2GP8

NMR SOLUTION STRUCTURE OF THE COAT PROTEIN-BINDING DOMAIN OF BACTERIOPHAGE P22 SCAFFOLDING PROTEIN

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	NOESY	10% WATER/90% D2O, 99.9% D2O			4.4	1 atm	293
2	TOCSY	10% WATER/90% D2O, 99.9% D2O			4.4	1 atm	293
3	COSY	10% WATER/90% D2O, 99.9% D2O			4.4	1 atm	293
4	15N EDITED 3D NOESY-HSQC	10% WATER/90% D2O, 99.9% D2O			4.4	1 atm	293
5	TOCSYHMQC	10% WATER/90% D2O, 99.9% D2O			4.4	1 atm	293

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	AM600	600
2	Varian	AVANCE600	600
3	Varian	INOVA600	600

NMR Refinement
Method	Details	Software
DISTANCE GEOMETRY AND SIMULATED ANNEALING	REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. THE REFINEMENT WAS CARRIED OUT ON THE C-TERMINAL 40-RESIDUE SEGMENT.	X-PLOR

NMR Ensemble Information
Conformer Selection Criteria	LEAST RESTRAINT VIOLATION
Conformers Calculated Total Number	100
Conformers Submitted Total Number	1
Representative Model	(minimized average structure)

Additional NMR Experimental Information
Details	AVERAGE STRUCTURE. EXPERIMENTS WERE DONE ON THE C-TERMINAL 67-RESIDUE (238-303 PLUS ALANINE AT THE N-TERNINUS) SCAFFOLDING PROTEIN.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	X-PLOR	3.851	BRUNGER
2	structure solution	X-PLOR

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.