BMRB Entry 18426

Title:
Solution-state NMR structure of the human prion protein
Deposition date:
2012-04-26
Original release date:
2012-06-18
Authors:
Biljan, Ivana; Ilc, Gregor; Giancin, Gabriele; Zhukov, Igor; Plavec, Janez; Legname, Guiseppe
Citation:

Citation: Biljan, Ivana; Giachin, Gabriele; Ilc, Gregor; Zhukov, Igor; Plavec, Janez; Legname, Giuseppe. "Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism."  Biochem. J. 446, 243-251 (2012).
PubMed: 22676969

Assembly members:

Assembly members:
entity, polymer, 142 residues, 16169.103 Da.

Natural source:

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

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts461
15N chemical shifts150
1H chemical shifts930

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human prion protein1

Entities:

Entity 1, human prion protein 142 residues - 16169.103 Da.

1   GLYGLNGLYGLYGLYTHRHISSERGLNTRP
2   ASNLYSPROSERLYSPROLYSTHRASNMET
3   LYSHISMETALAGLYALAALAALAALAGLY
4   ALAVALVALGLYGLYLEUGLYGLYTYRMET
5   LEUGLYSERALAMETSERARGPROILEILE
6   HISPHEGLYSERASPTYRGLUASPARGTYR
7   TYRARGGLUASNMETHISARGTYRPROASN
8   GLNVALTYRTYRARGPROMETASPGLUTYR
9   SERASNGLNASNASNPHEVALHISASPCYS
10   VALASNILETHRILELYSGLNHISTHRVAL
11   THRTHRTHRTHRLYSGLYGLUASNPHETHR
12   GLUTHRASPVALLYSMETMETGLUARGVAL
13   VALGLUGLNMETCYSILETHRGLNTYRGLU
14   ARGGLUSERGLNALATYRTYRGLNARGGLY
15   SERSER

Samples:

sample_1: huPrP, [U-100% 13C; U-100% 15N], 1.5 mM; H2O 90%; D2O 10%

sample_2: huPrP, [U-100% 13C; U-100% 15N], 1.5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.1 M; pD: 5.9; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_2

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA, (YASARA) - refinement

NMR spectrometers:

  • Varian Uniform NMR System 800 MHz

Related Database Links:

BMRB 15676 16743 16757 17714 17756 17757 17780 18550 19268 4379 4402 4434 4620 4641 4736
PDB
DBJ BAA00011 BAF62360 BAG32276 BAG32277 BAG32278
EMBL CAA58442 CAG46836 CAG46869 CAH92912
GB AAA19664 AAA60182 AAA68632 AAA68633 AAB59442
REF NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP P04156 P40252 P40256 P61766 P61767
TPE CAJ43808
AlphaFold P40252 P61766 P40256 P61767 P04156

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks