+Open data
-Basic information
Entry | Database: PDB / ID: 5fhg | ||||||
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Title | Structure of unliganded Pif1 from Bacteroides sp | ||||||
Components | Uncharacterized protein | ||||||
Keywords | HYDROLASE / Pif1 Helicase / DNA helicase | ||||||
Function / homology | Function and homology information DNA helicase activity / telomere maintenance / DNA repair / nucleotide binding Similarity search - Function | ||||||
Biological species | Bacteroides sp. 2_1_16 (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2 Å | ||||||
Authors | Zhou, X. / Ren, W. / Bharath, S.R. / Song, H. | ||||||
Citation | Journal: Cell Rep / Year: 2016 Title: Structural and Functional Insights into the Unwinding Mechanism of Bacteroides sp Pif1 Authors: Zhou, X. / Ren, W. / Bharath, S.R. / Tang, X. / He, Y. / Chen, C. / Liu, Z. / Li, D. / Song, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5fhg.cif.gz | 177.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5fhg.ent.gz | 138.8 KB | Display | PDB format |
PDBx/mmJSON format | 5fhg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5fhg_validation.pdf.gz | 430.5 KB | Display | wwPDB validaton report |
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Full document | 5fhg_full_validation.pdf.gz | 434.2 KB | Display | |
Data in XML | 5fhg_validation.xml.gz | 34.2 KB | Display | |
Data in CIF | 5fhg_validation.cif.gz | 52.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fh/5fhg ftp://data.pdbj.org/pub/pdb/validation_reports/fh/5fhg | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 49716.941 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacteroides sp. 2_1_16 (bacteria) / Gene: HMPREF0101_01022 / Production host: Escherichia coli (E. coli) / References: UniProt: D1JM21, UniProt: A0A7U8QDR9*PLUS #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.74 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 200 mM MgCl2, 0.1 M Tris, 10% PEG 8000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9791 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jan 2, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 2→61.7 Å / Num. obs: 61720 / % possible obs: 91.3 % / Redundancy: 3.2 % / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2→2.05 Å / Redundancy: 3.2 % / Mean I/σ(I) obs: 1.7 / % possible all: 88.9 |
-Processing
Software |
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Refinement | Resolution: 2→58.534 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 25.01 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→58.534 Å
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Refine LS restraints |
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LS refinement shell |
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