2HQ3 | pdb_00002hq3

Solution NMR structure of the apo-NosL protein from Achromobacter cycloclastes

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	HNCA	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100 mM sodium phosphate	6.5	ambient	303
2	HNCO	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100 mM sodium phosphate	6.5	ambient	303
3	HNCACB	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100 mM sodium phosphate	6.5	ambient	303
4	CBCA(CO)NH	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100 mM sodium phosphate	6.5	ambient	303
5	C(CO)NH	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100 mM sodium phosphate	6.5	ambient	303
6	HCC(CO)NH	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 90% H2O, 10% D2O	90% H2O/10% D2O	100 mM sodium phosphate	6.5	ambient	303
7	1H-13C-CT HSQC	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; > 95% D2O	> 95% D2O	100 mM sodium phosphate	6.5	ambient	303
8	HCCH-TOCSY	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; > 95% D2O	> 95% D2O	100 mM sodium phosphate	6.5	ambient	303
9	3D 15N NOESY	1.0 mM NosL, U-15N; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 95% H2O, 5% D2O	95% H2O/5% D2O	100 mM sodium phosphate	6.5	ambient	303
10	15N NOESY-HSQC	1.0 mM NosL, U-15N; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; 95% H2O, 5% D2O	95% H2O/5% D2O	100 mM sodium phosphate	6.5	ambient	303
11	13C NOESY-HSQC	1.0 mM NosL, U-15N, 13C; 100mM sodium phosphate; 1mM EDTA; 1mM DTT; > 95% D2O	> 95% D2O	100 mM sodium phosphate	6.5	ambient	303

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	600
2	Varian	INOVA	800

NMR Refinement
Method	Details	Software
Ambiguous Restraints for Iterative Assignments (ARIA 1.2), torsion angle dynamics, simulated annealing.		XwinNMR

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

Additional NMR Experimental Information
Details	Sequential and intra-residue 1H, 15N, and 13C backbone and side-chain chemical shift assignments were extracted from a series of double and triple resonance NMR experiments (HNCA, HNCO, HNCACB, CBCA(CO)NH, C(CO)NH, HCC(CO)NH, 1H-13C-CT HSQC,and HCCH-TOCSY) conducted on a DRX600. nOe data were obtained from 3D 15N NOESY experiments with mixing times (tmix) of 100, 120, and 140 msec and from 3D HCHC-NOESY (tmix=140 msec) spectra acquired at 600 MHz. Additional 15N NOESY-HSQC and 13C NOESY-HSQC experiments (nOe mixing times of 120 msec) were acquired on a Varian 800 INOVA (800 MHz) instrument.

Additional NMR Experimental Information

Details

Sequential and intra-residue 1H, 15N, and 13C backbone and side-chain chemical shift assignments were extracted from a series of double and triple resonance NMR experiments (HNCA, HNCO, HNCACB, CBCA(CO)NH, C(CO)NH, HCC(CO)NH, 1H-13C-CT HSQC,and HCCH-TOCSY) conducted on a DRX600. nOe data were obtained from 3D 15N NOESY experiments with mixing times (tmix) of 100, 120, and 140 msec and from 3D HCHC-NOESY (tmix=140 msec) spectra acquired at 600 MHz. Additional 15N NOESY-HSQC and 13C NOESY-HSQC experiments (nOe mixing times of 120 msec) were acquired on a Varian 800 INOVA (800 MHz) instrument.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	XwinNMR	3.1	Bruker Inc.
2	processing	NMRPipe	2.4	Delaglio
3	data analysis	NMRView	5.0	Johnson
4	structure solution	ARIA	1.2	Nilges
5	refinement	CNS	1.1	BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN

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 R01GM157729.

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Solution NMR structure of the apo-NosL protein from Achromobacter cycloclastes

2HQ3 | pdb_00002hq3