Experiment: 2JOA

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	2 mM [U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
2	3D HNCA	2 mM [U-13C; U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
3	3D HNCO	2 mM [U-13C; U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
4	3D HNCACB	2 mM [U-13C; U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
5	3D CBCA(CO)NH	2 mM [U-13C; U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
6	3D HN(CO)CA	2 mM [U-13C; U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
7	2D 1H-13C HSQC	2 mM [U-10% 13C; U-99% 15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	100% D2O	0.025	6.0	ambient	298
8	3D 1H-15N NOESY	2 mM [U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
9	3D 1H-13C NOESY	2 mM [U-13C; U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	100% D2O	0.025	6.0	ambient	298
10	3D HCCH-TOCSY	2 mM [U-13C; U-15N] HtrA1-PDZ, 4 mM synthetic peptide H1-C1	100% D2O	0.025	6.0	ambient	298
11	2D 1H-1H NOESY 13C,15N-filtered in F1	2 mM [U-13C; U-15N] HtrA1-PDZ, 1.8 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
12	2D 1H-1H TOCSY,13C,15N-filtered in F1	2 mM [U-13C; U-15N] HtrA1-PDZ, 1.8 mM synthetic peptide H1-C1	90% H2O/10% D2O	0.025	6.0	ambient	298
13	3D 1H-13C NOESY, 13C-filtered in F1	2 mM [U-13C; U-15N] HtrA1-PDZ, 1.8 mM synthetic peptide H1-C1	100% D2O	0.025	6.0	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	600
2	Bruker	DRX	800

NMR Refinement
Method	Details	Software
torsion angle dynamics	followed by cartesian dynamics and minimization	NMRPipe

NMR Ensemble Information
Conformer Selection Criteria	structures with the least restraint violations
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	NMRPipe	2005 for LINUX	Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
2	data analysis	Sparky	3.11	Goddard
3	chemical shift assignment	Monte	2.02	Hitchens, T.K., Lukin, J.A., Zhan, Y. and Rule, G.S.
4	automated noe assignment	CYANA	2.0	Guntert, Mumenthaler and Wuthrich
5	collection	TopSpin	1.3	Bruker Biospin
6	dihedral angle restraints	TALOS		Cornilescu, Delaglio and Bax
7	structure solution	CNX	2002	Accelrys Software Inc.
8	refinement	CNX	2002	Accelrys Software Inc.

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.