BMRB Entry 28040
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28040
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Title: Backbone and CB Chemical Shift Assignments of the Methanocaldococcus jannaschii Spt5-KOW domain PubMed: 36255050
Deposition date: 2019-11-11 Original release date: 2023-01-09
Authors: Zuber, Philipp; Schweimer, Kristian; Knauer, Stefan
Citation: Zuber, Philipp; Daviter, Tina; Heissmann, Ramona; Persau, Ulrike; Schweimer, Kristian; Knauer, Stefan. "Structural and thermodynamic analyses of the beta-to-alpha transformation in RfaH reveal principles of fold-switching proteins" Elife 11, e76630-e76630 (2022).
Assembly members:
MjSpt5-KOW, polymer, 69 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: 2190 Superkingdom: Archaea Kingdom: not available Genus/species: Methanocaldococcus jannaschii
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETGb1a
Entity Sequences (FASTA):
MjSpt5-KOW: GAMGKKIIENIEKGDVVEII
AGPFKGERAKVIRVDKHKEE
VTLELENAAVPIPITLPVEG
VKIVSKHKD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 189 |
| 15N chemical shifts | 62 |
| 1H chemical shifts | 62 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MjSpt5-KOW | 1 |
Entities:
Entity 1, MjSpt5-KOW 69 residues - Formula weight is not available
Residues 1-4 result from an engineered TEV-protease cleavage site; residues 5-69 correspond to residues 83-147 of MjSpt5
| 1 | GLY | ALA | MET | GLY | LYS | LYS | ILE | ILE | GLU | ASN | ||||
| 2 | ILE | GLU | LYS | GLY | ASP | VAL | VAL | GLU | ILE | ILE | ||||
| 3 | ALA | GLY | PRO | PHE | LYS | GLY | GLU | ARG | ALA | LYS | ||||
| 4 | VAL | ILE | ARG | VAL | ASP | LYS | HIS | LYS | GLU | GLU | ||||
| 5 | VAL | THR | LEU | GLU | LEU | GLU | ASN | ALA | ALA | VAL | ||||
| 6 | PRO | ILE | PRO | ILE | THR | LEU | PRO | VAL | GLU | GLY | ||||
| 7 | VAL | LYS | ILE | VAL | SER | LYS | HIS | LYS | ASP |
Samples:
sample_1: MjSpt5-KOW, [U-99% 13C; U-99% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 100 mM; EDTA 1 mM
sample_conditions_1: ionic strength: 0.139 M; pH: 6.5; 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 ctHSQC | 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 HN(CO)CACB | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN vv3.5 pl5, Bruker Biospin - collection
NMRViewJ vv9.2.0-b2, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Ascend Aeon 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts