BMRB Entry 16616

Title:
assignment for the I214V variant of rabbit prion protein (91-228)
Deposition date:
2009-11-24
Original release date:
2010-10-13
Authors:
Li, Jun; Wen, Yi; Lin, Donghai
Citation:

Citation: Wen, Yi; Li, Jun; Xiong, Minqian; Peng, Yu; Yao, Wenming; Hong, Jing; Lin, Donghai. "Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein."  PLoS ONE 5, e13273-. (2010).
PubMed: 20949107

Assembly members:

Assembly members:
prion, polymer, 145 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: rabbit   Taxonomy ID: 9986   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Oryctolagus cuniculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET30a

Data sets:
Data typeCount
13C chemical shifts362
15N chemical shifts139
1H chemical shifts874

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1peptide chain1

Entities:

Entity 1, peptide chain 145 residues - Formula weight is not available

The first residue (M) and the last six residues (His tag) come from the vector of pET30a.

1   METGLNGLYGLYTHRHISASNGLNTRPGLY
2   LYSPROSERLYSPROLYSTHRSERMETLYS
3   HISVALALAGLYALAALAALAALAGLYALA
4   VALVALGLYGLYLEUGLYGLYTYRMETLEU
5   GLYSERALAMETSERARGPROLEUILEHIS
6   PHEGLYASNASPTYRGLUASPARGTYRTYR
7   ARGGLUASNMETTYRARGTYRPROASNGLN
8   VALTYRTYRARGPROVALASPGLNTYRSER
9   ASNGLNASNSERPHEVALHISASPCYSVAL
10   ASNILETHRVALLYSGLNHISTHRVALTHR
11   THRTHRTHRLYSGLYGLUASNPHETHRGLU
12   THRASPILELYSILEMETGLUARGVALVAL
13   GLUGLNMETCYSVALTHRGLNTYRGLNGLN
14   GLUSERGLNALAALATYRGLNARGALAHIS
15   HISHISHISHISHIS

Samples:

sample_1: prion, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; sodium acetate 20 mM

sample_conditions_1: ionic strength: 0.04 M; pH: 4.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian Unity 600 MHz

Related Database Links:

BMRB 15394 15399 16328
PDB
GB AAC48697 AAD01554 ABL75505 AEM44421 AEM44422
REF NP_001075490 XP_008254357 XP_008254358
SP Q95211
AlphaFold Q95211

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