BMRB Entry 50201

Title:
Chemical shift assignment of the Connexin43 cytoplasmic loop domain
Deposition date:
2020-02-20
Original release date:
2021-08-11
Authors:
Spagnol, Gaelle; Chenavas, Sylvie; Kieken, Fabien; Trease, Andrew; Zheng, Li; Brownell, Sarah; Anbanandam, Asokan; Sorgen, Paul
Citation:

Citation: Zheng, Li; Chenavas, Sylvie; Kieken, Fabien; Trease, Andrew; Brownell, Sarah; Anbanandam, Asokan; Sorgen, Paul; Spagnol, Gaelle. "Calmodulin Directly Interacts with the Cx43 Carboxyl-Terminus and Cytoplasmic Loop Containing Three ODDD-Linked Mutants (M147T, R148Q, and T154A) that Retain \u03b1-Helical Structure, but Exhibit Loss-of-Function and Cellular Trafficking Defects"  Biomolecules 10, 1452-1452 (2020).
PubMed: 33080786

Assembly members:

Assembly members:
entity_1, polymer, 61 residues, 7071.2 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: pGEX6p2

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts59
1H chemical shifts448

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Cytoplasmic loop domain of connexin431

Entities:

Entity 1, Cytoplasmic loop domain of connexin43 61 residues - 7071.2 Da.

Residues 1-5 represent part of the remaining non-native affinity tag. This is the cytoplasmic loop domain (residues 100-155) of a 4-span transmembrane protein.

1   GLYPROLEUGLYSERMETARGLYSGLUGLU
2   LYSLEUASNLYSLYSGLUGLUGLULEULYS
3   VALALAGLNTHRASPGLYVALASNVALGLU
4   METHISLEULYSGLNILEGLUILELYSLYS
5   PHELYSTYRGLYILEGLUGLUHISGLYLYS
6   VALLYSMETARGGLYGLYLEULEUARGTHR
7   TYR

Samples:

sample_1: Cx43CL domain, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 10 mM; potassium phosphate 1.8 mM; potassium chloride 2.7 mM; sodium chloride 137 mM

sample_conditions_1: ionic strength: 0.154 M; pH: 5.8; pressure: 1 atm; temperature: 280 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRView v5.2.2.01 - chemical shift assignment, data analysis, peak picking

NMRPipe - processing

NMR spectrometers:

  • Varian INOVA 600 MHz

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