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 16184

Title: Mouse Prion Protein (121-231) with Mutations Y225A and Y226A   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, 13167.715 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 NQVYYRPVDQYSNQNNFVHD CVNITIKQHTVTTTTKGENF TETDVKMMERVVEQMCVTQY QKESQAAADGRRSS

Data sets:
Data typeCount
13C chemical shifts364
15N chemical shifts135
1H chemical shifts412

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 - 13167.715 Da.

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

Samples:

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

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
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_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

xwinnmr, Bruker Biospin - collection, processing

NMR spectrometers:

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

Related Database Links:

BMRB 15845 16071 16076 16077 16078 16079 16080 16185 16722 17081 17082 17084 17087 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