[English] 日本語
![](img/lk-miru.gif)
- PDB-5mf9: Solution structure of the RBM5 OCRE domain in complex with polypr... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 5mf9 | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Solution structure of the RBM5 OCRE domain in complex with polyproline SmN peptide. | |||||||||||||||
![]() |
| |||||||||||||||
![]() | SPLICING / OCRE / Poly proline binding domain / SmN / alternative splicing | |||||||||||||||
Function / homology | ![]() Gemini of coiled bodies / SMN complex / SMN-Sm protein complex / spliceosomal complex assembly / regulation of alternative mRNA splicing, via spliceosome / RNA processing / spliceosomal snRNP assembly / Cajal body / mRNA Splicing - Major Pathway / DNA-templated transcription termination ...Gemini of coiled bodies / SMN complex / SMN-Sm protein complex / spliceosomal complex assembly / regulation of alternative mRNA splicing, via spliceosome / RNA processing / spliceosomal snRNP assembly / Cajal body / mRNA Splicing - Major Pathway / DNA-templated transcription termination / spliceosomal complex / Z disc / mRNA splicing, via spliceosome / cytoplasmic ribonucleoprotein granule / nervous system development / snRNP Assembly / SARS-CoV-2 modulates host translation machinery / perikaryon / nuclear body / neuron projection / positive regulation of apoptotic process / negative regulation of cell population proliferation / axon / mRNA binding / apoptotic process / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||||||||
Biological species | ![]() | |||||||||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||||||||
![]() | Mourao, A. / Sattler, M. / Bonnal, S. / Komal, S. / Warner, L. / Bordonne, R. / Valcarcel, J. | |||||||||||||||
Funding support | ![]() ![]()
| |||||||||||||||
![]() | ![]() Title: Structural basis for the recognition ofspliceosomal SmN B B proteins by theRBM5 OCRE domain in splicing regulation Authors: Mourao, A. / Bonnal, S. / Komal, S. / Warner, L. / Bordonne, R. / Valcarcel, J. / Sattler, M. | |||||||||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 251.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 211.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 423.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 540.9 KB | Display | |
Data in XML | ![]() | 18.4 KB | Display | |
Data in CIF | ![]() | 28.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5mfyC C: citing same article ( |
---|---|
Similar structure data | |
Other databases |
|
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 7436.785 Da / Num. of mol.: 1 / Fragment: UNP residues 451-511 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Protein/peptide | Mass: 1136.371 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details | Type: solid Contents: 2 mM [U-99% 15N] 15N, 2 mM [U-99% 13C; U-99% 15N] 13C_15N, 2 mM [U-13C; U-15N] unlabel, 90% H2O/10% D2O Label: OCRE_SmN / Solvent system: 90% H2O/10% D2O | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||
Sample conditions | Ionic strength: 50 mM / Label: 15N_sample / pH: 6.5 / Pressure: 1 bar / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
NMR software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |