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 12016

Title: Backbone 1H and 15N Chemical Shift Assignments for Sup35NM   PubMed: 29467288

Deposition date: 2018-02-06 Original release date: 2018-02-27

Authors: Ohhashi, Yumiko; Yamaguchi, Yoshiki; Kamatari, Yuji; Hanashima, Shinya; Kuwata, Kazuo; Tanaka, Motomasa

Citation: Ohhashi, Yumiko; Yamaguchi, Yoshiki; Kurahashi, Hiroshi; Kamatari, Yuji; Sugiyama, Shinju; Uluca, Boran; Piechatzek, Timo; Komi, Yusuke; Shida, Toshinobu; Muller, Henrik; Hanashima, Shinya; Heise, Henrike; Kuwata, Kazuo; Tanaka, Motomasa. "Molecular basis for diversification of yeast prion strain conformation"  Proc. Natl. Acad. Sci. U.S.A. 115, 2389-2394 (2018).

Assembly members:
Sup35, polymer, 260 residues, Formula weight is not available

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):
Sup35: MSDSNQGNNQQNYQQYSQNG NQQQGNNRYQGYQAYNAQAQ PAGGYYQNYQGYSGYQQGGY QQYNPDAGYQQQYNPQGGYQ QYNPQGGYQQQFNPQGGRGN YKNFNYNNNLQGYQAGFQPQ SQGMSLNDFQKQQKQAAPKP KKTLKLVSSSGIKLANATKK VGTKPAESDKKEEEKSAETK EPTKEPTKVEEPVKKEEKPV QTEEKTEEKSELPKVEDLKI SESTHNTNNANVTSADALIK EQEEEVDDEVVNDHHHHHHH

Data sets:
Data typeCount
15N chemical shifts219
1H chemical shifts219

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sup35, component 11
2Sup35, component 21

Entities:

Entity 1, Sup35, component 1 260 residues - Formula weight is not available

1   METSERASPSERASNGLNGLYASNASNGLN
2   GLNASNTYRGLNGLNTYRSERGLNASNGLY
3   ASNGLNGLNGLNGLYASNASNARGTYRGLN
4   GLYTYRGLNALATYRASNALAGLNALAGLN
5   PROALAGLYGLYTYRTYRGLNASNTYRGLN
6   GLYTYRSERGLYTYRGLNGLNGLYGLYTYR
7   GLNGLNTYRASNPROASPALAGLYTYRGLN
8   GLNGLNTYRASNPROGLNGLYGLYTYRGLN
9   GLNTYRASNPROGLNGLYGLYTYRGLNGLN
10   GLNPHEASNPROGLNGLYGLYARGGLYASN
11   TYRLYSASNPHEASNTYRASNASNASNLEU
12   GLNGLYTYRGLNALAGLYPHEGLNPROGLN
13   SERGLNGLYMETSERLEUASNASPPHEGLN
14   LYSGLNGLNLYSGLNALAALAPROLYSPRO
15   LYSLYSTHRLEULYSLEUVALSERSERSER
16   GLYILELYSLEUALAASNALATHRLYSLYS
17   VALGLYTHRLYSPROALAGLUSERASPLYS
18   LYSGLUGLUGLULYSSERALAGLUTHRLYS
19   GLUPROTHRLYSGLUPROTHRLYSVALGLU
20   GLUPROVALLYSLYSGLUGLULYSPROVAL
21   GLNTHRGLUGLULYSTHRGLUGLULYSSER
22   GLULEUPROLYSVALGLUASPLEULYSILE
23   SERGLUSERTHRHISASNTHRASNASNALA
24   ASNVALTHRSERALAASPALALEUILELYS
25   GLUGLNGLUGLUGLUVALASPASPGLUVAL
26   VALASNASPHISHISHISHISHISHISHIS

Samples:

sample_1: Sup35, [U-95% 15N], 100 uM; MES 50 mM; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 5.2; pressure: 1 atm; temperature: 310.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

SPARKY v3.114, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

GB AFD29121.1

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