BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15394

Title: NMR structure of rabbit prion protein mutation S173N   PubMed: 20639199

Authors: Li, Jun; Lin, Donghai

Citation: Wen, Yi; Li, Jun; Yao, Wenming; Xiong, Minqian; Hong, Jing; Peng, Yu; Xiao, Gengfu; Lin, Donghai. "Unique structural characteristics of the rabbit prion protein."  J. Biol. Chem. 285, 31682-31693 (2010).

Assembly members:
rpp mutation S173N, polymer, 138 residues, 12512.979 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 mutation S173N: QGGTHNQWGKPSKPKTSMKH VAPAAAAGAVVGGLGGYMLG SAMSRPLIHFGNDYEDRYYR ENMYRYPNQVYYRPVDQYSN QNNFVHDCVNITVKQHTVTT TTKGENFTETDIKIMERVVE QMCITQYQQESQAAYQRA

Data sets:
Data typeCount
13C chemical shifts317
15N chemical shifts125
1H chemical shifts715

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1single chain polymers1

Entities:

Entity 1, single chain polymers 138 residues - 12512.979 Da.

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

Samples:

sample_1: rpp S173N, [U-13C; U-15N], 0.8 – 1 mM; sodium acetate 20 mM

sample_2: rpp S173N, [U-15N], 0.8 – 1 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
3D HNCACBsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O, . - structure solution

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15399 16328 16616
PDB
EMBL CBK44083
GB AAC48697 AAD01554 AAQ81748 AAQ81756 ABL75505
REF NP_001075490 XP_008254357 XP_008254358
SP Q95211