BMRB Entry 17649

Title:
Partial 13C, 15N chemical shift assignments of A53T alpha-synuclein fibrils
Deposition date:
2011-05-13
Original release date:
2011-07-07
Authors:
Comellas, Gemma; Lemkau, Luisel; Nieuwkoop, Andrew; Kloepper, Kathryn; Ladror, Daniel; Ebisu, Reika; Woods, Wendy; Lipton, Andrew; George, Julia; Rienstra, Chad
Citation:

Citation: Comellas, Gemma; Lemkau, Luisel; Nieuwkoop, Andrew; Kloepper, Kathryn; Ladror, Daniel; Ebisu, Reika; Woods, Wendy; Lipton, Andrew; George, Julia; Rienstra, Chad. "Structured Regions of -Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites."  J. Mol. Biol. 411, 881-895 (2011).
PubMed: 21718702

Assembly members:

Assembly members:
A53T_alpha-synuclein_fibrils, polymer, 140 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: BL21 DE3 peT28

Data sets:
Data typeCount
13C chemical shifts44
15N chemical shifts14

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1A53T alpha-synuclein1

Entities:

Entity 1, A53T alpha-synuclein 140 residues - Formula weight is not available

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

Samples:

sample_1: A53T alpha-synuclein fibrils, [U-13C; U-15N], mM; H2O 36%

sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
NCACX 50 ms DARRsample_1isotropicsample_conditions_1
NCOCX 50 ms DARRsample_1isotropicsample_conditions_1
CANcoCX 50 ms DARRsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Varian UnityPlus 600 MHz