6OCV

Solution structure of the H-NOX protein from Shewanella woodyi in the Fe(II)CO ligation state

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	500 uM [U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
20	2D 1H-15N TROSY	500 uM [U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Bruker AVANCE NEO 600
19	2D 1H-15N TROSY	500 uM [U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Bruker AVANCE NEO 600
8	2D 1H-13C HSQC aliphatic	800 uM [U-99% 13C; U-99% 15N] protein	100% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
9	2D 1H-13C HSQC aromatic	800 uM [U-99% 13C; U-99% 15N] protein	100% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
2	3D HNCO	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
3	3D HNCA	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
4	3D HNCACB	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
5	3D HN(CO)CA	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
6	3D CBCA(CO)NH	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
7	3D HCACOCANH	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
10	3D H(CCO)NH	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
11	3D C(CO)NH	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
12	3D HCCH-TOCSY	800 uM [U-99% 13C; U-99% 15N] protein	100% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
13	3D HCCH-COSY	800 uM [U-99% 13C; U-99% 15N] protein	100% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
14	3D HBHA(CO)NH	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
15	3D 1H-15N NOESY	800 uM [U-99% 13C; U-99% 15N] protein	90% H2O/10% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
16	3D 1H-13C NOESY aliphatic	800 uM [U-99% 13C; U-99% 15N] protein	100% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
17	3D 1H-13C NOESY aromatic	800 uM [U-99% 13C; U-99% 15N] protein	100% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800
18	2D 13C15Nfiltered NOESY	800 uM [U-99% 13C; U-99% 15N] protein	100% D2O	50 mM	7.5	1 atm	293	Agilent agilent 800 800

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Agilent	agilent 800	800
2	Bruker	AVANCE NEO	600
3	Bruker	AVANCE NEO	800

NMR Refinement
Method	Details	Software
simulated annealing	distance geometry, torsion angle dynamics, molecular dynamics	X-PLOR NIH

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	200
Conformers Submitted Total Number	20
Representative Model	1 (closest to the average)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	X-PLOR NIH		Schwieters, Kuszewski, Tjandra and Clore
2	structure calculation	X-PLOR NIH		Schwieters, Kuszewski, Tjandra and Clore
3	chemical shift assignment	Sparky		Sparky: Goddard NMRFAM-Sparky: Lee W, Tonelli M, Markley JL
4	peak picking	Sparky		Sparky: Goddard NMRFAM-Sparky: Lee W, Tonelli M, Markley JL
5	processing	NMRPipe		Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
6	collection	VNMR		Varian
7	collection	TopSpin		Bruker Biospin

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.

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6OCV

Solution structure of the H-NOX protein from Shewanella woodyi in the Fe(II)CO ligation state