HEADER TRANSFERASE 23-MAY-00 1E2M
TITLE HPT + HMTT
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 17);
SOURCE 3 ORGANISM_TAXID: 10299;
SOURCE 4 STRAIN: 17;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.VOGT,L.SCAPOZZA,G.E.SCHULZ
REVDAT 4 06-DEC-23 1E2M 1 REMARK
REVDAT 3 16-JUN-09 1E2M 1 REMARK
REVDAT 2 24-FEB-09 1E2M 1 VERSN
REVDAT 1 31-MAR-01 1E2M 0
JRNL AUTH C.WURTH,U.KESSLER,J.VOGT,G.E.SCHULZ,G.FOLKERS,L.SCAPOZZA
JRNL TITL THE EFFECT OF SUBSTRATE BINDING ON THE CONFORMATION AND
JRNL TITL 2 STRUCTURAL STABILITY OF HERPES SIMPLEX VIRUS TYPE 1
JRNL TITL 3 THYMIDINE KINASE
JRNL REF PROTEIN SCI. V. 10 63 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11266595
JRNL DOI 10.1110/PS.27401
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 KINASE FROM
REMARK 1 TITL 2 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,C.MELITZ,
REMARK 1 AUTH 2 W.C.SUMMERS,M.R.SANDERSON
REMARK 1 TITL CRYSTAL STRUCTURES OF THE THYMIDINE KINASE FROM HERPES
REMARK 1 TITL 2 SIMPLEX VIRUS TYPE-1 IN COMPLEX WITH DEOXYTHYMIDINE AND
REMARK 1 TITL 3 GANCICLOVIR
REMARK 1 REF NAT.STRUCT.BIOL. V. 2 876 1995
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 7552712
REMARK 1 DOI 10.1038/NSB1095-876
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 36554
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) : 0.217
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1728
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4700
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
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): 0.270
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.500
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.007 ; NULL
REMARK 3 ANGLE DISTANCE (A) : 0.018 ; 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 1E2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-00.
REMARK 100 THE DEPOSITION ID IS D_1290004485.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-99
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) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU2HC
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36554
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
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) : 0.10600
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : 0.49000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTR 1VTK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE, HEPES, DTT, PH 7.50
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 54.25000
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 54.25000
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 56.85000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.60000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.85000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.60000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.25000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 56.85000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 58.60000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 54.25000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 56.85000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 58.60000
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: 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.0 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 117.20000
REMARK 350 BIOMT3 2 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 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 PRO A 153
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 PRO B 153
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: 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. = 10.2 DEGREES
