BMRB Entry 27190

Title:
Backbone chemical shift assignments of apo calmodulin bound to human NaV1.1 IQ motif peptide
Deposition date:
2017-07-21
Original release date:
2018-05-08
Authors:
Kilpatrick, Adina; Lin, Zesen; Shea, Madeline
Citation:

Citation: Isbell, Holly; Kilpatrick, Adina; Lin, Zesen; Mahling, Ryan; Shea, Madeline. "Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaV1.1, NaV1.4 and NaV1.7"  Biomol. NMR Assignments 12, 283-289 (2018).
PubMed: 29728980

Assembly members:

Assembly members:
Calmodulin, polymer, 148 residues, 16706 Da.
Human_voltage-gated_sodium_channel_NaV1.1_IQ_motif_peptide, polymer, 31 residues, 3633 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):

Data sets:
Data typeCount
13C chemical shifts503
15N chemical shifts164
1H chemical shifts164

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Calmodulin1
2NaV1.1 IQ motif peptide2

Entities:

Entity 1, Calmodulin 148 residues - 16706 Da.

Initial alanine is residue 1.

1   ALAASPGLNLEUTHRGLUGLUGLNILEALA
2   GLUPHELYSGLUALAPHESERLEUPHEASP
3   LYSASPGLYASPGLYTHRILETHRTHRLYS
4   GLULEUGLYTHRVALMETARGSERLEUGLY
5   GLNASNPROTHRGLUALAGLULEUGLNASP
6   METILEASNGLUVALASPALAASPGLYASN
7   GLYTHRILEASPPHEPROGLUPHELEUTHR
8   METMETALAARGLYSMETLYSASPTHRASP
9   SERGLUGLUGLUILEARGGLUALAPHEARG
10   VALPHEASPLYSASPGLYASNGLYTYRILE
11   SERALAALAGLULEUARGHISVALMETTHR
12   ASNLEUGLYGLULYSLEUTHRASPGLUGLU
13   VALASPGLUMETILEARGGLUALAASPILE
14   ASPGLYASPGLYGLNVALASNTYRGLUGLU
15   PHEVALGLNMETMETTHRALALYS

Entity 2, NaV1.1 IQ motif peptide 31 residues - 3633 Da.

First four residues (GPGS) are part of a 3C protease cleavage site (numbered -4 to -1). Residue 5 of the peptide corresponds to residue 1911 in NaV1.1.

1   GLYPROGLYSERLYSARGLYSGLNGLUGLU
2   VALSERALAVALILEILEGLNARGALATYR
3   ARGARGHISLEULEULYSARGTHRVALLYS
4   GLN

Samples:

sample_1: Calmodulin, [U-99% 13C; U-99% 15N], 0.85 mM; Human voltage-gated sodium channel NaV1.1 IQ motif peptide, [U-99% 13C; U-99% 15N], 0.85 mM; EDTA 0.1 mM; potassium chloride 100 mM; imidazole 10 mM; sodium azide 0.01 % w/v

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_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

Related Database Links:

UNP P0DP23 P35498
NCBI 801 6323
AlphaFold Q96HK3 Q9C008

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