1JCU

Solution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicum

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	3mM MTH1692 U-15N; 50mM phosphate buffer; 0.15 M NaCl; 1mM DTT; 1mM NaN3	90% H2O/10% D2O	0.3M	6.0	ambient	320
2	3D_13C-separated_NOESY	3mM MTH1692 U-15N,13C; 50mM phosphate buffer; 0.15 M NaCl; 1mM DTT; 1mM NaN3	100% D2O	0.3M	6.0	ambient	320
3	2D NOESY	3mM MTH1692 unlabeled; 50mM phosphate buffer; 0.15 M NaCl; 1mM DTT; 1mM NaN3	90% H2O/10% D2O	0.3M	6.0	ambient	320
4	2D NOESY	3mM MTH1692 unlabeled; 50mM phosphate buffer; 0.15 M NaCl; 1mM DTT; 1mM NaN3	100% D2O	0.3M	6.0	ambient	320

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	UNITYPLUS	800
2	Bruker	DRX	500

NMR Refinement
Method	Details	Software
simulated annealing	The structures are based on 1467 non-redundant NOE-derived distance constraints, 197 dihedral angle restraints, and 86 hydrogen bonds.	XwinNMR

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

Additional NMR Experimental Information
Details	The structure was determined using standard triple-resonance NMR techniques.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	2.1	Bruker
2	processing	Gifa	4.31	Delsuc
3	data analysis	XEASY	1.3.13	Wuthrich
4	refinement	CNS	0.9	Brunger
5	structure solution	ARIA	0.9	Nilges

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.