BMRB Entry 25111

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25111

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Title:
Resonance assignment of the ligand-free cyclic nucleotide-binding domain from the murine ion channel HCN2
Deposition date:
2014-07-25
Original release date:
2022-05-12
Authors:
Boerger, Claudia; Willbold, Dieter; Lecher, Justin; Schuenke, Sven; Stoldt, Matthias
Citation:

Citation: Boerger, Claudia; Schuenke, Sven; Lecher, Justin; Stoldt, Matthias; Winkhaus, Friederike; Kaupp, Ulrich; Willbold, Dieter. "Resonance assignment of the ligand-free cyclic nucleotide-binding domain from the murine ion channel HCN2"  Biomol. NMR Assign. 9, 243-246 (2015).
PubMed: 25324217

Assembly members:

Assembly members:
HCN2N507, polymer, 144 residues, 16315.0116 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-6P2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HCN2N507: GPLGSNCRKLVASMPLFANA DPNFVTAMLTKLKFEVFQPG DYIIREGTIGKKMYFIQHGV VSVLTKGNKEMKLSDGSYFG EICLLTRGRRTASVRADTYC RLYSLSVDNFNEVLEEYPMM RRAFETVAIDRLDRIGKKNS ILLH

Data sets:
Data typeCount
13C chemical shifts637
15N chemical shifts151
1H chemical shifts1045

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HCN2N5071

Entities:

Entity 1, HCN2N507 144 residues - 16315.0116 Da.

1   GLYPROLEUGLYSERASNCYSARGLYSLEU
2   VALALASERMETPROLEUPHEALAASNALA
3   ASPPROASNPHEVALTHRALAMETLEUTHR
4   LYSLEULYSPHEGLUVALPHEGLNPROGLY
5   ASPTYRILEILEARGGLUGLYTHRILEGLY
6   LYSLYSMETTYRPHEILEGLNHISGLYVAL
7   VALSERVALLEUTHRLYSGLYASNLYSGLU
8   METLYSLEUSERASPGLYSERTYRPHEGLY
9   GLUILECYSLEULEUTHRARGGLYARGARG
10   THRALASERVALARGALAASPTHRTYRCYS
11   ARGLEUTYRSERLEUSERVALASPASNPHE
12   ASNGLUVALLEUGLUGLUTYRPROMETMET
13   ARGARGALAPHEGLUTHRVALALAILEASP
14   ARGLEUASPARGILEGLYLYSLYSASNSER
15   ILELEULEUHIS

Samples:

N507: HCN2N507, [U-100% 13C; U-100% 15N], 0.45 mM; DTT 0.50 mM; NaCl 50.00 mM; EDTA 0.50 mM; Citrate 25.00 mM; H2O 93%; D2O 7%

Standard: ionic strength: 75.000 mM; pH: 5.600; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCN507isotropicStandard
3D HNCACBN507isotropicStandard
3D HNCAN507isotropicStandard
3D HNCON507isotropicStandard
HNHA (H[N[ca[HA]]])N507isotropicStandard
2D 1H-13C HSQC/HMQCN507isotropicStandard
3D HCCH-COSYN507isotropicStandard
2D 1H-13C HSQC/HMQCN507isotropicStandard

Software:

CcpNmr_Analysis v2.4, CCPN - assignment, data evaluation

NMRPipe v8.1.2013.218.23.09, NIH - conversion, processing

TALOS-N v4.01.2013.148.15.55, Yang Shen and Ad Bax - dihedreal angle prediction

VnmrJ v3.2, Agilent Technologies (formerly Varian) - data recording, spectrometer operation

NMR spectrometers:

  • Varian VNMRS 900 MHz

Related Database Links:

UniProt O88703
AlphaFold O70506

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