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 19708

Title: Voltage Sensor Domain of human KCNQ1 (VSD-Q1)   PubMed: 24606221

Deposition date: 2013-12-26 Original release date: 2014-04-11

Authors: Peng, Dungeng; Law, Cheryl

Citation: Peng, Dungeng; Kim, Ji-Hun; Kroncke, Brett; Law, Cheryl; Xia, Yan; Droege, Kristin; Van Horn, Wade; Vanoye, Carlos; Sanders, Charles. "Purification and Structural Study of the Voltage-Sensor Domain of the Human KCNQ1 Potassium Ion Channel."  Biochemistry 53, 2032-2042 (2014).

Assembly members:
VSD-Q1, polymer, 153 residues, 17473 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
VSD-Q1: MGHHHHHHGVLARTHVQGRV YNFLERPTGWKCFVYHFAVF LIVLVCLIFSVLSTIEQYAA LATGTLFWMEIVLVVFFGTE YVVRLWSAGCRSKYVGLWGR LRFARKPISIIDLIVVVASM VVLCVGSKGQVFATSAIRGI RFLQILRMLHVDR

Data sets:
Data typeCount
13C chemical shifts278
15N chemical shifts137
1H chemical shifts137

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Voltage Sensor Domain1

Entities:

Entity 1, Voltage Sensor Domain 153 residues - 17473 Da.

Residues 1-9 are non-native hexa histidine-6 tag; Sequence number counts from the valine after the His-tag.

1   METGLYHISHISHISHISHISHISGLYVAL
2   LEUALAARGTHRHISVALGLNGLYARGVAL
3   TYRASNPHELEUGLUARGPROTHRGLYTRP
4   LYSCYSPHEVALTYRHISPHEALAVALPHE
5   LEUILEVALLEUVALCYSLEUILEPHESER
6   VALLEUSERTHRILEGLUGLNTYRALAALA
7   LEUALATHRGLYTHRLEUPHETRPMETGLU
8   ILEVALLEUVALVALPHEPHEGLYTHRGLU
9   TYRVALVALARGLEUTRPSERALAGLYCYS
10   ARGSERLYSTYRVALGLYLEUTRPGLYARG
11   LEUARGPHEALAARGLYSPROILESERILE
12   ILEASPLEUILEVALVALVALALASERMET
13   VALVALLEUCYSVALGLYSERLYSGLYGLN
14   VALPHEALATHRSERALAILEARGGLYILE
15   ARGPHELEUGLNILELEUARGMETLEUHIS
16   VALASPARG

Samples:

sample_1: VSD-Q1, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; MES buffer 50 mM; EDTA 0.5 mM; TCEP 2 mM

sample_2: VSD-Q1, [U-100% 15N], 0.5 mM; MES buffer 50 mM; EDTA 0.5 mM; TCEP 2 mM

sample_conditions_1: ionic strength: 50 mM; pH: 5.50; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1

Software:

SPARKY v3.106, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAA34738 BAC15571 BAE32460 BAF83307 BAG73570
EMBL CAB38863 CAB44649 CAB44650
GB AAB36518 AAC05498 AAC05705 AAC51776 AAC51781
REF NP_000209 NP_001166292 NP_001192370 NP_032460 NP_114462
SP O70344 P51787 P97414 Q9MYS6 Q9Z0N7
TPG DAA13511

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