[English] 日本語
Yorodumi- PDB-2dh8: Solution structure of the N-terminal RNA binding domain in DAZ-as... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2dh8 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the N-terminal RNA binding domain in DAZ-associated protein 1 | ||||||
Components | DAZ-associated protein 1 | ||||||
Keywords | RNA BINDING PROTEIN / RRM domain / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information poly(G) binding / maternal placenta development / poly(U) RNA binding / positive regulation of mRNA splicing, via spliceosome / male germ cell nucleus / mRNA 3'-UTR binding / RNA stem-loop binding / fibroblast proliferation / spermatogenesis / cell differentiation ...poly(G) binding / maternal placenta development / poly(U) RNA binding / positive regulation of mRNA splicing, via spliceosome / male germ cell nucleus / mRNA 3'-UTR binding / RNA stem-loop binding / fibroblast proliferation / spermatogenesis / cell differentiation / ribonucleoprotein complex / protein-containing complex / RNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, restrained molecular dynamics | ||||||
Authors | Arai, S. / Tsuda, K. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the N-terminal RNA binding domain in DAZ-associated protein 1 Authors: Arai, S. / Tsuda, K. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2dh8.cif.gz | 596.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2dh8.ent.gz | 499.2 KB | Display | PDB format |
PDBx/mmJSON format | 2dh8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2dh8_validation.pdf.gz | 344.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2dh8_full_validation.pdf.gz | 487.6 KB | Display | |
Data in XML | 2dh8_validation.xml.gz | 35.9 KB | Display | |
Data in CIF | 2dh8_validation.cif.gz | 55.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dh/2dh8 ftp://data.pdbj.org/pub/pdb/validation_reports/dh/2dh8 | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 11162.392 Da / Num. of mol.: 1 / Fragment: RNA recognition motif Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: DAZAP1 / Plasmid: P050704-07 / Production host: Cell free synthesis / References: UniProt: Q96EP5 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 20mM d-Tris-HCl(pH 7.0), 100mM NaCl, 1mM d-DTT, 0.02% NaN3, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 100mM / pH: 7 / 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: torsion angle dynamics, restrained molecular dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function, structures with the lowest energy, structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |