BMRB Entry 18243

Title:
WT AS fibrils (1H detection experiments)
Deposition date:
2012-02-07
Original release date:
2012-09-24
Authors:
Zhou, Donghua; Nieuwkoop, Andrew; Comellas, Gemma; Rienstra, Chad
Citation:

Citation: Zhou, Donghua; Nieuwkoop, Andrew; Berthold, Deborah; Comellas, Gemma; Sperling, Lindsay; Tang, Ming; Shah, Gautam; Brea, Elliott; Lemkau, Luisel; Rienstra, Chad. "Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy."  J. Biomol. NMR 54, 291-305 (2012).
PubMed: 22986689

Assembly members:

Assembly members:
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: LB21 DE3 peT28

Data sets:
Data typeCount
13C chemical shifts127
15N chemical shifts48
1H chemical shifts49

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alpha-synuclein1

Entities:

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

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

Samples:

sample_1: alpha-synuclein fibrils, [U-13C; U-15N; U-2H], 36%

sample_2: alpha-synuclein fibrils, [U-13C; U-15N; U-2H], 36%

sample_condition_1: pH: 7.4

Experiments:

NameSampleSample stateSample conditions
3D CANHsample_1isotropicsample_condition_1
3D CBCANHsample_1isotropicsample_condition_1
3D CONHsample_1isotropicsample_condition_1
3D COcaNHsample_1isotropicsample_condition_1
3D CAcoNHsample_1isotropicsample_condition_1
3D CBCAcoNHsample_1isotropicsample_condition_1
3D CONHsample_2isotropicsample_condition_1
3D CANHsample_2isotropicsample_condition_1

Software:

SPARKY, Goddard - chemical shift assignment

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

NMR spectrometers:

  • Varian INOVA 750 MHz

Related Database Links:

BMRB 16300 16302 16342 16543 16546 16547 16548 16904 16939 17214 17498 17648 17649 17654 17665 17910 18207 18208 18857 18860 19257 19337 19338 19344 19345 19350 19351 25227 25228
PDB
DBJ BAF82858 BAG73790
EMBL CAG33339 CAG46454
GB AAA16117 AAC02114 AAG30302 AAH13293 AAI08276
REF NP_000336 NP_001009158 NP_001032222 NP_001129014 NP_001139526
SP P37840 P61139 P61140 P61142 P61143
AlphaFold P61143 P37840 P61139 P61140 P61142

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