BMRB Entry 26958

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26958

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Title:
Backbone assignment of mouse prion (23-231) at pH 4 and 37C
Deposition date:
2016-11-25
Original release date:
2017-08-10
Authors:
Sengupta, Ishita; Bhate, Suhas; Udgaonkar, Jayant; Das, Ranabir
Citation:

Citation: Sengupta, Ishita; Bhate, Suhas; Das, Ranabir; Udgaonkar, Jayant. "Salt-Mediated Oligomerization of the Mouse Prion Protein Monitored by Real-Time NMR"  J. Mol. Biol. 429, 1852-1872 (2017).
PubMed: 28502793

Assembly members:

Assembly members:
MoPrp, 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MoPrp: MKKRPKPGGWNTGGSRYPGQ GSPGGNRYPPQGGTWGQPHG GGWGQPHGGSWGQPHGGSWG QPHGGGWGQGGGTHNQWNKP SKPKTNLKHVAGAAAAGAVV GGLGGYMLGSAMSRPMIHFG NDWEDRYYRENMYRYPNQVY YRPVDQYSNQNNFVHDCVNI TIKQHTVTTTTKGENFTETD VKMMERVVEQMCVTQYQKES QAYYDGRRSSS

Data sets:
Data typeCount
13C chemical shifts532
15N chemical shifts183
1H chemical shifts183

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Prion monomer1

Entities:

Entity 1, Prion monomer 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   THRILELYSGLNHISTHRVALTHRTHRTHR
18   THRLYSGLYGLUASNPHETHRGLUTHRASP
19   VALLYSMETMETGLUARGVALVALGLUGLN
20   METCYSVALTHRGLNTYRGLNLYSGLUSER
21   GLNALATYRTYRASPGLYARGARGSERSER
22   SER

Samples:

sample_1: MoPrp, [U-98% 13C; U-98% 15N], 0.5 mM; sodium acetate 10 mM

sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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