BMRB Entry 50201

Name: Chemical shift assignment of the Connexin43 cytoplasmic loop domain
Published: 2021-08-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50201

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
entity_1: GPLGSMRKEEKLNKKEEELK VAQTDGVNVEMHLKQIEIKK FKYGIEEHGKVKMRGGLLRT Y

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	259
15N chemical shifts	59
1H chemical shifts	448

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cytoplasmic loop domain of connexin43	1

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

GLY

PRO

LEU

GLY

SER

MET

ARG

LYS

GLU

2

LYS

LEU

ASN

LYS

GLU

LEU

LYS

3

VAL

ALA

GLN

THR

ASP

GLY

VAL

ASN

VAL

GLU

4

MET

HIS

LEU

LYS

GLN

ILE

GLU

ILE

LYS

5

PHE

LYS

TYR

GLY

ILE

GLU

HIS

GLY

LYS

6

VAL

LYS

MET

ARG

GLY

LEU

ARG

THR

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_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