2FVF | pdb_00002fvf

Structure of 10:0-ACP (protein with docked fatty acid)

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-separated_NOESY	2 mM protein, 10 mM MES pH 6.1, 100 mM NaCl	95% H2O/5% D2O	100 mM NaCl	6.1	1 atm	287
2	3D_13C-separated_NOESY	2 mM protein, 10 mM MES pH 6.1, 100 mM NaCl	95% H2O/5% D2O	100 mM NaCl	6.1	1 atm	287
3	f1 filtered NOESY-15N HSQC	2 mM protein, 10 mM MES pH 6.1, 100 mM NaCl	95% H2O/5% D2O	100 mM NaCl	6.1	1 atm	287
4	f1 filtered NOESY-13C HSQC	2 mM protein, 10 mM MES pH 6.1, 100 mM NaCl	95% H2O/5% D2O	100 mM NaCl	6.1	1 atm	287

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

NMR Refinement
Method	Details	Software
Initial structure from torsion angle dynamics (in CYANA). Fatty acid and phosphopantetheine were added and docked using ambiguous distance restraints in XPLOR-NIH		XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with lowest energy in a clustering of the fatty acid structures
Conformers Calculated Total Number	200
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR	2.6
2	data analysis	NMRPipe
3	data analysis	Sparky	3.111
4	structure solution	CYANA	2.1
5	refinement	XPLOR-NIH	2.12

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 R01GM157729.