Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51959
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Citation: Tuzincin, David; Padrta, Petr; Sanderova, Hana; Rabatinova, Alzebeta; Bendova, Katerina; Krasny, Libor; Zidek, Lukas; Kaderavek, Pavel. "Characterisation of a transitionally occupied state and thermal unfolding of domain 1.1 of sA factor of RNA polymerase from Bacillus subtilis" Proteins 91, 1276-1287 (2023).
PubMed: 37350110
Assembly members:
entity_1, polymer, 79 residues, 9379.02 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b
Entity Sequences (FASTA):
entity_1: ADKQTHETELTFDQVKEQLT
ESGKKRGVLTYEEIAERMSS
FEIESDQMDEYYEFLGEQGV
ELISENEETEDLEHHHHHH
Data type | Count |
13C chemical shifts | 284 |
15N chemical shifts | 150 |
1H chemical shifts | 149 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | sigma1.1 | 1 |
Entity 1, sigma1.1 79 residues - 9379.02 Da.
This protein sequence is a fragment (2-72) of sA primary transcription factor. The initial methionine at position 1 is N-terminally cleaved. Sequence numbering in our case begins with 1 ALA, 2 ASP, ... Residues 72-73 represent non-native residues inserted because of the restriction enzyme (XhoI) used for cloning. Residues 74-79 represent a non-native affinity tag.
1 | ALA | ASP | LYS | GLN | THR | HIS | GLU | THR | GLU | LEU | ||||
2 | THR | PHE | ASP | GLN | VAL | LYS | GLU | GLN | LEU | THR | ||||
3 | GLU | SER | GLY | LYS | LYS | ARG | GLY | VAL | LEU | THR | ||||
4 | TYR | GLU | GLU | ILE | ALA | GLU | ARG | MET | SER | SER | ||||
5 | PHE | GLU | ILE | GLU | SER | ASP | GLN | MET | ASP | GLU | ||||
6 | TYR | TYR | GLU | PHE | LEU | GLY | GLU | GLN | GLY | VAL | ||||
7 | GLU | LEU | ILE | SER | GLU | ASN | GLU | GLU | THR | GLU | ||||
8 | ASP | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Download HSQC peak lists in one of the following formats:
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