HEADER HYDROLASE 27-MAR-09 2WE0
TITLE EBV DUTPASE MUTANT CYS4SER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DUTP PYROPHOSPHATASE, DUTPASE;
COMPND 5 EC: 3.6.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4;
SOURCE 3 ORGANISM_COMMON: EPSTEIN-BARR VIRUS;
SOURCE 4 ORGANISM_TAXID: 10377;
SOURCE 5 STRAIN: B95-8;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB
KEYWDS DUTPASE, MONOMER, HYDROLASE, HUMAN HERPES VIRUS, EPSTEIN-BARR VIRUS,
KEYWDS 2 NUCLEOTIDE METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.FREEMAN,M.BUISSON,N.TARBOURIECH,W.P.BURMEISTER
REVDAT 4 13-DEC-23 2WE0 1 REMARK
REVDAT 3 15-SEP-09 2WE0 1 JRNL DBREF
REVDAT 2 21-JUL-09 2WE0 1 JRNL
REVDAT 1 07-JUL-09 2WE0 0
JRNL AUTH L.FREEMAN,M.BUISSON,N.TARBOURIECH,A.VAN DER HEYDEN,P.LABBE,
JRNL AUTH 2 W.P.BURMEISTER
JRNL TITL THE FLEXIBLE MOTIF V OF EPSTEIN-BARR VIRUS DEOXYURIDINE
JRNL TITL 2 5'-TRIPHOSPHATE PYROPHOSPHATASE IS ESSENTIAL FOR CATALYSIS.
JRNL REF J.BIOL.CHEM. V. 284 25280 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19586911
JRNL DOI 10.1074/JBC.M109.019315
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.TARBOURIECH,M.BUISSON,J.M.SEIGNEURIN,S.CUSACK,
REMARK 1 AUTH 2 W.P.BURMEISTER
REMARK 1 TITL THE MONOMERIC DUTPASE FROM EPSTEIN-BARR VIRUS MIMICS
REMARK 1 TITL 2 TRIMERIC DUTPASES.
REMARK 1 REF STRUCTURE V. 13 1299 2005
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 16154087
REMARK 1 DOI 10.1016/J.STR.2005.06.009
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0070
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 16536
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 882
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 856
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1954
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.65000
REMARK 3 B22 (A**2) : -0.26000
REMARK 3 B33 (A**2) : -1.39000
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): 0.203
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.185
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.748
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2049 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2795 ; 1.921 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 247 ; 6.983 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 83 ;29.149 ;21.325
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 323 ;14.889 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;21.457 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 312 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1544 ; 0.010 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1240 ; 1.165 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2022 ; 2.025 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 809 ; 3.058 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 772 ; 4.905 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2WE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-MAR-09.
REMARK 100 THE DEPOSITION ID IS D_1290039233.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
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 : 23739
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 56.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.870
