2CPB

SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS BACTERIOPHAGE M13 SOLUBILIZED IN DODECYLPHOSPHOCHOLINE MICELLES, 25 LOWEST ENERGY STRUCTURES

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	DQF-COSY	H2O			4.9		311
2	TOCSY	H2O			4.9		311
3	NOESY	H2O			4.9		311
4	NOESY-HMQC (15N AND 13C)	H2O			4.9		311
5	TOCSY-HMQC (15N)	H2O			4.9		311
6	HCCH-TOCSY	H2O			4.9		311
7	HMQC-J	H2O			4.9		311
8	HNHA	H2O			4.9		311

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	UNITY	400
2	Bruker	AM	500
3	Bruker	AMX	600

NMR Refinement
Method	Details	Software
RESTRAINED MOLECULAR DYNAMICS, SIMULATED ANNEALING, THIS VERSION OF X-PLOR WAS EXTENDED FOR FLOATING CHIRALITY		X-PLOR

NMR Ensemble Information
Conformer Selection Criteria	LOWEST ENERGY, DISTANCE RESTRAINTS SMALLER THAN 0.5 A, DIHEDRAL VIOLATIONS SMALLER THAN 5 DEGREES
Conformers Calculated Total Number	80
Conformers Submitted Total Number	25

Additional NMR Experimental Information
Details	THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N -LABELED M13 COAT PROTEIN SOLUBILIZED IN DEUTERATED DODECYLPHOSPHOCHOLINE MICELLES (CONCENTRATION COAT/DODPCHO = 1:200)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	X-PLOR	3.1	BRUNGER
2	structure solution	X-PLOR	3.1

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.