BMRB Entry 10089
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10089
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Title: Solution structure of phosphotyrosine interaction domain of mouse Numb protein
Deposition date: 2007-01-24 Original release date: 2008-08-14
Authors: Sato, M.; Tomizawa, T.; Koshiba, S.; Tochio, N.; Inoue, M.; Kigawa, T.; Yokoyama, S.
Citation: Sato, M.; Tomizawa, T.; Koshiba, S.; Tochio, N.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of phosphotyrosine interaction domain of mouse Numb protein" . ., .-..
Assembly members:
PID domain, polymer, 156 residues, Formula weight is not available
Natural source: Common Name: mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: cell free synthesis
Entity Sequences (FASTA):
PID domain: GSSGSSGASRPHQWQTDEEG
VRTGKCSFPVKYLGHVEVDE
SRGMHICEDAVKRLKATGKK
AVKAVLWVSADGLRVVDEKT
KDLIVDQTIEKVSFCAPDRN
FDRAFSYICRDGTTRRWICH
CFMAVKDTGERLSHAVGCAF
AACLERKQKRSGPSSG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 666 |
| 15N chemical shifts | 162 |
| 1H chemical shifts | 1038 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Numb protein | 1 |
Entities:
Entity 1, Numb protein 156 residues - Formula weight is not available
| 1 | GLY | SER | SER | GLY | SER | SER | GLY | ALA | SER | ARG | ||||
| 2 | PRO | HIS | GLN | TRP | GLN | THR | ASP | GLU | GLU | GLY | ||||
| 3 | VAL | ARG | THR | GLY | LYS | CYS | SER | PHE | PRO | VAL | ||||
| 4 | LYS | TYR | LEU | GLY | HIS | VAL | GLU | VAL | ASP | GLU | ||||
| 5 | SER | ARG | GLY | MET | HIS | ILE | CYS | GLU | ASP | ALA | ||||
| 6 | VAL | LYS | ARG | LEU | LYS | ALA | THR | GLY | LYS | LYS | ||||
| 7 | ALA | VAL | LYS | ALA | VAL | LEU | TRP | VAL | SER | ALA | ||||
| 8 | ASP | GLY | LEU | ARG | VAL | VAL | ASP | GLU | LYS | THR | ||||
| 9 | LYS | ASP | LEU | ILE | VAL | ASP | GLN | THR | ILE | GLU | ||||
| 10 | LYS | VAL | SER | PHE | CYS | ALA | PRO | ASP | ARG | ASN | ||||
| 11 | PHE | ASP | ARG | ALA | PHE | SER | TYR | ILE | CYS | ARG | ||||
| 12 | ASP | GLY | THR | THR | ARG | ARG | TRP | ILE | CYS | HIS | ||||
| 13 | CYS | PHE | MET | ALA | VAL | LYS | ASP | THR | GLY | GLU | ||||
| 14 | ARG | LEU | SER | HIS | ALA | VAL | GLY | CYS | ALA | PHE | ||||
| 15 | ALA | ALA | CYS | LEU | GLU | ARG | LYS | GLN | LYS | ARG | ||||
| 16 | SER | GLY | PRO | SER | SER | GLY |
Samples:
sample_1: PID domain, [U-13C; U-15N], 1.3 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 5 mM; NaN3 0.02%; H2O 90%; D2O 10%
condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | sample_1 | not available | condition_1 |
| 3D 15N-separated NOESY | sample_1 | not available | condition_1 |
Software:
xwinnmr v2.6, Bruker - collection
NMRPipe v20020425, Delaglio, F. - processing
NMRView v5.0.4, Johnson, B.A. - data analysis
Kujira v0.8996, Kobayashi, N. - data analysis
CYANA v1.0.7, Guntert, P. - refinement, structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAB23367 BAE45130 BAG37583 |
| EMBL | CAD66588 CAH91534 |
| GB | AAB09586 AAC97962 AAD47834 AAD49434 AAD54281 |
| REF | NP_001005745 NP_001095421 NP_001125900 NP_001258984 NP_001258985 |
| TPG | DAA25078 |
Download simulated HSQC data in one of the following formats:
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