BMRB Entry 10237

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR10237
MolProbity Validation Chart

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

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:
PID domain and APP peptide, polymer, 185 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: P060710-04

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PID domain and APP peptide: GSSGSSGPTPKTELVQKFRV QYLGMLPVDRPVGMDTLNSA IENLMTSSSKEDWPSVNMNV ADATVTVISEKNEEEVLVEC RVRFLSFMGVGKDVHTFAFI MDTGNQRFECHVFWCEPNAA NVSEAVQAACSGPSSGIEGR GSSGSSGSSGSSGDAAVTPE ERHLSKMQQNGYENPTYKFF EQMQN

Data sets:
Data typeCount
13C chemical shifts727
15N chemical shifts178
1H chemical shifts1148

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PID domain and APP peptide1

Entities:

Entity 1, PID domain and APP peptide 185 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYPROTHRPRO
2   LYSTHRGLULEUVALGLNLYSPHEARGVAL
3   GLNTYRLEUGLYMETLEUPROVALASPARG
4   PROVALGLYMETASPTHRLEUASNSERALA
5   ILEGLUASNLEUMETTHRSERSERSERLYS
6   GLUASPTRPPROSERVALASNMETASNVAL
7   ALAASPALATHRVALTHRVALILESERGLU
8   LYSASNGLUGLUGLUVALLEUVALGLUCYS
9   ARGVALARGPHELEUSERPHEMETGLYVAL
10   GLYLYSASPVALHISTHRPHEALAPHEILE
11   METASPTHRGLYASNGLNARGPHEGLUCYS
12   HISVALPHETRPCYSGLUPROASNALAALA
13   ASNVALSERGLUALAVALGLNALAALACYS
14   SERGLYPROSERSERGLYILEGLUGLYARG
15   GLYSERSERGLYSERSERGLYSERSERGLY
16   SERSERGLYASPALAALAVALTHRPROGLU
17   GLUARGHISLEUSERLYSMETGLNGLNASN
18   GLYTYRGLUASNPROTHRTYRLYSPHEPHE
19   GLUGLNMETGLNASN

Samples:

sample_1: PID domain and APP peptide, [U-13C; U-15N], 1.00 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