2ROZ

Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D 1H-15N NOESY	0.37mM [U-13C; U-15N] Fe65L1 PID2, 0.37mM APP-derived 32-mer peptide	90% H2O/10% D2O	0.120	7.0	ambient	296
2	3D 1H-13C NOESY	0.37mM [U-13C; U-15N] Fe65L1 PID2, 0.37mM APP-derived 32-mer peptide	90% H2O/10% D2O	0.120	7.0	ambient	296
3	3D_13C,15N F1-FILTERED 13C F3-EDITED NOESY	0.37mM [U-13C; U-15N] Fe65L1 PID2, 0.37mM APP-derived 32-mer peptide	90% H2O/10% D2O	0.120	7.0	ambient	296
4	3D_13C,15N F1-FILTERED 15N F3-EDITED NOESY	0.37mM [U-13C; U-15N] Fe65L1 PID2, 0.37mM APP-derived 32-mer peptide	90% H2O/10% D2O	0.120	7.0	ambient	296
5	2D_F2 13C,15N- FILTERED NOESY	0.37mM [U-13C; U-15N] Fe65L1 PID2, 0.37mM APP-derived 32-mer peptide	90% H2O/10% D2O	0.120	7.0	ambient	296

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE	900

NMR Refinement
Method	Details	Software
torsion angle dynamics		XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	target function
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	1 (fewest violations)

Additional NMR Experimental Information
Details	The experiments of the conventional NOESY spectra, 3D 1H-15N NOESY and 3D 1H-13C NOESY, are conducted at 900 MHZ BRUKER AVANCE machine. However, the other three filter-related experiments, 3D_13C,15N F1-FILTERED 13C F3-EDITED NOESY, 3D_13C,15N F1-FILTERED 15N F3-EDITED NOESY, and 2D_F2 13C,15N- FILTERED NOESY, are conducted at 800 MHZ BRUKER AVANCE machine.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	3.5	Bruker
2	processing	NMRPipe	20031121	Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
3	data analysis	NMRView	5.0.4	Johnson, One Moon Scientific
4	data analysis	KUJIRA	0.9820	Kobayashi, N.
5	structure solution	CYANA	1.0.8	Herrmann, Guntert and Wuthrich
6	refinement	CYANA	1.0.8	Herrmann, Guntert and Wuthrich

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.