+Open data
-Basic information
Entry | Database: PDB / ID: 2lea | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of human SRSF2 (SC35) RRM | ||||||
Components | Serine/arginine-rich splicing factor 2 | ||||||
Keywords | RNA BINDING PROTEIN / SR protein / splicing factor | ||||||
Function / homology | Function and homology information interchromatin granule / perichromatin fibrils / pre-mRNA binding / mRNA 3'-end processing / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA Polymerase II Transcription Termination / regulation of alternative mRNA splicing, via spliceosome / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / response to vitamin E ...interchromatin granule / perichromatin fibrils / pre-mRNA binding / mRNA 3'-end processing / Transport of Mature mRNA derived from an Intron-Containing Transcript / RNA Polymerase II Transcription Termination / regulation of alternative mRNA splicing, via spliceosome / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / response to vitamin E / mRNA Splicing - Major Pathway / protein kinase C binding / RNA splicing / spliceosomal complex / mRNA splicing, via spliceosome / mRNA processing / transcription corepressor activity / nuclear speck / RNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | closest to the average, model 17 | ||||||
Authors | Daubner, G.M. / Clery, A. / Jayne, S. / Stevenin, J. / Allain, F.H.-T. | ||||||
Citation | Journal: Embo J. / Year: 2012 Title: A syn-anti conformational difference allows SRSF2 to recognize guanines and cytosines equally well. Authors: Daubner, G.M. / Clery, A. / Jayne, S. / Stevenin, J. / Allain, F.H. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2lea.cif.gz | 625.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2lea.ent.gz | 522.2 KB | Display | PDB format |
PDBx/mmJSON format | 2lea.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/le/2lea ftp://data.pdbj.org/pub/pdb/validation_reports/le/2lea | HTTPS FTP |
---|
-Related structure data
Related structure data | 2lebC 2lecC C: citing same article (ref.) |
---|---|
Similar structure data | |
Other databases |
|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 15258.074 Da / Num. of mol.: 1 / Fragment: RRM domain residues 1-101 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SFRS2, SRSF2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q01130 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| ||||||||||||||||
Sample conditions | Ionic strength: 120 / pH: 5.5 / Pressure: ambient / Temperature: 310.8 K |
-NMR measurement
NMR spectrometer |
|
---|
-Processing
NMR software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR constraints | NOE constraints total: 2585 / NOE intraresidue total count: 458 / NOE long range total count: 973 / NOE medium range total count: 418 / NOE sequential total count: 736 | ||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 / Maximum upper distance constraint violation: 0.35 Å |