BMRB Entry 26613

Title:
Periplasmic chaperone Skp from E. coli in 8 m Urea
Deposition date:
2015-07-15
Original release date:
2020-08-30
Authors:
Burmann, Bjoern; Hiller, Sebastian
Citation:

Citation: Mas, Guillaume; Burmann, Bjorn; Sharpe, Timothy; Claudi, Beatrice; Bumann, Dirk; Hiller, Sebastian. "Regulation of chaperone function by coupled folding and oligomerization"  Sci. Adv. 6, eabc5822-eabc5822 (2020).
PubMed: 33087350

Assembly members:

Assembly members:
Skp, polymer, 162 residues, Formula weight is not available

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: pET28b

Data sets:
Data typeCount
13C chemical shifts417
15N chemical shifts141
1H chemical shifts141

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Skp1

Entities:

Entity 1, Skp 162 residues - Formula weight is not available

His-tag including thrombin-cleavage site (residues -20 - 0) followed by mature Skp (residues 1 - 141)

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METALAASPLYSILEALAILEVALASNMET
4   GLYSERLEUPHEGLNGLNVALALAGLNLYS
5   THRGLYVALSERASNTHRLEUGLUASNGLU
6   PHELYSGLYARGALASERGLULEUGLNARG
7   METGLUTHRASPLEUGLNALALYSMETLYS
8   LYSLEUGLNSERMETLYSALAGLYSERASP
9   ARGTHRLYSLEUGLULYSASPVALMETALA
10   GLNARGGLNTHRPHEALAGLNLYSALAGLN
11   ALAPHEGLUGLNASPARGALAARGARGSER
12   ASNGLUGLUARGGLYLYSLEUVALTHRARG
13   ILEGLNTHRALAVALLYSSERVALALAASN
14   SERGLNASPILEASPLEUVALVALASPALA
15   ASNALAVALALATYRASNSERSERASPVAL
16   LYSASPILETHRALAASPVALLEULYSGLN
17   VALLYS

Samples:

sample_1: Skp, [U-13C; U-15N; U-2H], 0.6 mM; D2O 10%; DSS 50 uM; MES 25 mM; NaCl 150 mM; urea 8 M; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 288.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
5D APSY HNCOCACBsample_1isotropicsample_conditions_1
4D APSY HNCACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.0, Bruker Biospin, Guntert, Herrmann and Wuthrich, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

  • Bruker Ascend 700 MHz

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