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 16706

Title: 1H, 13C, and 15N chemical shift assignments for H2H2, a mini prion protein   PubMed: 20375014

Deposition date: 2010-02-04 Original release date: 2010-03-31

Authors: Pastore, Annalisa; Pauwels, Kris; Adrover, Miquel; de Chiara, Cesira; Prigent, Stephanie; Rezeai, Human

Citation: Adrover, Miquel; Pauwels, Kris; Prigent, Stephanie; de Chiara, Cesira; Xu, Zhou; Chapuis, Celine; Pastore, Annalisa; Rezaei, Human. "Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3."  J. Biol. Chem. 285, 21004-21012 (2010).

Assembly members:
H2H3, polymer, 89 residues, 10227.3 Da.

Natural source:   Common Name: sheep   Taxonomy ID: 9940   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Ovis aries

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

Entity Sequences (FASTA):
H2H3: MGSSHHHHHHSSGLVPRGSH MRPVDQYSNQNNFVHDCVNI TVKQHTVTTTTKGENFTETD IKAMERVVEQMCITQYQRES QAYYQRGAS

Data sets:
Data typeCount
13C chemical shifts194
15N chemical shifts72
1H chemical shifts420

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1H2H31

Entities:

Entity 1, H2H3 89 residues - 10227.3 Da.

The first 21 residues represents a non-native his-tag. Residues 22-89 represent residues 167-234 of the native ovine PrP.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METARGPROVALASPGLNTYRSERASNGLN
4   ASNASNPHEVALHISASPCYSVALASNILE
5   THRVALLYSGLNHISTHRVALTHRTHRTHR
6   THRLYSGLYGLUASNPHETHRGLUTHRASP
7   ILELYSALAMETGLUARGVALVALGLUGLN
8   METCYSILETHRGLNTYRGLNARGGLUSER
9   GLNALATYRTYRGLNARGGLYALASER

Samples:

sample_1: H2H3, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 10%; H2O 90%; sodium citrate 5 mM

sample_conditions_1: ionic strength: 0.006 M; pH: 3.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
CBAROsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

ARIA vv2.2, Linge, O, . - data analysis, geometry optimization, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAQ81754 AIE40054

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