+Open data
-Basic information
Entry | Database: PDB / ID: 3d1d | ||||||
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Title | Hexagonal crystal structure of Tas3 C-terminal alpha motif | ||||||
Components | RNA-induced transcriptional silencing complex protein tas3 | ||||||
Keywords | NUCLEAR PROTEIN / all alpha motif / RITS complex immunoglobulin fold / Cell cycle / Chromosome partition / Nucleus / RNA-mediated gene silencing | ||||||
Function / homology | Function and homology information RITS complex / mating-type region heterochromatin / siRNA-mediated pericentric heterochromatin formation / regulatory ncRNA-mediated heterochromatin formation / chromosome, subtelomeric region / pericentric heterochromatin formation / silent mating-type cassette heterochromatin formation / spindle pole body / pericentric heterochromatin / chromosome segregation ...RITS complex / mating-type region heterochromatin / siRNA-mediated pericentric heterochromatin formation / regulatory ncRNA-mediated heterochromatin formation / chromosome, subtelomeric region / pericentric heterochromatin formation / silent mating-type cassette heterochromatin formation / spindle pole body / pericentric heterochromatin / chromosome segregation / heterochromatin formation / molecular adaptor activity / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Schizosaccharomyces pombe (fission yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Li, H. / Patel, D.J. | ||||||
Citation | Journal: Mol.Cell / Year: 2009 Title: An alpha motif at Tas3 C terminus mediates RITS cis spreading and promotes heterochromatic gene silencing. Authors: Li, H. / Motamedi, M.R. / Yip, C.K. / Wang, Z. / Walz, T. / Patel, D.J. / Moazed, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3d1d.cif.gz | 140.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3d1d.ent.gz | 112.2 KB | Display | PDB format |
PDBx/mmJSON format | 3d1d.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3d1d_validation.pdf.gz | 475.3 KB | Display | wwPDB validaton report |
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Full document | 3d1d_full_validation.pdf.gz | 494.3 KB | Display | |
Data in XML | 3d1d_validation.xml.gz | 28 KB | Display | |
Data in CIF | 3d1d_validation.cif.gz | 38.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d1/3d1d ftp://data.pdbj.org/pub/pdb/validation_reports/d1/3d1d | HTTPS FTP |
-Related structure data
Related structure data | 3d1bSC 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
#1: Protein | Mass: 13940.937 Da / Num. of mol.: 6 / Fragment: UNP residues 426-545 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Schizosaccharomyces pombe (fission yeast) Gene: tas3, SPBC83.03c / Production host: Escherichia coli (E. coli) / Strain (production host): Rossetta2(DE3) / References: UniProt: O94687 #2: Water | ChemComp-HOH / | |
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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: 1.99 Å3/Da / Density % sol: 38.17 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 10% PEG4000, 0.1 M Tris 7.5, 0.2 M KCl, 50 mM MgCl2, and 15% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X9A / Wavelength: 0.9791 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: May 4, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9791 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→20 Å / Num. all: 20741 / Num. obs: 19969 / % possible obs: 96.3 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 12.2 % / Rmerge(I) obs: 0.109 / Net I/σ(I): 21.8 |
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 12 % / Rmerge(I) obs: 0.65 / Mean I/σ(I) obs: 2.6 / Num. unique all: 2052 / % possible all: 90 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3D1B Resolution: 2.6→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→20 Å
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Refine LS restraints |
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