1DCJ

SOLUTION STRUCTURE OF YHHP, A NOVEL ESCHERICHIA COLI PROTEIN IMPLICATED IN THE CELL DIVISION

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-SEPARATED_NOESY	1MM YHHP U-15N; 10MM PHOSPHATE BUFFER K; 100MM NACL; 2MM NAN3; 2MM DTT; 90% H20, 10% D2O		100mM NACL	7.1	AMBIENT	298
2	HNHA	1MM YHHP U-15N; 10MM PHOSPHATE BUFFER K; 100MM NACL; 2MM NAN3; 2MM DTT; 90% H20, 10% D2O		100mM NACL	7.1	AMBIENT	298
3	HNHB	1MM YHHP U-15N; 10MM PHOSPHATE BUFFER K; 100MM NACL; 2MM NAN3; 2MM DTT; 90% H20, 10% D2O		100mM NACL	7.1	AMBIENT	298
4	4D_13C-SEPARATED_NOESY	1MM YHHP U-15N, 13C; 10MM PHOSPHATE BUFFER K; 100MM NACL; 2MM NAN3; 2MM DTT; 100% D2O		100mM NACL	7.1	AMBIENT	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DMX	750

NMR Refinement
Method	Details	Software
HYBRID DISTANCE GEOMETRY-SIMULATED ANNEALING	THE STRUCTURES ARE BASED ON A TOTAL OF 1655 RESTRAINTS, 1390 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 211 DIHEDRAL ANGLE RESTRAINTS, 54 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.	XwinNMR

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Additional NMR Experimental Information
Details	THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	collection	XwinNMR		BRUKER
2	processing	NMRPipe		DELAGLIO
3	data analysis	CAPP/PIPP/STAPP		GARRETT
4	structure solution	X-PLOR	3.1	BRUNGER
5	refinement	X-PLOR	3.1	BRUNGER

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.