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 16185

Title: Mouse Prion Protein (121-231) with Mutation V166A   PubMed: 19393664

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

Citation: Christen, Barbara; Hornemann, Simone; Damberger, Fred; Wuthrich, Kurt. "Prion Protein NMR Structure from Tammar Wallaby (Macropus eugenii) Shows that the beta2-alpha2 Loop Is Modulated by Long-Range Sequence Effects"  J. Mol. Biol. ., .-. (2009).

Assembly members:
mpp_121-231, polymer, 114 residues, 13380.906 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):
mpp_121-231: GSVVGGLGGYMLGSAMSRPM IHFGNDWEDRYYRENMYRYP NQVYYRPADQYSNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAYYDGRRSS

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts135
1H chemical shifts422

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1mpp_121-2311

Entities:

Entity 1, mpp_121-231 114 residues - 13380.906 Da.

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

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1.4 mM; sodium acetate, [U-100% 2H], 10 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.1 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

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, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 15845 16071 16075 16076 16077 16078 16079 16080 16184 16722 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