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 16722

Title: mPrP_D167S   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 QVYYRPVSQYSNQNNFVHDC VNITIKQHTVTTTTKGENFT ETDVKMMERVVEQMCVTQYQ KESQAYYDGRRSS

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts134
1H chemical shifts790

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   SERASNGLNASNASNPHEVALHISASPCYS
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 16075 16076 16077 16078 16079 16080 16184 16185 16723 17081 17082 17084 17174 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
SP P04925 P13852 Q9Z0T3