+Open data
-Basic information
Entry | Database: PDB / ID: 2mtf | ||||||
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Title | Solution structure of the La motif of human LARP6 | ||||||
Components | La-related protein 6 | ||||||
Keywords | RNA BINDING PROTEIN / LARP6 / La motif / La-related proteins / Acheron / LARP | ||||||
Function / homology | Function and homology information : / sequence-specific mRNA binding / myosin binding / positive regulation of collagen biosynthetic process / RNA processing / RNA stem-loop binding / mRNA 5'-UTR binding / regulation of translation / mRNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | closest to the average, model1 | ||||||
Authors | Martino, L. / Salisbury, N.JH. / Atkinson, A.R. / Kelly, G. / Conte, M.R. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2015 Title: Synergic interplay of the La motif, RRM1 and the interdomain linker of LARP6 in the recognition of collagen mRNA expands the RNA binding repertoire of the La module. Authors: Martino, L. / Pennell, S. / Kelly, G. / Busi, B. / Brown, P. / Atkinson, R.A. / Salisbury, N.J. / Ooi, Z.H. / See, K.W. / Smerdon, S.J. / Alfano, C. / Bui, T.T. / Conte, M.R. #1: Journal: To be Published Title: 1H, 15N and 13C chemical shift assignments of the La motif and RRM1 from human LARP6 Authors: Martino, L. / Pennell, S. / Kelly, G. / Busi, B. / Brown, P. / Atkinson, A.R. / Salisbury, N.JH. / Ooi, Z.H. / See, K.W. / Smerdon, S.J. / Alfano, C. / Bui, T.TT. / Conte, M.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mtf.cif.gz | 743.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mtf.ent.gz | 622.2 KB | Display | PDB format |
PDBx/mmJSON format | 2mtf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mt/2mtf ftp://data.pdbj.org/pub/pdb/validation_reports/mt/2mtf | HTTPS FTP |
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-Related 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: 13542.352 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: LARP6 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9BRS8 |
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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: 0.3-0.5 mM [U-95% 13C; U-95% 15N] LARP6-LaM, 50 mM TRIS, 100 mM potassium chloride, 1 mM DTT, 50 mM L-Arginine, 50 mM L-Glutamic acid, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.1 / pH: 7.25 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: DGSA-distance geometry 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: 100 / Conformers submitted total number: 20 |