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 18353

Title: 1H, 15N and 13C backbone resonance assignments of the Kelch domain of mouse Keap1   PubMed: 22688683

Deposition date: 2012-03-27 Original release date: 2012-06-11

Authors: Cino, Elio; Choy, Wing-Yiu; Fan, Jingsong; Yang, Daiwen

Citation: Cino, Elio; Fan, Jingsong; Yang, Daiwen; Choy, Wing-Yiu. "1H, 15N and 13C backbone resonance assignments of the Kelch domain of mouse Keap1."  Biomol. NMR Assignments 7, 149-153 (2013).

Assembly members:
Kelch_domain_of_mouse_Keap1, polymer, 290 residues, Formula weight is not available

Natural source:   Common Name: House Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
Kelch_domain_of_mouse_Keap1: GVGRLIYTAGGYFRQSLSYL EAYNPSNGSWLRLADLQVPR SGLAGCVVGGLLYAVGGRNN SPDGNTDSSALDCYNPMTNQ WSPCASMSVPRNRIGVGVID GHIYAVGGSHGCIHHSSVER YEPERDEWHLVAPMLTRRIG VGVAVLNRLLYAVGGFDGTN RLNSAECYYPERNEWRMITP MNTIRSGAGVCVLHNCIYAA GGYDGQDQLNSVERYDVETE TWTFVAPMRHHRSALGITVH QGKIYVLGGYDGHTFLDSVE CYDPDSDTWSEVTRMTSGRS GVGVAVTMEP

Data sets:
Data typeCount
13C chemical shifts490
15N chemical shifts251
1H chemical shifts251

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Kelch domain of mouse Keap11

Entities:

Entity 1, Kelch domain of mouse Keap1 290 residues - Formula weight is not available

The starting G was a non-native residue from the TEV recognition sequence that remained after cleavage

1   GLYVALGLYARGLEUILETYRTHRALAGLY
2   GLYTYRPHEARGGLNSERLEUSERTYRLEU
3   GLUALATYRASNPROSERASNGLYSERTRP
4   LEUARGLEUALAASPLEUGLNVALPROARG
5   SERGLYLEUALAGLYCYSVALVALGLYGLY
6   LEULEUTYRALAVALGLYGLYARGASNASN
7   SERPROASPGLYASNTHRASPSERSERALA
8   LEUASPCYSTYRASNPROMETTHRASNGLN
9   TRPSERPROCYSALASERMETSERVALPRO
10   ARGASNARGILEGLYVALGLYVALILEASP
11   GLYHISILETYRALAVALGLYGLYSERHIS
12   GLYCYSILEHISHISSERSERVALGLUARG
13   TYRGLUPROGLUARGASPGLUTRPHISLEU
14   VALALAPROMETLEUTHRARGARGILEGLY
15   VALGLYVALALAVALLEUASNARGLEULEU
16   TYRALAVALGLYGLYPHEASPGLYTHRASN
17   ARGLEUASNSERALAGLUCYSTYRTYRPRO
18   GLUARGASNGLUTRPARGMETILETHRPRO
19   METASNTHRILEARGSERGLYALAGLYVAL
20   CYSVALLEUHISASNCYSILETYRALAALA
21   GLYGLYTYRASPGLYGLNASPGLNLEUASN
22   SERVALGLUARGTYRASPVALGLUTHRGLU
23   THRTRPTHRPHEVALALAPROMETARGHIS
24   HISARGSERALALEUGLYILETHRVALHIS
25   GLNGLYLYSILETYRVALLEUGLYGLYTYR
26   ASPGLYHISTHRPHELEUASPSERVALGLU
27   CYSTYRASPPROASPSERASPTHRTRPSER
28   GLUVALTHRARGMETTHRSERGLYARGSER
29   GLYVALGLYVALALAVALTHRMETGLUPRO

Samples:

sample_1: Kelch domain, [U-13C; U-15N; U-2H], 0.2 – 0.3 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA34639 BAB23519 BAC32621 BAC36267 BAC97871
EMBL CAG15151
GB AAH55732 AAI51546 AAL84711 EDL25167 EDL25168
REF NP_001094612 NP_001103775 NP_001103776 NP_001103777 NP_001108143
SP Q684M4 Q9Z2X8
TPG DAA27941

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