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 16723

Title: mPrP_D1567D_N173K   PubMed: 20460128

Authors: Perez, Daniel; Damberger, Fred; Wuthrich, Kurt

Citation: Perez, Daniel; Damberger, Fred; Wuthrich, Kurt. "Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein."  J. Mol. Biol. 400, 121-128 (2010).

Assembly members:
mouse prion protein double mutant D167S, N173K, polymer, 113 residues, 13203.797 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

Entity Sequences (FASTA):
mouse prion protein double mutant D167S, N173K: SVVGGLGGYMLGSAMSRPMI HFGNDWEDRYYRENMYRYPN QVYYRPVSQYSNQKNFVHDC VNITIKQHTVTTTTKGENFT ETDVKMMERVVEQMCVTQYQ KESQAYYDGRRSS

Data sets:
Data typeCount
13C chemical shifts370
15N chemical shifts133
1H chemical shifts794

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1mouse prion protein double mutant D167S, N173K1

Entities:

Entity 1, mouse prion protein double mutant D167S, N173K 113 residues - 13203.797 Da.

1   SERVALVALGLYGLYLEUGLYGLYTYRMET
2   LEUGLYSERALAMETSERARGPROMETILE
3   HISPHEGLYASNASPTRPGLUASPARGTYR
4   TYRARGGLUASNMETTYRARGTYRPROASN
5   GLNVALTYRTYRARGPROVALSERGLNTYR
6   SERASNGLNLYSASNPHEVALHISASPCYS
7   VALASNILETHRILELYSGLNHISTHRVAL
8   THRTHRTHRTHRLYSGLYGLUASNPHETHR
9   GLUTHRASPVALLYSMETMETGLUARGVAL
10   VALGLUGLNMETCYSVALTHRGLNTYRGLN
11   LYSGLUSERGLNALATYRTYRASPGLYARG
12   ARGSERSER

Samples:

sample_1: sodium acetate, [U-2H], 10 ± 1 mM; H2O 90%; D2O 10%; entity 1.3 mM

sample_conditions_1: ionic strength: 10 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

ATHNOS-CANDID, Herrmann and Wuthrich - automatic peak picking and NOE assignment

NMR spectrometers:

  • Bruker DRX 750 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 15845 16071 16076 16077 16078 16079 16080 16185 16722 17081 17082 17084 17174 17213 17758
PDB
DBJ BAE34221 BAE34724 BAE34788 BAE34911 BAE35622
EMBL CAJ18553
GB AAA39997 AAC02804 AAD19985 AAH06703 AAL57230
REF NP_001265185 NP_035300
SP P04925