BMRB Entry 50689
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50689
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Title: Chemical shift assignments of the Campylobacter jejuni helical cell shape determining protein Pgp2 in its apo form PubMed: 33711341
Deposition date: 2021-01-04 Original release date: 2021-07-27
Authors: Lin, Chang Sheng-Huei; McIntosh, Lawrence; Murphy, Michael
Citation: Lin, Chang Sheng-Huei; Chan, Anson; Vermeulen, Jenny; Brockerman, Jacob; Soni, Arvind; Tanner, Martin; Gaynor, Erin; Mclntosh, Lawrence; Simorre, Jean-Pierre; Murphy, Michael. "Peptidoglycan binding by a pocket on the accessory NTF2-domain of Pgp2 directs helical cell shape of Campylobacter jejuni" J. Biol. Chem. 296, 100528-100528 (2021).
Assembly members:
entity_1, polymer, 287 residues, 33604 Da.
Natural source: Common Name: Campylobacter jejuni Taxonomy ID: 197 Superkingdom: Bacteria Kingdom: not available Genus/species: Campylobacter jejuni
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15
Entity Sequences (FASTA):
entity_1: GSHMQKDFWLSEIGDKNISL
GYYDDNVAIVLTNKTDKILR
VYSYEDGKIRKDFEQKEIIT
GLMGDKKIEGDLKTPVGFYE
LGRKFNPGDPYYGPFAFATT
YPNLLDKVQGKTGGGIWIHG
YPLDGSRLDEFKTRGCIALF
NNNLEKFAQVVQDKKVFVMT
EEKEKIRAKKDQIASLLADL
FTWKLAWTNSDTNTYLSFYD
EQEFKRFDKMKFEQFASMKK
SIFSRKEDKKIKFSDINISP
YPNLENETMYRISFYEDYYT
KNYQFRGDKILYVKIDSKGK
MKILAEQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 755 |
| 15N chemical shifts | 242 |
| 1H chemical shifts | 242 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Apo-Pgp2 monomer | 1 |
Entities:
Entity 1, Apo-Pgp2 monomer 287 residues - 33604 Da.
Residues 1-4 represent a non-native affinity tag
| 1 | GLY | SER | HIS | MET | GLN | LYS | ASP | PHE | TRP | LEU | ||||
| 2 | SER | GLU | ILE | GLY | ASP | LYS | ASN | ILE | SER | LEU | ||||
| 3 | GLY | TYR | TYR | ASP | ASP | ASN | VAL | ALA | ILE | VAL | ||||
| 4 | LEU | THR | ASN | LYS | THR | ASP | LYS | ILE | LEU | ARG | ||||
| 5 | VAL | TYR | SER | TYR | GLU | ASP | GLY | LYS | ILE | ARG | ||||
| 6 | LYS | ASP | PHE | GLU | GLN | LYS | GLU | ILE | ILE | THR | ||||
| 7 | GLY | LEU | MET | GLY | ASP | LYS | LYS | ILE | GLU | GLY | ||||
| 8 | ASP | LEU | LYS | THR | PRO | VAL | GLY | PHE | TYR | GLU | ||||
| 9 | LEU | GLY | ARG | LYS | PHE | ASN | PRO | GLY | ASP | PRO | ||||
| 10 | TYR | TYR | GLY | PRO | PHE | ALA | PHE | ALA | THR | THR | ||||
| 11 | TYR | PRO | ASN | LEU | LEU | ASP | LYS | VAL | GLN | GLY | ||||
| 12 | LYS | THR | GLY | GLY | GLY | ILE | TRP | ILE | HIS | GLY | ||||
| 13 | TYR | PRO | LEU | ASP | GLY | SER | ARG | LEU | ASP | GLU | ||||
| 14 | PHE | LYS | THR | ARG | GLY | CYS | ILE | ALA | LEU | PHE | ||||
| 15 | ASN | ASN | ASN | LEU | GLU | LYS | PHE | ALA | GLN | VAL | ||||
| 16 | VAL | GLN | ASP | LYS | LYS | VAL | PHE | VAL | MET | THR | ||||
| 17 | GLU | GLU | LYS | GLU | LYS | ILE | ARG | ALA | LYS | LYS | ||||
| 18 | ASP | GLN | ILE | ALA | SER | LEU | LEU | ALA | ASP | LEU | ||||
| 19 | PHE | THR | TRP | LYS | LEU | ALA | TRP | THR | ASN | SER | ||||
| 20 | ASP | THR | ASN | THR | TYR | LEU | SER | PHE | TYR | ASP | ||||
| 21 | GLU | GLN | GLU | PHE | LYS | ARG | PHE | ASP | LYS | MET | ||||
| 22 | LYS | PHE | GLU | GLN | PHE | ALA | SER | MET | LYS | LYS | ||||
| 23 | SER | ILE | PHE | SER | ARG | LYS | GLU | ASP | LYS | LYS | ||||
| 24 | ILE | LYS | PHE | SER | ASP | ILE | ASN | ILE | SER | PRO | ||||
| 25 | TYR | PRO | ASN | LEU | GLU | ASN | GLU | THR | MET | TYR | ||||
| 26 | ARG | ILE | SER | PHE | TYR | GLU | ASP | TYR | TYR | THR | ||||
| 27 | LYS | ASN | TYR | GLN | PHE | ARG | GLY | ASP | LYS | ILE | ||||
| 28 | LEU | TYR | VAL | LYS | ILE | ASP | SER | LYS | GLY | LYS | ||||
| 29 | MET | LYS | ILE | LEU | ALA | GLU | GLN |
Samples:
sample_1: Pgp2, [U-13C; U-15N; U-2H with amide-1H], 350 uM; TRIS 50 mM; sodium chloride 150 mM; DTT 1 mM; H2O 95%; D2O, [U-100% 2H], 5%
sample_conditions_1: pH: 7; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
TOPSPIN v3.0 - collection
NMRFAM-SPARKY v1.413 - chemical shift assignment, data analysis, peak picking
PINE - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 850 MHz
Related Database Links:
| NCBI | EAQ72310 |
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts