BMRB Entry 27397
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27397
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Title: 1H, 13C, 15N Chemical shift assignment for the TolAIII-TolB-peptide complex.
Deposition date: 2018-02-07 Original release date: 2020-03-16
Authors: Redfield, Christina; Holmes, Peter; Rajasekar, Karthik; Kleanthous, Colin
Citation: Holmes, Peter; Rajasekar, Karthik; Rassam, Patrice; Cassels, Eoin; Redfield, Christina; Kleanthous, Colin. "Structure of the TolA-TolB complex suggests 'Pal-uncapping' is the primary role of the Tol-Pal system in bacteria" Not known ., .-..
Assembly members:
TolAIII, polymer, 124 residues, Formula weight is not available
TolBp, polymer, 13 residues, Formula weight is not available
Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
TolAIII: HMRALAELLSDTTERQQALA
DEVGSEVTGSLDDLIVNLVS
QQWRRPPSARNGMSVEVLIE
MLPDGTITNASVSRSSGDKP
FDSSAVAAVRNVGRIPEMQQ
LPRATFDSLYRQRRIIFKPE
DLSL
TolBp: ADPLVISSGNDRA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 523 |
| 15N chemical shifts | 140 |
| 1H chemical shifts | 891 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | TolAIII | 1 |
| 2 | TolBp | 2 |
Entities:
Entity 1, TolAIII 124 residues - Formula weight is not available
This is the 3rd domain of TolA
| 1 | HIS | MET | ARG | ALA | LEU | ALA | GLU | LEU | LEU | SER | ||||
| 2 | ASP | THR | THR | GLU | ARG | GLN | GLN | ALA | LEU | ALA | ||||
| 3 | ASP | GLU | VAL | GLY | SER | GLU | VAL | THR | GLY | SER | ||||
| 4 | LEU | ASP | ASP | LEU | ILE | VAL | ASN | LEU | VAL | SER | ||||
| 5 | GLN | GLN | TRP | ARG | ARG | PRO | PRO | SER | ALA | ARG | ||||
| 6 | ASN | GLY | MET | SER | VAL | GLU | VAL | LEU | ILE | GLU | ||||
| 7 | MET | LEU | PRO | ASP | GLY | THR | ILE | THR | ASN | ALA | ||||
| 8 | SER | VAL | SER | ARG | SER | SER | GLY | ASP | LYS | PRO | ||||
| 9 | PHE | ASP | SER | SER | ALA | VAL | ALA | ALA | VAL | ARG | ||||
| 10 | ASN | VAL | GLY | ARG | ILE | PRO | GLU | MET | GLN | GLN | ||||
| 11 | LEU | PRO | ARG | ALA | THR | PHE | ASP | SER | LEU | TYR | ||||
| 12 | ARG | GLN | ARG | ARG | ILE | ILE | PHE | LYS | PRO | GLU | ||||
| 13 | ASP | LEU | SER | LEU |
Entity 2, TolBp 13 residues - Formula weight is not available
| 1 | ALA | ASP | PRO | LEU | VAL | ILE | SER | SER | GLY | ASN | ||||
| 2 | ASP | ARG | ALA |
Samples:
sample_1: TolAIII, [U-98% 15N], 0.6 ± 0.05 mM; TolBp 3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM
sample_2: TolAIII, [U-98% 13C; U-98% 15N], 0.6 ± 0.05 mM; TolBp 3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM
sample_3: TolAIII 1.1 ± 0.05 mM; TolBp, [U-98% 13C; U-98% 15N], 0.2 ± 0.02 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM
sample_4: TolAIII, [U-98% 13C; U-98% 15N], 0.6 ± 0.05 mM; TolBp 3 ± 0.1 mM; sodium phosphate 20 ± 0.5 mM; sodium chloride 60 ± 0.5 mM
sample_conditions_1: ionic strength: 140 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 2D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 2D HBHA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 2D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 2D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Analysis v2.3, CCPN - chemical shift assignment, peak picking
ARIA, Linge, O'Donoghue and Nilges - structure solution
NMR spectrometers:
- Bruker Avance 500 MHz
- Home-built OMEGA 750 MHz
- Home-built OMEGA 950 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts