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 17087

Title: Mouse prion protein (121-231) with the mutations Y169A, Y225A, and Y226A.

Authors: Christen, Barbara; Damberger, Fred; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt

Citation: Christen, Barbara; Damberger, Fred; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt. "Temperature-dependent conformational exchange in the cellular form of prion proteins"  J. Mol. Biol. ., .-..

Assembly members:
Prion with Y169A, Y225A, Y226A mutation, polymer, 114 residues, Formula weight is not available

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

Entity Sequences (FASTA):
Prion with Y169A, Y225A, Y226A mutation: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQASNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAAADGRRSS

Data sets:
Data typeCount
13C chemical shifts363
15N chemical shifts135
1H chemical shifts784

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1prion1

Entities:

Entity 1, prion 114 residues - Formula weight is not available

1   GLYSERVALVALGLYGLYLEUGLYGLYTYR
2   METLEUGLYSERALAMETSERARGPROMET
3   ILEHISPHEGLYASNASPTRPGLUASPARG
4   TYRTYRARGGLUASNMETTYRARGTYRPRO
5   ASNGLNVALTYRTYRARGPROVALASPGLN
6   ALASERASNGLNASNASNPHEVALHISASP
7   CYSVALASNILETHRILELYSGLNHISTHR
8   VALTHRTHRTHRTHRLYSGLYGLUASNPHE
9   THRGLUTHRASPVALLYSMETMETGLUARG
10   VALVALGLUGLNMETCYSVALTHRGLNTYR
11   GLNLYSGLUSERGLNALAALAALAASPGLY
12   ARGARGSERSER

Samples:

sample_1: prion, [U-99% 13C; U-99% 15N], 1.4 mM; sodium acetate, [U-2H], 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.2 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking

DYANA v1.0.3, Guntert, Mumenthaler and Wuthrich - structure solution

OPALP, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 900 MHz
  • Bruker DRX 750 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 16075 16184 17081 17084 17174 17213 17758
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