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 17174

Title: MOUSE PRION PROTEIN FRAGMENT 121-231 AT 37 C   PubMed: 21987789

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

Citation: Damberger, Fred; Christen, Barbara; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt. "Cellular prion protein conformation and function."  Proc. Natl. Acad. Sci. U.S.A. 108, 17308-17313 (2011).

Assembly members:
Mouse_prion, polymer, 114 residues, Formula weight is not available

Natural source:   Common Name: House 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):
Mouse_prion: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPVDQYSNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAYYDGRRSS

Data sets:
Data typeCount
13C chemical shifts369
15N chemical shifts135
1H chemical shifts790

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mouse_prion1

Entities:

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

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

Samples:

sample_1: Mouse_prion, [U-99% 13C; U-99% 15N], 1.6 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: 310.2 K

Experiments:

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

Software:

xwinnmr, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - 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 v1.2, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

Molmol v2K.2, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 15845 16071 16075 16076 16077 16078 16079 16080 16184 16185 16722 16723 17081 17082 17084 17087 17213 17758 17759
PDB
DBJ BAA08790 BAE28320 BAE28693 BAE29994 BAE34221
EMBL CAJ18553
GB AAA39996 AAA39997 AAA39998 AAA41947 AAB30728
REF NP_001265185 NP_035300 NP_036763 XP_006235124 XP_006984054
SP P04925 P13852 Q9Z0T3