BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 10239

Title: Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L   PubMed: 18650440

Deposition date: 2008-08-22 Original release date: 2009-03-19

Authors: Li, H.; Koshiba, S.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.

Citation: Li, H.; Koshiba, S.; Hayashi, F.; Tochio, N.; Tomozawa, T.; Kasai, T.; Yabuki, T.; Motoda, Y.; Harada, T.; Watanabe, S.; Inoue, M.; Hayashizaki, Y.; Tanaka, A.; Kigawa, T.; Yokoyama, S.. "Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode"  J. Biol. Chem. 283, 27165-27178 (2008).

Assembly members:
APP peptide and PID domain, polymer, 185 residues, Formula weight is not available

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
APP peptide and PID domain: GSSGSSGDAAVTPEERHLSK MQQNGYENPTYKFFEQMQNS GPSSGIEGRGSSGSSGSSGS SGPTPKTELVQKFRVQYLGM LPVDRPVGMDTLNSAIENLM TSSSKEDWPSVNMNVADATV TVISEKNEEEVLVECRVRFL SFMGVGKDVHTFAFIMDTGN QRFECHVFWCEPNAANVSEA VQAAC

Data sets:
Data typeCount
13C chemical shifts725
15N chemical shifts179
1H chemical shifts1152

Additional metadata:

  • Assembly
  • Samples and Experiments
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  • Spectrometers
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Related Database Links:

BMRB 10235
PDB 1WGU 2ROZ 2YT1
DBJ BAB23568 BAE31851 BAE39700 BAE41482 BAE42990
GB AAH76587 EDL37768 EDL90042 EGW02447 ERE91473
REF NP_001188342 NP_001188343 NP_001188344 NP_001188345 NP_001297555
SP Q9DBR4

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