BMRB Entry 19797
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19797
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: STRUCTURE OF THE NA,K-ATPASE REGULATORY PROTEIN FXYD2b IN MICELLES PubMed: 24794573
Deposition date: 2014-02-13 Original release date: 2014-05-12
Authors: Marassi, Francesca; Gong, Xiao-Min
Citation: Gong, Xiao-Min; Marassi, Francesca. "Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: Implications for membrane-water interfacial arginines" Biochim. Biophys. Acta ., .-..
Assembly members:
entity, polymer, 64 residues, 7331.390 Da.
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
Entity Sequences (FASTA):
entity: LDRWYLGGSPKGDVDPFYYD
YETVRNGGLIFAGLAFIVGL
LILLSRRFRSGGNKKRRQIN
EDEP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 169 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 229 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FXYD2b | 1 |
Entities:
Entity 1, FXYD2b 64 residues - 7331.390 Da.
| 1 | LEU | ASP | ARG | TRP | TYR | LEU | GLY | GLY | SER | PRO | ||||
| 2 | LYS | GLY | ASP | VAL | ASP | PRO | PHE | TYR | TYR | ASP | ||||
| 3 | TYR | GLU | THR | VAL | ARG | ASN | GLY | GLY | LEU | ILE | ||||
| 4 | PHE | ALA | GLY | LEU | ALA | PHE | ILE | VAL | GLY | LEU | ||||
| 5 | LEU | ILE | LEU | LEU | SER | ARG | ARG | PHE | ARG | SER | ||||
| 6 | GLY | GLY | ASN | LYS | LYS | ARG | ARG | GLN | ILE | ASN | ||||
| 7 | GLU | ASP | GLU | PRO |
Samples:
sample_1: FXYD2b, [U-99% 13C; U-99% 15N], 0.2 mM; SDS micelles 500 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 50 mM; pH: 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts