BMRB Entry 17000
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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/BMR17000
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Title: Structure of E1-69 of Yeast V-ATPase PubMed: 21399923
Deposition date: 2010-06-14 Original release date: 2011-03-24
Authors: Sankaranarayanan, Rishikesan; Gruber, Gerhard
Citation: Rishikesan, Sankaranarayanan; Thaker, Youg; Gruber, Gerhard. "NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase." J. Bioenerg. Biomembr. 43, 187-193 (2011).
Assembly members:
entity, polymer, 69 residues, 7908.008 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MASAITALTPNQVNDELNKM
QAFIRKEAEEKAKEIQLKAD
QEYEIEKTNIVRNETNNIDG
NFKSKLKKA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 202 |
| 15N chemical shifts | 68 |
| 1H chemical shifts | 427 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E1-69 | 1 |
Entities:
Entity 1, E1-69 69 residues - 7908.008 Da.
| 1 | MET | ALA | SER | ALA | ILE | THR | ALA | LEU | THR | PRO | ||||
| 2 | ASN | GLN | VAL | ASN | ASP | GLU | LEU | ASN | LYS | MET | ||||
| 3 | GLN | ALA | PHE | ILE | ARG | LYS | GLU | ALA | GLU | GLU | ||||
| 4 | LYS | ALA | LYS | GLU | ILE | GLN | LEU | LYS | ALA | ASP | ||||
| 5 | GLN | GLU | TYR | GLU | ILE | GLU | LYS | THR | ASN | ILE | ||||
| 6 | VAL | ARG | ASN | GLU | THR | ASN | ASN | ILE | ASP | GLY | ||||
| 7 | ASN | PHE | LYS | SER | LYS | LEU | LYS | LYS | ALA |
Samples:
sample_1: protein, [U-100% 13C; U-100% 15N], 2 mM; Na2PO4 25 mM; NaCl 200 mM; EDTA 5 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
Molmol, Koradi, Billeter and Wuthrich - structure solution
SPARKY, Goddard - peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | GAA26638 |
| EMBL | CAA89978 CAA99654 CAY86613 |
| GB | AAA35209 AHY77605 AJP41835 AJT71258 AJT71746 |
| REF | NP_014977 |
| SP | P22203 |
| TPG | DAA11094 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts