BMRB Entry 16946

Title:
15N, 13C and 1H Resonance Assignments of the PAS domain of hERG (KV11.1)
Deposition date:
2010-05-24
Original release date:
2010-08-18
Authors:
Muskett, Frederick; Mitcheson, John
Citation:

Citation: Muskett, Frederick; Mitcheson, John. "Resonance assignment and secondary structure prediction of the N-terminal domain of hERG (Kv11.1)."  Biomol. NMR Assignments 5, 15-17 (2011).
PubMed: 20711762

Assembly members:

Assembly members:
hERG1-135, polymer, 150 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: pET-21a

Data sets:
Data typeCount
13C chemical shifts522
15N chemical shifts141
1H chemical shifts873

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hERG1-1351

Entities:

Entity 1, hERG1-135 150 residues - Formula weight is not available

1   METPROVALARGARGGLYHISVALALAPRO
2   GLNASNTHRPHELEUASPTHRILEILEARG
3   LYSPHEGLUGLYGLNSERARGLYSPHEILE
4   ILEALAASNALAARGVALGLUASNCYSALA
5   VALILETYRCYSASNASPGLYPHECYSGLU
6   LEUCYSGLYTYRSERARGALAGLUVALMET
7   GLNARGPROCYSTHRCYSASPPHELEUHIS
8   GLYPROARGTHRGLNARGARGALAALAALA
9   GLNILEALAGLNALALEULEUGLYALAGLU
10   GLUARGLYSVALGLUILEALAPHETYRARG
11   LYSASPGLYSERCYSPHELEUCYSLEUVAL
12   ASPVALVALPROVALLYSASNGLUASPGLY
13   ALAVALILEMETPHEILELEUASNPHEGLU
14   VALVALMETGLULYSGLUASNLEUTYRPHE
15   GLNSERLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: hERG1-135, [U-100% 13C; U-100% 15N], 0.2 mM; H20 90%; D20 10%; EDTA 500 uM; AEBSF 200 uM; DTT 200 uM; Sodium_Azide 0.02 % w/v; acetate buffer 20 mM

sample_2: hERG1-135, [U-100% 15N], 0.2 mM; H20 90%; D20 10%; EDTA 500 uM; AEBSF 200 uM; DTT 200 uM; Sodium_Azide 0.02 % w/v; acetate buffer 20 mM

sample_conditions_1: ionic strength: 0.02 M; pH: 5.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment

TALOS v1.2, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16928 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