BMRB Entry 25251

Title:
Solution structure of Ovis Aries PrP with mutation delta193-196
Deposition date:
2014-09-25
Original release date:
2015-10-05
Authors:
Munoz, Carola; Egalon, Angelique; Beringue, Vincent; Rezaei, Human; Dron, Michel; Sizun, Christina
Citation:

Citation: Munoz, Carola; Sizun, Christina; Egalon, Angelique; Beringue, Vincent; Rezaei, Human; Dron, Michel. "Conversion ability of prion protein helix 2 deletion mutants"  .

Assembly members:

Assembly members:
PrPdelta193-196, polymer, 150 residues, 17123.1885 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b

Data sets:
Data typeCount
13C chemical shifts138
15N chemical shifts146
1H chemical shifts786

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 150 residues - 17123.1885 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERASNLYSPROSERLYSPROLYSTHR
4   ASNMETLYSHISVALALAGLYALAALAALA
5   ALAGLYALAVALVALGLYGLYLEUGLYGLY
6   TYRMETLEUGLYSERVALMETSERARGPRO
7   LEUILEHISPHEGLYASNASPTYRGLUASP
8   ARGTYRTYRARGGLUASNMETTYRARGTYR
9   PROASNGLNVALTYRTYRARGPROVALASP
10   GLNTYRSERASNGLNASNASNPHEVALHIS
11   ASPCYSVALASNILETHRVALLYSGLNHIS
12   THRVALLYSGLYGLUASNPHETHRGLUTHR
13   ASPILELYSILEMETGLUARGVALVALGLU
14   GLNMETCYSILETHRGLNTYRGLNARGGLU
15   SERGLNALATYRTYRGLNARGGLYALASER

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.15 ± 2e-05 mM; Sodium acetate 10.00 ± 0.001 mM; H2O 90 ± 0.001 mM; D2O 10 ± 0.001 mM

sample_2: entity, [U-99% 15N], 0.46 ± 2e-05 mM; Sodium acetate 10.00 ± 0.001 mM; H2O 90 ± 0.001 mM; D2O 10 ± 0.001 mM

condition1: ionic strength: 0 M; pH: 5.300; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropiccondition1
3D HN(CO)CAsample_1isotropiccondition1
2D 1H-15N HSQCsample_1isotropiccondition1
3D 1H-15N NOESYsample_2isotropiccondition1
3D 1H-15N TOCSYsample_2isotropiccondition1
2D 1H-15N HSQCsample_2isotropiccondition1
2D 1H-1H NOESYsample_2isotropiccondition1
2D 1H-15N HSQCsample_2isotropiccondition1

Software:

CYANA v3.0, Peter Guntert - Structure calculation

CcpNmr_Analysis v2.2, CCPN - Data analysis

Talos+ v1.0, Yang Shen - Dihedral angles

Topspin v3.1, Bruker - collection, procession

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 950 MHz

Related Database Links:

GenBank CAA04276
GB AJ000738.1 AAW88332
BMRB 25250
EMBL CAA04276 CAE00190

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