+Open data
-Basic information
Entry | Database: PDB / ID: 2bgw | ||||||
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Title | XPF from Aeropyrum pernix, complex with DNA | ||||||
Components |
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Keywords | HYDROLASE / STRUCTURE SPECIFIC ENDONUCLEASE / NUCLEOTIDE EXCISION REPAIR | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Aeropyrum pernix (archaea) synthetic construct (others) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Newman, M. / Murray-Rust, J. / Lally, J. / Rudolf, J. / Fadden, A. / Knowles, P.P. / White, M.F. / McDonald, N.Q. | ||||||
Citation | Journal: EMBO J. / Year: 2005 Title: Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition. Authors: Newman, M. / Murray-Rust, J. / Lally, J. / Rudolf, J. / Fadden, A. / Knowles, P.P. / White, M.F. / McDonald, N.Q. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bgw.cif.gz | 114 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bgw.ent.gz | 83.9 KB | Display | PDB format |
PDBx/mmJSON format | 2bgw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bg/2bgw ftp://data.pdbj.org/pub/pdb/validation_reports/bg/2bgw | HTTPS FTP |
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-Related structure data
Related structure data | 2bhnC 1j25S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1 / Refine code: 6
NCS oper:
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 25006.939 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aeropyrum pernix (archaea) Description: A PERNIX GENOME SEQUENCING PROJECT GENE APE1436, ACCESSION CODE C72622 Plasmid: PET-14B-3C / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): ROSETTA/PLYSS References: UniProt: Q9YC15, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases |
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-DNA chain , 2 types, 2 molecules CD
#2: DNA chain | Mass: 4618.023 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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#3: DNA chain | Mass: 4559.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 3 types, 14 molecules
#4: Chemical | ChemComp-MG / | ||
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#5: Chemical | ChemComp-SO4 / #6: 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: 4.15 Å3/Da / Density % sol: 75 % |
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Crystal grow | Method: vapor diffusion, hanging drop Details: 0.1M SODIUM ACETATE, 0.2M AMMONIUM SULFATE, 20% PEG MME 2K, HANGING DROP, ROOM TEMPERATURE |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX9.6 / Wavelength: 0.9789 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9789 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→46.1 Å / Num. obs: 21619 / % possible obs: 97.5 % / Observed criterion σ(I): 0 / Redundancy: 5.4 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 1.9 / % possible all: 92.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1J25 Resolution: 2.8→30 Å / Cor.coef. Fo:Fc: 0.917 / Cor.coef. Fo:Fc free: 0.879 / SU ML: 0.235 / Cross valid method: THROUGHOUT / ESU R: 0.472 / ESU R Free: 0.313 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: 40.13 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→30 Å
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Refine LS restraints |
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