BMRB Entry 27075

Title:
1H and 15N Chemical Shift Assignments for phosphorylated S129 alpha-synuclein
Deposition date:
2017-04-18
Original release date:
2018-05-22
Authors:
El Turk, Farah; De Genst, Erwin; Guilliams, Tim; Fauvet, Bruno; Hejjaoui, Mirva; Vendruscolo, Michele; Lashuel, Hilal; Dobson, Christopher
Citation:

Citation: El Turk, Farah; De Genst, Erwin; Guilliams, Tim; Fauvet, Bruno; Hejjaoui, Mirva; Di Trani, Justin; Chiki, Anass; Mittermaier, Anthony; Vendruscolo, Michele; Lashuel, Hilal; Dobson, Christopher. "Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding"  Protein Sci. 27, 1262-1274 (2018).
PubMed: 29603451

Assembly members:

Assembly members:
pS129_alpha-synuclein, polymer, 140 residues, 14704 Da.

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: pET

Data sets:
Data typeCount
15N chemical shifts126
1H chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pS129 alpha-synuclein1

Entities:

Entity 1, pS129 alpha-synuclein 140 residues - 14704 Da.

1   METASPVALPHEMETLYSGLYLEUSERLYS
2   ALALYSGLUGLYVALVALALAALAALAGLU
3   LYSTHRLYSGLNGLYVALALAGLUALAALA
4   GLYLYSTHRLYSGLUGLYVALLEUTYRVAL
5   GLYSERLYSTHRLYSGLUGLYVALVALHIS
6   GLYVALALATHRVALALAGLULYSTHRLYS
7   GLUGLNVALTHRASNVALGLYGLYALAVAL
8   VALTHRGLYVALTHRALAVALALAGLNLYS
9   THRVALGLUGLYALAGLYSERILEALAALA
10   ALATHRGLYPHEVALLYSLYSASPGLNLEU
11   GLYLYSASNGLUGLUGLYALAPROGLNGLU
12   GLYILELEUGLUASPMETPROVALASPPRO
13   ASPASNGLUALATYRGLUMETPROSEPGLU
14   GLUGLYTYRGLNASPTYRGLUPROGLUALA

Samples:

sample_1: pS129 alpha-synuclein, [U-100% 13C; U-100% 15N], 100 uM; NaCl 100 mM; tris 25 mM

sample_conditions_1: ionic strength: 123 mM; pH: 7.40; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz

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