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
  • Hide all

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   CYMVALASNILETHRILELYSGLNHISTHR
8   VALTHRTHRTHRTHRLYSGLYGLUASNPHE
9   THRGLUTHRASPVALLYSMETMETGLUARG
10   VALVALGLUGLNMETCYMVALTHRGLNTYR
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:

BMRB 15845 16071 16076 16077 16078 16079 16080 16185 16722 17081 17082 17084 17174 17213 17758
PDB
DBJ BAE34221 BAE34724 BAE34788 BAE34911 BAE35622
EMBL CAJ18553
GB AAA39997 AAC02804 AAD19985 AAH06703 AAL57230
REF NP_001265185 NP_035300
SP P04925