BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17759

Title: Backbone 1H and 13C Chemical Shift Assignments of murine prion protein (residues 121-232) in its reduced state   PubMed: 20541558

Authors: Schwalbe, Harald; Schlepckow, Kai

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).

Assembly members:
mPrP(121-232), polymer, 114 residues, Formula weight is not available

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

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

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

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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

Samples:

sample_1: mPrP(121-232), [U-13C; U-15N], 0.2 – 0.5 mM; TSP 1 mM; urea 8 M; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 2.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links: