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 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

Assembly:

Entity Assembly IDEntity NameEntity ID
1H_member_21

Entities:

Entity 1, H_member_2 136 residues - 45860.719 Da.

Residue 1 is from TEV cleavage site. This polypeptide is the N-terminal PAS domain of hERG Potassium channel.

1   SERMETPROVALARGARGGLYHISVALALA
2   PROGLNASNTHRPHELEUASPTHRILEILE
3   ARGLYSPHEGLUGLYGLNSERARGLYSPHE
4   ILEILEALAASNALAARGVALGLUASNCYS
5   ALAVALILETYRCYSASNASPGLYPHECYS
6   GLULEUCYSGLYTYRSERARGALAGLUVAL
7   METGLNARGPROCYSTHRCYSASPPHELEU
8   HISGLYPROARGTHRGLNARGARGALAALA
9   ALAGLNILEALAGLNALALEULEUGLYALA
10   GLUGLUARGLYSVALGLUILEALAPHETYR
11   ARGLYSASPGLYSERCYSPHELEUCYSLEU
12   VALASPVALVALPROVALLYSASNGLUASP
13   GLYALAVALILEMETPHEILELEUASNPHE
14   GLUVALVALMETGLULYS

Samples:

sample: sodium chloride 150 mM; HEPES 10 mM; TCEP 3 mM; D2O, [U-100% 2H], 7%; Octyl Glucoside 5 mM; H2O 93%; N15 labeled PAS, [U-99% 15N], 99%

sample_1: sodium chloride 150 mM; HEPES 10 mM; TCEP 3 mM; D2O, [U-100% 2H], 100%; Octyl Glucoside 5 mM; N15/C13 labeled PAS, [U-99% 13C; U-99% 15N], 99%

sample_conditions_1: ionic strength: 150 mM; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsampleisotropicsample_conditions_1
2D 1H-15N HSQCsampleisotropicsample_conditions_1
3D CBCA(CO)NHsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D C(CO)NHsampleisotropicsample_conditions_1
3D H(CCO)NHsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
3D HN(CO)CAsampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement

AMBER v10, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - Dihedral angles calculation

TOPSPIN v2, Bruker Biospin - collection, processing

NMR spectrometers:

  • BRUKER Avance II 900 MHz

Related Database Links:

BMRB 16928 16946
PDB
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