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Yorodumi- PDB-1pbu: Solution structure of the C-terminal domain of the human eEF1Bgam... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1pbu | ||||||
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Title | Solution structure of the C-terminal domain of the human eEF1Bgamma subunit | ||||||
Components | Elongation factor 1-gamma | ||||||
Keywords | TRANSLATION / ALPHA/BETA | ||||||
Function / homology | Function and homology information Eukaryotic Translation Elongation / translational elongation / translation elongation factor activity / response to virus / Signaling by ALK fusions and activated point mutants / cadherin binding / extracellular exosome / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Authors | Vanwetswinkel, S. / Kriek, J. / Andersen, G.R. / Guntert, P. / Dijk, J. / Canters, G.W. / Siegal, G. | ||||||
Citation | Journal: J.Biomol.Nmr / Year: 2003 Title: 1H, (15)N and (13)C resonance assignments of the highly conserved 19 kDa C-terminal domain from human Elongation Factor 1Bgamma. Authors: Vanwetswinkel, S. / Kriek, J. / Andersen, G.R. / Dijk, J. / Siegal, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pbu.cif.gz | 1016.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1pbu.ent.gz | 851.3 KB | Display | PDB format |
PDBx/mmJSON format | 1pbu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1pbu_validation.pdf.gz | 354.8 KB | Display | wwPDB validaton report |
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Full document | 1pbu_full_validation.pdf.gz | 464.7 KB | Display | |
Data in XML | 1pbu_validation.xml.gz | 61.2 KB | Display | |
Data in CIF | 1pbu_validation.cif.gz | 81.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pb/1pbu ftp://data.pdbj.org/pub/pdb/validation_reports/pb/1pbu | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 19066.301 Da / Num. of mol.: 1 / Fragment: C-terminal domain (residues 276-437) / Mutation: V289A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EEF1G OR EF1G / Plasmid: pET16b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P26641 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 75mM KCl / pH: 7.5 / Pressure: ambient / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 25 Å / Num. obs: 51350 / % possible obs: 90.9 % / Num. measured all: 192792 / Rmerge(I) obs: 0.069 | ||||||||||||||||||||
Reflection shell | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 2.34 Å / % possible obs: 93.1 % / Rmerge(I) obs: 0.23 / Mean I/σ(I) obs: 2.7 |
-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 3920 NOE-derived distance constraints | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |