BMRB Entry 34341
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34341
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NMR-STAR v3 text file.
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Title: Structural investigation of the TasA anchoring protein TapA from Bacillus subtilis PubMed: 37068239
Deposition date: 2018-12-20 Original release date: 2020-01-24
Authors: Higman, V.; Schmieder, P.; Diehl, A.; Oschkinat, H.
Citation: Roske, Yvette; Lindemann, Florian; Diehl, Anne; Cremer, Nils; Higman, Victoria; Schlegel, Brigitte; Leidert, Martina; Driller, Kristina; Turgay, Kursad; Schmieder, Peter; Heinemann, Udo; Oschkinat, Hartmut. "TapA acts as specific chaperone in TasA filament formation by strand complementation" Proc. Natl. Acad. Sci. U.S.A. 120, e2217070120-e2217070120 (2023).
Assembly members:
entity_1, polymer, 147 residues, 17010.301 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: AFHDIETFDVSLQTCKDFQH
TDKNCHYDKRWDQSDLHISD
QTDTKGTVCSPFALFAVLEN
TGEKLKKSKWKWELHKLENA
RKPLKDGNVIEKGFVSNQIG
DSLYKIETKKKMKPGIYAFK
VYKPAGYPANGSTFEWSEPM
RLAKCDE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 522 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 804 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 147 residues - 17010.301 Da.
| 1 | ALA | PHE | HIS | ASP | ILE | GLU | THR | PHE | ASP | VAL | ||||
| 2 | SER | LEU | GLN | THR | CYS | LYS | ASP | PHE | GLN | HIS | ||||
| 3 | THR | ASP | LYS | ASN | CYS | HIS | TYR | ASP | LYS | ARG | ||||
| 4 | TRP | ASP | GLN | SER | ASP | LEU | HIS | ILE | SER | ASP | ||||
| 5 | GLN | THR | ASP | THR | LYS | GLY | THR | VAL | CYS | SER | ||||
| 6 | PRO | PHE | ALA | LEU | PHE | ALA | VAL | LEU | GLU | ASN | ||||
| 7 | THR | GLY | GLU | LYS | LEU | LYS | LYS | SER | LYS | TRP | ||||
| 8 | LYS | TRP | GLU | LEU | HIS | LYS | LEU | GLU | ASN | ALA | ||||
| 9 | ARG | LYS | PRO | LEU | LYS | ASP | GLY | ASN | VAL | ILE | ||||
| 10 | GLU | LYS | GLY | PHE | VAL | SER | ASN | GLN | ILE | GLY | ||||
| 11 | ASP | SER | LEU | TYR | LYS | ILE | GLU | THR | LYS | LYS | ||||
| 12 | LYS | MET | LYS | PRO | GLY | ILE | TYR | ALA | PHE | LYS | ||||
| 13 | VAL | TYR | LYS | PRO | ALA | GLY | TYR | PRO | ALA | ASN | ||||
| 14 | GLY | SER | THR | PHE | GLU | TRP | SER | GLU | PRO | MET | ||||
| 15 | ARG | LEU | ALA | LYS | CYS | ASP | GLU |
Samples:
sample_1: TasA anchoring/assembly protein, [U-99% 15N], 1 mM; sodium chloride 50 mM; potassium phosphate 20 mM
sample_2: TasA anchoring/assembly protein, [U-99% 13C; U-99% 15N], 0.54 mM; sodium chloride 50 mM; potassium phosphate 20 mM
sample_conditions_1: ionic strength: 76 mM; pH: 7; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - collection, processing
CcpNmr Analysis, CCPN - chemical shift assignment, peak picking
ARIA, Linge, O'Donoghue and Nilges - structure calculation
NMR spectrometers:
- Bruker AVANCE 750 MHz
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts