BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34169

Title: Solution NMR structure of truncated, human Hv1/VSOP (Voltage-gated proton channel)

Deposition date: 2017-08-12 Original release date: 2019-03-28

Authors: Bayrhuber, M.; Maslennikov, I.; Kwiatowski, W.; Sobol, A.; Wierschem, C.; Eichmann, C.; Riek, R.

Citation: Bayrhuber, M.; Maslennikov, I.; Kwiatowski, W.; Sobol, A.; Wierschem, C.; Eichmann, C.; Riek, R.. "Insights into the mechanism of proton channels investigated by NMR"  . ., .-..

Assembly members:
entity_1, polymer, 147 residues, 17352.062 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: SHMRAPLDFRGMLRKLFSSH RFQVIIICLVVLDALLVLAE LILDLKIIQPDKNNYAAMVF HYMSITILVFFMMEIIFKLF VFRLEFFHHKFEILDAVVVV VSFILDIVLLFQEHQFEALG LLILLRLWRVARIINGIIIS VKTRSER

Data sets:
Data typeCount
13C chemical shifts360
15N chemical shifts109
1H chemical shifts711

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 147 residues - 17352.062 Da.

1   SERHISMETARGALAPROLEUASPPHEARG
2   GLYMETLEUARGLYSLEUPHESERSERHIS
3   ARGPHEGLNVALILEILEILECYSLEUVAL
4   VALLEUASPALALEULEUVALLEUALAGLU
5   LEUILELEUASPLEULYSILEILEGLNPRO
6   ASPLYSASNASNTYRALAALAMETVALPHE
7   HISTYRMETSERILETHRILELEUVALPHE
8   PHEMETMETGLUILEILEPHELYSLEUPHE
9   VALPHEARGLEUGLUPHEPHEHISHISLYS
10   PHEGLUILELEUASPALAVALVALVALVAL
11   VALSERPHEILELEUASPILEVALLEULEU
12   PHEGLNGLUHISGLNPHEGLUALALEUGLY
13   LEULEUILELEULEUARGLEUTRPARGVAL
14   ALAARGILEILEASNGLYILEILEILESER
15   VALLYSTHRARGSERGLUARG

Samples:

sample_1: Hv1/VSOP, [U-99% 13C; U-99% 15N; 50% 2H], 0.4 mM; MES 20 mM; BisTris 20 mM; FC-12 2 mM; LDAO 2 mM; TCEP 1 mM; ZnCl2 10 mM

sample_conditions_1: ionic strength: 30 mM; pH: 5.8; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P. - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz

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