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- PDB-4od8: Crystal structure of the vaccinia virus DNA polymerase holoenzyme... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4od8 | ||||||
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Title | Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit D4 in complex with the A20 N-terminus | ||||||
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![]() | HYDROLASE/REPLICATION / DNA polymerase processivity factor / DNA binding / DNA polymerase binding / HYDROLASE-REPLICATION complex | ||||||
Function / homology | ![]() uracil-DNA glycosylase / viral DNA genome replication / uracil DNA N-glycosylase activity / DNA replication / DNA repair / DNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Contesto-Richefeu, C. / Tarbouriech, N. / Brazzolotto, X. / Burmeister, W.P. / Iseni, F. | ||||||
![]() | ![]() Title: Crystal structure of the vaccinia virus DNA polymerase holoenzyme subunit d4 in complex with the a20 N-terminal domain. Authors: Contesto-Richefeu, C. / Tarbouriech, N. / Brazzolotto, X. / Betzi, S. / Morelli, X. / Burmeister, W.P. / Iseni, F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 239.9 KB | Display | ![]() |
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PDB format | ![]() | 195 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 478.7 KB | Display | ![]() |
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Full document | ![]() | 488.4 KB | Display | |
Data in XML | ![]() | 26.6 KB | Display | |
Data in CIF | ![]() | 37.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4odaC ![]() 2owqS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 26729.486 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 5777.560 Da / Num. of mol.: 2 / Fragment: N-terminal residues 1-50 / Mutation: T2A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Chemical | ChemComp-SO4 / #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.72 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.7 Details: 100 mM bicine, 1.5 M ammonium sulfate, pH 8.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 12, 2012 / Details: Si111 monochromator plus toroidal mirror |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→48.62 Å / Num. all: 61990 / Num. obs: 61957 / % possible obs: 99.9 % / Redundancy: 7.1 % / Rmerge(I) obs: 0.072 / Net I/σ(I): 15.8 |
Reflection shell | Resolution: 1.85→1.95 Å / Redundancy: 7 % / Rmerge(I) obs: 0.542 / Mean I/σ(I) obs: 3.5 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2OWQ Resolution: 1.85→46.31 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.945 / SU B: 5.561 / SU ML: 0.086 / Cross valid method: THROUGHOUT / ESU R: 0.114 / ESU R Free: 0.117 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.112 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→46.31 Å
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Refine LS restraints |
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