BMRB Entry 15988
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15988
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Title: TonB2 PROTEIN FROM Vibrio anguillarum PubMed: 18973471
Deposition date: 2008-10-15 Original release date: 2009-02-09
Authors: Lopez, Claudia; Peacock, Sean; Crosa, Jorge; Vogel, Hans
Citation: Lopez, Claudia; Peacock, Sean; Crosa, Jorge; Vogel, Hans. "MOLECULAR CHARACTERIZATION OF THE TonB2 PROTEIN FROM Vibrio anguillarum" Biochem. J. 418, 49-59 (2009).
Assembly members:
TonB2-CTD, polymer, 106 residues, Formula weight is not available
Natural source: Common Name: Listonella Anguillarum Taxonomy ID: 55601 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio Anguillarum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TonB2-CTD: AHPFTSAPTFGDFGSNQQAM
PLYRVEPVYPSRALKRGVEG
FVTLSFTIDTTGKAVDINVV
DANPKRMFEREAMQALKKWK
YQPQIVDGKAIEQPGQTVTV
EFKIAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 279 |
| 15N chemical shifts | 100 |
| 1H chemical shifts | 636 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TonB-CTD | 1 |
Entities:
Entity 1, TonB-CTD 106 residues - Formula weight is not available
Residues 101-105 are leftover residues of the cleavage product of the expressed protein construct
| 1 | ALA | HIS | PRO | PHE | THR | SER | ALA | PRO | THR | PHE | ||||
| 2 | GLY | ASP | PHE | GLY | SER | ASN | GLN | GLN | ALA | MET | ||||
| 3 | PRO | LEU | TYR | ARG | VAL | GLU | PRO | VAL | TYR | PRO | ||||
| 4 | SER | ARG | ALA | LEU | LYS | ARG | GLY | VAL | GLU | GLY | ||||
| 5 | PHE | VAL | THR | LEU | SER | PHE | THR | ILE | ASP | THR | ||||
| 6 | THR | GLY | LYS | ALA | VAL | ASP | ILE | ASN | VAL | VAL | ||||
| 7 | ASP | ALA | ASN | PRO | LYS | ARG | MET | PHE | GLU | ARG | ||||
| 8 | GLU | ALA | MET | GLN | ALA | LEU | LYS | LYS | TRP | LYS | ||||
| 9 | TYR | GLN | PRO | GLN | ILE | VAL | ASP | GLY | LYS | ALA | ||||
| 10 | ILE | GLU | GLN | PRO | GLY | GLN | THR | VAL | THR | VAL | ||||
| 11 | GLU | PHE | LYS | ILE | ALA | LYS |
Samples:
sample_1: TonB2-CTD, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 90%; DSS 1 mM; H2O 10 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v102.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts