BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 50131

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50131

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Title: Backbone 1H and 15N chemical shift assignments of KL Sup35NM   PubMed: 32284601

Deposition date: 2019-12-15 Original release date: 2020-03-30

Authors: Shida, Toshinobu; Kamatari, Yuji; Yamaguchi, Yoshiki; Kuwata, Kazuo; Tanaka, Motomasa

Citation: Shida, Toshinobu; Kamatari, Yuji; Yoda, Takao; Yamaguchi, Yoshiki; Feig, Michael; Ohhashi, Yumiko; Sugita, Yuji; Kuwata, Kazuo; Tanaka, Motomasa. "Short Disordered Protein Segment Regulates Cross-Species Transmission of a Yeast Prion"  Nat. Chem. Biol. 16, 756-765 (2020).

Assembly members:
entity_1, polymer, 274 residues, Formula weight is not available

Natural source:   Common Name: budding yeasts   Taxonomy ID: 28985   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Kluyveromyces lactis

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

Entity Sequences (FASTA):
entity_1: MSDQQNQDQGQGQGYNQYNQ YGQYNQYYNQQGYQGYNGQQ GAPQGYQAYQAYGQQPQGAY QGYNPQQAQGYQPYQGYNAQ QQGYNAQQGGHNNNYNKNYN NKNSYNNYNKQGYQGAQGYN AQQPTGYAAPAQSSSQGMTL KDFQNQQGSTNAAKPKPKLK LASSSGIKLVGAKKPVAPKT EKTDESKEATKTTDDNEEAQ SELPKIDDLKISEAEKPKTK ENTPSADDTSSEKTTSAKAD TSTGGANSVDALIKEQEDEV DEEVVKDHHHHHHH

Data sets:
Data typeCount
15N chemical shifts259
1H chemical shifts259

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KL Sup35NM1

Entities:

Entity 1, KL Sup35NM 274 residues - Formula weight is not available

1   METSERASPGLNGLNASNGLNASPGLNGLY
2   GLNGLYGLNGLYTYRASNGLNTYRASNGLN
3   TYRGLYGLNTYRASNGLNTYRTYRASNGLN
4   GLNGLYTYRGLNGLYTYRASNGLYGLNGLN
5   GLYALAPROGLNGLYTYRGLNALATYRGLN
6   ALATYRGLYGLNGLNPROGLNGLYALATYR
7   GLNGLYTYRASNPROGLNGLNALAGLNGLY
8   TYRGLNPROTYRGLNGLYTYRASNALAGLN
9   GLNGLNGLYTYRASNALAGLNGLNGLYGLY
10   HISASNASNASNTYRASNLYSASNTYRASN
11   ASNLYSASNSERTYRASNASNTYRASNLYS
12   GLNGLYTYRGLNGLYALAGLNGLYTYRASN
13   ALAGLNGLNPROTHRGLYTYRALAALAPRO
14   ALAGLNSERSERSERGLNGLYMETTHRLEU
15   LYSASPPHEGLNASNGLNGLNGLYSERTHR
16   ASNALAALALYSPROLYSPROLYSLEULYS
17   LEUALASERSERSERGLYILELYSLEUVAL
18   GLYALALYSLYSPROVALALAPROLYSTHR
19   GLULYSTHRASPGLUSERLYSGLUALATHR
20   LYSTHRTHRASPASPASNGLUGLUALAGLN
21   SERGLULEUPROLYSILEASPASPLEULYS
22   ILESERGLUALAGLULYSPROLYSTHRLYS
23   GLUASNTHRPROSERALAASPASPTHRSER
24   SERGLULYSTHRTHRSERALALYSALAASP
25   THRSERTHRGLYGLYALAASNSERVALASP
26   ALALEUILELYSGLUGLNGLUASPGLUVAL
27   ASPGLUGLUVALVALLYSASPHISHISHIS
28   HISHISHISHIS

Samples:

sample_1: KL Sup35NM, [U-99% 15N], 60 uM; MES 50 mM; H2O 90%; D2O, [U-99% 2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 4.0; 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 AF206288 AB039749

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