BMRB Entry 51006

Title:
Assignment of the full length A6 mouse prion protein at 37degC pH 4
Deposition date:
2021-07-06
Original release date:
2021-11-10
Authors:
Bhate, Suhas; Udgaonkar, Jayant; Das, Ranabir
Citation:

Citation: Bhate, Suhas; Udgaonkar, Jayant. "Destabilization of polar interactions in the prion protein triggers misfolding and oligomerization"  Protein Sci. 30, 2258-2271 (2021).
PubMed: 34558139

Assembly members:

Assembly members:
entity_1, polymer, 211 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-17b

Data sets:
Data typeCount
13C chemical shifts265
15N chemical shifts158
1H chemical shifts158

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1A6 mouse prion protein1

Entities:

Entity 1, A6 mouse prion protein 211 residues - Formula weight is not available

1   METLYSLYSARGPROLYSPROGLYGLYTRP
2   ASNTHRGLYGLYSERARGTYRPROGLYGLN
3   GLYSERPROGLYGLYASNARGTYRPROPRO
4   GLNGLYGLYTHRTRPGLYGLNPROHISGLY
5   GLYGLYTRPGLYGLNPROHISGLYGLYSER
6   TRPGLYGLNPROHISGLYGLYSERTRPGLY
7   GLNPROHISGLYGLYGLYTRPGLYGLNGLY
8   GLYGLYTHRHISASNGLNTRPASNLYSPRO
9   SERLYSPROLYSTHRASNLEULYSHISVAL
10   ALAGLYALAALAALAALAGLYALAVALVAL
11   GLYGLYLEUGLYGLYTYRMETLEUGLYSER
12   ALAMETSERARGPROMETILEHISPHEGLY
13   ASNASPTRPGLUASPARGTYRTYRARGGLU
14   ASNMETTYRARGTYRPROASNGLNVALTYR
15   TYRARGPROVALASPGLNTYRSERASNGLN
16   ASNASNPHEVALHISASPCYSVALASNILE
17   THRILELYSGLNHISALAALAALAALAALA
18   ALALYSGLYGLUASNPHETHRGLUTHRASP
19   VALLYSMETMETGLUARGVALVALGLUGLN
20   METCYSVALTHRGLNTYRGLNLYSGLUSER
21   GLNALATYRTYRASPGLYARGARGSERSER
22   SER

Samples:

sample_1: A6 mouse prion protein, [U-99% 13C; U-99% 15N], 500 uM; Sodium Acetate 10 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

Related Database Links:

BMRB 26958

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