BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19344

Title: alpha synuclein mutant S87N in PBS - human/mouse chimera   PubMed: 24058647

Deposition date: 2013-07-09 Original release date: 2013-09-25

Authors: Baum, Jean

Citation: Kang, Lijuan; Janowska, Maria; Moriarty, Gina; Baum, Jean. "Mechanistic Insight into the Relationship between N-Terminal Acetylation of -Synuclein and Fibril Formation Rates by NMR and Fluorescence."  PLoS ONE 8, e75018-e75018 (2013).

Assembly members:
aSyn_S87N, polymer, 140 residues, Formula weight is not available

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: p7-T7

Entity Sequences (FASTA):
aSyn_S87N: MDVFMKGLSKAKEGVVAAAE KTKQGVAEAAGKTKEGVLYV GSKTKEGVVHGVATVAEKTK EQVTNVGGAVVTGVTAVAQK TVEGAGNIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA

Data sets:
Data typeCount
13C chemical shifts397
15N chemical shifts128
1H chemical shifts128

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1aSyn_S87N1

Entities:

Entity 1, aSyn_S87N 140 residues - Formula weight is not available

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

Samples:

sample_1: aSyn_S87N, [U-100% 13C; U-100% 15N], 350 uM; H2O 90%; D2O 10%; Phosphate 10 mM; NaCl 138 mM; KCl 2 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

BMRB 16300 16302 16342 16543 16546 16547 16548 16904 16939 17214 17498 17648 17649 17654 17665 17910 18207 18208 18243 18857 18860 19257 19337 19338 19345 19350 19351 25227 25228
PDB
DBJ BAB29375 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 P61139 P61142 P61143 P37840 P61140

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