+Open data
-Basic information
Entry | Database: PDB / ID: 2lgj | ||||||
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Title | Solution structure of MsPTH | ||||||
Components | Peptidyl-tRNA hydrolaseAlternative ribosome-rescue factor B | ||||||
Keywords | HYDROLASE / MsPTH | ||||||
Function / homology | Function and homology information peptidyl-tRNA hydrolase / aminoacyl-tRNA hydrolase activity / translation / cytoplasm Similarity search - Function | ||||||
Biological species | Mycobacterium smegmatis (bacteria) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Yadav, R. / Pathak, P. / Pulavarti, S. / Jain, A. / Kumar, A. / Shukla, V. / Arora, A. | ||||||
Citation | Journal: To be Published Title: Solution structure and backbone dynamics of Peptidyl t-RNA hydrolase from Mycobacterium smegmatis Authors: Yadav, R. / Pathak, P. / Pulavarti, S. / Jain, A. / Kumar, A. / Shukla, V. / Arora, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lgj.cif.gz | 650.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lgj.ent.gz | 554.8 KB | Display | PDB format |
PDBx/mmJSON format | 2lgj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lg/2lgj ftp://data.pdbj.org/pub/pdb/validation_reports/lg/2lgj | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 20306.324 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium smegmatis (bacteria) / Strain: ATCC 700084 / mc(2)155 / Gene: pth / Production host: Escherichia coli (E. coli) / References: UniProt: A0R3D3, peptidyl-tRNA hydrolase |
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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 |
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Sample conditions | Ionic strength: 50 / pH: 6.5 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2188 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 10 / Representative conformer: 1 |