BMRB Entry 52503

Title:
1H, 13C, and 15N backbone chemical shift assignments of TauK18
Deposition date:
2024-06-14
Original release date:
2024-06-28
Authors:
Muwonge, Kevin; Volkov, Alexander; Tompa, Peter
Citation:

Citation: Muwonge, Kevin; Yaman, Bedri; Meszaros, Attila; Russo, Giorgio; Volkov, Alexander; Tompa, Peter. "Improved expression of aggregation-prone Tau proteins using a spidroin-derived solubility tag"  Separations 11, 198-198 (2024).

Assembly members:

Assembly members:
entity_1, polymer, 149 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: MaSp-Tau-MTBR

Data sets:
Data typeCount
13C chemical shifts390
15N chemical shifts126
1H chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1tauK181

Entities:

Entity 1, tauK18 149 residues - Formula weight is not available

1   METLYSVALALAVALVALARGTHRPROPRO
2   LYSSERPROSERSERALALYSSERARGLEU
3   GLNTHRALAPROVALPROMETPROASPLEU
4   LYSASNVALLYSSERLYSILEGLYSERTHR
5   GLUASNLEULYSHISGLNPROGLYGLYGLY
6   LYSVALGLNILEILEASNLYSLYSLEUASP
7   LEUSERASNVALGLNSERLYSCYSGLYSER
8   LYSASPASNILELYSHISVALPROGLYGLY
9   GLYSERVALGLNILEVALTYRLYSPROVAL
10   ASPLEUSERLYSVALTHRSERLYSCYSGLY
11   SERLEUGLYASNILEHISHISLYSPROGLY
12   GLYGLYGLNVALGLUVALLYSSERGLULYS
13   LEUASPPHELYSASPARGVALGLNSERLYS
14   ILEGLYSERLEUASPASNILETHRHISVAL
15   PROGLYGLYGLYASNLYSLYSILEGLU

Samples:

sample_1: TauK18, [U-100% 13C; U-100% 15N], 0.4 mM; TRIS 20 mM; sodium chloride 100 mM; D2O, [U-100% 2H], 6%

sample_conditions_1: ionic strength: 118 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.6 - collection, processing

qMDD - processing

CcpNMR v2.4 - chemical shift assignment, data analysis, peak picking

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks