BMRB Entry 17759

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17759

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Title:
Backbone 1H and 13C Chemical Shift Assignments of murine prion protein (residues 121-232) in its reduced state
Deposition date:
2011-07-05
Original release date:
2011-07-14
Authors:
Schwalbe, Harald; Schlepckow, Kai
Citation:

Citation: Gerum, Christian; Schlepckow, Kai; Schwalbe, Harald. "The unfolded state of the murine prion protein and properties of single-point mutants related to human prion diseases"  J. Mol. Biol. 401, 7-12 (2010).
PubMed: 20541558

Assembly members:

Assembly members:
mPrP(121-232), polymer, 114 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: pRSET A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
mPrP(121-232): GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQYSNQNNFVHD XVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMXVTQY QKESQAYYDGRRSS

Data sets:
Data typeCount
13C chemical shifts301
1H chemical shifts100

Additional metadata:

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Assembly:

Entity Assembly IDEntity NameEntity ID
1murine prion protein (residues 121-232)1

Entities:

Entity 1, murine prion protein (residues 121-232) 114 residues - Formula weight is not available

Construct constitutes C-terminal domain (residues 121-232). First two residues are a remnant of the N-terminal (his)6 tag.

1   GLYSERVALVALGLYGLYLEUGLYGLYTYR
2   METLEUGLYSERALAMETSERARGPROMET
3   ILEHISPHEGLYASNASPTRPGLUASPARG
4   TYRTYRARGGLUASNMETTYRARGTYRPRO
5   ASNGLNVALTYRTYRARGPROVALASPGLN
6   TYRSERASNGLNASNASNPHEVALHISASP
7   SMCVALASNILETHRILELYSGLNHISTHR
8   VALTHRTHRTHRTHRLYSGLYGLUASNPHE
9   THRGLUTHRASPVALLYSMETMETGLUARG
10   VALVALGLUGLNMETSMCVALTHRGLNTYR
11   GLNLYSGLUSERGLNALATYRTYRASPGLY
12   ARGARGSERSER