BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 34003

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34003
MolProbity Validation Chart

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Title: PrP226* - Solution-state NMR structure of truncated human prion protein   PubMed: 28109886

Deposition date: 2016-05-31 Original release date: 2016-09-30

Authors: Kovac, V.; Zupancic, B.; Ilc, G.; Curin Serbec, V.; Plavec, J.

Citation: Kovac, Valerija; Zupancic, Blaz; Ilc, Gregor; Plavec, Janez; Curin Serbec, Vladka. "Truncated prion protein PrP226* - A structural view on its role in amyloid disease"  Biochem. Biophys. Res. Commun. 484, 45-50 (2017).

Assembly members:
entity_1, polymer, 145 residues, 16595.449 Da.

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 BL21(DE3)

Entity Sequences (FASTA):
entity_1: GQGGGTHSQWNKPSKPKTNM KHMAGAAAAGAVVGGLGGYM LGSAMSRPIIHFGSDYEDRY YRENMHRYPNQVYYRPMDEY SNQNNFVHDCVNITIKQHTV TTTTKGENFTETDVKMMERV VEQMCITQYERESQAYYGGH HHHHH

Data sets:
Data typeCount
13C chemical shifts427
15N chemical shifts143
1H chemical shifts865

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 145 residues - 16595.449 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   ARGGLUSERGLNALATYRTYRGLYGLYHIS
15   HISHISHISHISHIS

Samples:

sample_1: PrP226, [U-13C; U-15N], 0.9 mM

sample_conditions_1: ionic strength: 150 mM; pH: 4.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CHIMERA, Resource for Biocomputing, Visualization, and Informatics - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

VNMR, Varian - collection

YASARA, Prof. Dr. Gregor Hoegenauer, Prof. Dr. Guenther Koraimann, Prof. Dr. Andreas Kungl, Prof. Dr. Gert Vriend - refinement

NMR spectrometers:

  • Agilent VNMRS 800 MHz

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