BMRB Entry 15870
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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/BMR15870
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Title: The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47 PubMed: 19580766
Deposition date: 2008-07-09 Original release date: 2009-07-10
Authors: Biukovic, Goran; Gayen, Shovanlal; Pervushin, Konstantin; Gruber, Gerhard
Citation: Biukovic, Goran; Gayen, Shovanlal; Pervushin, Konstantin; Gruber, Gerhard. "Domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H(1-47)." Biophys. J. 97, 286-294 (2009).
Assembly members:
H1-47_subunit_A_ATP_synthase, polymer, 47 residues, 5208.114 Da.
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: E. coli
Entity Sequences (FASTA):
H1-47_subunit_A_ATP_synthase: MGVSVMEAIKEVKLAEEQAV
KEIEEAKNRAEQIKAEAIEE
AKKLIAC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 160 |
| 15N chemical shifts | 49 |
| 1H chemical shifts | 340 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | H1-47_subunit_A_ATP_synthase | 1 |
Entities:
Entity 1, H1-47_subunit_A_ATP_synthase 47 residues - 5208.114 Da.
| 1 | MET | GLY | VAL | SER | VAL | MET | GLU | ALA | ILE | LYS | ||||
| 2 | GLU | VAL | LYS | LEU | ALA | GLU | GLU | GLN | ALA | VAL | ||||
| 3 | LYS | GLU | ILE | GLU | GLU | ALA | LYS | ASN | ARG | ALA | ||||
| 4 | GLU | GLN | ILE | LYS | ALA | GLU | ALA | ILE | GLU | GLU | ||||
| 5 | ALA | LYS | LYS | LEU | ILE | ALA | CYS |
Samples:
sample_1: H1-47 subunit A ATP synthase, [U-99% 13C; U-99% 15N], 0.5 - 1 mM; sodium azide 0.1%; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.113, Goddard - chemical shift assignment, peak picking
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN v1.3, Bruker Biospin - collection, processing
TALOS, Cornilescu, Delaglio and Bax - torsional angle calculation
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