1SSU

Structural and biochemical evidence for disulfide bond heterogeneity in active forms of the somatomedin B domain of human vitronectin

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D NOESY	N15-labeled protein 20 mM sodium phosphate pH 7.5	90% H2O/10% D2O	180 mM	7.5	1 atm	293
2	2D TOCSY	N15-labeled protein 20 mM sodium phosphate pH 7.5	90% H2O/10% D2O	180 mM	7.5	1 atm	293
3	3D_15N-separated_NOESY	N15-labeled protein 20 mM sodium phosphate pH 7.5	90% H2O/10% D2O	180 mM	7.5	1 atm	293
4	2D NOESY	unlabeled protein 20 mM sodium phosphate pH 7.5	90% H2O/10% D2O	180 mM	7.5	1 atm	293

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AVANCE	600
2	Bruker	DRX	750
3	Bruker	AVANCE	900

NMR Refinement
Method	Details	Software
torsion angle dynamics in DYANA followed by simulated annealing and energy minimization in AMBER		DYANA

NMR Ensemble Information
Conformer Selection Criteria	20 lowest energy structures
Conformers Calculated Total Number	200
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Additional NMR Experimental Information
Details	not applicable

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	DYANA	1.5	Peter Guntert
2	structure solution	Amber	7	D. Case, D. Pearlman et al.
3	processing	NMRPipe	2003	DeLaglio, F.
4	data analysis	NMRView	4.1.3	Bruce Johnson
5	refinement	Amber	7	D. Case, D. Pearlman et al.

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.