BMRB Entry 27866

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27866

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Title:
A ubiquitin-like dimerization domain controls protein kinase D activation by trans-autophosphorylation
Deposition date:
2019-04-02
Original release date:
2019-08-14
Authors:
Leonard, Thomas
Citation:

Citation: Elsner, Daniel; Siess, Katharina; Gossenreiter, Thomas; Hartl, Markus; Leonard, Thomas. "A ubiquitin-like dimerization domain controls protein kinase D activation by trans-autophosphorylation"  J. Biol. Chem. 294, 14422-14441 (2019).
PubMed: 31406020

Assembly members:

Assembly members:
Dkf1, polymer, 153 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Roundworm   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGST-parallel

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dkf1: GAMDGSQGSTDYGDHVVLRY GGTREMVPLIRHEQMLDMLM ERARQIVQGFGNLDTRNMYL FRHEYNSPTLLYPITSASQI TSGSILEIILVDRTEAAVIP HVVEPESYMRPTFCDFCGEM LTGLMRQGVKCKNCNGNFHK RCSNAARNNCGAP

Data sets:
Data typeCount
13C chemical shifts115
15N chemical shifts106
1H chemical shifts124

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1Dkf1, chain 11
2Dkf1, chain 21

Entities:

Entity 1, Dkf1, chain 1 153 residues - Formula weight is not available

1   GLYALAMETASPGLYSERGLNGLYSERTHR
2   ASPTYRGLYASPHISVALVALLEUARGTYR
3   GLYGLYTHRARGGLUMETVALPROLEUILE
4   ARGHISGLUGLNMETLEUASPMETLEUMET
5   GLUARGALAARGGLNILEVALGLNGLYPHE
6   GLYASNLEUASPTHRARGASNMETTYRLEU
7   PHEARGHISGLUTYRASNSERPROTHRLEU
8   LEUTYRPROILETHRSERALASERGLNILE
9   THRSERGLYSERILELEUGLUILEILELEU
10   VALASPARGTHRGLUALAALAVALILEPRO
11   HISVALVALGLUPROGLUSERTYRMETARG
12   PROTHRPHECYSASPPHECYSGLYGLUMET
13   LEUTHRGLYLEUMETARGGLNGLYVALLYS
14   CYSLYSASNCYSASNGLYASNPHEHISLYS
15   ARGCYSSERASNALAALAARGASNASNCYS
16   GLYALAPRO

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