BMRB Entry 16928

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16928

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Title:
1H, 13C and 15N chemical shift assignment of the N-terminal domain of the voltage-gated potassium channel-hERG
Deposition date:
2010-05-14
Original release date:
2010-07-16
Authors:
Li, Qingxin; Kang, Congbao
Citation:

Citation: Li, Qingxin; Raida, Manfred; Kang, CongBao. "1H, 13C and 15N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG."  Biomol. NMR Assignments 4, 211-213 (2010).
PubMed: 20607461

Assembly members:

Assembly members:
hERG_NTD, polymer, 136 residues, Formula weight is not available

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: pET16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hERG_NTD: HMPVRRGHVAPQNTFLDTII RKFEGQSRKFIIANARVENC AVIYCNDGFCELCGYSRAEV MQRPCTCDFLHGPRTQRRAA AQIAQALLGAEERKVEIAFY RKDGSCFLCLVDVVPVKNED GAVIMFILNFEVVMEK

Data sets:
Data typeCount
13C chemical shifts516
15N chemical shifts139
1H chemical shifts610

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hERG N-terminal 135 residues1

Entities:

Entity 1, hERG N-terminal 135 residues 136 residues - Formula weight is not available

Residue 0 H was from Factor Xa cleavage. This residue is not included in the assignment.

1   HISMETPROVALARGARGGLYHISVALALA
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_1: hERG NTD, [U-100% 15N], 0.3 – 1.0 mM; Na-PO4 20 mM; NaCl 150 mM; DTT 2 mM

sample_2: hERG NTD, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; Na-PO4 20 mM; NaCl 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1

Software:

NMRPipe v5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16946 17066
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
AlphaFold O08962 O35219 Q12809 Q8WNY2 Q9TSZ3

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