BMRB Entry 25645

Title:
Chemical Shift Assignments and Structure of HSPB1_ACD
Deposition date:
2015-06-03
Original release date:
2015-08-17
Authors:
Rajagopal, Ponni; Shi, Lei; Klevit, Rachel
Citation:

Citation: Rajagopal, Ponni; Liu, Ying; Shi, Lei; Clouser, Amanda; Klevit, Rachel. "Structure of the alpha-crystallin domain from the redox-sensitive chaperone, HSPB1"  J. Biomol. NMR 63, 223-228 (2015).
PubMed: 26243512

Assembly members:

Assembly members:
entity, polymer, 98 residues, 10894.250 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET24a

Data sets:
Data typeCount
13C chemical shifts176
15N chemical shifts81
1H chemical shifts233

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_21

Entities:

Entity 1, entity_1 98 residues - 10894.250 Da.

1   METGLNLEUSERSERGLYVALSERGLUILE
2   ARGHISTHRALAASPARGTRPARGVALSER
3   LEUASPVALASNHISPHEALAPROASPGLU
4   LEUTHRVALLYSTHRLYSASPGLYVALVAL
5   GLUILETHRGLYLYSHISGLUGLUARGGLN
6   ASPGLUHISGLYTYRILESERARGCYSPHE
7   THRARGLYSTYRTHRLEUPROPROGLYVAL
8   ASPPROTHRGLNVALSERSERSERLEUSER
9   PROGLUGLYTHRLEUTHRVALGLUALAPRO
10   METPROLYSLEUALATHRGLNSER

Related Database Links:

UNP P04792
AlphaFold Q9UC36

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks