BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15399

Title: NMR structure of rabbit prion protein mutation I214V   PubMed: 20949107

Authors: Li, Jun; Lin, Donghai

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).

Assembly members:
rpp I214V, polymer, 138 residues, 12471.928 Da.

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

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

Entity Sequences (FASTA):
rpp I214V: QGGTHNQWGKPSKPKTSMKH VAGAAAAGAVVGGLGGYMLG SAMSRPLIHFGNDYEDRYYR ENMYRYPNQVYYRPVDQYSN QNSFVHDCVNITVKQHTVTT TTKGENFTETDIKIMERVVE QMCVTQYQQESQAAYQRA

Data sets:
Data typeCount
13C chemical shifts532
15N chemical shifts156
1H chemical shifts926

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1rpp I214V1

Entities:

Entity 1, rpp I214V 138 residues - 12471.928 Da.

1   GLNGLYGLYTHRHISASNGLNTRPGLYLYS
2   PROSERLYSPROLYSTHRSERMETLYSHIS
3   VALALAGLYALAALAALAALAGLYALAVAL
4   VALGLYGLYLEUGLYGLYTYRMETLEUGLY
5   SERALAMETSERARGPROLEUILEHISPHE
6   GLYASNASPTYRGLUASPARGTYRTYRARG
7   GLUASNMETTYRARGTYRPROASNGLNVAL
8   TYRTYRARGPROVALASPGLNTYRSERASN
9   GLNASNSERPHEVALHISASPCYSVALASN
10   ILETHRVALLYSGLNHISTHRVALTHRTHR
11   THRTHRLYSGLYGLUASNPHETHRGLUTHR
12   ASPILELYSILEMETGLUARGVALVALGLU
13   GLNMETCYSVALTHRGLNTYRGLNGLNGLU
14   SERGLNALAALATYRGLNARGALA

Samples:

sample_1: rpp I214V, [U-13C; U-15N], 0.7 – 0.8 mM; sodium acetate 20 mM

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298.13 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O, . - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15394 16328 16616
PDB
GB AAC48697 AAD01554 ABL75505 AEM44421 AEM44422
REF NP_001075490 XP_008254357 XP_008254358
SP Q95211