BMRB Entry 25692

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25692
MolProbity Validation Chart

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Title:
SOLUTION STRUCTURE OF OVIS ARIES PRP
Deposition date:
2015-07-06
Original release date:
2016-05-23
Authors:
Munoz, Carola; Egalon, Angelique; Beringue, Vincent; Rezaei, Human; Dron, Michel; Sizun, Christina
Citation:

Citation: Munoz-Montesino, Carola; Sizun, Christina; Moudjou, Mohammed; Herzog, Laetitia; Reine, Fabienne; Chapuis, Jerome; Ciric, Danica; Igel-Egalon, Angelique; Laude, Hubert; Beringue, Vincent; Rezaei, Human; Dron, Michel. "Generating Bona Fide Mammalian Prions with Internal Deletions"  J. Virol. 90, 6963-6975 (2016).
PubMed: 27226369

Assembly members:

Assembly members:
entity, polymer, 206 residues, 16263.355 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MGSSHHHHHHSSGLVPRGSH MSNKPSKPKTNMKHVAGAAA AGAVVGGLGGYMLGSVMSRP LIHFGNDYEDRYYRENMYRY PNQVYYRPVDQYSNQNNFVH DCVNITVKQHTVTTTTKGEN FTETDIKIMERVVEQMCITQ YQRESQAYYQRGASVNITVK QHTVTTTTKGENFTETDIKI MERVVEQMCITQYQRESQAY YQRGAS

Data sets:
Data typeCount
15N chemical shifts148
1H chemical shifts836

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 206 residues - 16263.355 Da.

Residues 92-102 correspond to anN-terminal His-tag for purification purposes.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERASNLYSPROSERLYSPROLYSTHR
4   ASNMETLYSHISVALALAGLYALAALAALA
5   ALAGLYALAVALVALGLYGLYLEUGLYGLY
6   TYRMETLEUGLYSERVALMETSERARGPRO
7   LEUILEHISPHEGLYASNASPTYRGLUASP
8   ARGTYRTYRARGGLUASNMETTYRARGTYR
9   PROASNGLNVALTYRTYRARGPROVALASP
10   GLNTYRSERASNGLNASNASNPHEVALHIS
11   ASPCYSVALASNILETHRVALLYSGLNHIS
12   THRVALTHRTHRTHRTHRLYSGLYGLUASN
13   PHETHRGLUTHRASPILELYSILEMETGLU
14   ARGVALVALGLUGLNMETCYSILETHRGLN
15   TYRGLNARGGLUSERGLNALATYRTYRGLN
16   ARGGLYALASERVALASNILETHRVALLYS
17   GLNHISTHRVALTHRTHRTHRTHRLYSGLY
18   GLUASNPHETHRGLUTHRASPILELYSILE
19   METGLUARGVALVALGLUGLNMETCYSILE
20   THRGLNTYRGLNARGGLUSERGLNALATYR
21   TYRGLNARGGLYALASER

Samples:

N15_H2O: PrPWT, [U-99% 15N], 0.3 ± 3e-05 mM; Sodium acetate 10.0 ± 0.001 mM; H2O 90 ± 0.001 %; D2O 10 ± 0.001 %

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCN15_H2Oisotropiccondition1
3D 1H-15N NOESYN15_H2Oisotropiccondition1
3D 1H-15N TOCSY 20msN15_H2Oisotropiccondition1
3D 1H-15N TOCSY 50msN15_H2Oisotropiccondition1
2D 1H-1H NOESYN15_H2Oisotropiccondition1

Software:

CcpNmr_Analysis v2.2, CCPN - Assignment and NMR data analysis

Cyana v3.0, Peter Guntert - Structure calculation

Talos+ v1.0, Yang Shen - Secondary structure prediction

Topspin v3.1, Bruker - NMR data processing

NMR spectrometers:

  • Bruker Avance 950 MHz

Related Database Links:

GB CAA04276

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