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Yorodumi- PDB-5odl: Single-stranded DNA-binding protein from bacteriophage Enc34 in c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5odl | ||||||
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Title | Single-stranded DNA-binding protein from bacteriophage Enc34 in complex with ssDNA | ||||||
Components |
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Keywords | DNA BINDING PROTEIN / DNA replication / DUF2815 / SSB / OB fold | ||||||
Function / homology | Enterobacter phage Enc34, ssDNA-binding protein / Enterobacter phage Enc34, ssDNA-binding protein / Nucleic acid-binding, OB-fold / DNA binding / metal ion binding / DNA / SsDNA-binding protein Function and homology information | ||||||
Biological species | Enterobacter phage Enc34 (virus) synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.56 Å | ||||||
Authors | Cernooka, E. / Rumnieks, J. / Kazaks, A. / Tars, K. | ||||||
Citation | Journal: Sci Rep / Year: 2017 Title: Structural Basis for DNA Recognition of a Single-stranded DNA-binding Protein from Enterobacter Phage Enc34. Authors: Cernooka, E. / Rumnieks, J. / Tars, K. / Kazaks, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5odl.cif.gz | 102.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5odl.ent.gz | 77 KB | Display | PDB format |
PDBx/mmJSON format | 5odl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5odl_validation.pdf.gz | 438.8 KB | Display | wwPDB validaton report |
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Full document | 5odl_full_validation.pdf.gz | 439.6 KB | Display | |
Data in XML | 5odl_validation.xml.gz | 10.7 KB | Display | |
Data in CIF | 5odl_validation.cif.gz | 14.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/od/5odl ftp://data.pdbj.org/pub/pdb/validation_reports/od/5odl | HTTPS FTP |
-Related structure data
Related structure data | 5odjC 5odkSC C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 20228.146 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacter phage Enc34 (virus) / Plasmid: pETDuet-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: H6WYG2 | ||||
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#2: DNA chain | Mass: 2692.778 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) | ||||
#3: Chemical | ChemComp-GOL / #4: Chemical | ChemComp-NA / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 42 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.1 M HEPES, 30% Jeffamine ED-2001 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 27, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 1.56→59.6 Å / Num. obs: 27151 / % possible obs: 99.7 % / Redundancy: 4.8 % / CC1/2: 0.999 / Rmerge(I) obs: 0.071 / Rpim(I) all: 0.036 / Net I/σ(I): 9.5 |
Reflection shell | Resolution: 1.56→1.56 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.679 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 3942 / CC1/2: 0.389 / Rpim(I) all: 0.344 / % possible all: 99.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5ODK Resolution: 1.56→37.66 Å / Cor.coef. Fo:Fc: 0.978 / Cor.coef. Fo:Fc free: 0.963 / Cross valid method: THROUGHOUT / ESU R: 0.095 / ESU R Free: 0.08 / 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: 29.285 Å2
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Refinement step | Cycle: 1 / Resolution: 1.56→37.66 Å
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