+Open data
-Basic information
Entry | Database: PDB / ID: 2rrb | ||||||
---|---|---|---|---|---|---|---|
Title | Refinement of RNA binding domain in human Tra2 beta protein | ||||||
Components | cDNA FLJ40872 fis, clone TUTER2000283, highly similar to Homo sapiens transformer-2-beta (SFRS10) gene | ||||||
Keywords | RNA BINDING PROTEIN / RRM domain / RBD / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information cerebral cortex regionalization / embryonic brain development / pre-mRNA binding / RNA splicing, via transesterification reactions / positive regulation of mRNA splicing, via spliceosome / RHOBTB1 GTPase cycle / nuclear inner membrane / regulation of alternative mRNA splicing, via spliceosome / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA ...cerebral cortex regionalization / embryonic brain development / pre-mRNA binding / RNA splicing, via transesterification reactions / positive regulation of mRNA splicing, via spliceosome / RHOBTB1 GTPase cycle / nuclear inner membrane / regulation of alternative mRNA splicing, via spliceosome / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / RHOBTB2 GTPase cycle / mRNA Splicing - Major Pathway / cellular response to glucose stimulus / spliceosomal complex / mRNA splicing, via spliceosome / protein domain specific binding / mRNA binding / protein-containing complex / RNA binding / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | fewest violations, model 1 | ||||||
Authors | Tsuda, K. / Kuwasako, K. / Takahashi, M. / Someya, T. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Sugano, S. / Muto, Y. ...Tsuda, K. / Kuwasako, K. / Takahashi, M. / Someya, T. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Sugano, S. / Muto, Y. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2011 Title: Structural basis for the dual RNA-recognition modes of human Tra2-beta RRM. Authors: Tsuda, K. / Someya, T. / Kuwasako, K. / Takahashi, M. / He, F. / Unzai, S. / Inoue, M. / Harada, T. / Watanabe, S. / Terada, T. / Kobayashi, N. / Shirouzu, M. / Kigawa, T. / Tanaka, A. / ...Authors: Tsuda, K. / Someya, T. / Kuwasako, K. / Takahashi, M. / He, F. / Unzai, S. / Inoue, M. / Harada, T. / Watanabe, S. / Terada, T. / Kobayashi, N. / Shirouzu, M. / Kigawa, T. / Tanaka, A. / Sugano, S. / Guntert, P. / Yokoyama, S. / Muto, Y. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2rrb.cif.gz | 581.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2rrb.ent.gz | 508.6 KB | Display | PDB format |
PDBx/mmJSON format | 2rrb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rr/2rrb ftp://data.pdbj.org/pub/pdb/validation_reports/rr/2rrb | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 10891.192 Da / Num. of mol.: 1 / Fragment: RNA recognition motif Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q8N1H4, UniProt: P62995*PLUS |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1 mM [U-100% 13C; U-100% 15N] Human transformer 2 beta-1, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample | Conc.: 1 mM / Component: Human transformer 2 beta-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | Ionic strength: 100 / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 800 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |