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 17756

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

Authors: Schwalbe, Harald

Citation: Gerum, Christian; Silvers, Robert; Wirmer-Bartoschek, Julia; Schwalbe, Harald. "Unfolded-State Structure and Dynamics Influence the 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 DCVNITIKQHTVTTTTKGEN FTETDVKMMERVVEQMCITQ YERESQAYYQRGS

Data sets:
Data typeCount
13C chemical shifts254
1H chemical shifts177

Additional metadata:

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

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   ASPCYSVALASNILETHRILELYSGLNHIS
8   THRVALTHRTHRTHRTHRLYSGLYGLUASN
9   PHETHRGLUTHRASPVALLYSMETMETGLU
10   ARGVALVALGLUGLNMETCYSILETHRGLN
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
2D 1H-13C HSQCsample_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 15676 16743 16757 17714 17757 17780 18426 18550 19268 4379 4402 4434 4620 4641 4736
PDB
DBJ BAA00011 BAF62360 BAG32276 BAG32277 BAG32278
EMBL CAA58442 CAG46836 CAG46869
GB AAA19664 AAA60182 AAA68632 AAA68633 AAB59442
REF NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP P04156 P40252 P61766 P61767 P61768