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 26925

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

Deposition date: 2016-10-26 Original release date: 2017-02-15

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:
huPrP23-144, polymer, 126 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
huPrP23-144: GSDPKKRPKPGGWNTGGSRY PGQGSPGGNRYPPQGGGGWG QPHGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQGGGTHSQ WNKPSKPKTNMKHMAGAAAA GAVVGGLGGYMLGSAMSRPI IHFGSD

Data sets:
Data typeCount
13C chemical shifts92
15N chemical shifts28

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1huPrP23-1441

Entities:

Entity 1, huPrP23-144 126 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   TYRPROPROGLNGLYGLYGLYGLYTRPGLY
5   GLNPROHISGLYGLYGLYTRPGLYGLNPRO
6   HISGLYGLYGLYTRPGLYGLNPROHISGLY
7   GLYGLYTRPGLYGLNPROHISGLYGLYGLY
8   TRPGLYGLNGLYGLYGLYTHRHISSERGLN
9   TRPASNLYSPROSERLYSPROLYSTHRASN
10   METLYSHISMETALAGLYALAALAALAALA
11   GLYALAVALVALGLYGLYLEUGLYGLYTYR
12   METLEUGLYSERALAMETSERARGPROILE
13   ILEHISPHEGLYSERASP

Samples:

sample_1: huPrP23-144, [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
2D DARRsample_1solidsample_conditions_1

Software:

VNMR, 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