BMRB Entry 10238

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR10238
MolProbity Validation Chart

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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
Deposition date:
2008-08-22
Original release date:
2009-03-19
Authors:
Li, H.; Koshiba, S.; Tochio, N.; Watanabe, S.; Harada, T.; Kigawa, T.; Yokoyama, S.
Citation:

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).
PubMed: 18650440

Assembly members:

Assembly members:
APP peptide and PID domain, polymer, 176 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis   Vector: P060710-06

Entity Sequences (FASTA):

Entity Sequences (FASTA):
APP peptide and PID domain: GSSGSSGDAAVTPEERHLSK MQQNGYENPTYKFFEQMQNS GSSGSSGSSGSSGPTPKTEL VQKFRVQYLGMLPVDRPVGM DTLNSAIENLMTSSSKEDWP SVNMNVADATVTVISEKNEE EVLVECRVRFLSFMGVGKDV HTFAFIMDTGNQRFECHVFW CEPNAANVSEAVQAAC

Data sets:
Data typeCount
13C chemical shifts696
15N chemical shifts170
1H chemical shifts1104

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1APP peptide and PID domain1

Entities:

Entity 1, APP peptide and PID domain 176 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYASPALAALA
2   VALTHRPROGLUGLUARGHISLEUSERLYS
3   METGLNGLNASNGLYTYRGLUASNPROTHR
4   TYRLYSPHEPHEGLUGLNMETGLNASNSER
5   GLYSERSERGLYSERSERGLYSERSERGLY
6   SERSERGLYPROTHRPROLYSTHRGLULEU
7   VALGLNLYSPHEARGVALGLNTYRLEUGLY
8   METLEUPROVALASPARGPROVALGLYMET
9   ASPTHRLEUASNSERALAILEGLUASNLEU
10   METTHRSERSERSERLYSGLUASPTRPPRO
11   SERVALASNMETASNVALALAASPALATHR
12   VALTHRVALILESERGLULYSASNGLUGLU
13   GLUVALLEUVALGLUCYSARGVALARGPHE
14   LEUSERPHEMETGLYVALGLYLYSASPVAL
15   HISTHRPHEALAPHEILEMETASPTHRGLY
16   ASNGLNARGPHEGLUCYSHISVALPHETRP
17   CYSGLUPROASNALAALAASNVALSERGLU
18   ALAVALGLNALAALACYS

Samples:

sample_1: APP peptide and PID domain, [U-13C; U-15N], 1.04 mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 296 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20031121, Delaglio, F - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.9820, Kobayashi, N. - data analysis

CYANA v2.0.17, Guentert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 900 MHz

Related Database Links:

BMRB 10235
PDB
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
AlphaFold Q9DBR4

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks