BMRB Entry 16167
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16167
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Title: NMR data for FXYD4 in micelles PubMed: 17567018
Deposition date: 2009-02-11 Original release date: 2009-03-12
Authors: Marassi, Francesca; Franzin, Carla; Teriete, Peter
Citation: Franzin, Carla; Teriete, Peter; Marassi, Francesca. "Structural similarity of a membrane protein in micelles and membranes." J. Am. Chem. Soc. 129, 8078-8079 (2007).
Assembly members:
FXYD4, polymer, 67 residues, Formula weight is not available
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FXYD4: NGPVDKGSPFYYDWESLQLG
GLIFGGLLCIAGIALALSGK
CKCRRNHTPSSLPEKVTPLI
TPGSAST
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 123 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 136 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FXYD4 subunit | 1 |
Entities:
Entity 1, FXYD4 subunit 67 residues - Formula weight is not available
| 1 | ASN | GLY | PRO | VAL | ASP | LYS | GLY | SER | PRO | PHE | ||||
| 2 | TYR | TYR | ASP | TRP | GLU | SER | LEU | GLN | LEU | GLY | ||||
| 3 | GLY | LEU | ILE | PHE | GLY | GLY | LEU | LEU | CYS | ILE | ||||
| 4 | ALA | GLY | ILE | ALA | LEU | ALA | LEU | SER | GLY | LYS | ||||
| 5 | CYS | LYS | CYS | ARG | ARG | ASN | HIS | THR | PRO | SER | ||||
| 6 | SER | LEU | PRO | GLU | LYS | VAL | THR | PRO | LEU | ILE | ||||
| 7 | THR | PRO | GLY | SER | ALA | SER | THR |
Samples:
sample_1: FXYD4, [U-100% 13C; U-100% 15N], 0.75 mM; FXYD4, [U-100% 15N], 0.75 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 20 mM; pH: 5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
SPARKY, Goddard - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts