BMRB Entry 12016

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR12016

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

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).
PubMed: 29467288

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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 peaks
SPARKY: Backbone or all simulated peaks