2KKP

Solution NMR structure of the phage integrase SAM-like Domain from Moth 1796 from Moorella thermoacetica. Northeast Structural Genomics Consortium Target MtR39K (residues 64-171).

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
2	2D 1H-13C HSQC	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
3	3D CBCA(CO)NH	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
4	3D C(CO)NH	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
5	3D HNCO	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
6	3D HNCA	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
7	3D HNCACB	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
8	3D HBHA(CO)NH	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
9	3D H(CCO)NH	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
10	3D HCCH-TOCSY	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
11	3D 1H-15N NOESY	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
12	3D 1H-13C NOESY	0.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM potassium chloride-3	90% H2O/10% D2O	0.2	6.5	ambient	293
13	4D 1H-13C NOESY	.9 mM [U-100% 13C; U-100% 15N] Moth_1796, 20 mM MES, 200 mM sodium chloride	100% D2O	0.2	6.5	ambient	293

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Varian	INOVA	600
2	Bruker	AVANCE	850

NMR Refinement
Method	Details	Software
simulated annealing	Original NOE assgnments were done with CYANA. This NOE restraints list was refined using iterative cycles of XPLOR-NIH standalone, and XPLOR+HB and CNSw refinement.	AutoAssign

NMR Ensemble Information
Conformer Selection Criteria	structures with the least restraint violations
Conformers Calculated Total Number	150
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	chemical shift assignment	AutoAssign	2.3	Zimmerman, Moseley, Kulikowski and Montelione
2	processing	NMRPipe	2008	Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
3	collection	VNMR	6.1C	Varian
4	collection	TopSpin	2.1.3	Bruker Biospin
5	structure solution	AutoStructure	2.2.1	Huang, Tejero, Powers and Montelione
6	structure solution	X-PLOR NIH		Schwieters, Kuszewski, Tjandra and Clore
7	refinement	CNS	1.2	Brunger, Adams, Clore, Gros, Nilges and Read
8	data analysis	Sparky	3.113	Goddard
9	structure solution	PSVS		Bhattacharya and Montelione
10	structure solution	PdbStat	5.1	Roberto Tejero and Gaetano T. Montelione
11	structure solution	CYANA		Guntert, Mumenthaler and Wuthrich

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.