BMRB Entry 50312

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50312

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
13C and 15N Chemical Shift Assignments for human A117V variant Y145Stop Prion Protein Amyloid Fibrils
Deposition date:
2020-06-10
Original release date:
2021-07-27
Authors:
Dao, Hanh; Hlaing, May; Ma, Yixuan; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher
Citation:

Citation: Dao, Hanh; Hlaing, May; Ma, Yixuan; Surewicz, Krystyna; Surewicz, Witold; Jaroniec, Christopher. "13C and 15N chemical shift assignments of A117V and M129V human Y145Stop prion protein amyloid fibrils"  Biomol. NMR Assignments 15, 45-51 (2021).
PubMed: 33123960

Assembly members:

Assembly members:
huPrP23-144 A117V, polymer, 126 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
huPrP23-144 A117V: GSDPKKRPKPGGWNTGGSRY PGQGSPGGNRYPPQGGGGWG QPHGGGWGQPHGGGWGQPHG GGWGQPHGGGWGQGGGTHSQ WNKPSKPKTNMKHMAGAAVA GAVVGGLGGYMLGSAMSRPI IHFGSD

Data sets:
Data typeCount
13C chemical shifts71
15N chemical shifts19

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1huPrP23-144 amyloid fibrils1

Entities:

Entity 1, huPrP23-144 amyloid fibrils 126 residues - Formula weight is not available

The four N-terminal residues (GSDP) correspond to non-native thrombin cleavage sites used for protein purification. This is a truncated version of the human prion protein. This Y145Stop human prion protein includes residues 23 to 144, starting at 23K, 24K, 25R, and ending at 142G, 143S, 144D.

1   GLYSERASPPROLYSLYSARGPROLYSPRO
2   GLYGLYTRPASNTHRGLYGLYSERARGTYR
3   PROGLYGLNGLYSERPROGLYGLYASNARG
4   TYRPROPROGLNGLYGLYGLYGLYTRPGLY
5   GLNPROHISGLYGLYGLYTRPGLYGLNPRO
6   HISGLYGLYGLYTRPGLYGLNPROHISGLY
7   GLYGLYTRPGLYGLNPROHISGLYGLYGLY
8   TRPGLYGLNGLYGLYGLYTHRHISSERGLN
9   TRPASNLYSPROSERLYSPROLYSTHRASN
10   METLYSHISMETALAGLYALAALAVALALA
11   GLYALAVALVALGLYGLYLEUGLYGLYTYR
12   METLEUGLYSERALAMETSERARGPROILE
13   ILEHISPHEGLYSERASP

Samples:

sample_1: huPrP23-144 A117V, [U-100% 13C; U-100% 15N], 16.5 mg

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 275 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 CANCOCXsample_1solidsample_conditions_1
2D NCOCXsample_1solidsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - data collection

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

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz