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- PDB-1opi: SOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2... -
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Basic information
Entry | Database: PDB / ID: 1opi | ||||||
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Title | SOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2AF65 IN COMPLEX WITH AN N-TERMINAL SF1 PEPTIDE | ||||||
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![]() | RNA BINDING PROTEIN / NON-CANONICAL RNA RECOGNITION MOTIF / 4-STRANDED ANTI-PARALLEL BETA-SHEET / 2 ALPHA HELICES ADDITIONALLY EXTENDED BY A THIRD HELIX C | ||||||
Function / homology | ![]() 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 / C2H2 zinc finger domain binding / regulation of mRNA splicing, via spliceosome ...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 / C2H2 zinc finger domain binding / regulation of mRNA splicing, via spliceosome / 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 processing / mRNA splicing, via spliceosome / 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 | ![]() | ||||||
Method | SOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS USING CNS, ARIA FOR AMBIGUOUS DISTANCE RESTRAINTS | ||||||
![]() | Selenko, P. / Gregorovic, G. / Sprangers, R. / Stier, G. / Rhani, Z. / Kramer, A. / Sattler, M. | ||||||
![]() | ![]() Title: Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP Authors: Selenko, P. / Gregorovic, G. / Sprangers, R. / Stier, G. / Rhani, Z. / Kramer, A. / Sattler, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 373.8 KB | Display | ![]() |
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PDB format | ![]() | 309.3 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 355.9 KB | Display | ![]() |
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Full document | ![]() | 465.4 KB | Display | |
Data in XML | ![]() | 19.4 KB | Display | |
Data in CIF | ![]() | 32.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 11976.615 Da / Num. of mol.: 1 / Fragment: C-TERMINAL RRM DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1691.936 Da / Num. of mol.: 1 / Fragment: N-TERMINAL PEPTIDE / Source method: obtained synthetically Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED AND DERIVED FROM THE N-TERMINUS OF SF1. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN). References: UniProt: Q15637 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1MM 15N,13C U2AF65-RRM3 + 1MM UNLABELED SF1_10-25, 30MM PHOSPHATE BUFFER, 20MM NACL, 3MM DTT Solvent system: D2O |
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Sample conditions | Ionic strength: 50mM SALT / pH: 6.4 / Pressure: AMBIENT / Temperature: 295 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | ||||||||||||||||||||
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Radiation wavelength | Relative weight: 1 | ||||||||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: RESTRAINED MOLECULAR DYNAMICS USING CNS, ARIA FOR AMBIGUOUS DISTANCE RESTRAINTS Software ordinal: 1 Details: REFINEMENT OF PROTEIN STRUCTURES IN WATER SOLVENT, ACCORDING TO LINGE ET AL. (PROTEINS 50:496 -506, 2003) | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS, STRUCTURES WITH THE LOWEST ENERGY Conformers calculated total number: 100 / Conformers submitted total number: 10 |