+Open data
-Basic information
Entry | Database: PDB / ID: 4a9a | ||||||
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Title | Structure of Rbg1 in complex with Tma46 dfrp domain | ||||||
Components |
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Keywords | TRANSLATION / DRG-DFRP COMPLEX / RIBOSOME BINDING GTPASE | ||||||
Function / homology | Function and homology information : / positive regulation of cellular response to amino acid starvation / cytoplasmic stress granule / cytoplasmic translation / mRNA binding / GTP binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 2.67 Å | ||||||
Authors | Francis, S.M. / Gas, M. / Daugeron, M. / Seraphin, B. / Bravo, J. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2012 Title: Rbg1-Tma46 Dimer Structure Reveals New Functional Domains and Their Role in Polysome Recruitment. Authors: Francis, S.M. / Gas, M. / Daugeron, M. / Bravo, J. / Seraphin, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4a9a.cif.gz | 366.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4a9a.ent.gz | 304.2 KB | Display | PDB format |
PDBx/mmJSON format | 4a9a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a9/4a9a ftp://data.pdbj.org/pub/pdb/validation_reports/a9/4a9a | HTTPS FTP |
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-Related structure data
Similar structure data |
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-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: 41717.035 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Plasmid: PBS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS-RIPL / References: UniProt: P39729 #2: Protein | Mass: 16039.022 Da / Num. of mol.: 2 / Fragment: DFRP DOMAIN, RESIDUES 205-345 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Plasmid: PBS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): CODONPLUS-RIPL / References: UniProt: Q12000 #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.55 Å3/Da / Density % sol: 65.41 % / Description: NONE |
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Crystal grow | pH: 7 Details: 2.38 SODIUM FORMATE, 0.2-0.25 SODIUM CITRATE PH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9795 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Nov 5, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.67→79.42 Å / Num. obs: 47671 / % possible obs: 99.9 % / Observed criterion σ(I): 1.9 / Redundancy: 7.14 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 2.67→2.82 Å / Redundancy: 7 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 1.9 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: SIRAS Starting model: NONE Resolution: 2.67→56.22 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.948 / SU B: 18.68 / SU ML: 0.181 / Cross valid method: THROUGHOUT / ESU R: 0.331 / ESU R Free: 0.234 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 76.935 Å2
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Refinement step | Cycle: LAST / Resolution: 2.67→56.22 Å
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