+Open data
-Basic information
Entry | Database: PDB / ID: 1jh3 | ||||||
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Title | Solution structure of tyrosyl-tRNA synthetase C-terminal domain. | ||||||
Components | TYROSYL-TRNA SYNTHETASE | ||||||
Keywords | LIGASE / aminoacyl-tRNA synthetase / anticodon-arm binding domain | ||||||
Function / homology | Function and homology information tyrosyl-tRNA aminoacylation / tyrosine-tRNA ligase / tyrosine-tRNA ligase activity / regulation of protein complex stability / tRNA binding / protein homodimerization activity / protein-containing complex / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Geobacillus stearothermophilus (bacteria) | ||||||
Method | SOLUTION NMR / torsion angle dynamics simulated annealing | ||||||
Authors | Guijarro, J.I. / Pintar, A. / Prochnicka-Chalufour, A. / Guez, V. / Gilquin, B. / Bedouelle, H. / Delepierre, M. | ||||||
Citation | Journal: Structure / Year: 2002 Title: Structure and Dynamics of the Anticodon Arm Binding Domain of Bacillus stearothermophilus Tyrosyl-tRNA Synthetase Authors: Guijarro, J.I. / Pintar, A. / Prochnicka-Chalufour, A. / Guez, V. / Gilquin, B. / Bedouelle, H. / Delepierre, M. #1: Journal: FEBS Lett. / Year: 1999 Title: Secondary structure of the C-terminal domain of the tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus: a novel type of anticodon binding domain? Authors: Pintar, A. / Guez, V. / Castagne, C. / Bedouelle, H. / Delepierre, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jh3.cif.gz | 601.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jh3.ent.gz | 502.7 KB | Display | PDB format |
PDBx/mmJSON format | 1jh3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jh/1jh3 ftp://data.pdbj.org/pub/pdb/validation_reports/jh/1jh3 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12001.544 Da / Num. of mol.: 1 / Fragment: C-terminal domain (Residues 321-419) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Geobacillus stearothermophilus (bacteria) Gene: tyrS / Plasmid: PET-20b(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P00952, tyrosine-tRNA ligase |
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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 | pH: 6.8 / Pressure: ambient / Temperature: 308 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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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics simulated annealing / Software ordinal: 1 Details: Structures were calculated using 1352 meaningful upper distance restraints, 71 dihedral angle restraints and 33 hydrogen bonds. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |