BMRB Entry 28034
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28034
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Citation: Alderson, T. Reid; Ying, Jinfa; Bax, Ad; Benesch, Justin; Baldwin, Andrew. "Conditional disorder in small heat-shock proteins" J. Mol. Biol. 432, 3033-3049 (2020).
PubMed: 32081587
Assembly members:
HSP27 (HSPB1), polymer, 88 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: pET-29b
Entity Sequences (FASTA):
HSP27 (HSPB1): GVSEIRHTADRWRVSLDVNH
FAPDELTVKTKDGVVEITGK
HEERQDEHGYISRSFTRKYT
LPPGVDPTQVSSSLSPEGTL
TVEAPMPK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 167 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 80 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HSP27 (HSPB1) | 1 |
Entities:
Entity 1, HSP27 (HSPB1) 88 residues - Formula weight is not available
This construct contains the C137S mutation to prevent disulfide bond formation."
| 1 | GLY | VAL | SER | GLU | ILE | ARG | HIS | THR | ALA | ASP | ||||
| 2 | ARG | TRP | ARG | VAL | SER | LEU | ASP | VAL | ASN | HIS | ||||
| 3 | PHE | ALA | PRO | ASP | GLU | LEU | THR | VAL | LYS | THR | ||||
| 4 | LYS | ASP | GLY | VAL | VAL | GLU | ILE | THR | GLY | LYS | ||||
| 5 | HIS | GLU | GLU | ARG | GLN | ASP | GLU | HIS | GLY | TYR | ||||
| 6 | ILE | SER | ARG | SER | PHE | THR | ARG | LYS | TYR | THR | ||||
| 7 | LEU | PRO | PRO | GLY | VAL | ASP | PRO | THR | GLN | VAL | ||||
| 8 | SER | SER | SER | LEU | SER | PRO | GLU | GLY | THR | LEU | ||||
| 9 | THR | VAL | GLU | ALA | PRO | MET | PRO | LYS |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks