BMRB Entry 50523
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50523
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Title: SsoSSB 1-114 PubMed: 33405014
Deposition date: 2020-10-20 Original release date: 2021-06-30
Authors: Yang, Min June; Park, Chin-Ju; Lee, Woonghee
Citation: Yang, Min June; Lee, Woonghee; Park, Chin-Ju. "Resonance assignments and secondary structure of thermophile single-stranded DNA binding protein from Sulfolobus solfataricus at 323K." Biomol. NMR Assign. 15, 159-164 (2021).
Assembly members:
entity_1, polymer, 129 residues, Formula weight is not available
Natural source: Common Name: Sulfolobus solfataricus Taxonomy ID: 2287 Superkingdom: Archaea Kingdom: not available Genus/species: Saccharolobus solfataricus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET C-terminal TEV His6 cloning vector with BioBrick polycistronic restriction sites (9Bc)
Entity Sequences (FASTA):
entity_1: MEEKVGNLKPNMESVNVTVR
VLEASEARQIQTKNGVRTIS
EAIVGDETGRVKLTLWGKHA
GSIKEGQVVKIENAWTTAFK
GQVQLNAGSKTKIAEASEDG
FPESSQIPENTPTAENLYFQ
SGSHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 483 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 756 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SsoSSB | 1 |
Entities:
Entity 1, SsoSSB 129 residues - Formula weight is not available
| 1 | MET | GLU | GLU | LYS | VAL | GLY | ASN | LEU | LYS | PRO | ||||
| 2 | ASN | MET | GLU | SER | VAL | ASN | VAL | THR | VAL | ARG | ||||
| 3 | VAL | LEU | GLU | ALA | SER | GLU | ALA | ARG | GLN | ILE | ||||
| 4 | GLN | THR | LYS | ASN | GLY | VAL | ARG | THR | ILE | SER | ||||
| 5 | GLU | ALA | ILE | VAL | GLY | ASP | GLU | THR | GLY | ARG | ||||
| 6 | VAL | LYS | LEU | THR | LEU | TRP | GLY | LYS | HIS | ALA | ||||
| 7 | GLY | SER | ILE | LYS | GLU | GLY | GLN | VAL | VAL | LYS | ||||
| 8 | ILE | GLU | ASN | ALA | TRP | THR | THR | ALA | PHE | LYS | ||||
| 9 | GLY | GLN | VAL | GLN | LEU | ASN | ALA | GLY | SER | LYS | ||||
| 10 | THR | LYS | ILE | ALA | GLU | ALA | SER | GLU | ASP | GLY | ||||
| 11 | PHE | PRO | GLU | SER | SER | GLN | ILE | PRO | GLU | ASN | ||||
| 12 | THR | PRO | THR | ALA | GLU | ASN | LEU | TYR | PHE | GLN | ||||
| 13 | SER | GLY | SER | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SsoSSB, [U-100% 13C; U-100% 15N], 1.2 mM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 323 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
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