+Open data
-Basic information
Entry | Database: PDB / ID: 5we1 | ||||||
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Title | Structural Basis for Shelterin Bridge Assembly | ||||||
Components |
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Keywords | GENE REGULATION / Telomere / Shelterin / Cooperativity | ||||||
Function / homology | Function and homology information telomere-telomerase complex assembly / telomere cap complex / chromosome, telomeric repeat region / mitotic telomere maintenance via semi-conservative replication / shelterin complex / telomere capping / protein localization to chromosome, telomeric region / telomeric DNA binding / telomere maintenance via telomerase / telomere organization ...telomere-telomerase complex assembly / telomere cap complex / chromosome, telomeric repeat region / mitotic telomere maintenance via semi-conservative replication / shelterin complex / telomere capping / protein localization to chromosome, telomeric region / telomeric DNA binding / telomere maintenance via telomerase / telomere organization / telomere maintenance / DNA binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Schizosaccharomyces pombe (fission yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.202 Å | ||||||
Authors | Kim, J.-K. / Liu, J. / Hu, X. / Yu, C. / Roskamp, K. / Sankaran, B. / Huang, L. / Komives, E.-A. / Qiao, F. | ||||||
Citation | Journal: Mol. Cell / Year: 2017 Title: Structural Basis for Shelterin Bridge Assembly. Authors: Kim, J.K. / Liu, J. / Hu, X. / Yu, C. / Roskamp, K. / Sankaran, B. / Huang, L. / Komives, E.A. / Qiao, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5we1.cif.gz | 101.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5we1.ent.gz | 76.5 KB | Display | PDB format |
PDBx/mmJSON format | 5we1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/we/5we1 ftp://data.pdbj.org/pub/pdb/validation_reports/we/5we1 | HTTPS FTP |
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-Related structure data
Related structure data | 5we0C 5we2SC 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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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 25314.229 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast), (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast) Strain: 972 / ATCC 24843 / Gene: poz1, SPAC19G12.13c / Production host: Escherichia coli (E. coli) / References: UniProt: O13852 #2: Protein/peptide | Mass: 3964.574 Da / Num. of mol.: 2 / Fragment: UNP residues 476-508 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast) Strain: 972 / ATCC 24843 / Gene: tpz1, mug169, SPAC6F6.16c, SPAC6F6.18c / Production host: Escherichia coli (E. coli) / References: UniProt: O14246 #3: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 53.93 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.1 M Tris-HCl pH 8.0, 4% Reagent Alcohol, 0.3 M MgCl2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.977408 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 28, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.977408 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→57.25 Å / Num. obs: 9911 / % possible obs: 99.7 % / Redundancy: 5.3 % / Rmerge(I) obs: 0.104 / Net I/σ(I): 11.5 |
Reflection shell | Resolution: 3.2→3.37 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.765 / Mean I/σ(I) obs: 2.6 / % possible all: 99.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5WE2 Resolution: 3.202→51.917 Å / SU ML: 0.56 / Cross valid method: FREE R-VALUE / σ(F): 2 / Phase error: 40.96
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.202→51.917 Å
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Refine LS restraints |
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LS refinement shell |
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