1V60

Solution structure of BolA1 protein from Mus musculus

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	0.5mM U-13C,15N BolA1; 20mM sodium phosphate buffer, 100mM sodium chloride, 0.02% sodium azide, 1mM d-DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100mM	6.0	ambient	298
2	3D_13C-separated_NOESY	0.5mM U-13C,15N BolA1; 20mM sodium phosphate buffer, 100mM sodium chloride, 0.02% sodium azide, 1mM d-DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100mM	6.0	ambient	298

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

NMR Refinement
Method	Details	Software
simulated annealing, torsion angle dynamics	The structure are based on 3720 NOESY cross-peaks, 91 dihedral angle restraints and 22 hydrogen bond restraints.	NMRPipe

NMR Ensemble Information
Conformer Selection Criteria	target function
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 triple-resonance NMR spectroscopy.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	NMRPipe	2.1	Delaglio
2	data analysis	NMRView	5.0.4	Johnson
3	structure solution	CYANA	1.0.7	Guentert
4	refinement	CYANA	1.0.7	Guentert

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.