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 27886

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Shaker-VSD   PubMed: 31301804

Deposition date: 2019-04-30 Original release date: 2019-05-30

Authors: Chen, Hongbo; Chanda, Baron; Henzler-Wildman, Katherine

Citation: Chen, Hongbo; Pan, Junkun; Gandhi, Disha; Dockendorff, Christopher; Cui, Qiang; Chanda, Baron; Henzler-Wildman, Katherine. "NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles"  Biophys. J. 117, 388-398 (2019).

Assembly members:
Shaker-VSD, polymer, 185 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet15b

Entity Sequences (FASTA):
Shaker-VSD: GGGGFEYPESSQAARVVAII SVFVILLSIVIFCLETLPEF KHYKVFNTTTNGTKIEEDEV PDITDPFFLIETLCIIWFTF ELTVRFLACPNKLNFCRDVM NVIDIIAIIPYFITLATVVA EEEDTLNLPKAPVSPQDKSS NQAMSLAILRVIRLVRVFRI FKLSRHSKGLQILGRTLKAS MRELG

Data sets:
Data typeCount
13C chemical shifts524
15N chemical shifts163
1H chemical shifts178

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Shaker-VSD1

Entities:

Entity 1, Shaker-VSD 185 residues - Formula weight is not available

G213, G214, G215, G216 (first four) are resides left after TEV protease cleavage and do not belong to Shaker-VSD.

1   GLYGLYGLYGLYPHEGLUTYRPROGLUSER
2   SERGLNALAALAARGVALVALALAILEILE
3   SERVALPHEVALILELEULEUSERILEVAL
4   ILEPHECYSLEUGLUTHRLEUPROGLUPHE
5   LYSHISTYRLYSVALPHEASNTHRTHRTHR
6   ASNGLYTHRLYSILEGLUGLUASPGLUVAL
7   PROASPILETHRASPPROPHEPHELEUILE
8   GLUTHRLEUCYSILEILETRPPHETHRPHE
9   GLULEUTHRVALARGPHELEUALACYSPRO
10   ASNLYSLEUASNPHECYSARGASPVALMET
11   ASNVALILEASPILEILEALAILEILEPRO
12   TYRPHEILETHRLEUALATHRVALVALALA
13   GLUGLUGLUASPTHRLEUASNLEUPROLYS
14   ALAPROVALSERPROGLNASPLYSSERSER
15   ASNGLNALAMETSERLEUALAILELEUARG
16   VALILEARGLEUVALARGVALPHEARGILE
17   PHELYSLEUSERARGHISSERLYSGLYLEU
18   GLNILELEUGLYARGTHRLEULYSALASER
19   METARGGLULEUGLY

Samples:

sample_1: Shaker-VSD, [U-13C; U-15N; U-2H], 0.3 mM; H2O 90%; D2O, [U-2H], 10%; sodium azide 0.05%; TCEP 4 mM; potassium chloride 50 mM; MOPS 100 mM; LPPG ~40 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.7; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

CcpNmr_Analysis, Vranken, Boucher, Stevens, Fogh, Pajon, Llinas, Ulrich, Markley, Ionides, Laue - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 750 MHz

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