BMRB Entry 52752
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52752
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Pizzolato-Cezar, Luis; Vitale, Phelipe; Liria, Cleber; Pineda, Mario; Lacerda, Caroline; Marana, Sandro; Nascimento, Andrey; Sassonia, Rogerio; Sgro, German; Salinas, Roberto; Machini, M Teresa. "Development of a Potent and Functional In Vivo Peptide Competitive Inhibitor for the Toxin MazF" J. Med. Chem. 68, 21665-21682 (2025).
PubMed: 41081386
Assembly members:
entity_1, polymer, 111 residues, Formula weight is not available
entity_2, polymer, 12 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: pETDuet-1
Entity Sequences (FASTA):
entity_1: MVSRYVPDMGDLIWVDFDPT
KGSAQAGHRPAVVLSPFMYN
NKTGMCLCVPCTTQSKGYPF
EVVLSGQERDGVALADQVKS
IAWRARGATKKGTVAPEELQ
LIKAKINVLIG
entity_2: XSHLFWAQFDEYFX
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 434 |
| 15N chemical shifts | 106 |
| 1H chemical shifts | 668 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MazF(E24A), chain 1 | 1 |
| 2 | MazF(E24A), chain 2 | 1 |
| 3 | SamF, chain 1 | 2 |
| 4 | SamF, chain 2 | 2 |
Entities:
Entity 1, MazF(E24A), chain 1 111 residues - Formula weight is not available
| 1 | MET | VAL | SER | ARG | TYR | VAL | PRO | ASP | MET | GLY | ||||
| 2 | ASP | LEU | ILE | TRP | VAL | ASP | PHE | ASP | PRO | THR | ||||
| 3 | LYS | GLY | SER | ALA | GLN | ALA | GLY | HIS | ARG | PRO | ||||
| 4 | ALA | VAL | VAL | LEU | SER | PRO | PHE | MET | TYR | ASN | ||||
| 5 | ASN | LYS | THR | GLY | MET | CYS | LEU | CYS | VAL | PRO | ||||
| 6 | CYS | THR | THR | GLN | SER | LYS | GLY | TYR | PRO | PHE | ||||
| 7 | GLU | VAL | VAL | LEU | SER | GLY | GLN | GLU | ARG | ASP | ||||
| 8 | GLY | VAL | ALA | LEU | ALA | ASP | GLN | VAL | LYS | SER | ||||
| 9 | ILE | ALA | TRP | ARG | ALA | ARG | GLY | ALA | THR | LYS | ||||
| 10 | LYS | GLY | THR | VAL | ALA | PRO | GLU | GLU | LEU | GLN | ||||
| 11 | LEU | ILE | LYS | ALA | LYS | ILE | ASN | VAL | LEU | ILE | ||||
| 12 | GLY |
Entity 2, SamF, chain 1 12 residues - Formula weight is not available
| 1 | ACE | SER | HIS | LEU | PHE | TRP | ALA | GLN | PHE | ASP | ||||
| 2 | GLU | TYR | PHE | NH2 |
Samples:
sample_1: MazF(E24A), [U-100% 15N] [U-100% 13C], 1 mM; SamF 2 mM; NaHPO4 20 mM; NaCl 100 mM; EDTA 0.5 mM; DTT 4 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(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 HBHANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 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:
NMRPipe - processing
CcpNMR v3 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Related Database Links:
| NCBI | P0AE70 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks