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 4402

Title: 1H, 13C and 15N chemical shift assignment of human prion protein hPrP(23-230)

Deposition date: 1999-09-14 Original release date: 2000-02-01

Authors: Liu, Aizhuo; Riek, Roland; Wider, Gerhard; von Schroetter, Christine; Zahn, Ralph; Wuthrich, Kurt

Citation: Zahn, Ralph; Liu, Aizhuo; Luhrs, Thorsten; Riek, Roland; von Schroetter, Christine; Lopez Garcia, Francisco; Billeter, Martin; Calzolai, Luigi; Wider, Gerhard; Wuthrich, Kurt. "NMR Solution Structure of the Human Prion Protein."  Proc. Natl. Acad. Sci. U. S. A. 97, 145-150 (2000).

Assembly members:
human prion protein, polymer, 210 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

Entity Sequences (FASTA):
human prion protein: GSKKRPKPGGWNTGGSRYPG QGSPGGNRYPPQGGGGWGQP HGGGWGQPHGGGWGQPHGGG WGQPHGGGWGQGGGTHSQWN KPSKPKTNMKHMAGAAAAGA VVGGLGGYMLGSAMSRPIIH FGSDYEDRYYRENMHRYPNQ VYYRPMDEYSNQNNFVHDCV NITIKQHTVTTTTKGENFTE TDVKMMERVVEQMCITQYER ESQAYYQRGS

Data sets:
Data typeCount
13C chemical shifts600
15N chemical shifts246
1H chemical shifts1311

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hPrP(23-230)1

Entities:

Entity 1, hPrP(23-230) 210 residues - Formula weight is not available

1   GLYSERLYSLYSARGPROLYSPROGLYGLY
2   TRPASNTHRGLYGLYSERARGTYRPROGLY
3   GLNGLYSERPROGLYGLYASNARGTYRPRO
4   PROGLNGLYGLYGLYGLYTRPGLYGLNPRO
5   HISGLYGLYGLYTRPGLYGLNPROHISGLY
6   GLYGLYTRPGLYGLNPROHISGLYGLYGLY
7   TRPGLYGLNPROHISGLYGLYGLYTRPGLY
8   GLNGLYGLYGLYTHRHISSERGLNTRPASN
9   LYSPROSERLYSPROLYSTHRASNMETLYS
10   HISMETALAGLYALAALAALAALAGLYALA
11   VALVALGLYGLYLEUGLYGLYTYRMETLEU
12   GLYSERALAMETSERARGPROILEILEHIS
13   PHEGLYSERASPTYRGLUASPARGTYRTYR
14   ARGGLUASNMETHISARGTYRPROASNGLN
15   VALTYRTYRARGPROMETASPGLUTYRSER
16   ASNGLNASNASNPHEVALHISASPCYSVAL
17   ASNILETHRILELYSGLNHISTHRVALTHR
18   THRTHRTHRLYSGLYGLUASNPHETHRGLU
19   THRASPVALLYSMETMETGLUARGVALVAL
20   GLUGLNMETCYSILETHRGLNTYRGLUARG
21   GLUSERGLNALATYRTYRGLNARGGLYSER

Samples:

sample_1: human prion protein, [U-13C; U-15N], 1 mM

Ex-cond1: ionic strength: 0.01 M; pH: 4.5; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
HNCAnot availablenot availablenot available
ct-HNCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCA(CO)NNHnot availablenot availablenot available
HN(COCA)NNHnot availablenot availablenot available
(H)N(CO-TOCSY)NHnot availablenot availablenot available
(H)CA(CO-TOCSY)NHnot availablenot availablenot available
(H)CBCA(CO-TOCSY)NHnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 16743 16757 17714 17756 17757 17780 18426 18550 19268 4379 4434 4620 4641 4736
PDB
DBJ BAA00011 BAF62360 BAG32276 BAG32277 BAG32278
EMBL CAG46836 CAG46869 CAH92912
GB AAA19664 AAA60182 AAA68632 AAA68633 AAB59443
REF NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP P04156 P40252 P40256 P61766 P61767
TPE CAJ43808

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts