BMRB Entry 27693

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27693

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Title:
Backbone and Sidechian 1H, 13C, and 15N Chemical Shift Assignments for Escherichia Coli Periplasmic Chaperone HdeA at pH 1.5
Deposition date:
2018-11-19
Original release date:
2018-12-19
Authors:
Yu, Xing-Chi; Jin, Changwen; Hu, Yunfei
Citation:

Citation: Yu, Xing-Chi; Hu, Yunfei; Ding, Jienv; Li, Hongwei; Jin, Changwen. "Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone"  J. Biol. Chem. 294, 3192-3206 (2019).
PubMed: 30573682

Assembly members:

Assembly members:
HdeA_F28W, polymer, 89 residues, 9779.95 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: pET-28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HdeA_F28W: ADAQKAADNKKPVNSWTCED FLAVDESWQPTAVGFAEALN NKDKPEDAVLDVQGIATVTP AIVQACTQDKQANFKDKVKG EWDKIKKDM

Data sets:
Data typeCount
13C chemical shifts344
15N chemical shifts84
1H chemical shifts531

Additional metadata:

  • Assembly
  • Samples and Experiments
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HdeA monomer1

Entities:

Entity 1, HdeA monomer 89 residues - 9779.95 Da.

The sequence is numbered according to the mature protein in which the signal peptide is cleaved.

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

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