BMRB Entry 19165

Title:
Backbone and side chain chemical shift assignments of bacterial acid-stress chaperone HdeA at pH 6
Deposition date:
2013-04-15
Original release date:
2013-12-12
Authors:
Crowhurst, Karin
Citation:

Citation: Garrison, McKinzie; Crowhurst, Karin. "NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation."  Protein Sci. 23, 167-178 (2014).
PubMed: 24375557

Assembly members:

Assembly members:
HdeA, polymer, 89 residues, 9741 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: pET21a

Data sets:
Data typeCount
13C chemical shifts358
15N chemical shifts91
1H chemical shifts493

Time Domain Data

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1HdeA homodimer, 11
2HdeA homodimer, 21

Entities:

Entity 1, HdeA homodimer, 1 89 residues - 9741 Da.

1   ALAASPALAGLNLYSALAALAASPASNLYS
2   LYSPROVALASNSERTRPTHRCYSGLUASP
3   PHELEUALAVALASPGLUSERPHEGLNPRO
4   THRALAVALGLYPHEALAGLUALALEUASN
5   ASNLYSASPLYSPROGLUASPALAVALLEU
6   ASPVALGLNGLYILEALATHRVALTHRPRO
7   ALAILEVALGLNALACYSTHRGLNASPLYS
8   GLNALAASNPHELYSASPLYSVALLYSGLY
9   GLUTRPASPLYSILELYSLYSASPMET

Related Database Links:

PDB 1BG8 1DJ8
DBJ BAA01883 BAB37813 BAE77784 BAG79302 BAI27765
EMBL CAP77965 CAQ33828 CAR00456 CAR05133 CAR10321
GB AAB18486 AAC76535 AAG58651 AAN44999 AAN82757
PRF 1912293A
REF NP_312417 NP_417967 NP_709292 WP_000756547 WP_000756548
SP P0AES9 P0AET0 P0AET1
AlphaFold P0AES9 P0AET0 P0AET1

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