BMRB Entry 18770
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18770
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Title: TatA T22P PubMed: 23471988
Deposition date: 2012-10-08 Original release date: 2013-03-18
Authors: Rodriguez, Fernanda; Berks, Ben; Schnell, Jason
Citation: Rodriguez, Fernanda; Rouse, Sarah; Tait, Claudia; Harmer, Jeffrey; De Riso, Antonio; Timmel, Christiane; Sansom, Mark; Berks, Ben; Schnell, Jason. "Structural model for the protein-translocating element of the twin-arginine transport system." Proc. Natl. Acad. Sci. U.S.A. 110, E1092-E1101 (2013).
Assembly members:
TatA_T22P, polymer, 49 residues, 5177.260 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TatA_T22P: XGGISIWQLLIIAVIVVLLF
GPKKLGSIGSDLGASIKGFK
KAMSDDEPK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 144 |
| 15N chemical shifts | 48 |
| 1H chemical shifts | 339 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TatA_T22P | 1 |
Entities:
Entity 1, TatA_T22P 49 residues - 5177.260 Da.
| 1 | FME | GLY | GLY | ILE | SER | ILE | TRP | GLN | LEU | LEU | ||||
| 2 | ILE | ILE | ALA | VAL | ILE | VAL | VAL | LEU | LEU | PHE | ||||
| 3 | GLY | PRO | LYS | LYS | LEU | GLY | SER | ILE | GLY | SER | ||||
| 4 | ASP | LEU | GLY | ALA | SER | ILE | LYS | GLY | PHE | LYS | ||||
| 5 | LYS | ALA | MET | SER | ASP | ASP | GLU | PRO | LYS |
Samples:
N: TatA_T22P, [U-100% 15N], 0.5 mM; DPC 240 mM; H2O 95%; D2O 5%; sodium phosphate 0.05 M
NC: TatA_T22P, [U-100% 13C; U-100% 15N], 0.5 mM; DPC 240 mM; H2O 95%; D2O 5%; sodium phosphate 0.05 M
NC_deutDPC: TatA_T22P, [U-100% 13C; U-100% 15N], 0.5 mM; DPC, [U-100% 2H], 240 mM; H2O 95%; D2O 5%; sodium phosphate 0.05 M
sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | N | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | N | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | NC_deutDPC | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | NC_deutDPC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | anisotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Homebuilt OMEGA 950 MHz
- Homebuilt OMEGA 600 MHz
- Homebuilt OMEGA 750 MHz
- Bruker AVII 500 MHz
Related Database Links:
| BMRB | 18771 19714 19881 |
| PDB | |
| DBJ | BAB38189 BAE77465 BAG79648 BAI27909 BAI33032 |
| EMBL | CAA06724 CAP78301 CAQ34195 CAQ91106 CAR00812 |
| GB | AAA67633 AAC19240 AAC76839 AAG59032 AAN45349 |
| PIR | D86071 |
| REF | NP_312793 NP_418280 NP_709642 WP_000508966 WP_000508967 |
| SP | P69428 P69429 P69430 P69431 |
Download simulated HSQC data in one of the following formats:
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