BMRB Entry 50088
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR50088
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Title: Structure and function of the bacterial toxin phenomycin PubMed: 32220302
Deposition date: 2019-11-14 Original release date: 2020-01-10
Authors: Nielsen, Jakob
Citation: Hansen, Bente; Larsen, Camilla; Nielsen, Jakob; Svenningsen, Esben; Van, Lan; Jacobsen, Kristian; Bjerring, Morten; Flygaard, Rasmus; Jenner, Lasse; Nejsum, Lene; Brodersen, Ditlev; Mulder, Frans; Tyrring, Thomas; Poulsen, Thomas. "Structure and Function of the Bacterial Protein Toxin Phenomycin" Structure 28, 528-539 (2020).
Assembly members:
Phenomycin, polymer, 93 residues, Formula weight is not available
Natural source: Common Name: Streptomyces fervens MA 564-Cl Taxonomy ID: 66429 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces fervens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Phenomycin: NPKTIKAAAYNQARSTLADA
GSRTAAKSHPIHGKTDVPVS
YGTSLLAAARDEFRQADKKL
PAKDKKSDMSIAHYNAVHSA
AKTMGIDTW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 389 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 619 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Phenomycin | 1 |
Entities:
Entity 1, Phenomycin 93 residues - Formula weight is not available
| 1 | GLY | ALA | MET | ALA | ASN | PRO | LYS | THR | ILE | LYS | ||||
| 2 | ALA | ALA | ALA | TYR | ASN | GLN | ALA | ARG | SER | THR | ||||
| 3 | LEU | ALA | ASP | ALA | GLY | SER | ARG | THR | ALA | ALA | ||||
| 4 | LYS | SER | HIS | PRO | ILE | HIS | GLY | LYS | THR | ASP | ||||
| 5 | VAL | PRO | VAL | SER | TYR | GLY | THR | SER | LEU | LEU | ||||
| 6 | ALA | ALA | ALA | ARG | ASP | GLU | PHE | ARG | GLN | ALA | ||||
| 7 | ASP | LYS | LYS | LEU | PRO | ALA | LYS | ASP | LYS | LYS | ||||
| 8 | SER | ASP | MET | SER | ILE | ALA | HIS | TYR | ASN | ALA | ||||
| 9 | VAL | HIS | SER | ALA | ALA | LYS | THR | MET | GLY | ILE | ||||
| 10 | ASP | THR | TRP |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 1-2 mM; potassium phosphate 10 mM
sample_conditions_1: ionic strength: 10 mM; pH: 3.25; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | 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:
SPARKY, Goddard - peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 950 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts