BMRB Entry 19814

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments Cterminal domain (residues 374-426)of mPannexin 1
Published: 2019-07-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19814

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments Cterminal domain (residues 374-426)of mPannexin 1

Deposition date:

2014-02-24

Original release date:

2019-07-12

Authors:

Spagnol, Gaelle; Sorgen, Paul; Spray, David

Citation:

Citation: Spagnol, Gaelle; Sorgen, Paul; Spray, David. "Structural order in Pannexin 1 cytoplasmic domains" Channels (Austin) 8, 157-166 (2014).
PubMed: 24751934

Assembly members:

Assembly members:
mPanx1CT(374-426), polymer, 58 residues, 6217.8 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-6-p2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mPanx1CT(374-426): GPLGSMDIIDGKIPTSLQTK GEDQGSQRVEFKDLDLSSEA AANNGEKNSRQRLLNPSC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	231
15N chemical shifts	54
1H chemical shifts	364

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	mPanx1CT(374-426), 1	1
2	mPanx1CT(374-426), 2	1

Entities:

Entity 1, mPanx1CT(374-426), 1 58 residues - 6217.8 Da.

Residues 1-5 represent a non-native cloning linker

1

GLY

PRO

LEU

GLY

SER

MET

ASP

ILE

ASP

2

GLY

LYS

ILE

PRO

THR

SER

LEU

GLN

THR

LYS

3

GLY

GLU

ASP

GLN

GLY

SER

GLN

ARG

VAL

GLU

4

PHE

LYS

ASP

LEU

ASP

LEU

SER

GLU

ALA

5

ALA

ASN

GLY

GLU

LYS

ASN

SER

ARG

6

GLN

ARG

LEU

ASN

PRO

SER

CYS

Samples:

sample_1: mPanx1CT(374-426), [U-98% 13C; U-98% 15N], 3 mM; potassium phosphate 11.9 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; DTT 1 mM; H2O 90%; D2O 10%; PBS 1 X

sample_conditions_1: ionic strength: 137 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

NMRView v5.2.2.01, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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