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2BSY
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 150 MM MALIC ACID PH 7.5, 25 % PEG
REMARK 280 3350 AND 10 MM DUTP.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 28.02400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.68700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.39150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.68700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.02400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.39150
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 4 TO SER
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 GLY A -7
REMARK 465 ALA A -6
REMARK 465 MET A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 GLY A -2
REMARK 465 ILE A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 MET A 116
REMARK 465 GLU A 117
REMARK 465 GLU A 118
REMARK 465 ASP A 119
REMARK 465 LYS A 120
REMARK 465 GLY A 257
REMARK 465 ASP A 258
REMARK 465 SER A 259
REMARK 465 GLY A 260
REMARK 465 LEU A 261
REMARK 465 SER A 262
REMARK 465 GLU A 263
REMARK 465 ALA A 264
REMARK 465 LEU A 265
REMARK 465 GLU A 266
REMARK 465 GLY A 267
REMARK 465 ARG A 268
REMARK 465 GLN A 269
REMARK 465 GLY A 270
REMARK 465 ARG A 271
REMARK 465 GLY A 272
REMARK 465 PHE A 273
REMARK 465 GLY A 274
REMARK 465 SER A 275
REMARK 465 SER A 276
REMARK 465 GLY A 277
REMARK 465 GLN A 278
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 GLN A 12 CG CD OE1 NE2
REMARK 470 ASP A 14 OD1 OD2
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 CD2 HIS A 229 O HOH A 2159 2.10
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 A 2012 O HOH A 2104 2554 2.16
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 ASN A 13 112.84 -161.89
REMARK 500 SER A 100 -1.04 77.28
REMARK 500 PRO A 129 121.77 -34.37
REMARK 500 TYR A 208 -11.98 81.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UMP A 1257
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO A 1259
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BSY RELATED DB: PDB
REMARK 900 EPSTEIN BARR VIRUS DUTPASE
REMARK 900 RELATED ID: 2BT1 RELATED DB: PDB
REMARK 900 EPSTEIN BARR VIRUS DUTPASE IN COMPLEX WITH A,B-IMINO DUTP
REMARK 900 RELATED ID: 2WE1 RELATED DB: PDB
REMARK 900 EBV DUTPASE MUTANT ASP131ASN WITH BOUND DUMP
REMARK 900 RELATED ID: 2WE3 RELATED DB: PDB
REMARK 900 EBV DUTPASE INACTIVE MUTANT DELETED OF MOTIF V
REMARK 900 RELATED ID: 2WE2 RELATED DB: PDB
REMARK 900 EBV DUTPASE DOUBLE MUTANT GLY78ASP-ASP131SER WITH DUMP
DBREF 2WE0 A -7 0 PDB 2WE0 2WE0 -7 0
DBREF 2WE0 A 1 278 UNP P03195 DUT_EBVB9 1 278
SEQADV 2WE0 SER A 4 UNP P03195 CYS 4 ENGINEERED MUTATION
SEQRES 1 A 286 GLY ALA MET GLY SER GLY ILE PRO MET GLU ALA SER PRO
SEQRES 2 A 286 HIS ILE ARG TYR ALA PHE GLN ASN ASP LYS LEU LEU LEU
SEQRES 3 A 286 GLN GLN ALA SER VAL GLY ARG LEU THR LEU VAL ASN LYS
SEQRES 4 A 286 THR THR ILE LEU LEU ARG PRO MET LYS THR THR THR VAL
SEQRES 5 A 286 ASP LEU GLY LEU TYR ALA ARG PRO PRO GLU GLY HIS GLY
SEQRES 6 A 286 LEU MET LEU TRP GLY SER THR SER ARG PRO VAL THR SER
SEQRES 7 A 286 HIS VAL GLY ILE ILE ASP PRO GLY TYR THR GLY GLU LEU
SEQRES 8 A 286 ARG LEU ILE LEU GLN ASN GLN ARG ARG TYR ASN SER THR
