1V5O

Solution Structure of the Ubiquitin-like Domain from Mouse Hypothetical 1700011N24Rik Protein

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_13C-separated_NOESY	1.17mM Protein U-15N, 13C; 20mM Phosphate Na (pH6.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O; 10% D2O	90% H2O/10% D2O	120mM	6.0	ambient	298.0
2	3D_15N-separated_NOESY	1.17mM Protein U-15N, 13C; 20mM Phosphate Na (pH6.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O; 10% D2O	90% H2O/10% D2O	120mM	6.0	ambient	298.0

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE	800

NMR Refinement
Method	Details	Software
torsion angle dynamics		XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with the least restraint violations, target function
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	2.6	Bruker
2	processing	NMRPipe	20020425	Delaglio, F.
3	data analysis	NMRView	5.0.4	Johnson, B. A.
4	data analysis	KUJIRA	0.860	Kobayashi, N.
5	structure solution	CYANA	1.0.7	Guentert, P.
6	refinement	CYANA	1.0.7	Guentert, P.

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.