   8 A  331  ALA VAL LEU ALA PRO HIS ILE GLY GLY GLU ALA GLY SER
SEQRES   9 A  331  SER HIS ALA PRO PRO PRO ALA LEU THR LEU ILE PHE ASP
SEQRES  10 A  331  ARG HIS PRO ILE ALA ALA LEU LEU CYS TYR PRO ALA ALA
SEQRES  11 A  331  ARG TYR LEU MET GLY SER MET THR PRO GLN ALA VAL LEU
SEQRES  12 A  331  ALA PHE VAL ALA LEU ILE PRO PRO THR LEU PRO GLY THR
SEQRES  13 A  331  ASN ILE VAL LEU GLY ALA LEU PRO GLU ASP ARG HIS ILE
SEQRES  14 A  331  ASP ARG LEU ALA LYS ARG GLN ARG PRO GLY GLU ARG LEU
SEQRES  15 A  331  ASP LEU ALA MET LEU ALA ALA ILE ARG ARG VAL TYR GLY
SEQRES  16 A  331  LEU LEU ALA ASN THR VAL ARG TYR LEU GLN CYS GLY GLY
SEQRES  17 A  331  SER TRP ARG GLU ASP TRP GLY GLN LEU SER GLY THR ALA
SEQRES  18 A  331  VAL PRO PRO GLN GLY ALA GLU PRO GLN SER ASN ALA GLY
SEQRES  19 A  331  PRO ARG PRO HIS ILE GLY ASP THR LEU PHE THR LEU PHE
SEQRES  20 A  331  ARG ALA PRO GLU LEU LEU ALA PRO ASN GLY ASP LEU TYR
SEQRES  21 A  331  ASN VAL PHE ALA TRP ALA LEU ASP VAL LEU ALA LYS ARG
SEQRES  22 A  331  LEU ARG SER MET HIS VAL PHE ILE LEU ASP TYR ASP GLN
SEQRES  23 A  331  SER PRO ALA GLY CYS ARG ASP ALA LEU LEU GLN LEU THR
SEQRES  24 A  331  SER GLY MET VAL GLN THR HIS VAL THR THR PRO GLY SER
SEQRES  25 A  331  ILE PRO THR ILE CYS ASP LEU ALA ARG THR PHE ALA ARG
SEQRES  26 A  331  GLU MET GLY GLU ALA ASN
SEQRES   1 B  331  MET PRO THR LEU LEU ARG VAL TYR ILE ASP GLY PRO HIS
SEQRES   2 B  331  GLY MET GLY LYS THR THR THR THR GLN LEU LEU VAL ALA
SEQRES   3 B  331  LEU GLY SER ARG ASP ASP ILE VAL TYR VAL PRO GLU PRO
SEQRES   4 B  331  MET THR TYR TRP ARG VAL LEU GLY ALA SER GLU THR ILE
SEQRES   5 B  331  ALA ASN ILE TYR THR THR GLN HIS ARG LEU ASP GLN GLY
SEQRES   6 B  331  GLU ILE SER ALA GLY ASP ALA ALA VAL VAL MET THR SER
SEQRES   7 B  331  ALA GLN ILE THR MET GLY MET PRO TYR ALA VAL THR ASP
SEQRES   8 B  331  ALA VAL LEU ALA PRO HIS ILE GLY GLY GLU ALA GLY SER
SEQRES   9 B  331  SER HIS ALA PRO PRO PRO ALA LEU THR LEU ILE PHE ASP
SEQRES  10 B  331  ARG HIS PRO ILE ALA ALA LEU LEU CYS TYR PRO ALA ALA
SEQRES  11 B  331  ARG TYR LEU MET GLY SER MET THR PRO GLN ALA VAL LEU
SEQRES  12 B  331  ALA PHE VAL ALA LEU ILE PRO PRO THR LEU PRO GLY THR
SEQRES  13 B  331  ASN ILE VAL LEU GLY ALA LEU PRO GLU ASP ARG HIS ILE
SEQRES  14 B  331  ASP ARG LEU ALA LYS ARG GLN ARG PRO GLY GLU ARG LEU
SEQRES  15 B  331  ASP LEU ALA MET LEU ALA ALA ILE ARG ARG VAL TYR GLY
SEQRES  16 B  331  LEU LEU ALA ASN THR VAL ARG TYR LEU GLN CYS GLY GLY
SEQRES  17 B  331  SER TRP ARG GLU ASP TRP GLY GLN LEU SER GLY THR ALA
SEQRES  18 B  331  VAL PRO PRO GLN GLY ALA GLU PRO GLN SER ASN ALA GLY
SEQRES  19 B  331  PRO ARG PRO HIS ILE GLY ASP THR LEU PHE THR LEU PHE
SEQRES  20 B  331  ARG ALA PRO GLU LEU LEU ALA PRO ASN GLY ASP LEU TYR
SEQRES  21 B  331  ASN VAL PHE ALA TRP ALA LEU ASP VAL LEU ALA LYS ARG
SEQRES  22 B  331  LEU ARG SER MET HIS VAL PHE ILE LEU ASP TYR ASP GLN
SEQRES  23 B  331  SER PRO ALA GLY CYS ARG ASP ALA LEU LEU GLN LEU THR
SEQRES  24 B  331  SER GLY MET VAL GLN THR HIS VAL THR THR PRO GLY SER
SEQRES  25 B  331  ILE PRO THR ILE CYS ASP LEU ALA ARG THR PHE ALA ARG
SEQRES  26 B  331  GLU MET GLY GLU ALA ASN
HET    SO4  A 400       5
HET    SO4  B 400       5
HETNAM     SO4 SULFATE ION
FORMUL   3  SO4    2(O4 S 2-)
FORMUL   5  HOH   *276(H2 O1)
HELIX    1   1 GLY A   61  LEU A   69  1                                   9
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  LEU A  193  1                                  11
HELIX    8   8 PRO A  209  LYS A  219  1                                  11
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  SER A  263  5                                   4
HELIX   12  12 HIS A  283  THR A  287  5                                   5
HELIX   13  13 THR A  287  ARG A  293  5                                   7
HELIX   14  14 ALA A  294  LEU A  297  5                                   4
HELIX   15  15 TYR A  305  SER A  321  1                                  17
HELIX   16  16 SER A  332  THR A  344  1                                  13
HELIX   17  17 SER A  345  MET A  347  5                                   3
HELIX   18  18 GLY A  356  GLY A  373  1                                  18
HELIX   19  19 GLY B   61  GLY B   73  1                                  13
HELIX   20  20 PRO B   84  VAL B   90  1                                   7
HELIX   21  21 GLU B   95  GLN B  109  1                                  15
HELIX   22  22 SER B  113  GLY B  129  1                                  17
HELIX   23  23 GLY B  129  ALA B  140  1                                  12
HELIX   24  24 HIS B  164  LEU B  170  1                                   7
HELIX   25  25 LEU B  170  MET B  179  1                                  10
HELIX   26  26 THR B  183  LEU B  193  1                                  11
HELIX   27  27 PRO B  209  ALA B  218  1                                  10
HELIX   28  28 ASP B  228  CYS B  251  1                                  24
HELIX   29  29 SER B  254  TRP B  259  1                                   6
HELIX   30  30 GLY B  260  LEU B  262  5                                   3
HELIX   31  31 HIS B  283  THR B  287  5                                   5
HELIX   32  32 THR B  287  ALA B  294  5                                   8
HELIX   33  33 ALA B  294  LEU B  297  5                                   4
HELIX   34  34 TYR B  305  SER B  321  1                                  17
HELIX   35  35 SER B  332  SER B  345  1                                  14
HELIX   36  36 GLY B  356  MET B  372  1                                  17
SHEET    1   A 5 HIS A 323  ASP A 328  0
SHEET    2   A 5 ASN A 202  ALA A 207  1  N  ILE A 203   O  HIS A 323
SHEET    3   A 5 LEU A  49  ILE A  54  1  N  TYR A  53   O  ASN A 202
SHEET    4   A 5 LEU A 157  ASP A 162  1  N  LEU A 157   O  LEU A  50
SHEET    5   A 5 ILE A  78  VAL A  81  1  N  VAL A  79   O  THR A 158
SHEET    1   B 4 GLN B 349  HIS B 351  0
SHEET    2   B 4 THR B  48  ILE B  54 -1  N  LEU B  49   O  THR B 350
SHEET    3   B 4 LEU B 157  ASP B 162  1  N  LEU B 157   O  LEU B  50
SHEET    4   B 4 ILE B  78  VAL B  81  1  N  VAL B  79   O  THR B 158
SHEET    1   C 3 VAL B  52  ILE B  54  0
SHEET    2   C 3 ASN B 202  ALA B 207  1  N  ASN B 202   O  TYR B  53
SHEET    3   C 3 HIS B 323  ASP B 328  1  N  HIS B 323   O  ILE B 203
SITE     1 AC1  9 HIS A  58  GLY A  59  MET A  60  GLY A  61
SITE     2 AC1  9 LYS A  62  THR A  63  ARG A 220  ARG A 222
SITE     3 AC1  9 HOH A2143
SITE     1 AC2  7 GLY B  59  MET B  60  GLY B  61  LYS B  62
SITE     2 AC2  7 THR B  63  HOH B2004  HOH B2133
CRYST1  113.900  117.300  107.900  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      0.008780  0.000000  0.000000        0.00000
SCALE2      0.000000  0.008525  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009268        0.00000
MTRIX1   1 -0.928570 -0.313860 -0.198110       74.95680    1
MTRIX2   1 -0.323200  0.421380  0.847330       22.60310    1
MTRIX3   1 -0.182460  0.850840 -0.492730      -10.07007    1
      
PROCHECK
Go to PROCHECK summary
 References