1FRY | pdb_00001fry

THE SOLUTION STRUCTURE OF SHEEP MYELOID ANTIMICROBIAL PEPTIDE, RESIDUES 1-29 (SMAP29)

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D NOESY	1mM smap29; 50mM phosphate buffer, pH 5.94	60% H2O, 40% D3-trifluoroethanol	ca. 50mM	5.94	1 atm	298
2	DQF-COSY	1mM smap29; 50mM phosphate buffer, pH 5.94	60% H2O, 40% D3-trifluoroethanol	ca. 50mM	5.94	1 atm	298
3	tocsy	1mM smap29; 50mM phosphate buffer, pH 5.94	60% H2O, 40% D3-trifluoroethanol	ca. 50mM	5.94	1 atm	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	UNITY	500

NMR Refinement
Method	Details	Software
torsion angle dynamics	Structure based on 217 noe contstraints and 8 HA-NH coupling constants	DYANA

NMR Ensemble Information
Conformer Selection Criteria	structures with acceptable covalent geometry, structures with the least restraint violations,structures with the lowest energy
Conformers Calculated Total Number	300
Conformers Submitted Total Number	40
Representative Model	1,21 (lowest energy)

Additional NMR Experimental Information
Details	This structure was determined using standard 2D homonuclear techniques.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	structure solution	DYANA	1.5
2	collection	VNMR	4.3b
3	data analysis	VNMR	6.1b
4	refinement	VNMR	6.1b

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.