[English] 日本語
Yorodumi- PDB-1j0g: Solution Structure of Mouse Hypothetical 9.1 kDa Protein, A Ubiqu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1j0g | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of Mouse Hypothetical 9.1 kDa Protein, A Ubiquitin-like Fold | ||||||
Components | Hypothetical Protein 1810045K17 | ||||||
Keywords | structural genomics / unknown function / Hypothetical protein / Ubiquitin-like fold / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information protein ufmylation / protein K69-linked ufmylation / regulation of intracellular estrogen receptor signaling pathway / reticulophagy / negative regulation of protein import into nucleus / response to endoplasmic reticulum stress / brain development / negative regulation of apoptotic process / endoplasmic reticulum / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Zhao, C. / Kigawa, T. / Koshiba, S. / Tochio, N. / Kobayashi, N. / Inoue, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution Structure of Mouse Hypothetical 9.1 kDa Protein, A Ubiquitin-like Fold Authors: Zhao, C. / Kigawa, T. / Koshiba, S. / Tochio, N. / Kobayashi, N. / Inoue, M. / Yokoyama, S. | ||||||
History |
| ||||||
Remark 650 | HELIX Determination method: Author determined |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1j0g.cif.gz | 536.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1j0g.ent.gz | 446.6 KB | Display | PDB format |
PDBx/mmJSON format | 1j0g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1j0g_validation.pdf.gz | 342.7 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1j0g_full_validation.pdf.gz | 500.3 KB | Display | |
Data in XML | 1j0g_validation.xml.gz | 34.1 KB | Display | |
Data in CIF | 1j0g_validation.cif.gz | 52.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j0/1j0g ftp://data.pdbj.org/pub/pdb/validation_reports/j0/1j0g | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 9702.107 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 1810045K17 / Plasmid: P020401-41 / References: UniProt: P61961 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1.0mM Protein U-15N,13C; 20mM phosphate buffer NA; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 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: 800 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,structures with the lowest energy,target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |