BMRB Entry 25250

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25250
MolProbity Validation Chart

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Title:
Solution structure of Ovis Aries PrP with mutation delta190-197
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 PrP helix 2 deletion mutants"  .

Assembly members:

Assembly members:
PrPdelta190-197, polymer, 146 residues, 16655.6213 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):
PrPdelta190-197: MGSSHHHHHHSSGLVPRGSH MSNKPSKPKTNMKHVAGAAA AGAVVGGLGGYMLGSVMSRP LIHFGNDYEDRYYRENMYRY PNQVYYRPVDQYSNQNNFVH DCVNITVKQGENFTETDIKI MERVVEQMCITQYQRESQAY YQRGAS

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts141
1H chemical shifts898

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 146 residues - 16655.6213 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERASNLYSPROSERLYSPROLYSTHR
4   ASNMETLYSHISVALALAGLYALAALAALA
5   ALAGLYALAVALVALGLYGLYLEUGLYGLY
6   TYRMETLEUGLYSERVALMETSERARGPRO
7   LEUILEHISPHEGLYASNASPTYRGLUASP
8   ARGTYRTYRARGGLUASNMETTYRARGTYR
9   PROASNGLNVALTYRTYRARGPROVALASP
10   GLNTYRSERASNGLNASNASNPHEVALHIS
11   ASPCYSVALASNILETHRVALLYSGLNGLY
12   GLUASNPHETHRGLUTHRASPILELYSILE
13   METGLUARGVALVALGLUGLNMETCYSILE
14   THRGLNTYRGLNARGGLUSERGLNALATYR
15   TYRGLNARGGLYALASER

Samples:

sample_1: PrPdelta190-197, [U-99% 13C; U-99% 15N], 0.35 ± 2e-05 mM; Sodium acetate 10.00 ± 0.001 mM; H2O 90 ± 0.001 mM; D2O 10 ± 0.001 mM

sample_2: PrPdelta190-197, [U-99% 15N], 0.45 ± 2e-05 mM; Sodium acetate 10.00 ± 0.001 mM; H2O 90 ± 0.001 mM; D2O 10 ± 0.001 mM

sample_3: PrPdelta190-197, [U-99% 13C; U-99% 15N], 0.35 ± 0.02 mM; Sodium acetate 10.00 ± 0.1 mM; D2O 100 ± 0.001 mM

Condition1: ionic strength: 0 M; pH: 5.300; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicCondition1
3D HNCOsample_1isotropicCondition1
3D HNCAsample_1isotropicCondition1
3D HN(CO)CAsample_1isotropicCondition1
3D CBCA(CO)NHsample_1isotropicCondition1
3D 1H-15N NOESYsample_1isotropicCondition1
2D 1H-1H NOESYsample_2isotropicCondition1
2D 1H-15N HSQCsample_2isotropicCondition1
2D 1H-13C HSQCsample_1isotropicCondition1
3D hCCH-TOCSYsample_1isotropicCondition1
2D 1H-13C HSQCsample_3isotropicCondition1
3D hCCH-TOCSYsample_3isotropicCondition1
2D 1H-1H NOESYsample_3isotropicCondition1
2D 1H-13C HSQCsample_3isotropicCondition1
3D aromatic HCCH-TOCSYsample_3isotropicCondition1
3D 1H-13C NOESYsample_3isotropicCondition1

Software:

CYANA v3.0, Peter Guntert - Structure calculation

CcpNmr_Analysis v2.2, CCPN - Assignment

Talos+ v1.0, Yang Shen - Dihedral angles

Topspin v3.1, Bruker - collection, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 950 MHz

Related Database Links:

GenBank CAA04276
GB AJ000738.1

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