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- PDB-2bsy: Epstein Barr Virus dUTPase -

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Basic information

Entry
Database: PDB / ID: 2bsy
TitleEpstein Barr Virus dUTPase
ComponentsDEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE
KeywordsHYDROLASE / DUTPASE / MONOMER / NUCLEOTIDE METABOLISM / STRUCTURAL PROTEOMICS IN EUROPE / SPINE / STRUCTURAL GENOMICS
Function / homology
Function and homology information


dUTP metabolic process / dUTP diphosphatase / dUTP diphosphatase activity / metal ion binding
Similarity search - Function
Deoxyuridine 5'-triphosphate nucleotidohydrolase / Deoxyuridine triphosphatase (dUTPase) / Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A / dUTPase-like / dUTPase / dUTPase, trimeric / dUTPase-like superfamily / Distorted Sandwich / Mainly Beta
Similarity search - Domain/homology
2'-DEOXYURIDINE 5'-MONOPHOSPHATE / Deoxyuridine 5'-triphosphate nucleotidohydrolase
Similarity search - Component
Biological speciesHUMAN HERPESVIRUS 4 (Epstein-Barr virus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.5 Å
AuthorsTarbouriech, N. / Buisson, M. / Seigneurin, J.-M. / Cusack, S. / Burmeister, W.P.
CitationJournal: Structure / Year: 2005
Title: The Monomeric Dutpase from Epstein-Barr Virus Mimics Trimeric Dutpases
Authors: Tarbouriech, N. / Buisson, M. / Seigneurin, J.-M. / Cusack, S. / Burmeister, W.P.
History
DepositionMay 24, 2005Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 15, 2005Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 8, 2023Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / struct_conn / struct_conn_type
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Revision 1.4Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature
Item: _pdbx_entry_details.has_protein_modification
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,6876
Polymers30,9951
Non-polymers6925
Water5,495305
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)56.655, 55.787, 81.053
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE / DUTPASE / DUTP PYROPHOSPHATASE


Mass: 30994.539 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HUMAN HERPESVIRUS 4 (Epstein-Barr virus)
Strain: B95-8 / Plasmid: PPROEX-HTB / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P03195, dUTP diphosphatase
#2: Chemical ChemComp-UMP / 2'-DEOXYURIDINE 5'-MONOPHOSPHATE / DUMP


Mass: 308.182 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H13N2O8P
#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 305 / Source method: isolated from a natural source / Formula: H2O
Compound detailsTHE SIDECHAIN OF RESIDUE ARG A187 IS OBSERVED IN TWO CONFORMATIONS. A SULFATE MOEITY IS OBSERVED IN ...THE SIDECHAIN OF RESIDUE ARG A187 IS OBSERVED IN TWO CONFORMATIONS. A SULFATE MOEITY IS OBSERVED IN THE VICINITY OF RESIDUE A187, AND HAS BEEN MODELLED TO CO-EXIST ONLY WITH THE A-CONFORMER.
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 1.86 Å3/Da / Density % sol: 50 %
Crystal growpH: 8.5 / Details: 100 MM TRIS/HCL PH 8.5, 20% PEG 3350, 200 MM LISO4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 1.07
DetectorType: ADSC CCD / Detector: CCD / Date: Apr 30, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.07 Å / Relative weight: 1
ReflectionResolution: 1.5→40 Å / Num. obs: 38985 / % possible obs: 98.1 % / Observed criterion σ(I): 2 / Redundancy: 4.5 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 9.6
Reflection shellResolution: 1.5→1.54 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.27 / Mean I/σ(I) obs: 2.9 / % possible all: 95.4

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Processing

Software
NameVersionClassification
REFMAC5.2.0005refinement
MOSFLMdata reduction
SCALAdata scaling
SOLVEphasing
RefinementMethod to determine structure: SAD / Resolution: 1.5→46.47 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.955 / SU B: 2.285 / SU ML: 0.04 / Cross valid method: THROUGHOUT / ESU R: 0.087 / ESU R Free: 0.072 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.187 2088 5.1 %RANDOM
Rwork0.148 ---
obs0.15 38985 98.1 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 14.77 Å2
Baniso -1Baniso -2Baniso -3
1-0.13 Å20 Å20 Å2
2---0.4 Å20 Å2
3---0.27 Å2
Refinement stepCycle: LAST / Resolution: 1.5→46.47 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1974 0 40 305 2319
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.0222206
X-RAY DIFFRACTIONr_bond_other_d0.0020.022075
X-RAY DIFFRACTIONr_angle_refined_deg1.8481.992991
X-RAY DIFFRACTIONr_angle_other_deg3.31834848
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9825249
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.57520.51597
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.39115404
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.2141528
X-RAY DIFFRACTIONr_chiral_restr0.1940.2325
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.022304
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02470
X-RAY DIFFRACTIONr_nbd_refined0.2030.2355
X-RAY DIFFRACTIONr_nbd_other0.2060.22129
X-RAY DIFFRACTIONr_nbtor_refined0.1790.2997
X-RAY DIFFRACTIONr_nbtor_other0.0950.21307
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1820.2202
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1890.221
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2180.274
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1920.239
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.8841.51606
X-RAY DIFFRACTIONr_mcbond_other0.6451.5499
X-RAY DIFFRACTIONr_mcangle_it2.29522090
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.7531080
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.6674.5901
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.5→1.54 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.252 142 -
Rwork0.167 2729 -
obs--95.45 %

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