BMRB Entry 28034

Title:
Backbone resonance assignments for the HSP27 (HSPB1) alpha-crystallin domain monomer
Deposition date:
2019-10-29
Original release date:
2020-02-26
Authors:
Alderson, Reid; Bax, Ad; Baldwin, Andrew
Citation:

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:

Assembly members:
HSP27 (HSPB1), polymer, 88 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-29b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts167
15N chemical shifts80
1H chemical shifts80

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1HSP27 (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   GLYVALSERGLUILEARGHISTHRALAASP
2   ARGTRPARGVALSERLEUASPVALASNHIS
3   PHEALAPROASPGLULEUTHRVALLYSTHR
4   LYSASPGLYVALVALGLUILETHRGLYLYS
5   HISGLUGLUARGGLNASPGLUHISGLYTYR
6   ILESERARGSERPHETHRARGLYSTYRTHR
7   LEUPROPROGLYVALASPPROTHRGLNVAL
8   SERSERSERLEUSERPROGLUGLYTHRLEU
9   THRVALGLUALAPROMETPROLYS

Samples:

sample_1: HSP27 (HSPB1), [U-13C; U-15N; U-2H], 0.1 mM; sodium phosphate 30 mM; EDTA 2 mM

sample_conditions_1: pH: 4.1; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY vNMRFAM-SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

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