REMARK 500 ARG A 320 CD - NE - CZ ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG A 320 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 320 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 ARG B 51 CD - NE - CZ ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG B 237 CD - NE - CZ ANGL. DEV. = 8.5 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 -154.03 -132.91
REMARK 500 LEU A 68 84.65 -58.52
REMARK 500 VAL A 90 -61.32 -128.56
REMARK 500 ALA A 93 -179.77 -171.43
REMARK 500 GLU A 95 78.70 33.25
REMARK 500 ARG A 163 156.31 81.09
REMARK 500 LEU A 170 -63.06 -130.36
REMARK 500 LEU A 227 97.29 -67.08
REMARK 500 VAL B 90 -60.78 -125.39
REMARK 500 ALA B 93 -179.64 -170.21
REMARK 500 GLU B 95 79.65 41.66
REMARK 500 ALA B 147 -68.85 -105.05
REMARK 500 ARG B 163 163.69 78.32
REMARK 500 LEU B 170 -60.40 -140.60
REMARK 500 LEU B 208 124.38 -172.20
REMARK 500 LEU B 227 70.62 45.91
REMARK 500 SER B 263 148.42 160.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 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 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPT A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HPT B 500
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: 1E2H RELATED DB: PDB
REMARK 900 RELATED ID: 1E2K RELATED DB: PDB
REMARK 900 RELATED ID: 1E2L RELATED DB: PDB
REMARK 900 RELATED ID: 1E2J RELATED DB: PDB
REMARK 900 RELATED ID: 1E2N RELATED DB: PDB
REMARK 900 RELATED ID: 1E2P RELATED DB: PDB
DBREF 1E2M A 46 376 UNP P03176 KITH_HSV11 46 376
DBREF 1E2M 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 HPT A 500 13
HET SO4 B 400 5
HET HPT B 500 13
HETNAM SO4 SULFATE ION
HETNAM HPT 6-HYDROXYPROPYLTHYMINE
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 HPT 2(C8 H12 N2 O3)
FORMUL 7 HOH *229(H2 O)
HELIX 1 1 GLY A 61 LEU A 68 1 8
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 PRO A 165 LEU A 170 1 6
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 ALA A 294 5 8
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 ALA B 140 1 28
HELIX 23 23 HIS B 164 LEU B 170 1 7
HELIX 24 24 LEU B 170 MET B 179 1 10
HELIX 25 25 THR B 183 ILE B 194 1 12
HELIX 26 26 PRO B 209 ALA B 218 1 10
HELIX 27 27 ASP B 228 CYS B 251 1 24
HELIX 28 28 SER B 254 TRP B 259 1 6
HELIX 29 29 GLY B 260 LEU B 262 5 3
HELIX 30 30 HIS B 283 THR B 287 5 5
HELIX 31 31 THR B 287 ARG B 293 5 7
HELIX 32 32 ALA B 294 LEU B 297 5 4
HELIX 33 33 TYR B 305 SER B 321 1 17
HELIX 34 34 SER B 332 THR B 344 1 13
HELIX 35 35 SER B 345 MET B 347 5 3
HELIX 36 36 GLY B 356 GLY B 373 1 18
SHEET 1 A 4 GLN A 349 HIS A 351 0
SHEET 2 A 4 THR A 48 ILE A 54 -1 N LEU A 49 O THR A 350
SHEET 3 A 4 LEU A 157 ASP A 162 1 N LEU A 157 O LEU A 50
SHEET 4 A 4 ILE A 78 VAL A 81 1 N VAL A 79 O THR A 158
SHEET 1 B 3 VAL A 52 ILE A 54 0
SHEET 2 B 3 ASN A 202 ALA A 207 1 N ASN A 202 O TYR A 53
SHEET 3 B 3 HIS A 323 ASP A 328 1 N HIS A 323 O ILE A 203
SHEET 1 C 5 HIS B 323 ASP B 328 0
SHEET 2 C 5 ASN B 202 ALA B 207 1 N ILE B 203 O HIS B 323
SHEET 3 C 5 LEU B 49 ILE B 54 1 N TYR B 53 O ASN B 202
SHEET 4 C 5 LEU B 157 ASP B 162 1 N LEU B 157 O LEU B 50
SHEET 5 C 5 ILE B 78 VAL B 81 1 N VAL B 79 O THR B 158
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 A2008
SITE 1 AC2 8 HIS B 58 GLY B 59 MET B 60 GLY B 61
SITE 2 AC2 8 LYS B 62 THR B 63 HOH B2108 HOH B2111
SITE 1 AC3 11 GLU A 83 ILE A 100 GLN A 125 ARG A 163
SITE 2 AC3 11 ALA A 168 TYR A 172 ARG A 222 HOH A2034
SITE 3 AC3 11 HOH A2057 HOH A2117 HOH A2118
SITE 1 AC4 11 HIS B 58 GLU B 83 GLN B 125 MET B 128
SITE 2 AC4 11 ARG B 163 ALA B 168 TYR B 172 HOH B2024
SITE 3 AC4 11 HOH B2109 HOH B2110 HOH B2111
CRYST1 113.700 117.200 108.500 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 0.008795 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008532 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009216 0.00000
MTRIX1 1 -0.924280 -0.328710 -0.194070 74.93742 1
MTRIX2 1 -0.326630 0.417940 0.847730 22.90658 1
MTRIX3 1 -0.197550 0.846920 -0.493660 -9.49576 1
(ATOM LINES ARE NOT SHOWN.)
END
