BMRB Entry 51429
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51429
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Title: Full-length Variant 5 (CTD only) PubMed: 35778397
Deposition date: 2022-05-06 Original release date: 2022-05-16
Authors: Porter, Lauren; Starich, Mary
Citation: Porter, Lauren; Kim, Allen; Rimal, Swechha; Looger, Loren; Majumdar, Ananya; Mensh, Brett; Starich, Mary; Strub, Marie-Paule. "Many dissimilar NusG protein domains switch between alpha-helix and beta-sheet folds" Nat. Commun. 13, 3802-3802 (2022).
Assembly members:
entity_1, polymer, 64 residues, Formula weight is not available
Natural source: Common Name: Calditerrivibrio nitroreducens Taxonomy ID: 477976 Superkingdom: Bacteria Kingdom: not available Genus/species: Calditerrivibrio nitroreducens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pPAL7
Entity Sequences (FASTA):
entity_1: FIDTKSEEFKKGDTILIKDG
PFKDFVGIFQEELDSKGRVS
ILLKTLALQPRITVDKDMIE
KLHN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 128 |
| 15N chemical shifts | 45 |
| 1H chemical shifts | 45 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Variant 5 full-length (CTD only) | 1 |
Entities:
Entity 1, Variant 5 full-length (CTD only) 64 residues - Formula weight is not available
| 1 | PHE | ILE | ASP | THR | LYS | SER | GLU | GLU | PHE | LYS | ||||
| 2 | LYS | GLY | ASP | THR | ILE | LEU | ILE | LYS | ASP | GLY | ||||
| 3 | PRO | PHE | LYS | ASP | PHE | VAL | GLY | ILE | PHE | GLN | ||||
| 4 | GLU | GLU | LEU | ASP | SER | LYS | GLY | ARG | VAL | SER | ||||
| 5 | ILE | LEU | LEU | LYS | THR | LEU | ALA | LEU | GLN | PRO | ||||
| 6 | ARG | ILE | THR | VAL | ASP | LYS | ASP | MET | ILE | GLU | ||||
| 7 | LYS | LEU | HIS | ASN |
Samples:
sample_1: Variant 5 full-length (CTD only), [U-13C; U-15N; U-2H], 135 uM; HEPES 25 mM; NaCl 50 mM; deuterated glycerol (Sigma Aldrich) 5%; DTT 1 mM
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY - chemical shift assignment
NMRPipe - processing
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts