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 16301

Title: intrinsically unfolded alpha-synuclein variant SaS   PubMed: 19481090

Authors: Rao, Jampani Nageswara; Kim, Yujin; Park, Leena; Ulmer, Tobias

Citation: Rao, Jampani Nageswara; Kim, Yujin; Park, Leena; Ulmer, Tobias. "Effect of Pseudorepeat Rearrangement on alpha-Synuclein Misfolding, Vesicle Binding, and Micelle Binding"  J. Mol. Biol. 390, 516-529 (2009).

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

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not applicable

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
SaS: MDVFMKGLEKTKEQVTNVGS KTKEGVVHGVGAVVTGVTAV AEKTKQGVAEAAATVASKAK EGVVAAAGKTKEGVLYVGQK TVEGAGSIAAATGFVKKDQL GKNEEGAPQEGILEDMPVDP DNEAYEMPSEEGYQDYEPEA

Data sets:
Data typeCount
13C chemical shifts236
15N chemical shifts128
1H chemical shifts128

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1monomer1

Entities:

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

1   METASPVALPHEMETLYSGLYLEUGLULYS
2   THRLYSGLUGLNVALTHRASNVALGLYSER
3   LYSTHRLYSGLUGLYVALVALHISGLYVAL
4   GLYALAVALVALTHRGLYVALTHRALAVAL
5   ALAGLULYSTHRLYSGLNGLYVALALAGLU
6   ALAALAALATHRVALALASERLYSALALYS
7   GLUGLYVALVALALAALAALAGLYLYSTHR
8   LYSGLUGLYVALLEUTYRVALGLYGLNLYS
9   THRVALGLUGLYALAGLYSERILEALAALA
10   ALATHRGLYPHEVALLYSLYSASPGLNLEU
11   GLYLYSASNGLUGLUGLYALAPROGLNGLU
12   GLYILELEUGLUASPMETPROVALASPPRO
13   ASPASNGLUALATYRGLUMETPROSERGLU
14   GLUGLYTYRGLNASPTYRGLUPROGLUALA

Samples:

sample_1: SaS, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; H2O 95%; D2O 5%; HEPES NaCl 25 mM; NaCl 50 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 0.075 M; pH: 7.4; pressure: 1 atm; temperature: 288.2 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 16303