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 30517

Title: Solution NMR structure of the KCNQ1 voltage-sensing domain

Deposition date: 2018-09-19 Original release date: 2020-02-28

Authors: Taylor, K.; Kuenze, G.; Smith, J.; Meiler, J.; McFeeters, R.; Sanders, C.

Citation: Taylor, K.; Kang, P.; Hou, P.; Kuenze, G.; Yang, N.; Smith, J.; Shi, J.; Huang, H.; White, K.; Peng, D.; George, A.; Meiler, J.; McFeeters, R.; Cui, J.; Sanders, C.. "Structure of the Intermediate State of the Human KCNQ1 Channel Voltage-Sensor Domain"  . ., .-..

Assembly members:
entity_1, polymer, 159 residues, 18184.631 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):
entity_1: MGHHHHHHGVLARTHVQGRV YNFLERPTGWKCFVYHFAVF LIVLVCLIFSVLSTIEQYAA LATGTLFWMEIVLVVFFGTE YVVRLWSAGCRSKYVGLWGR LRFARKPISIIDLIVVVASM VVLCVGSKGQVFATSAIRGI RFLQILRMLHVDRQGGTWR

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts145
1H chemical shifts926

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 159 residues - 18184.631 Da.

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   VALASPARGGLNGLYGLYTHRTRPARG

Samples:

sample_1: KCNQ1-VSD, [U-100% 13C; U-100% 15N; U-80% 2H], 0.4 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_2: KCNQ1-VSD, [U-100% 13C; U-100% 15N], 0.4 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_3: KCNQ1-VSD, [U-100% 13C; U-100% 15N], 0.4 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; Deuterated LMPG 4 % w/v

sample_4: KCNQ1-VSD, [U-100% 15N], 0.4 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_5: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 mM

sample_6: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 mM

sample_7: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_8: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_9: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_10: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_11: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_12: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_13: KCNQ1-VSD, [U-100% 15N], 0.2 mM; MES 50 mM; EDTA 0.5 mM; TCEP 2 mM; LMPG 4 % w/v

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
2D IPAP-HSQCsample_4isotropicsample_conditions_1
2D IPAP-HSQCsample_5anisotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_7isotropicsample_conditions_1
2D 1H-15N HSQCsample_8isotropicsample_conditions_1
2D 1H-15N HSQCsample_9isotropicsample_conditions_1
2D 1H-15N HSQCsample_10isotropicsample_conditions_1
2D 1H-15N HSQCsample_11isotropicsample_conditions_1
2D 1H-15N HSQCsample_12isotropicsample_conditions_1
2D 1H-15N HSQCsample_13isotropicsample_conditions_1

Software:

AMBER v16, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

XPLOR-NIH v2.48, C.D. Schwieters, J.J. Kuszewski, N. Tjandra and G.M. Clore - structure calculation

SPARKY vNMRFAM, Goddard - chemical shift assignment, peak picking

TOPSPIN v3.2, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 900 MHz

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