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Open data
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Basic information
Entry | Database: PDB / ID: 5we0 | ||||||
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Title | Structural Basis for Shelterin Bridge Assembly | ||||||
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![]() | GENE REGULATION / Telomere / Shelterin / Cooperativity | ||||||
Function / homology | ![]() meiotic attachment of telomeric heterochromatin to spindle pole body / meiotic spindle pole body / nucleus leading edge / telomere-telomerase complex assembly / mitotic telomere tethering at nuclear periphery / Removal of the Flap Intermediate from the C-strand / telomere cap complex / chromosome, telomeric repeat region / protection from non-homologous end joining at telomere / telomere maintenance via telomere lengthening ...meiotic attachment of telomeric heterochromatin to spindle pole body / meiotic spindle pole body / nucleus leading edge / telomere-telomerase complex assembly / mitotic telomere tethering at nuclear periphery / Removal of the Flap Intermediate from the C-strand / telomere cap complex / chromosome, telomeric repeat region / protection from non-homologous end joining at telomere / telomere maintenance via telomere lengthening / mitotic telomere maintenance via semi-conservative replication / shelterin complex / nuclear telomere cap complex / telomere capping / protein localization to chromosome, telomeric region / telomeric DNA binding / negative regulation of telomere maintenance via telomerase / telomere maintenance via telomerase / telomere organization / telomere maintenance / regulation of DNA-templated transcription / DNA binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kim, J.-K. / Liu, J. / Hu, X. / Yu, C. / Roskamp, K. / Sankaran, B. / Huang, L. / Komives, E.-A. / Qiao, F. | ||||||
Funding support | ![]()
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![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 232 KB | Display | ![]() |
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PDB format | ![]() | 193.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 510.1 KB | Display | ![]() |
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Full document | ![]() | 523.4 KB | Display | |
Data in XML | ![]() | 40.9 KB | Display | |
Data in CIF | ![]() | 57.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 29695.090 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 972 / ATCC 24843 / Gene: poz1, SPAC19G12.13c / Production host: ![]() ![]() #2: Protein/peptide | Mass: 3964.574 Da / Num. of mol.: 4 / Fragment: UNP residues 476-508 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 972 / ATCC 24843 / Gene: tpz1, mug169, SPAC6F6.16c, SPAC6F6.18c / Production host: ![]() ![]() #3: Protein/peptide | Mass: 3343.561 Da / Num. of mol.: 4 / Fragment: UNP residues 467-496 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: 972 / ATCC 24843 / Gene: rap1, SPBC1778.02 / Production host: ![]() ![]() #4: Chemical | ChemComp-ZN / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.13 Å3/Da / Density % sol: 65.78 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 0.2 M Sodium citrate tribasic dihydrate, 21% w/v PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 19, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.999996 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→62.71 Å / Num. obs: 77768 / % possible obs: 97.6 % / Redundancy: 2.3 % / Net I/σ(I): 5.4 |
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Processing
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Refinement | Method to determine structure: ![]()
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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: 2.3→62.705 Å
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Refine LS restraints |
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LS refinement shell |
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