BMRB Entry 16247
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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/BMR16247
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Title: NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase PubMed: 19820091
Deposition date: 2009-04-08 Original release date: 2009-10-16
Authors: Priya, Ragunathan; Biukovic, Goran; Gayen, Shovanlal; Vivekanandan, Subramanian; Gruber, Gerhard
Citation: Priya, Ragunathan; Biukovic, Goran; Gayen, Shovanlal; Vivekanandan, Subramanian; Gruber, Gerhard. "Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase." J. Bacteriol. 191, 7538-7544 (2009).
Assembly members:
subunit_b_30-82, polymer, 53 residues, 5785.686 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
subunit_b_30-82: MAAIEKRQKEIADGLASAER
AHKDLDLAKASATDQLKKAK
AEAQVIIEQANKR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 210 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 326 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit b 30-82 | 1 |
Entities:
Entity 1, subunit b 30-82 53 residues - 5785.686 Da.
| 1 | MET | ALA | ALA | ILE | GLU | LYS | ARG | GLN | LYS | GLU | ||||
| 2 | ILE | ALA | ASP | GLY | LEU | ALA | SER | ALA | GLU | ARG | ||||
| 3 | ALA | HIS | LYS | ASP | LEU | ASP | LEU | ALA | LYS | ALA | ||||
| 4 | SER | ALA | THR | ASP | GLN | LEU | LYS | LYS | ALA | LYS | ||||
| 5 | ALA | GLU | ALA | GLN | VAL | ILE | ILE | GLU | GLN | ALA | ||||
| 6 | ASN | LYS | ARG |
Samples:
sample_1: subunit b 30-82, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; NaH2PO4 25 mM; Na2HPO4 25 mM; NaN3 0.1%
sample_conditions_1: ionic strength: 0 mM; pH: 6.8; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 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 HNCO | 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 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
SPARKY, Goddard - chemical shift assignment
TOPSPIN v1.3, Bruker Biospin - processing
Molmol, Koradi, Billeter and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB38101 BAE77552 BAG79550 BAI28000 BAI33123 |
| EMBL | CAA23516 CAA23523 CAA25778 CAD03126 CAP78194 |
| GB | AAA24733 AAA24741 AAA62088 AAA83871 AAC76759 |
| PIR | AB0954 |
| REF | NP_312705 NP_418192 NP_458074 NP_462768 NP_709549 |
| SP | A7ZTU8 A8A6J9 A8ACP2 A9MJR5 A9MXB0 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts