BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 50195

Title: Skp_A108L_monomer   PubMed: 33087350

Deposition date: 2020-02-12 Original release date: 2020-12-17

Authors: Mas, Guillaume

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).

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

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):
Skp: MGSSHHHHHHSSGLVPRGSH MADKIAIVNMGSLFQQVAQK TGVSNTLENEFKGRASELQR METDLQAKMKKLQSMKAGSD RTKLEKDVMAQRQTFAQKAQ AFEQDRARRSNEERGKLVTR IQTAVKSVLNSQDIDLVVDA NAVAYNSSDVKDITADVLKQ VK

Data sets:
Data typeCount
13C chemical shifts203
15N chemical shifts104
1H chemical shifts104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Skp_A108L1

Entities:

Entity 1, Skp_A108L 162 residues - Formula weight is not available

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   ILEGLNTHRALAVALLYSSERVALLEUASN
14   SERGLNASPILEASPLEUVALVALASPALA
15   ASNALAVALALATYRASNSERSERASPVAL
16   LYSASPILETHRALAASPVALLEULYSGLN
17   VALLYS

Samples:

sample_1: entity_1, [U-99% 13C; U-99% 15N], 1 mM; MES 25 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 0.150 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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