BMRB Entry 26921

Name: Chemical Shift Assignments of the Connexin37 Carboxyl Terminal Domain
Published: 2017-05-23

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26921

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Chemical Shift Assignments of the Connexin37 Carboxyl Terminal Domain PubMed: 28251507

Deposition date: 2016-10-21 Original release date: 2017-05-23

Authors: Li, Hanjun; Spagnol, Gaelle; Nelson, Tasha; Burt, Janis; Sorgen, Paul

Citation: Li, Hanjun; Spagnol, Gaelle; Pontifex, Tasha; Burt, Janis; Spagnol, Paul. "Chemical shift assignments of the connexin37 carboxyl terminal domain" Biomol. NMR Assignments 11, 137-141 (2017).

Assembly members:
Cx37CT_Domain, polymer, 103 residues, 11257.41 Da.

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

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

Entity Sequences (FASTA):
Cx37CT_Domain: GSCRCVSREIKARRDHDARP AQGSASDPYPEQVFFYLPMG EGPSSPPCPTYNGLSSTEQN WANLTTEERLTSSRPPPFVN TAPQGGRKSPSRPNSSASKK QYV

Data sets:

assigned_chemical_shifts
- assignments_cx37

Data type	Count
13C chemical shifts	397
15N chemical shifts	88
1H chemical shifts	632

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Cx37CT Domain	1

Entities:

Entity 1, Cx37CT Domain 103 residues - 11257.41 Da.

Residues 1 and 2 represent part of the remaining non-native affinity tag. This is the C-terminal cytoplasmic domain of a membrane protein.

1

GLY

SER

CYS

ARG

CYS

VAL

SER

ARG

GLU

ILE

2

LYS

ALA

ARG

ASP

HIS

ASP

ALA

ARG

PRO

3

ALA

GLN

GLY

SER

ALA

SER

ASP

PRO

TYR

PRO

4

GLU

GLN

VAL

PHE

TYR

LEU

PRO

MET

GLY

5

GLU

GLY

PRO

SER

PRO

CYS

PRO

THR

6

TYR

ASN

GLY

LEU

SER

THR

GLU

GLN

ASN

7

TRP

ALA

ASN

LEU

THR

GLU

ARG

LEU

8

THR

SER

ARG

PRO

PHE

VAL

ASN

9

THR

ALA

PRO

GLN

GLY

ARG

LYS

SER

PRO

10

SER

ARG

PRO

ASN

SER

ALA

SER

LYS

11

GLN

TYR

VAL

Samples:

sample_1: Cx37CT Domain, [U-99% 13C; U-99% 15N], 650 uM; sodium phosphate 10 mM; potassium phosphate 1.8 mM; potassium chloride 2.7 mM; sodium chloride 137 mM; DTT 2 mM; D2O 5%; H2O 95%

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 HN(CA)CO	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

Software:

NMRView v5.2.2 01, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 600 MHz

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