Experiment: 1N7T

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	2 mM Erbin PDZ (15N) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	90% H2O, 10% D20	250 mM	6.5	1 atm	298
2	HNHA	2 mM Erbin PDZ (15N) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	90% H2O, 10% D20	250 mM	6.5	1 atm	298
3	3D HNHB	2 mM Erbin PDZ (15N) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	90% H2O, 10% D20	250 mM	6.5	1 atm	298
4	3D 15N-separated low mixing time TOCSY	2 mM Erbin PDZ (15N) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	90% H2O, 10% D20	250 mM	6.5	1 atm	298
5	2D-15N-filtered NOESY	2 mM Erbin PDZ (15N) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	90% H2O, 10% D20	250 mM	6.5	1 atm	298
6	3D_13C-separated_NOESY	2 mM Erbin PDZ (15N,13C) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	100% D2O	250 mM	6.5	1 atm	298
7	3D-13_filtered, 13C-edited NOESY	2 mM Erbin PDZ (15N,13C) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	100% D2O	250 mM	6.5	1 atm	298
8	2D-13C-filtered NOESY	2 mM Erbin PDZ (15N,13C) + 2.2 mM peptide; 25 mM sodium phosphate pH 6.5; 50 mM sodium chloride	100% D2O	250 mM	6.5	1 atm	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, simulated annealing	The complex was determined using a total of 1717 NOE distance restraints (148 intra residue, 339 sequential, 328 medium range, 699 long-range and 203 intermolecular), 36 hydrogen bond restraints, 156 dihedral angle restraints (86 phi, 44 psi and 26 chi-1) and 82 15N residual dipolar coupling restraints. The best 20 conformers (of 100) had no distance violations greater than 0.12A and no dihedral angle violations greater than 3.0 degrees. RMSD from experimental distance restraints was 0.0055+/-0.0007. The mean backbone rmsd from the mean structure was 0.40+/- 0.05 A for N, Ca and C atoms of residues 10-100. 74% (25%) of residues were in the most favoured (allowed) region of phi/psi space; no residues were in the disallowed region.	XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	least violation of experimental restraints
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	2 (closest to the average)

Additional NMR Experimental Information
Details	The resonance assignments were determined using triple-resonance NMR spectroscopy.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	3.1	bruker
2	data analysis	Felix	98	Accelrys
3	refinement	CNS	2000.1	Accelrys

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.