BMRB Entry 17241
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17241
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Title: YAP WW2 PubMed: 21417403
Deposition date: 2010-10-07 Original release date: 2011-03-30
Authors: Webb, Claire; Upadhyay, Abhishek; Furutani-Seiki, Makoto; Bagby, Stefan
Citation: Webb, Claire; Upadhyay, Abhishek; Giuntini, Francesca; Eggleston, Ian; Furutani-Seiki, Makoto; Ishima, Rieko; Bagby, Stefan. "Structural Features and Ligand Binding Properties of Tandem WW Domains from YAP and TAZ, Nuclear Effectors of the Hippo Pathway." Biochemistry 50, 3300-3309 (2011).
Assembly members:
entity, polymer, 46 residues, 5130.625 Da.
Natural source: Common Name: Japanese medaka Taxonomy ID: 8090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Oryzias latipes
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GSPNSSPASGPLPEGWEQAI
TPEGEIYYINHKNKTTSWLD
PRLETR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 193 |
| 15N chemical shifts | 46 |
| 1H chemical shifts | 264 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YAP | 1 |
Entities:
Entity 1, YAP 46 residues - 5130.625 Da.
The first 5 residues (residues 177-181) are remains of a non-native affinity tag.
| 1 | GLY | SER | PRO | ASN | SER | SER | PRO | ALA | SER | GLY | ||||
| 2 | PRO | LEU | PRO | GLU | GLY | TRP | GLU | GLN | ALA | ILE | ||||
| 3 | THR | PRO | GLU | GLY | GLU | ILE | TYR | TYR | ILE | ASN | ||||
| 4 | HIS | LYS | ASN | LYS | THR | THR | SER | TRP | LEU | ASP | ||||
| 5 | PRO | ARG | LEU | GLU | THR | ARG |
Samples:
sample_1: potassium phosphate 50 mM; sodium chloride 200 mM; EDTA 5 mM; YAP WW2 protein, [U-15N], 400 – 600 mM; H2O 93%; D2O 7%
sample_2: potassium phosphate 50 mM; sodium chloride 200 mM; EDTA 5 mM; YAP WW2 protein, [U-13C; U-15N], 400 – 600 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 0.2 M; pH: 5.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPN_Analysis, CCPN - chemical shift assignment, data analysis, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR spectrometers:
- Varian Unity INOVA 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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