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 26926

Title: 13C and 15N Chemical Shift Assignments for Syrian Hamster 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:
ShaPrP23-144, polymer, 126 residues, Formula weight is not available

Natural source:   Common Name: golden hamster   Taxonomy ID: 10036   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mesocricetus auratus

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

Entity Sequences (FASTA):
ShaPrP23-144: GSDPKKRPKPGGWNTGGSRY PGQGSPGGNRYPPQGGGTWG QPHGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQGGGTHNQ WNKPSKPKTNMKHMAGAAAA GAVVGGLGGYMLGSAMSRPM MHFGND

Data sets:
Data typeCount
13C chemical shifts77
15N chemical shifts27

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ShaPrP23-1441

Entities:

Entity 1, ShaPrP23-144 126 residues - Formula weight is not available

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

1   GLYSERASPPROLYSLYSARGPROLYSPRO
2   GLYGLYTRPASNTHRGLYGLYSERARGTYR
3   PROGLYGLNGLYSERPROGLYGLYASNARG
4   TYRPROPROGLNGLYGLYGLYTHRTRPGLY
5   GLNPROHISGLYGLYGLYTRPGLYGLNPRO
6   HISGLYGLYGLYTRPGLYGLNPROHISGLY
7   GLYGLYTRPGLYGLNPROHISGLYGLYGLY
8   TRPGLYGLNGLYGLYGLYTHRHISASNGLN
9   TRPASNLYSPROSERLYSPROLYSTHRASN
10   METLYSHISMETALAGLYALAALAALAALA
11   GLYALAVALVALGLYGLYLEUGLYGLYTYR
12   METLEUGLYSERALAMETSERARGPROMET
13   METHISPHEGLYASNASP

Samples:

sample_1: ShaPrP23-144, [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
2D NCACXsample_1solidsample_conditions_1
3D NCACXsample_1solidsample_conditions_1
3D NCOCXsample_1solidsample_conditions_1
3D CONCAsample_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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