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 26924

Title: 13C and 15N Chemical Shift Assignments for Mouse Y145Stop Prion Protein Amyloid Fibrils   PubMed: 28004358

Authors: Theint, Theint; Nadaud, Philippe; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher

Citation: Theint, Theint; Nadaud, Philippe; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher. "13C and 15N Chemical Shift Assignments of Mammalian Y145Stop Prion Protein Amyloid Fibrils"  Biomol. NMR Assign. 11, 75-80 (2017).

Assembly members:
moPrP23-144, polymer, 125 residues, Formula weight is not available

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
moPrP23-144: GSDPKKRPKPGGWNTGGSRY PGQGSPGGNRYPPQGGTWGQ PHGGGWGQPHGGSWGQPHGG SWGQPHGGGWGQGGGTHNQW NKPSKPKTNLKHVAGAAAAG AVVGGLGGYMLGSAMSRPMI HFGND

Data sets:
Data typeCount
13C chemical shifts83
15N chemical shifts30

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1moPrP23-1441

Entities:

Entity 1, moPrP23-144 125 residues - Formula weight is not available

The four N-terminal residues (GSDP) correspond to a non-native thrombin cleavage site used for protein purification.

1   GLYSERASPPROLYSLYSARGPROLYSPRO
2   GLYGLYTRPASNTHRGLYGLYSERARGTYR
3   PROGLYGLNGLYSERPROGLYGLYASNARG
4   TYRPROPROGLNGLYGLYTHRTRPGLYGLN
5   PROHISGLYGLYGLYTRPGLYGLNPROHIS
6   GLYGLYSERTRPGLYGLNPROHISGLYGLY
7   SERTRPGLYGLNPROHISGLYGLYGLYTRP
8   GLYGLNGLYGLYGLYTHRHISASNGLNTRP
9   ASNLYSPROSERLYSPROLYSTHRASNLEU
10   LYSHISVALALAGLYALAALAALAALAGLY
11   ALAVALVALGLYGLYLEUGLYGLYTYRMET
12   LEUGLYSERALAMETSERARGPROMETILE
13   HISPHEGLYASNASP

Samples:

sample_1: mouse PrP23-144, [U-100% 13C; U-100% 15N], 20 mg

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D NCAsample_1solidsample_conditions_1
3D NCACXsample_1solidsample_conditions_1
3D NCOCXsample_1solidsample_conditions_1
3D CONCAsample_1solidsample_conditions_1
3D NCACXsample_1solidsample_conditions_1

Software:

VnmrJ v2.2C, Varian - collection

SPARKY, Goddard - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS-N, Shen and Bax - secondary structure analysis

nmrglue, Helmus, Jaroniec - processing

NMR spectrometers:

  • Varian VNMRS 500 MHz

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