+Open data
-Basic information
Entry | Database: PDB / ID: 1wh0 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the CS domain of human USP19 | ||||||
Components | Ubiquitin carboxyl-terminal hydrolase 19 | ||||||
Keywords | HYDROLASE / USP / CS domain / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information regulation of ERAD pathway / positive regulation of cell cycle process / negative regulation of skeletal muscle tissue development / regulation of cellular response to hypoxia / protein deubiquitination / : / response to endoplasmic reticulum stress / Hsp90 protein binding / regulation of protein stability / ubiquitinyl hydrolase 1 ...regulation of ERAD pathway / positive regulation of cell cycle process / negative regulation of skeletal muscle tissue development / regulation of cellular response to hypoxia / protein deubiquitination / : / response to endoplasmic reticulum stress / Hsp90 protein binding / regulation of protein stability / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / protein stabilization / Ub-specific processing proteases / endoplasmic reticulum membrane / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Nakanishi, T. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the CS domain of human USP19 Authors: Nakanishi, T. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
| ||||||
Remark 650 | HELIX AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED | ||||||
Remark 700 | SHEET AUTHOR DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1wh0.cif.gz | 798.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1wh0.ent.gz | 692.1 KB | Display | PDB format |
PDBx/mmJSON format | 1wh0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wh/1wh0 ftp://data.pdbj.org/pub/pdb/validation_reports/wh/1wh0 | HTTPS FTP |
---|
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 14913.787 Da / Num. of mol.: 1 / Fragment: CS domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: KAZUSA cDNA hk08201 / Plasmid: P040114-29 / References: UniProt: O94966, EC: 3.1.2.15 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1.15mM CS domain U-15N, 13C; 20mM NaPi; 100mM NaCl; 2mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 120mM / pH: 6.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
-Processing
NMR software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |