BMRB Entry 28039
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28039
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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).
PubMed: 36255050
Assembly members:
hSpt5-KOW5, polymer, 59 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETGb1a
Entity Sequences (FASTA):
hSpt5-KOW5: GAMGRRDNELIGQTVRISQG
PYKGYIGVVKDATESTARVE
LHSTCQTISVDRQRLTTVG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 160 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 54 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | monomer 1 | 1 |
Entities:
Entity 1, monomer 1 59 residues - Formula weight is not available
Residues 1-3 result from an engineered TEV-protease cleavage site; residues 3 -5 correspond to residues 699-754 of hSpt5
| 1 | GLY | ALA | MET | GLY | ARG | ARG | ASP | ASN | GLU | LEU | ||||
| 2 | ILE | GLY | GLN | THR | VAL | ARG | ILE | SER | GLN | GLY | ||||
| 3 | PRO | TYR | LYS | GLY | TYR | ILE | GLY | VAL | VAL | LYS | ||||
| 4 | ASP | ALA | THR | GLU | SER | THR | ALA | ARG | VAL | GLU | ||||
| 5 | LEU | HIS | SER | THR | CYS | GLN | THR | ILE | SER | VAL | ||||
| 6 | ASP | ARG | GLN | ARG | LEU | THR | THR | VAL | GLY |
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