[English] 日本語
Yorodumi- PDB-2di0: Solution Structure of the CUE Domain in the Human Activating Sign... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2di0 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of the CUE Domain in the Human Activating Signal Cointegrator 1 Complex Subunit 2 (ASCC2) | ||||||
Components | Activating signal cointegrator 1 complex subunit 2 | ||||||
Keywords | TRANSCRIPTION / activating signal cointegrator 1 complex subunit 2 / ASCC2 / CUE domain / structural genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information ALKBH3 mediated reversal of alkylation damage / activating signal cointegrator 1 complex / DNA alkylation repair / ribosome disassembly / ribosome-associated ubiquitin-dependent protein catabolic process / DNA repair complex / DNA duplex unwinding / K63-linked polyubiquitin modification-dependent protein binding / cytosolic ribosome / rescue of stalled ribosome ...ALKBH3 mediated reversal of alkylation damage / activating signal cointegrator 1 complex / DNA alkylation repair / ribosome disassembly / ribosome-associated ubiquitin-dependent protein catabolic process / DNA repair complex / DNA duplex unwinding / K63-linked polyubiquitin modification-dependent protein binding / cytosolic ribosome / rescue of stalled ribosome / ubiquitin binding / nuclear speck / regulation of DNA-templated transcription / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, restrained molecular dynamics | ||||||
Authors | Zhao, C. / Kigawa, T. / Tochio, N. / Koshiba, S. / Harada, T. / Watanabe, S. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution Structure of the CUE Domain in the Human Activating Signal Cointegrator 1 Complex Subunit 2 (ASCC2) Authors: Zhao, C. / Kigawa, T. / Tochio, N. / Koshiba, S. / Harada, T. / Watanabe, S. / Yokoyama, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2di0.cif.gz | 420.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2di0.ent.gz | 351.9 KB | Display | PDB format |
PDBx/mmJSON format | 2di0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/di/2di0 ftp://data.pdbj.org/pub/pdb/validation_reports/di/2di0 | HTTPS FTP |
---|
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 7891.792 Da / Num. of mol.: 1 / Fragment: CUE domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: ASCC2, ASC1P100 / Plasmid: P060116-03 / Production host: Cell free synthesis / References: UniProt: Q9H1I8 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1.24mM CUE domain U-15N, 13C; 20mM d-Tris-HCl (pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 296.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 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 / Conformers calculated total number: 100 / Conformers submitted total number: 20 |