BMRB Entry 50314
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50314
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Title: FtsZ CTD (317-383) PubMed: 35481648
Deposition date: 2020-06-10 Original release date: 2022-04-13
Authors: Perdikari, Theodora Myrto; Murthy, Anastasia; Chua, Xien; Xuan, Botai; Mathews, Kaylee; Fawzi, Nicolas; Camberg, Jodi
Citation: Viola, Marissa; Perdikari, Theodora; Trebino, Catherine; Rahmani, Negar; Mathews, Kaylee; Pena, Carolina; Chua, XienYu; Xuan, Botai; LaBreck, Christopher; Fawzi, Nicolas; Camberg, Jodi. "An enhancer sequence in the intrinsically disordered region of FtsZ promotes polymer-guided substrate processing by ClpXP protease" Protein Sci. 31, e4306-e4306 (2022).
Assembly members:
entity_1, polymer, 68 residues, Formula weight is not available
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 Vector: pET_6xHis_GFP_TEV_FtsZ_CTD
Entity Sequences (FASTA):
entity_1: GMDKRPEITLVTNKQVQQPV
MDRYQQHGMAPLTQEQKPVA
KVVNDNAPQTAKEPDYLDIP
AFLRKQAD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 200 |
| 15N chemical shifts | 58 |
| 1H chemical shifts | 58 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | E. Coli FtsZ | 1 |
Entities:
Entity 1, E. Coli FtsZ 68 residues - Formula weight is not available
| 1 | GLY | MET | ASP | LYS | ARG | PRO | GLU | ILE | THR | LEU | ||||
| 2 | VAL | THR | ASN | LYS | GLN | VAL | GLN | GLN | PRO | VAL | ||||
| 3 | MET | ASP | ARG | TYR | GLN | GLN | HIS | GLY | MET | ALA | ||||
| 4 | PRO | LEU | THR | GLN | GLU | GLN | LYS | PRO | VAL | ALA | ||||
| 5 | LYS | VAL | VAL | ASN | ASP | ASN | ALA | PRO | GLN | THR | ||||
| 6 | ALA | LYS | GLU | PRO | ASP | TYR | LEU | ASP | ILE | PRO | ||||
| 7 | ALA | PHE | LEU | ARG | LYS | GLN | ALA | ASP |
Samples:
sample_1: E. coli FtsZ CTD, [U-13C; U-15N], 163 uM; MES 50 mM; KCl 100 mM; MgCl2 10 mM
sample_conditions_1: ionic strength: 110 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker Avance 850 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts