BMRB Entry 51502
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51502
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 13C, and 15N chemical shift assignments of MqsR in complex with its canonical antitoxin MqsA (Residues 1-76) PubMed: 36162504
Deposition date: 2022-06-21 Original release date: 2022-10-31
Authors: Yu, Victor; Ronzone, Erik; Peti, Wolfgang; Page, Rebecca
Citation: Yu, Victor; Ronzone, Eric; Lord, Dana; Peti, Wolfgang; Page, Rebecca. "MqsR is a noncanonical microbial RNase toxin that is inhibited by antitoxin MqsA via steric blockage of substrate binding" J. Biol. Chem. 298, 102535-102535 (2022).
Assembly members:
entity_1, polymer, 98 residues, Formula weight is not available
entity_2, polymer, 86 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: pET30a
Entity Sequences (FASTA):
entity_1: MEKRTPHTRLSQVKKLVNAG
QVRTTRSALLNADELGLDFD
GMCNVIIGLSESDFYKSMTT
YSDHTIWQDVYRPRLVTGQV
YLKITVIHDVLIVSFKEK
entity_2: MAHHHHHHAAMKCPVCHQGE
MVSGIKDIPYTFRGRKTVLK
GIHGLYCVHCEESIMNKEES
DAFMAQVKAFRASVNAETVA
PEFIVK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 88 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 88 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MqsR | 1 |
| 2 | MqsA | 2 |
Entities:
Entity 1, MqsR 98 residues - Formula weight is not available
| 1 | MET | GLU | LYS | ARG | THR | PRO | HIS | THR | ARG | LEU | ||||
| 2 | SER | GLN | VAL | LYS | LYS | LEU | VAL | ASN | ALA | GLY | ||||
| 3 | GLN | VAL | ARG | THR | THR | ARG | SER | ALA | LEU | LEU | ||||
| 4 | ASN | ALA | ASP | GLU | LEU | GLY | LEU | ASP | PHE | ASP | ||||
| 5 | GLY | MET | CYS | ASN | VAL | ILE | ILE | GLY | LEU | SER | ||||
| 6 | GLU | SER | ASP | PHE | TYR | LYS | SER | MET | THR | THR | ||||
| 7 | TYR | SER | ASP | HIS | THR | ILE | TRP | GLN | ASP | VAL | ||||
| 8 | TYR | ARG | PRO | ARG | LEU | VAL | THR | GLY | GLN | VAL | ||||
| 9 | TYR | LEU | LYS | ILE | THR | VAL | ILE | HIS | ASP | VAL | ||||
| 10 | LEU | ILE | VAL | SER | PHE | LYS | GLU | LYS |
Entity 2, MqsA 86 residues - Formula weight is not available
MAHHHHHHAA purification tag and cloning artifact
| 1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | ALA | ALA | ||||
| 2 | MET | LYS | CYS | PRO | VAL | CYS | HIS | GLN | GLY | GLU | ||||
| 3 | MET | VAL | SER | GLY | ILE | LYS | ASP | ILE | PRO | TYR | ||||
| 4 | THR | PHE | ARG | GLY | ARG | LYS | THR | VAL | LEU | LYS | ||||
| 5 | GLY | ILE | HIS | GLY | LEU | TYR | CYS | VAL | HIS | CYS | ||||
| 6 | GLU | GLU | SER | ILE | MET | ASN | LYS | GLU | GLU | SER | ||||
| 7 | ASP | ALA | PHE | MET | ALA | GLN | VAL | LYS | ALA | PHE | ||||
| 8 | ARG | ALA | SER | VAL | ASN | ALA | GLU | THR | VAL | ALA | ||||
| 9 | PRO | GLU | PHE | ILE | VAL | LYS |
Samples:
sample_1: sodium chloride 50 mM; sodium phosphate 20 mM; TCEP 0.5 mM; MqsR, [U-99% 13C; U-99% 15N], 150 uM; MqsA 150 uM
sample_conditions_1: ionic strength: 50 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.9 - chemical shift assignment
TOPSPIN v4.1.1 - collection, processing
NMR spectrometers:
- Bruker Avance 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts