1OWW

Solution structure of the first type III module of human fibronectin determined by 1H, 15N NMR spectroscopy

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	1-2 mM [U-15N] protein	90% H2O/10% D2O	unbuffered	6	ambient	313
2	3D_15N-separated_TOCSY	1-2 mM [U-15N] protein	90% H2O/10% D2O	unbuffered	6	ambient	313
3	HNHA	1-2 mM [U-15N] protein	90% H2O/10% D2O	unbuffered	6	ambient	313
4	2D NOESY	1-2 mM [U-15N] protein	90% H2O/10% D2O	unbuffered	6	ambient	313
5	2D TOCSY	1-2 mM [U-15N] protein	90% H2O/10% D2O	unbuffered	6	ambient	313

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Oxford	OMEGA	750
2	Oxford	OMEGA	600
3	Oxford	OMEGA	500
4	Bruker	DMX	500

NMR Refinement
Method	Details	Software
torsion angle dynamics	Structures refined by molecular dynamics using residual dipolar couplings. Structures based on a total of 1113 distance restraints, 81 dihedral angle restraints and 57 residual dipolar couplings.	X-PLOR

NMR Ensemble Information
Conformer Selection Criteria	target function
Conformers Calculated Total Number	24
Conformers Submitted Total Number	24

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	Felix	2.3	Molecular Simulations Inc.
2	processing	XwinNMR	2.6	Bruker
3	data analysis	XEASY	1.3	Xia and Bartels
4	structure calculation	DYANA	1.5	Guentert
5	refinement	X-PLOR	3.8	Brunger

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.