BMRB Entry 51015
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51015
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Title: Olduvai domain CON1 assignments at 25C PubMed: 35098449
Deposition date: 2021-07-13 Original release date: 2022-02-18
Authors: Paukovich, Natasia; Issaian, Aaron; Henen, Morkos; Vogeli, Beat
Citation: Paukovich, Natasia; Henen, Morkos; Hussain, Alya; Issaian, Aaron; Sikela, James; Hansen, Kirk; Vogeli, Beat. "Solution NMR backbone assignments of disordered Olduvai protein domain CON1 employing Ha-detected experiments" Biomol. NMR Assign. 16, 113-119 (2022).
Assembly members:
entity_1, polymer, 91 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHLmMBP-11 Sec-mMBP-TEV-6xHis
Entity Sequences (FASTA):
entity_1: SAAAASSASVQVEVAEKVQK
SSAPREMQKAEEKEVPEDSL
EECAITCSNSHGPYDSNQPH
KKTKITFEEDKVDSTLIGSS
SHVLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 222 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 151 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CON1 | 1 |
Entities:
Entity 1, CON1 91 residues - Formula weight is not available
| 1 | SER | ALA | ALA | ALA | ALA | SER | SER | ALA | SER | VAL | ||||
| 2 | GLN | VAL | GLU | VAL | ALA | GLU | LYS | VAL | GLN | LYS | ||||
| 3 | SER | SER | ALA | PRO | ARG | GLU | MET | GLN | LYS | ALA | ||||
| 4 | GLU | GLU | LYS | GLU | VAL | PRO | GLU | ASP | SER | LEU | ||||
| 5 | GLU | GLU | CYS | ALA | ILE | THR | CYS | SER | ASN | SER | ||||
| 6 | HIS | GLY | PRO | TYR | ASP | SER | ASN | GLN | PRO | HIS | ||||
| 7 | LYS | LYS | THR | LYS | ILE | THR | PHE | GLU | GLU | ASP | ||||
| 8 | LYS | VAL | ASP | SER | THR | LEU | ILE | GLY | SER | SER | ||||
| 9 | SER | HIS | VAL | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 10 | HIS |
Samples:
sample_1: CON1, [U-100% 13C; U-100% 15N], 500 uM; sodium phosphate 50 mM; sodium chloride 150 mM
sample_conditions_1: ionic strength: 0.05 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 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HA(CA)CON | sample_1 | isotropic | sample_conditions_1 |
| 3D iHACANCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HACA(CON)CAHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HACACON | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.4.2 - chemical shift assignment, data analysis
NMRPipe - processing
NMRFAM-SPARKY - data analysis
NMR spectrometers:
- Bruker AVANCE NEO 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts