BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 17066

Title: SOLUTION NMR STRUCTURE OF THE N-TERMINAL PAS DOMAIN OF HERG POTASSIUM CHANNEL   PubMed: 21249148

Deposition date: 2010-07-19 Original release date: 2011-05-23

Authors: Vandenberg, Jamie; Ng, Chai; Hunter, Mark; Mobli, Mehdi; King, Glenn; Kuchel, Philip

Citation: Ng, Chai Ann; Hunter, Mark; Perry, Matthew; Mobli, Mehdi; Ke, Ying; Kuchel, Philip; King, Glenn; Stock, Daniela; Vandenberg, Jamie. "The N-terminal tail of hERG contains an amphipathic -helix that regulates channel deactivation."  PLoS ONE 6, .-. (2011).

Assembly members:
Potassium_voltage-gated_channel_subfamily_H_member_2, polymer, 136 residues, 45860.719 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

Entity Sequences (FASTA):
Potassium_voltage-gated_channel_subfamily_H_member_2: SMPVRRGHVAPQNTFLDTII RKFEGQSRKFIIANARVENC AVIYCNDGFCELCGYSRAEV MQRPCTCDFLHGPRTQRRAA AQIAQALLGAEERKVEIAFY RKDGSCFLCLVDVVPVKNED GAVIMFILNFEVVMEK

Data sets:
Data typeCount
13C chemical shifts531
15N chemical shifts146
1H chemical shifts887

Additional metadata:

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

Related Database Links:

BMRB 16928 16946
PDB 1BYW 2L0W 2L1M 2L4R 4HP9 4HQA
DBJ BAA37096 BAB19682
EMBL CAA09232 CAB09536 CAB64868
GB AAA62473 AAC53418 AAC53420 AAC53422 AAC99425
REF NP_000229 NP_001003145 NP_001092571 NP_001166444 NP_001180587
SP O08962 O35219 Q12809 Q8WNY2 Q9TSZ3
TPG DAA30311

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