BMRB Entry 10239
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PDB ID: 2yt1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10239
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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
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 725 |
15N chemical shifts | 179 |
1H chemical shifts | 1152 |
Additional metadata:
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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