BMRB Entry 50799

Title:
Backbone chemical shift assignment of the alpha-crystallin domain of the Small heat shock protein, IbpB from E. coli
Deposition date:
2021-03-04
Original release date:
2021-05-27
Authors:
Pirog, Artur; Cantini, Francesca; Nierzwicki, Lukasz; Obuchowski, Igor; Tomiczek, Bartlomiej; Czub, Jacek; Liberek, Krzysztof
Citation:

Citation: Pirog, Artur; Cantini, Francesca; Nierzwicki, Lukasz; Obuchowski, Igor; Tomiczek, Bartlomiej; Czub, Jacek; Liberek, Krzysztof. "Two bacterial small heat shock proteins, IbpA and IbpB, form a functional heterodimer"  J. Mol. Biol. 433, 167054-167054 (2021).
PubMed: 34022209

Assembly members:

Assembly members:
entity_1, polymer, 97 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 shifts132
15N chemical shifts58
1H chemical shifts58

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IbpB1

Entities:

Entity 1, IbpB 97 residues - Formula weight is not available

The first three aminoacids GSH belong to the tag

1   GLYSERHISSERGLNSERPHEPROPROTYR
2   ASNILEGLULYSSERASPASPASNHISTYR
3   ARGILETHRLEUALALEUALAGLYPHEARG
4   GLNGLUASPLEUGLUILEGLNLEUGLUGLY
5   THRARGLEUSERVALLYSGLYTHRPROGLU
6   GLNPROLYSGLUGLULYSLYSTRPLEUHIS
7   GLNGLYLEUMETASNGLNPROPHESERLEU
8   SERPHETHRLEUALAGLUASNMETGLUVAL
9   SERGLYALATHRPHEVALASNGLYLEULEU
10   HISILEASPLEUILEARGASN

Samples:

sample_1: 15N alpha-crystallin domain of IbpB, [U-100% 15N], 700 uM; phosphate buffer 20 mM; KCl 35 mM

sample_2: 15N-13C alpha-crystallin domain of IbpB, [U-100% 13C; U-100% 15N], 700 uM; phosphate buffer 20 mM; KCl 35 mM

sample_conditions_1: ionic strength: 0.105 M; pH: 7.2; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCACONHsample_2isotropicsample_conditions_1
3D CBCANHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
T1/R1 relaxationsample_1isotropicsample_conditions_1

Software:

TOPSPIN v4.01 - collection, processing

TALOS+ - data analysis

CARA v1.8 - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

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