BMRB Entry 16354
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16354
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Title: NMR solution structure of the N terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii PubMed: 19760172
Deposition date: 2009-06-16 Original release date: 2009-09-29
Authors: Gayen, Shovanlal; Balakrishna, Asha; Gruber, Gerhard
Citation: Gayen, Shovanlal; Balakrishna, Asha; Gruber, Gerhard. "NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii." J. Bioenerg. Biomembr. 41, 343-348 (2009).
Assembly members:
E(1-52), polymer, 52 residues, Formula weight is not available
Natural source: Common Name: Methanococcus jannaschii Taxonomy ID: 2190 Superkingdom: Archaea Kingdom: not available Genus/species: Methanococcus jannaschii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
E(1-52): MAVKLMGVDKIKSKILDDAK
AEANKIISEAEAEKAKILEK
AKEEAEKRKAEI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 155 |
| 15N chemical shifts | 52 |
| 1H chemical shifts | 377 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E subunit | 1 |
Entities:
Entity 1, E subunit 52 residues - Formula weight is not available
| 1 | MET | ALA | VAL | LYS | LEU | MET | GLY | VAL | ASP | LYS | ||||
| 2 | ILE | LYS | SER | LYS | ILE | LEU | ASP | ASP | ALA | LYS | ||||
| 3 | ALA | GLU | ALA | ASN | LYS | ILE | ILE | SER | GLU | ALA | ||||
| 4 | GLU | ALA | GLU | LYS | ALA | LYS | ILE | LEU | GLU | LYS | ||||
| 5 | ALA | LYS | GLU | GLU | ALA | GLU | LYS | ARG | LYS | ALA | ||||
| 6 | GLU | ILE |
Samples:
sample_1: sodium phosphate 25 mM; D2O 10%; sodium azide 0.1 mM; TFE 60%; H2O 90%
sample_conditions_1: ionic strength: 0 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
TOPSPIN v2.1, Bruker Biospin - collection
Molmol, Koradi, Billeter and Wuthrich - structure solution
SPARKY, Goddard - chemical shift assignment
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