BMRB: 10237

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

Authors

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

Assembly

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

Entity

1. Amyloid beta A4 precursor protein-binding family B member 2 and Amyloid beta A4 protein (polymer, Thiol state: all free), 185 monomers, 19989.95 Da Detail

GSSGSSGPTP KTELVQKFRV QYLGMLPVDR PVGMDTLNSA IENLMTSSSK EDWPSVNMNV ADATVTVISE KNEEEVLVEC RVRFLSFMGV GKDVHTFAFI MDTGNQRFEC HVFWCEPNAA NVSEAVQAAC SGPSSGIEGR GSSGSSGSSG SSGDAAVTPE ERHLSKMQQN GYENPTYKFF EQMQN

Formula weight

19989.95 Da

Source organism

Mus musculus

Exptl. method

solution NMR

Refine. method

torsion angle dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 94.1 %, Completeness: 93.0 %, Completeness (bb): 91.5 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	93.0 % (1892 of 2035)	92.4 % (974 of 1054)	93.6 % (734 of 784)	93.4 % (184 of 197)
Backbone	91.5 % (999 of 1092)	90.7 % (343 of 378)	91.6 % (493 of 538)	92.6 % (163 of 176)
Sidechain	94.6 % (1051 of 1111)	93.3 % (631 of 676)	96.4 % (399 of 414)	100.0 % (21 of 21)
Aromatic	92.0 % (138 of 150)	89.3 % (67 of 75)	94.5 % (69 of 73)	100.0 % (2 of 2)
Methyl	98.1 % (155 of 158)	97.5 % (77 of 79)	98.7 % (78 of 79)

1. PID domain and APP peptide

GSSGSSGPTP KTELVQKFRV QYLGMLPVDR PVGMDTLNSA IENLMTSSSK EDWPSVNMNV ADATVTVISE KNEEEVLVEC RVRFLSFMGV GKDVHTFAFI MDTGNQRFEC HVFWCEPNAA NVSEAVQAAC SGPSSGIEGR GSSGSSGSSG SSGDAAVTPE ERHLSKMQQN GYENPTYKFF EQMQN

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	PID domain and APP peptide	[U-13C; U-15N]	protein	1.00 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: -0.12 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; CB

Referencing offset: -0.12 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; HA

Referencing offset: -0.02 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: 0.09 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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Protein Blocks Logo

Calculated from 20 models in PDB: 2YSZ, 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

Entries sharing articles BMRB: 4 entries Detail

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

Experiments performed 2 experiments Detail