Experiment: 1POZ

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	1 mM [U-13C; U-15N] protein	95% H2O/5% D2O	<5mM	6.5	ambient	298
2	2D NOESY	1 mM protein	95% H2O/5% D2O	<5mM	6.5	ambient	298
3	2D NOESY	1 mM protein	100% D2O	<5mM	6.5	ambient	298
4	2D TOCSY	1 mM protein	95% H2O/5% D2O	<5mM	6.5	ambient	298
5	HMQC-J	1 mM [U-15N] protein	95% H2O/5% D2O	<5mM	6.5	ambient	298
6	CBCA(CO)NH	1 mM [U-13C; U-15N] protein	95% H2O/5% D2O	<5mM	6.5	ambient	298
7	NH-Exchange HSQC	1 mM [U-15N] protein	100% D2O	<5mM	6.5	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	GE	OMEGA	750
2	GE	OMEGA	600
3	GE	OMEGA	500

NMR Refinement
Method	Details	Software
torsion angle dynamics simulated annealing refinement by molecular dynamics	The structures are calculated from 2271 restraints, 2168 are NOE based, 47 dihedral constraints and 56 distance restraints from hydrogen bonds	CNS

NMR Ensemble Information
Conformer Selection Criteria	structures with the least restraint violations,structures with the lowest energy,target function
Conformers Calculated Total Number	500
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	CNS	1.1	Brunger, A.T.
2	processing	Felix	2.3	MSI, San Diego
3	structure solution	SOPHIE	1.0	Pickford, A.R.
4	data analysis	Sparky	2.0	Goddard, T.D.
5	data analysis	XEASY	3.13	Xia, T
6	refinement	SOPHIE	1.0	Pickford, A.R.

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 R01GM157729.