[English] 日本語
Yorodumi- PDB-1sj6: NMR Structure and Regulated Expression in APL Cell of Human SH3BGRL3 -
+Open data
-Basic information
Entry | Database: PDB / ID: 1sj6 | ||||||
---|---|---|---|---|---|---|---|
Title | NMR Structure and Regulated Expression in APL Cell of Human SH3BGRL3 | ||||||
Components | SH3 domain-binding glutamic acid-rich-like protein 3 | ||||||
Keywords | PROTEIN BINDING / thioredoxin / Nuclear protein | ||||||
Function / homology | Function and homology information protein-disulfide reductase activity / nuclear body / electron transfer activity / extracellular exosome / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics | ||||||
Authors | Xu, C. / Tang, Y. / Xu, Y. / Wu, J. / Shi, Y. / Zhang, Q. / Zheng, P. / Du, Y. | ||||||
Citation | Journal: Febs Lett. / Year: 2005 Title: NMR structure and regulated expression in APL cell of human SH3BGRL3. Authors: Xu, C. / Zheng, P. / Shen, S. / Xu, Y. / Wei, L. / Gao, H. / Wang, S. / Zhu, C. / Tang, Y. / Wu, J. / Zhang, Q. / Shi, Y. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1sj6.cif.gz | 578.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1sj6.ent.gz | 483.5 KB | Display | PDB format |
PDBx/mmJSON format | 1sj6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1sj6_validation.pdf.gz | 345.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1sj6_full_validation.pdf.gz | 510.3 KB | Display | |
Data in XML | 1sj6_validation.xml.gz | 34 KB | Display | |
Data in CIF | 1sj6_validation.cif.gz | 53.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sj/1sj6 ftp://data.pdbj.org/pub/pdb/validation_reports/sj/1sj6 | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 11518.832 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SHEBGRL3 / Plasmid: PET22B(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q9H299 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||||||||||||||||||||||
NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy |
-Sample preparation
Details | Contents: 2mM SH3BGRL3 U-15N, 13C; 20mM phosphate buffer NA; 100mM NaCl, pH7.0; 90% H2O, 10% D2O Solvent system: 90% H20, 10% D20 |
---|---|
Sample conditions | Ionic strength: 100mM NaCl, 20mM phosphate buffer / pH: 7 / Pressure: 1 atm / Temperature: 295 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: distance geometry, simulated annealing, molecular dynamics, torsion angle dynamics Software ordinal: 1 Details: the structures are based on a total of 1463 restraints, 1306 are NOE-derived distance constraints, 101 dihedral angle restraints, 56 distance restraints from hydrogen bonds | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |