+Open data
-Basic information
Entry | Database: PDB / ID: 2ktl | ||||||
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Title | Structure of C-terminal domain from mtTyrRS of A. nidulans | ||||||
Components | Tyrosyl-tRNA synthetase | ||||||
Keywords | LIGASE / S4 fold / Aminoacyl-tRNA synthetase | ||||||
Function / homology | Function and homology information tRNA aminoacylation / tyrosyl-tRNA aminoacylation / tyrosine-tRNA ligase / tyrosine-tRNA ligase activity / mitochondrion / RNA binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Aspergillus nidulans FGSC A4 (mold) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Chari, N.S. | ||||||
Citation | Journal: To be Published Title: Structure of C-terminal domain from mtTyrRS of A. nidulans Authors: Hoffman, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ktl.cif.gz | 586.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ktl.ent.gz | 489.8 KB | Display | PDB format |
PDBx/mmJSON format | 2ktl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kt/2ktl ftp://data.pdbj.org/pub/pdb/validation_reports/kt/2ktl | 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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NMR ensembles |
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-Components
#1: Protein | Mass: 17675.160 Da / Num. of mol.: 1 / Fragment: C-terminal domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aspergillus nidulans FGSC A4 (mold) / Gene: ANIA_01709 / Plasmid: pET11d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: C8VNV9, UniProt: Q5BCM1*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 20 mg/mL [U-100% 15N] protein, 20 mg/mL [U-100% 13C] protein, 500 mM sodium chloride, 10 mM TRIS, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.5 / pH: 7.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 12 |