BMRB Entry 27094

Name: Backbone chemical shift assignments of the apo calmodulin C-domain bound to the NaV1.2 IQ motif peptide
Published: 2017-09-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27094

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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 chemical shift assignments of the apo calmodulin C-domain bound to the NaV1.2 IQ motif peptide

Deposition date:

2017-05-04

Original release date:

2017-09-11

Authors:

Mahling, Ryan; Kilpatrick, Adina; Shea, Madeline

Citation:

Citation: Mahling, Ryan; Kilpatrick, Adina; Shea, Madeline. "Backbone resonance assignments of complexes of human voltage-dependent sodium channel NaV1.2 IQ motif peptide bound to apo calmodulin and to the C-domain fragment of apo calmodulin" Biomol. NMR Assignments 11, 297-303 (2017).
PubMed: 28823028

Assembly members:

Assembly members:
Calmodulin_C-domain, polymer, 73 residues, Formula weight is not available
Voltage-gated_sodium_channel_NaV1-2_IQ_motif_peptide, polymer, 31 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pT7-7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Calmodulin_C-domain: MKDTDSEEEIREAFRVFDKD GNGYISAAELRHVMTNLGEK LTDEEVDEMIREADIDGDGQ VNYEEFVQMMTAK
Voltage-gated_sodium_channel_NaV1-2_IQ_motif_peptide: GPGSKRKQEEVSAIIIQRAY RRYLLKQKVKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	286
15N chemical shifts	98
1H chemical shifts	98

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Calmodulin C-domain	1
2	NaV1.2 IQ motif peptide	2

Entities:

Entity 1, Calmodulin C-domain 73 residues - Formula weight is not available

Initial methionine is residue 76 of calmodulin.

1

MET

LYS

ASP

THR

ASP

SER

GLU

ILE

2

ARG

GLU

ALA

PHE

ARG

VAL

PHE

ASP

LYS

ASP

3

GLY

ASN

GLY

TYR

ILE

SER

ALA

GLU

LEU

4

ARG

HIS

VAL

MET

THR

ASN

LEU

GLY

GLU

LYS

5

LEU

THR

ASP

GLU

VAL

ASP

GLU

MET

ILE

6

ARG

GLU

ALA

ASP

ILE

ASP

GLY

ASP

GLY

GLN

7

VAL

ASN

TYR

GLU

PHE

VAL

GLN

MET

8

THR

ALA

LYS

Entity 2, NaV1.2 IQ motif peptide 31 residues - Formula weight is not available

First four residues (GPGS) are part of a 3C protease cleavage site (numbered -4 to -1). NaV1.2 residue 1901 is residue 5 of the peptide.

1

GLY

PRO

GLY

SER

LYS

ARG

LYS

GLN

GLU

2

VAL

SER

ALA

ILE

GLN

ARG

ALA

TYR

3

ARG

TYR

LEU

LYS

GLN

LYS

VAL

LYS

4

LYS

Samples:

sample_1: Calmodulin C-domain, [U-99% 13C; U-99% 15N], 0.85 mM; Voltage-gated sodium channel NaV1.2 IQ motif peptide, [U-99% 13C; U-99% 15N], 0.85 mM; potassium chloride 100 mM; imidazole 10 mM; sodium azide 0.01%; EDTA 0.1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCO	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

NMRPipe, (NMRpipe) Delaglio, Grzesiek, Vuister, Zhu, Pfeifer, and Bax - processing

Analysis, (Analysis) CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian INOVA 600 MHz

NCBI	AAD45181.1 NP_001035232.1
UNP	P0DP23 Q99250
AlphaFold	Q96HK3 Q9BZD0