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 17757

Title: Backbone 1H and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its reduced state   PubMed: 19882604

Authors: Schwalbe, Harald; Schlepckow, Kai

Citation: Gerum, Christian; Silvers, Robert; Wirmer-Bartoschek, Julia; Schwalbe, Harald. "Unfolded-state Structure and Dynamics Influence Fibril Formation of Human Prion Protein"  Angew. Chem. Int. Ed. 48, 9452-9456 (2009).

Assembly members:
hPrP(121-230), polymer, 113 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
hPrP(121-230): GHMVVGGLGGYMLGSAMSRP IIHFGSDYEDRYYRENMHRY PNQVYYRPMDEYSNQNNFVH DXVNITIKQHTVTTTTKGEN FTETDVKMMERVVEQMXITQ YERESQAYYQRGS

Data sets:
Data typeCount
13C chemical shifts257
1H chemical shifts174

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1human prion protein (residues 121-230)1

Entities:

Entity 1, human prion protein (residues 121-230) 113 residues - Formula weight is not available

Construct constitutes C-terminal domain (residues 121-230). First three residues are a remnant of the N-terminal (his)6 tag.

1   GLYHISMETVALVALGLYGLYLEUGLYGLY
2   TYRMETLEUGLYSERALAMETSERARGPRO
3   ILEILEHISPHEGLYSERASPTYRGLUASP
4   ARGTYRTYRARGGLUASNMETHISARGTYR
5   PROASNGLNVALTYRTYRARGPROMETASP
6   GLUTYRSERASNGLNASNASNPHEVALHIS
7   ASPSMCVALASNILETHRILELYSGLNHIS
8   THRVALTHRTHRTHRTHRLYSGLYGLUASN
9   PHETHRGLUTHRASPVALLYSMETMETGLU
10   ARGVALVALGLUGLNMETSMCILETHRGLN
11   TYRGLUARGGLUSERGLNALATYRTYRGLN
12   ARGGLYSER

Samples:

sample_1: hPrP(121-230), [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

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