BMRB Entry 52317
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52317
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Title: 1H, 13C, and 15N backbone resonance assignments of E. coli Peptide Deformylase (1-147) bound to 2-(5-bromo-1H-indol-3-yl)-N-hydroxyacetamide PubMed: 38574272
Deposition date: 2024-02-09 Original release date: 2024-07-22
Authors: Kirschner, Hendrik; Heister, Nicole; Stoll, Raphael
Citation: Kirschner, Hendrik; Heister, Nicole; Zouatom, Manuela; Zhou, Tianyi; Hofmann, Eckhard; Scherkenbeck, Jurgen; Stoll, Raphael. "Toward More Selective Antibiotic Inhibitors: A Structural View of the Complexed Binding Pocket of E. coli Peptide Deformylase" J. Med. Chem. 67, 6384-6396 (2024).
Assembly members:
entity_1, polymer, 150 residues, Formula weight is not available
entity_BB4, non-polymer, 269.095 Da.
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: modified pET19
Entity Sequences (FASTA):
entity_1: GHMSVLQVLHIPDERLRKVA
KPVEEVNAEIQRIVDDMFET
MYAEEGIGLAATQVDIHQRI
IVIDVSENRDERLVLINPEL
LEKSGETGIEEGCLSIPEQR
ALVPRAEKVKIRALDRDGKP
FELEADGLLAICIQHEMDHL
VGKLFMDYLS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 425 |
15N chemical shifts | 116 |
1H chemical shifts | 116 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Peptide Deformylase | 1 |
2 | ligand, BB4 | 2 |
Entities:
Entity 1, Peptide Deformylase 150 residues - Formula weight is not available
1 | GLY | HIS | MET | SER | VAL | LEU | GLN | VAL | LEU | HIS | |
2 | ILE | PRO | ASP | GLU | ARG | LEU | ARG | LYS | VAL | ALA | |
3 | LYS | PRO | VAL | GLU | GLU | VAL | ASN | ALA | GLU | ILE | |
4 | GLN | ARG | ILE | VAL | ASP | ASP | MET | PHE | GLU | THR | |
5 | MET | TYR | ALA | GLU | GLU | GLY | ILE | GLY | LEU | ALA | |
6 | ALA | THR | GLN | VAL | ASP | ILE | HIS | GLN | ARG | ILE | |
7 | ILE | VAL | ILE | ASP | VAL | SER | GLU | ASN | ARG | ASP | |
8 | GLU | ARG | LEU | VAL | LEU | ILE | ASN | PRO | GLU | LEU | |
9 | LEU | GLU | LYS | SER | GLY | GLU | THR | GLY | ILE | GLU | |
10 | GLU | GLY | CYS | LEU | SER | ILE | PRO | GLU | GLN | ARG | |
11 | ALA | LEU | VAL | PRO | ARG | ALA | GLU | LYS | VAL | LYS | |
12 | ILE | ARG | ALA | LEU | ASP | ARG | ASP | GLY | LYS | PRO | |
13 | PHE | GLU | LEU | GLU | ALA | ASP | GLY | LEU | LEU | ALA | |
14 | ILE | CYS | ILE | GLN | HIS | GLU | MET | ASP | HIS | LEU | |
15 | VAL | GLY | LYS | LEU | PHE | MET | ASP | TYR | LEU | SER |
Entity 2, ligand, BB4 - C10 H9 Br N2 O2 - 269.095 Da.
1 | BB4 |
Samples:
sample_1: Peptide Deformylase, [U-15N], 0.45 mM; Peptide Deformylase, [U-13C; U-15N], 0.45 mM; KH2PO4 20 mM
sample_conditions_1: ionic strength: 0.052 M; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
1D 1H | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
1D 1H | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C 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 HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.5.2 - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts