BMRB Entry 4379

Title:
NMR Solution Structure of the Human Prion Protein Domain reveals Species Dependent Structural Disorder and Intramolecular Association with the Flexible Tail
Deposition date:
1999-08-18
Original release date:
2000-02-01
Authors:
Zahn, Ralph; Aizhuo, Liu; Luhrs, Thorsten; Wuthrich, Kurt
Citation:

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:

Assembly members:
human prion protein, polymer, 112 residues, 13246 Da.

Natural source:

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

Experimental source:   Production method: recombinant technology

Experimental source:

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

Experimental source:   Production method: recombinant technology

Data sets:
  • assigned_chemical_shifts
Data typeCount
13C chemical shifts354
15N chemical shifts126
1H chemical shifts767

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hPrP(121-230)1

Entities:

Entity 1, hPrP(121-230) 112 residues - 13246 Da.

1   GLYSERVALVALGLYGLYLEUGLYGLYTYR
2   METLEUGLYSERALAMETSERARGPROILE
3   ILEHISPHEGLYSERASPTYRGLUASPARG
4   TYRTYRARGGLUASNMETHISARGTYRPRO
5   ASNGLNVALTYRTYRARGPROMETASPGLU
6   TYRSERASNGLNASNASNPHEVALHISASP
7   CYSVALASNILETHRILELYSGLNHISTHR
8   VALTHRTHRTHRTHRLYSGLYGLUASNPHE
9   THRGLUTHRASPVALLYSMETMETGLUARG
10   VALVALGLUGLNMETCYSILETHRGLNTYR
11   GLUARGGLUSERGLNALATYRTYRGLNARG
12   GLYSER

Samples:

sample_1: human prion protein 1.0 mM

sample_2: human prion protein, [U-15N], 1.0 mM

sample_3: human prion protein, [U-15N; U-13C], 1.0 mM

Ex-cond_1: ionic strength: 0.01 M; pH: 4.5; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
1H-1H-15N NOESYnot availablenot availablenot available
1H-1H-13C NOESYnot availablenot availablenot available
HCCH COSYnot availablenot availablenot available
HCCH TOCSYnot availablenot availablenot available
HNCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available

Software:

PROSA -

XEASY -

DYANA -

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 750 MHz

Related Database Links:

BMRB 15676 16743 17714 17756 17757 17780 18426 18550 19268 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
AlphaFold P61768

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