+Open data
-Basic information
Entry | Database: PDB / ID: 3zuz | ||||||
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Title | Structure of Shq1p C-terminal domain | ||||||
Components | PROTEIN SHQ1 | ||||||
Keywords | CELL CYCLE / RNP ASSEMBLY / X-LINKED DYSKERATOSIS CONGENITA / TELOMERASE | ||||||
Function / homology | Function and homology information Telomere Extension By Telomerase / box H/ACA snoRNP assembly / unfolded protein binding / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.5 Å | ||||||
Authors | Walbott, H. / Machado-Pinilla, R. / Liger, D. / Blaud, M. / Rety, S. / Grozdanov, P.N. / Godin, K. / vanTilbeurgh, H. / Varani, G. / Meier, U.T. / Leulliot, N. | ||||||
Citation | Journal: Genes Dev. / Year: 2011 Title: The H/Aca Rnp Assembly Factor Shq1 Functions as an RNA Mimic. Authors: Walbott, H. / Machado-Pinilla, R. / Liger, D. / Blaud, M. / Rety, S. / Grozdanov, P.N. / Godin, K. / Van Tilbeurgh, H. / Varani, G. / Meier, U.T. / Leulliot, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3zuz.cif.gz | 87.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3zuz.ent.gz | 68.5 KB | Display | PDB format |
PDBx/mmJSON format | 3zuz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zu/3zuz ftp://data.pdbj.org/pub/pdb/validation_reports/zu/3zuz | HTTPS FTP |
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-Related 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: 42936.160 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN, RESIDUES 143-507 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Strain: S288C / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): ROSETTA PLYSS / References: UniProt: P40486 | ||
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#2: Chemical | #3: 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: 2.51 Å3/Da / Density % sol: 51.09 % / Description: NONE |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: CRYSTALLIZED AT 291 KELVIN BY THE SITTING DROP VAPOR DIFFUSION METHOD FROM A 1:1 MIXTURE OF PROTEIN AND PRECIPITANT CONTAINING 20 TO 25 % PEG 4000, 10 % ISOPROPANOL, 100 MM HEPES PH 7.5, 50 MM MGSO4 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.979 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 18, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→35 Å / Num. obs: 54338 / % possible obs: 93.9 % / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Biso Wilson estimate: 20.23 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 14.5 |
Reflection shell | Resolution: 1.5→1.58 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.43 / Mean I/σ(I) obs: 2.6 / % possible all: 92.4 |
-Processing
Software |
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Refinement | Method to determine structure: SAD Starting model: NONE Resolution: 1.5→21.96 Å / Cor.coef. Fo:Fc: 0.9493 / Cor.coef. Fo:Fc free: 0.9412 / Cross valid method: THROUGHOUT / σ(F): 0 Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY RESIDUES 143-163, 345- 361, 473-481, 506-507 ARE DISORDERED.
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Displacement parameters | Biso mean: 26.77 Å2
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Refine analyze | Luzzati coordinate error obs: 0.174 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→21.96 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.54 Å / Total num. of bins used: 20
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