BMRB Entry 31097
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31097
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Title: Solution NMR structure of a RiPP proteusin precursor protein
Deposition date: 2023-06-28 Original release date: 2024-02-08
Authors: McShan, A.; Vinayak, A.; Nguyen, N.
Citation: McShan, A.; Vinayak, A.; Nguyen, N.. "Solution NMR structure of a RiPP proteusin precursor protein" .
Assembly members:
entity_1, polymer, 91 residues, 9677.898 Da.
Natural source: Common Name: Methylovulum psychrotolerans Taxonomy ID: 1704499 Superkingdom: Bacteria Kingdom: not available Genus/species: Methylovulum psychrotolerans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: GSHMMNEEQTQQYSQIVAKC
WADAEFKAKLIADPKATLAA
ESIAVPDGIELRVLENTATV
VNLVLPPPPAEGELSDEDLG
AVTGGLTVLPW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 173 |
| 15N chemical shifts | 60 |
| 1H chemical shifts | 60 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 91 residues - 9677.898 Da.
| 1 | GLY | SER | HIS | MET | MET | ASN | GLU | GLU | GLN | THR | ||||
| 2 | GLN | GLN | TYR | SER | GLN | ILE | VAL | ALA | LYS | CYS | ||||
| 3 | TRP | ALA | ASP | ALA | GLU | PHE | LYS | ALA | LYS | LEU | ||||
| 4 | ILE | ALA | ASP | PRO | LYS | ALA | THR | LEU | ALA | ALA | ||||
| 5 | GLU | SER | ILE | ALA | VAL | PRO | ASP | GLY | ILE | GLU | ||||
| 6 | LEU | ARG | VAL | LEU | GLU | ASN | THR | ALA | THR | VAL | ||||
| 7 | VAL | ASN | LEU | VAL | LEU | PRO | PRO | PRO | PRO | ALA | ||||
| 8 | GLU | GLY | GLU | LEU | SER | ASP | GLU | ASP | LEU | GLY | ||||
| 9 | ALA | VAL | THR | GLY | GLY | LEU | THR | VAL | LEU | PRO | ||||
| 10 | TRP |
Samples:
sample_1: MprE7-TH1, [U-100% 13C; U-100% 15N], 0.4 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
Sparky, Goddard - chemical shift assignment
CS-ROSETTA, Shen, Vernon, Baker and Bax - structure calculation
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Bruker AVIIIHD-800 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts