BMRB Entry 16910
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16910
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Title: Assignment of HN,HA,HB,N,CA,CB and C' of the STAS domain of motor protein Prestin (Anion Transporter SLC26A5) PubMed: 20471983
Deposition date: 2010-04-30 Original release date: 2011-05-02
Authors: Bellanda, Massimo; Gesiot, Lorenzo
Citation: Pasqualetto, Elisa; Aiello, Rosa; Gesiot, Lorenzo; Bonetto, Greta; Bellanda, Massimo; Battistutta, Roberto. "Structure of the cytosolic portion of motor protein prestin and functional role of the STAS domain in SLC26/SulP anion transporters." J. Mol. Biol. 400, 448-462 (2010).
Assembly members:
Prestin_STAS, polymer, 152 residues, Formula weight is not available
Natural source: Common Name: Norway rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET SUMO (Invitrogen)
Entity Sequences (FASTA):
Prestin_STAS: SPSYTVLGQLPDTDVYIDID
AYEEVKEIPGIKIFQINAPI
YYANSDLYSSALKRKTGVNG
SENIHTVILDFTQVNFMDSV
GVKTLAGIVKEYGDVGIYVY
LAGCSAQVVNDLTSNRFFEN
PALKELLFHSIHDAVLGSQV
REAMAEQETTVL
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 372 |
15N chemical shifts | 121 |
1H chemical shifts | 453 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Prestin_STAS | 1 |
Entities:
Entity 1, Prestin_STAS 152 residues - Formula weight is not available
1 | SER | PRO | SER | TYR | THR | VAL | LEU | GLY | GLN | LEU | ||||
2 | PRO | ASP | THR | ASP | VAL | TYR | ILE | ASP | ILE | ASP | ||||
3 | ALA | TYR | GLU | GLU | VAL | LYS | GLU | ILE | PRO | GLY | ||||
4 | ILE | LYS | ILE | PHE | GLN | ILE | ASN | ALA | PRO | ILE | ||||
5 | TYR | TYR | ALA | ASN | SER | ASP | LEU | TYR | SER | SER | ||||
6 | ALA | LEU | LYS | ARG | LYS | THR | GLY | VAL | ASN | GLY | ||||
7 | SER | GLU | ASN | ILE | HIS | THR | VAL | ILE | LEU | ASP | ||||
8 | PHE | THR | GLN | VAL | ASN | PHE | MET | ASP | SER | VAL | ||||
9 | GLY | VAL | LYS | THR | LEU | ALA | GLY | ILE | VAL | LYS | ||||
10 | GLU | TYR | GLY | ASP | VAL | GLY | ILE | TYR | VAL | TYR | ||||
11 | LEU | ALA | GLY | CYS | SER | ALA | GLN | VAL | VAL | ASN | ||||
12 | ASP | LEU | THR | SER | ASN | ARG | PHE | PHE | GLU | ASN | ||||
13 | PRO | ALA | LEU | LYS | GLU | LEU | LEU | PHE | HIS | SER | ||||
14 | ILE | HIS | ASP | ALA | VAL | LEU | GLY | SER | GLN | VAL | ||||
15 | ARG | GLU | ALA | MET | ALA | GLU | GLN | GLU | THR | THR | ||||
16 | VAL | LEU |
Samples:
sample_1: Prestin_STAS, [U-13C; U-15N], 1.2 mM; DTT 10 mM; EDTA 1 mM; potassium phosphate 30 mM; sodium chloride 50 mM; sodium azide 0.05 %w/v; DSS 0.5 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HA(CA)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
TOPSPIN, Bruker Biospin - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Related Database Links:
PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts