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Yorodumi- PDB-2l9v: NMR structure of the FF domain L24A mutant's folding transition state -
+Open data
-Basic information
Entry | Database: PDB / ID: 2l9v | ||||||
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Title | NMR structure of the FF domain L24A mutant's folding transition state | ||||||
Components | Pre-mRNA-processing factor 40 homolog A | ||||||
Keywords | RNA BINDING PROTEIN | ||||||
Function / homology | Function and homology information mRNA cis splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / cytoskeleton organization / mRNA Splicing - Major Pathway / regulation of cytokinesis / nuclear matrix / mRNA splicing, via spliceosome / cell migration / regulation of cell shape ...mRNA cis splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / cytoskeleton organization / mRNA Splicing - Major Pathway / regulation of cytokinesis / nuclear matrix / mRNA splicing, via spliceosome / cell migration / regulation of cell shape / nuclear speck / cell cycle / cell division / RNA binding / nucleoplasm / membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / Monte Carlo | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Korzhnev, D.M. / Vernon, R.M. / Religa, T.L. / Hansen, A. / Baker, D. / Fersht, A.R. / Kay, L.E. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 2011 Title: Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study. Authors: Korzhnev, D.M. / Vernon, R.M. / Religa, T.L. / Hansen, A.L. / Baker, D. / Fersht, A.R. / Kay, L.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l9v.cif.gz | 157.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l9v.ent.gz | 125.5 KB | Display | PDB format |
PDBx/mmJSON format | 2l9v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l9/2l9v ftp://data.pdbj.org/pub/pdb/validation_reports/l9/2l9v | 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: 8152.335 Da / Num. of mol.: 1 / Fragment: FF 1 domain residues 390-438 / Mutation: L24A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: FBP11, FLAF1, FNBP3, HIP10, HSPC225, HYPA, PRPF40A / Production host: Escherichia coli (E. coli) / References: UniProt: O75400 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: CPMG |
-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 145 / pH: 5.7 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: Monte Carlo / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 10000 / Conformers submitted total number: 9 |