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Yorodumi- PDB-2m0g: Structure, phosphorylation and U2AF65 binding of the Nterminal Do... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2m0g | ||||||
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Title | Structure, phosphorylation and U2AF65 binding of the Nterminal Domain of splicing factor 1 during 3 splice site Recognition | ||||||
Components |
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Keywords | SPLICING / spliceosome assembly / SF1 / UHM / ULM | ||||||
Function / homology | Function and homology information nuclear body organization / U2AF complex / regulation of steroid biosynthetic process / poly-pyrimidine tract binding / pre-mRNA 3'-splice site binding / Leydig cell differentiation / male sex determination / mRNA 3'-end processing / regulation of mRNA splicing, via spliceosome / C2H2 zinc finger domain binding ...nuclear body organization / U2AF complex / regulation of steroid biosynthetic process / poly-pyrimidine tract binding / pre-mRNA 3'-splice site binding / Leydig cell differentiation / male sex determination / mRNA 3'-end processing / regulation of mRNA splicing, via spliceosome / C2H2 zinc finger domain binding / commitment complex / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA Polymerase II Transcription Termination / U2-type prespliceosome / molecular function inhibitor activity / spliceosomal complex assembly / Protein hydroxylation / negative regulation of mRNA splicing, via spliceosome / mRNA 3'-splice site recognition / negative regulation of protein ubiquitination / mRNA Splicing - Major Pathway / positive regulation of RNA splicing / negative regulation of smooth muscle cell proliferation / spliceosomal complex / mRNA splicing, via spliceosome / mRNA processing / transcription corepressor activity / nuclear body / ribosome / nuclear speck / mRNA binding / enzyme binding / RNA binding / zinc ion binding / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Madl, T. / Sattler, M. / Zhang, Y. / Bagdiul, I. / Kern, T. / Kang, H. / Zou, P. / Maeusbacher, N. / Sieber, S.A. / Kraemer, A. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2013 Title: Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition. Authors: Zhang, Y. / Madl, T. / Bagdiul, I. / Kern, T. / Kang, H.S. / Zou, P. / Mausbacher, N. / Sieber, S.A. / Kramer, A. / Sattler, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m0g.cif.gz | 784.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m0g.ent.gz | 660.6 KB | Display | PDB format |
PDBx/mmJSON format | 2m0g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2m0g_validation.pdf.gz | 419.9 KB | Display | wwPDB validaton report |
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Full document | 2m0g_full_validation.pdf.gz | 558.2 KB | Display | |
Data in XML | 2m0g_validation.xml.gz | 52.9 KB | Display | |
Data in CIF | 2m0g_validation.cif.gz | 64.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m0/2m0g ftp://data.pdbj.org/pub/pdb/validation_reports/m0/2m0g | 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: 16675.066 Da / Num. of mol.: 1 / Fragment: UNP residues 1-145 / Mutation: S137C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SF1, ZFM1, ZNF162 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15637 |
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#2: Protein | Mass: 11976.615 Da / Num. of mol.: 1 / Fragment: RRM 3 domain residues 372-475 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: U2AF2, U2AF65 / Production host: Escherichia coli (E. coli) / References: UniProt: P26368 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 100-600 uM [U-15N] protein, 100-600 uM [U-13C; U-15N] entity, 100-600 uM [U-13C; U-15N; U-2H] entity, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 70 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 10 |