BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 51633

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Alpha-synuclein linker region mutant "4G" bound to SDS micelles   PubMed: 36551244

Deposition date: 2022-09-16 Original release date: 2023-02-08

Authors: Das, Tapojyoti; Ramezani, Meraj; Snead, David; Follmer, Cristian; Chung, Peter; Lee, Ka-Yee; Holowka, David; Baird, Barbara; Eliezer, David

Citation: Das, Tapojyoti; Ramezani, Meraj; Snead, David; Follmer, Cristian; Chung, Peter; Lee, Ka-Yee; Holowka, David; Baird, Barbara; Eliezer, David. "The Role of Membrane Affinity and Binding Modes in Alpha-Synuclein Regulation of Vesicle Release and Trafficking"  Biomolecules 12, 1816-1816 (2022).

Assembly members:
entity_1, polymer, 140 residues, Formula weight is not available
entity_SDS, non-polymer, 266.397 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7.7

Entity Sequences (FASTA):
entity_1: MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLGG GGKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQK TVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts133
1H chemical shifts133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Alpha-synuclein1
22H-SDS2

Entities:

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

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

Entity 2, 2H-SDS - C12 H26 O4 S - 266.397 Da.

1   SDS

Samples:

sample_1: Alpha-synuclein linker mutant 4G, [U-10% 13C; U-100% 15N], 100 uM; SDS, [U-99% 2H], 40 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 600 MHz

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