[English] 日本語
Yorodumi- PDB-2ell: Solution structure of the Leucine Rich Repeat of human Acidic leu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ell | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the Leucine Rich Repeat of human Acidic leucine-rich nuclear phosphoprotein 32 family member B | ||||||
Components | Acidic leucine-rich nuclear phosphoprotein 32 family member B | ||||||
Keywords | GENE REGULATION / PHAPI2 protein / Silver-stainable protein SSP29 / Acidic protein rich in leucines / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information ventricular system development / vasculature development / RNA polymerase binding / roof of mouth development / inner ear development / negative regulation of cell differentiation / positive regulation of protein export from nucleus / : / nucleosome assembly / histone binding ...ventricular system development / vasculature development / RNA polymerase binding / roof of mouth development / inner ear development / negative regulation of cell differentiation / positive regulation of protein export from nucleus / : / nucleosome assembly / histone binding / regulation of apoptotic process / extracellular exosome / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tochio, N. / Koshiba, S. / Watanabe, S. / Harada, T. / Umehara, T. / Tanaka, A. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2010 Title: Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain. Authors: Tochio, N. / Umehara, T. / Munemasa, Y. / Suzuki, T. / Sato, S. / Tsuda, K. / Koshiba, S. / Kigawa, T. / Nagai, R. / Yokoyama, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2ell.cif.gz | 1022.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2ell.ent.gz | 860.1 KB | Display | PDB format |
PDBx/mmJSON format | 2ell.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ell_validation.pdf.gz | 343.1 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2ell_full_validation.pdf.gz | 511.4 KB | Display | |
Data in XML | 2ell_validation.xml.gz | 74.5 KB | Display | |
Data in CIF | 2ell_validation.cif.gz | 91.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/el/2ell ftp://data.pdbj.org/pub/pdb/validation_reports/el/2ell | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 18842.559 Da / Num. of mol.: 1 / Fragment: LRR_1 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: cell-free protein synthesis / Gene: ANP32B / Plasmid: P060227-01 / References: UniProt: Q92688 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1.3mM sample U-15N, 13C; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |