HEADER TRANSFERASE 01-APR-97 2VTK
TITLE THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS TYPE 1 IN COMPLEX WITH ADP
TITLE 2 AND DEOXYTHYMIDINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDINE KINASE;
COMPND 3 CHAIN: A;
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 F);
SOURCE 3 ORGANISM_TAXID: 10304;
SOURCE 4 STRAIN: F;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: KY 895;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS KEY ENZYME IN THYMIDINE SALVAGE PATHWAY, ADDITIONAL THYMIDYLATE
KEYWDS 2 KINASE ACTIVITY, TARGET FOR ANTI-HERPES VIRAL DRUGS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.WILD,G.E.SCHULZ
REVDAT 4 21-FEB-24 2VTK 1 REMARK ATOM
REVDAT 3 13-JUL-11 2VTK 1 VERSN
REVDAT 2 24-FEB-09 2VTK 1 VERSN
REVDAT 1 22-OCT-97 2VTK 0
JRNL AUTH K.WILD,T.BOHNER,G.FOLKERS,G.E.SCHULZ
JRNL TITL THE STRUCTURES OF THYMIDINE KINASE FROM HERPES SIMPLEX VIRUS
JRNL TITL 2 TYPE 1 IN COMPLEX WITH SUBSTRATES AND A SUBSTRATE ANALOGUE.
JRNL REF PROTEIN SCI. V. 6 2097 1997
JRNL REFN ISSN 0961-8368
JRNL PMID 9336833
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 REFERENCE 2
REMARK 1 AUTH J.FETZER,M.MICHAEL,T.BOHNER,R.HOFBAUER,G.FOLKERS
REMARK 1 TITL A FAST METHOD FOR OBTAINING HIGHLY PURE RECOMBINANT HERPES
REMARK 1 TITL 2 SIMPLEX VIRUS TYPE 1 THYMIDINE KINASE
REMARK 1 REF PROTEIN EXPR.PURIF. V. 5 432 1994
REMARK 1 REFN ISSN 1046-5928
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 83.4
REMARK 3 NUMBER OF REFLECTIONS : 11171
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 SET) : 0.175
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1099
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 64.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 918
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 104
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.032
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2391
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 28
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.50
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.46
REMARK 3 LOW RESOLUTION CUTOFF (A) : 4.80
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.480
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.680
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 5.000 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 6.600 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 8.100 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 11.400; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : TOP19.SOL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2VTK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178741.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : JAN-96
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : 5.5
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : MERGE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11472
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 83.1
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 3555 -Y,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X,Z+3/4
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y,Z
REMARK 290 7555 -Y+1/2,X,Z+3/4
REMARK 290 8555 Y,-X+1/2,Z+1/4
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 42.05000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 42.05000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.68000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 42.05000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 38.84000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 42.05000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 116.52000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 42.05000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.05000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 77.68000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 42.05000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 116.52000
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 42.05000
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 38.84000
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 84.10000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 625 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 LYS A 45
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 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 ALA A 71 32.99 -87.70
REMARK 500 ARG A 75 -146.31 42.62
REMARK 500 VAL A 90 -65.93 -133.75
REMARK 500 ALA A 147 62.37 -102.33
REMARK 500 PRO A 154 103.18 -38.62
REMARK 500 ARG A 163 145.30 83.80
REMARK 500 LEU A 170 -60.17 -135.20
REMARK 500 PRO A 223 104.29 -54.30
REMARK 500 SER A 263 58.57 -63.62
REMARK 500 ASP A 330 66.04 -66.57
REMARK 500 GLN A 331 -175.60 -170.69
REMARK 500 ALA A 375 51.66 -166.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE THM A 500
DBREF 2VTK A 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
HET ADP A 400 27
HET THM A 500 17
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM THM THYMIDINE
HETSYN THM DEOXYTHYMIDINE; 2'-DEOXYTHYMIDINE
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 THM C10 H14 N2 O5
FORMUL 4 HOH *28(H2 O)
HELIX 1 1 LYS A 62 LEU A 72 1 11
HELIX 2 2 MET A 85 ARG A 89 1 5
HELIX 3 3 THR A 96 ASP A 108 1 13
HELIX 4 4 ALA A 114 HIS A 142 1 29
HELIX 5 5 PRO A 165 LEU A 169 1 5
HELIX 6 6 CYS A 171 MET A 179 1 9
HELIX 7 7 PRO A 184 LEU A 193 1 10
HELIX 8 8 GLU A 210 LYS A 219 1 10
HELIX 9 9 LEU A 229 GLN A 250 1 22
HELIX 10 10 TRP A 255 LEU A 262 1 8
HELIX 11 11 ILE A 284 ASP A 286 5 3
HELIX 12 12 LEU A 288 PHE A 292 5 5
HELIX 13 13 PRO A 295 LEU A 297 5 3
HELIX 14 14 ASN A 306 ARG A 320 1 15
HELIX 15 15 PRO A 333 GLY A 346 1 14
HELIX 16 16 SER A 357 MET A 372 1 16
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
SITE 1 AC1 11 GLY A 59 MET A 60 GLY A 61 LYS A 62
SITE 2 AC1 11 THR A 63 THR A 64 ARG A 216 ARG A 220
SITE 3 AC1 11 ARG A 222 GLN A 331 HOH A 615
SITE 1 AC2 10 GLU A 83 ILE A 100 TYR A 101 GLN A 125
SITE 2 AC2 10 ALA A 168 ARG A 222 GLU A 225 HOH A 606
SITE 3 AC2 10 HOH A 615 HOH A 616
CRYST1 84.100 84.100 155.360 90.00 90.00 90.00 I 41 8
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 0.011891 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011891 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006437 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