SEQRES 9 A 286 LEU ARG PRO SER GLU LEU LYS ILE HIS LEU ALA ALA PHE
SEQRES 10 A 286 ARG TYR ALA THR PRO GLN MET GLU GLU ASP LYS GLY PRO
SEQRES 11 A 286 ILE ASN HIS PRO GLN TYR PRO GLY ASP VAL GLY LEU ASP
SEQRES 12 A 286 VAL SER LEU PRO LYS ASP LEU ALA LEU PHE PRO HIS GLN
SEQRES 13 A 286 THR VAL SER VAL THR LEU THR VAL PRO PRO PRO SER ILE
SEQRES 14 A 286 PRO HIS HIS ARG PRO THR ILE PHE GLY ARG SER GLY LEU
SEQRES 15 A 286 ALA MET GLN GLY ILE LEU VAL LYS PRO CYS ARG TRP ARG
SEQRES 16 A 286 ARG GLY GLY VAL ASP VAL SER LEU THR ASN PHE SER ASP
SEQRES 17 A 286 GLN THR VAL PHE LEU ASN LYS TYR ARG ARG PHE CYS GLN
SEQRES 18 A 286 LEU VAL TYR LEU HIS LYS HIS HIS LEU THR SER PHE TYR
SEQRES 19 A 286 SER PRO HIS SER ASP ALA GLY VAL LEU GLY PRO ARG SER
SEQRES 20 A 286 LEU PHE ARG TRP ALA SER CYS THR PHE GLU GLU VAL PRO
SEQRES 21 A 286 SER LEU ALA MET GLY ASP SER GLY LEU SER GLU ALA LEU
SEQRES 22 A 286 GLU GLY ARG GLN GLY ARG GLY PHE GLY SER SER GLY GLN
HET UMP A1257 20
HET SO4 A1258 5
HET TEO A1259 9
HETNAM UMP 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
HETNAM SO4 SULFATE ION
HETNAM TEO MALATE LIKE INTERMEDIATE
HETSYN UMP DUMP
FORMUL 2 UMP C9 H13 N2 O8 P
FORMUL 3 SO4 O4 S 2-
FORMUL 4 TEO C4 H4 O5 2-
FORMUL 5 HOH *173(H2 O)
HELIX 1 1 ARG A 171 GLN A 177 1 7
HELIX 2 2 PRO A 252 ALA A 255 5 4
SHEET 1 AA 5 VAL A 68 SER A 70 0
SHEET 2 AA 5 LEU A 83 ASN A 89 -1 O GLN A 88 N THR A 69
SHEET 3 AA 5 THR A 41 ARG A 51 -1 O THR A 42 N LEU A 87
SHEET 4 AA 5 HIS A 6 PHE A 11 -1 O ARG A 8 N ARG A 51
SHEET 5 AA 5 THR A 247 GLU A 250 1 O THR A 247 N ILE A 7
SHEET 1 AB 5 LEU A 16 SER A 22 0
SHEET 2 AB 5 ARG A 25 ASN A 30 -1 O ARG A 25 N SER A 22
SHEET 3 AB 5 LYS A 103 ALA A 112 -1 O ILE A 104 N LEU A 28
SHEET 4 AB 5 HIS A 56 SER A 63 -1 O GLY A 57 N PHE A 109
SHEET 5 AB 5 GLY A 73 ILE A 75 -1 O GLY A 73 N LEU A 60
SHEET 1 AC 4 LEU A 16 SER A 22 0
SHEET 2 AC 4 ARG A 25 ASN A 30 -1 O ARG A 25 N SER A 22
SHEET 3 AC 4 LYS A 103 ALA A 112 -1 O ILE A 104 N LEU A 28
SHEET 4 AC 4 ARG A 210 HIS A 218 -1 O TYR A 216 N ALA A 112
SHEET 1 AD 2 ILE A 34 LEU A 36 0
SHEET 2 AD 2 SER A 95 LEU A 97 -1 O SER A 95 N LEU A 36
SHEET 1 AE 2 LEU A 142 LEU A 144 0
SHEET 2 AE 2 VAL A 203 LEU A 205 -1 O VAL A 203 N LEU A 144
SHEET 1 AF 3 GLN A 148 LEU A 154 0
SHEET 2 AF 3 VAL A 191 ASN A 197 -1 O VAL A 191 N LEU A 154
SHEET 3 AF 3 ILE A 179 VAL A 181 -1 O LEU A 180 N THR A 196
SHEET 1 AG 3 LEU A 222 THR A 223 0
SHEET 2 AG 3 LEU A 240 ARG A 242 -1 O LEU A 240 N THR A 223
SHEET 3 AG 3 SER A 230 ASP A 231 -1 O ASP A 231 N PHE A 241
CISPEP 1 GLY A 121 PRO A 122 0 -12.45
SITE 1 AC1 14 HIS A 71 GLY A 73 ASP A 76 LEU A 83
SITE 2 AC1 14 ARG A 84 ASN A 94 ARG A 171 SER A 172
SITE 3 AC1 14 HOH A2066 HOH A2169 HOH A2170 HOH A2171
SITE 4 AC1 14 HOH A2172 HOH A2173
SITE 1 AC2 3 HIS A 163 ARG A 165 LYS A 219
SITE 1 AC3 8 LEU A 35 ARG A 37 ASP A 76 GLY A 78
SITE 2 AC3 8 TYR A 79 ASN A 94 ASP A 131 HOH A2173
CRYST1 56.048 56.783 81.374 90.00 90.00 90.00 P 21 21 21 4
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 0.017842 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017611 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012289 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
