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 16077

Title: Mouse prion protein fragment mPrP[P105L](91-231) at pH 7.0   PubMed: 19546219

Deposition date: 2008-12-22 Original release date: 2009-06-26

Authors: Damberger, Fred; Wuthrich, Kurt; Hornemann, Simone; von Schroetter, Christine

Citation: Hornemann, Simone; von Schroetter, Christine; Damberger, Fred; Wuthrich, Kurt. "Prion protein-detergent micelle interactions studied by NMR in solution."  J. Biol. Chem. 284, 22713-22721 (2009).

Assembly members:
mPrP90_P105L, polymer, 141 residues, 16141.9 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
mPrP90_P105L: QGGGTHNQWNKPSKLKTNLK HVAGAAAAGAVVGGLGGYML GSAMSRPMIHFGNDWEDRYY RENMYRYPNQVYYRPVDQYS NQNNFVHDCVNITIKQHTVT TTTKGENFTETDVKMMERVV EQMCVTQYQKESQAYYDGRR S

Data sets:
Data typeCount
13C chemical shifts268
15N chemical shifts127
1H chemical shifts127

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1mPrP90_P105L1

Entities:

Entity 1, mPrP90_P105L 141 residues - 16141.9 Da.

1   GLNGLYGLYGLYTHRHISASNGLNTRPASN
2   LYSPROSERLYSLEULYSTHRASNLEULYS
3   HISVALALAGLYALAALAALAALAGLYALA
4   VALVALGLYGLYLEUGLYGLYTYRMETLEU
5   GLYSERALAMETSERARGPROMETILEHIS
6   PHEGLYASNASPTRPGLUASPARGTYRTYR
7   ARGGLUASNMETTYRARGTYRPROASNGLN
8   VALTYRTYRARGPROVALASPGLNTYRSER
9   ASNGLNASNASNPHEVALHISASPCYSVAL
10   ASNILETHRILELYSGLNHISTHRVALTHR
11   THRTHRTHRLYSGLYGLUASNPHETHRGLU
12   THRASPVALLYSMETMETGLUARGVALVAL
13   GLUGLNMETCYSVALTHRGLNTYRGLNLYS
14   GLUSERGLNALATYRTYRASPGLYARGARG
15   SER

Samples:

sample_1: mPrP90_P105L, [U-99% 13C; U-99% 15N], 1.2 ± 0.05 mM; sodium phosphate buffer 5 mM

sample_conditions_1: ionic strength: 0.03 M; pH: 7.0; pressure: 1 atm; temperature: 293.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CARA v1.8, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

GB AAA39997

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