BMRB: 10238

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

Authors

Li, H., Koshiba, S., Tochio, N., Watanabe, S., Harada, T., Kigawa, T., Yokoyama, S.

Assembly

Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2

Entity

1. Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2 (polymer, Thiol state: all free), 176 monomers, 19149.07 Da Detail

GSSGSSGDAA VTPEERHLSK MQQNGYENPT YKFFEQMQNS GSSGSSGSSG SSGPTPKTEL VQKFRVQYLG MLPVDRPVGM DTLNSAIENL MTSSSKEDWP SVNMNVADAT VTVISEKNEE EVLVECRVRF LSFMGVGKDV HTFAFIMDTG NQRFECHVFW CEPNAANVSE AVQAAC

Formula weight

19149.07 Da

Source organism

Mus musculus

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 92.0 %, Completeness: 92.7 %, Completeness (bb): 90.1 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	92.7 % (1807 of 1949)	93.3 % (940 of 1008)	92.7 % (697 of 752)	89.9 % (170 of 189)
Backbone	90.1 % (937 of 1040)	89.9 % (322 of 358)	90.7 % (466 of 514)	88.7 % (149 of 168)
Sidechain	95.3 % (1021 of 1071)	95.1 % (618 of 650)	95.5 % (382 of 400)	100.0 % (21 of 21)
Aromatic	95.3 % (143 of 150)	97.3 % (73 of 75)	93.2 % (68 of 73)	100.0 % (2 of 2)
Methyl	97.4 % (150 of 154)	97.4 % (75 of 77)	97.4 % (75 of 77)

1. APP peptide and PID domain

GSSGSSGDAA VTPEERHLSK MQQNGYENPT YKFFEQMQNS GSSGSSGSSG SSGPTPKTEL VQKFRVQYLG MLPVDRPVGM DTLNSAIENL MTSSSKEDWP SVNMNVADAT VTVISEKNEE EVLVECRVRF LSFMGVGKDV HTFAFIMDTG NQRFECHVFW CEPNAANVSE AVQAAC

Show sample condition

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 (±0.001) atm, Temperature 296 (±0.1) K, pH 7.0 (±0.05)

#	Name	Isotope labeling	Type	Concentration
1	APP peptide and PID domain	[U-13C; U-15N]	protein	1.04 mM
2	d-Tris-HCl		buffer	20 mM
3	NaCl		salt	100 mM
4	d-DTT		salt	1 mM
5	NaN3		salt	0.02 %
6	H2O		solvent	90 %
7	D2O		solvent	10 %

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LACS Plot; CA

Referencing offset: -0.09 ppm, Outliers: 2 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CB

Referencing offset: -0.09 ppm, Outliers: 2 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; HA

Referencing offset: -0.03 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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LACS Plot; CO

Referencing offset: 0.13 ppm, Outliers: 1 Detail

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Chemical shift reference

Atom type	Mol. common name	Atom group	Value	Ref. method	Ref. type	Shift ratio
13C	DSS	methyl protons	0.0 ppm	null	indirect	0.2514495
1H	DSS	methyl protons	0.0 ppm	null	indirect	1.0
15N	DSS	methyl protons	0.0 ppm	null	indirect	0.1013291

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Protein Blocks Logo

Calculated from 20 models in PDB: 2YT0, Strand ID: A Detail

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Release date

2009-03-18

Citation

Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 complexed with the cytoplasmic tail of amyloid precursor protein reveals a novel peptide binding mode
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.
J. Biol. Chem. (2008), 283, 27165-27178, PubMed 18650440 , DOI 10.1074/jbc.M803892200 , Abstract

Related entities 1. Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2, : 1 : 6 entities Detail

Experiments performed 2 experiments Detail