BMRB Entry 27745

Name: Backbone chemical shift assignments of the calcium-saturated human calmodulin bound to the human NaV1.2 IQ motif peptide
Published: 2021-07-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27745

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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 calcium-saturated human calmodulin bound to the human NaV1.2 IQ motif peptide

Deposition date:

2018-12-28

Original release date:

2021-07-21

Authors:

Mahling, Ryan; Shea, Madeline

Citation:

Citation: Mahling, Ryan; Hovey, Liam; Isbell, Holly; Marx, Dagan; Miller, Mark; Kilpatrick, Adina; Weaver, Lisa; Yoder, Jesse; Kim, Elaine; Andresen, Corinne; Li, Shuxiang; Shea, Madeline. "Na V 1.2 EFL domain allosterically enhances Ca 2+ binding to sites I and II of WT and pathogenic calmodulin mutants bound to the channel CTD" Structure 29, 1339-1356 (2021).
PubMed: 33770503

Assembly members:

Assembly members:
Calmodulin, polymer, 148 residues, Formula weight is not available
voltage-gated_sodium_channel_NaV1.2_IQ_motif_peptide, polymer, 31 residues, Formula weight is not available
entity_CA, non-polymer, 40.078 Da.

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: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE FVQMMTAK
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	458
15N chemical shifts	153
1H chemical shifts	153

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Calmodulin	1
2	Nav1.2 IQ Motif Peptide	2
3	Calcium, 1	3
4	Calcium, 2	3
5	Calcium, 3	3
6	Calcium, 4	3

Entities:

Entity 1, Calmodulin 148 residues - Formula weight is not available

Initial Alanine is residue 1 of calmodulin

1

ALA

ASP

GLN

LEU

THR

GLU

GLN

ILE

ALA

2

GLU

PHE

LYS

GLU

ALA

PHE

SER

LEU

PHE

ASP

3

LYS

ASP

GLY

ASP

GLY

THR

ILE

THR

LYS

4

GLU

LEU

GLY

THR

VAL

MET

ARG

SER

LEU

GLY

5

GLN

ASN

PRO

THR

GLU

ALA

GLU

LEU

GLN

ASP

6

MET

ILE

ASN

GLU

VAL

ASP

ALA

ASP

GLY

ASN

7

GLY

THR

ILE

ASP

PHE

PRO

GLU

PHE

LEU

THR

8

MET

ALA

ARG

LYS

MET

LYS

ASP

THR

ASP

9

SER

GLU

ILE

ARG

GLU

ALA

PHE

ARG

10

VAL

PHE

ASP

LYS

ASP

GLY

ASN

GLY

TYR

ILE

11

SER

ALA

GLU

LEU

ARG

HIS

VAL

MET

THR

12

ASN

LEU

GLY

GLU

LYS

LEU

THR

ASP

GLU

13

VAL

ASP

GLU

MET

ILE

ARG

GLU

ALA

ASP

ILE

14

ASP

GLY

ASP

GLY

GLN

VAL

ASN

TYR

GLU

15

PHE

VAL

GLN

MET

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

Entity 3, Calcium, 1 - Ca - 40.078 Da.

1

CA

Samples:

sample_1: Calmodulin, [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; imidazole 10 mM; potassium chloride 100 mM; sodium azide 0.01 % w/v; calcium chloride 10 mM

sample_conditions_1: ionic strength: 120 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 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection

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

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

NMR spectrometers:

Varian INOVA 600 MHz

UNP	P62158
NCBI	AAD45181.1