Download MendeleySolution structure of phosphotyrosine interaction domain of mouse Numb protein
Sato, M., Tomizawa, T., Koshiba, S., Tochio, N., Inoue, M., Kigawa, T., Yokoyama, S.To be published.
1WJ1
Solution structure of phosphotyrosine interaction domain of mouse Numb protein
- PDB DOI: https://doi.org/10.2210/pdb1WJ1/pdb
- BMRB: 10089
- Classification: SIGNALING PROTEIN
- Organism(s): Mus musculus
- Mutation(s): No
- Deposited: 2004-05-28 Released: 2004-11-28
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations, target function
wwPDB Validation 3D Report Full Report
This is version 1.3 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Numb protein | 156 | Mus musculus | Mutation(s): 0 Gene Names: RIKEN cDNA 1200002O22 |  | |
UniProt | |||||
Find proteins for Q9QZS3 (Mus musculus) Explore Q9QZS3 Go to UniProtKB: Q9QZS3 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9QZS3 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations, target function
Entry History
Deposition Data
- Released Date: 2004-11-28 Deposition Author(s): Sato, M., Tomizawa, T., Koshiba, S., Tochio, N., Inoue, M., Kigawa, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2004-11-28
Type: Initial release - Version 1.1: 2008-04-30
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2022-03-02
Changes: Data collection, Database references, Derived calculations
