BMRB Entry 27193
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27193
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Title: Backbone 1H, 15N chemical shift for Y39E EVH1 PubMed: 28783324
Deposition date: 2017-07-22 Original release date: 2017-08-23
Authors: Acevedo, Lucila; Greenwood, Alexander; Nicholson, Linda
Citation: Acevedo, Lucila Andrea; Greenwood, Alexander; Nicholson, Linda. "A Noncanonical Binding Site in the EVH1 Domain of Vasodilator-Stimulated Phosphoprotein Regulates Its Interactions with the Proline Rich Region of Zyxin" Biochemistry 56, 4626-4636 (2017).
Assembly members:
Y39E_EVH1, polymer, 121 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMW172
Entity Sequences (FASTA):
Y39E_EVH1: GPGGRMSSETVICSSRATVM
LYDDGNKRWLPAGTGPQAFS
RVQIEHNPTANSFRVVGRKM
QPDQQVVINCAIVRGVKYNQ
ATPNFHQWRDARQVWGLNFG
SKEDAAQFAAGMASALEALE
G
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 123 |
| 1H chemical shifts | 134 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Y39E EVH1 | 1 |
Entities:
Entity 1, Y39E EVH1 121 residues - Formula weight is not available
GPGGRMS is an artifact of cloning and 3cpro recognition, Y39E EVH1 is a mutation of Y39, and this contains the sequence from 2-115.
| 1 | GLY | PRO | GLY | GLY | ARG | MET | SER | SER | GLU | THR | ||||
| 2 | VAL | ILE | CYS | SER | SER | ARG | ALA | THR | VAL | MET | ||||
| 3 | LEU | TYR | ASP | ASP | GLY | ASN | LYS | ARG | TRP | LEU | ||||
| 4 | PRO | ALA | GLY | THR | GLY | PRO | GLN | ALA | PHE | SER | ||||
| 5 | ARG | VAL | GLN | ILE | GLU | HIS | ASN | PRO | THR | ALA | ||||
| 6 | ASN | SER | PHE | ARG | VAL | VAL | GLY | ARG | LYS | MET | ||||
| 7 | GLN | PRO | ASP | GLN | GLN | VAL | VAL | ILE | ASN | CYS | ||||
| 8 | ALA | ILE | VAL | ARG | GLY | VAL | LYS | TYR | ASN | GLN | ||||
| 9 | ALA | THR | PRO | ASN | PHE | HIS | GLN | TRP | ARG | ASP | ||||
| 10 | ALA | ARG | GLN | VAL | TRP | GLY | LEU | ASN | PHE | GLY | ||||
| 11 | SER | LYS | GLU | ASP | ALA | ALA | GLN | PHE | ALA | ALA | ||||
| 12 | GLY | MET | ALA | SER | ALA | LEU | GLU | ALA | LEU | GLU | ||||
| 13 | GLY |
Samples:
sample_1: Y39E EVH1, [U-99% 15N], 0.23 mM; potassium chloride 50 mM; potassium phosphate 20 mM; TCEP 1 mM; sodium azide 5 mM
sample_conditions_1: ionic strength: 94.76 mM; pH: 6.7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
SPARKY, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts