+Open data
-Basic information
Entry | Database: PDB / ID: 2mtg | ||||||
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Title | Solution structure of the RRM1 of human LARP6 | ||||||
Components | La-related protein 6 | ||||||
Keywords | RNA BINDING PROTEIN / LARP6 / RRM / 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 / mRNA 5'-UTR binding / RNA stem-loop binding / regulation of translation / ribonucleoprotein complex / 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. / 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. / 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 | 2mtg.cif.gz | 734.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mtg.ent.gz | 612.5 KB | Display | PDB format |
PDBx/mmJSON format | 2mtg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mtg_validation.pdf.gz | 409.6 KB | Display | wwPDB validaton report |
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Full document | 2mtg_full_validation.pdf.gz | 606.1 KB | Display | |
Data in XML | 2mtg_validation.xml.gz | 61.9 KB | Display | |
Data in CIF | 2mtg_validation.cif.gz | 81.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mt/2mtg ftp://data.pdbj.org/pub/pdb/validation_reports/mt/2mtg | HTTPS FTP |
-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: 13432.703 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: 0.3-0.7 mM [U-95% 13C; U-95% 15N] LARP6 RRM1, 50 mM TRIS, 100 mM potassium chloride, 1 mM DTT, 10 % [U-100% 2H] D2O, 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 |