2KHM

Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	0.2-1mM [U-99% 15N] NR3-5	95% H2O/5% D2O	0.02	6.0	ambient	298
2	2D 1H-13C HSQC	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
3	3D HNCO	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
4	3D HNCA	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
5	3D HNCACB	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
6	3D CBCA(CO)NH	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
7	3D HN(CO)CA	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
8	3D HN(CA)CO	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
9	3D HCCH-TOCSY	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
10	3D HNHA	0.2-1mM [U-99% 15N] NR3-5	95% H2O/5% D2O	0.02	6.0	ambient	298
11	3D HNHB	0.2-1mM [U-99% 15N] NR3-5	95% H2O/5% D2O	0.02	6.0	ambient	298
12	3D CCH-COSY	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
13	3D C(CO)NH	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
14	3D 1H-15N NOESY	0.2-1mM [U-99% 15N] NR3-5	95% H2O/5% D2O	0.02	6.0	ambient	298
15	3D 1H-13C NOESY	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
16	3D CNH NOESY	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
17	3D NNH NOESY	0.2-1mM [U-99% 15N] NR3-5	95% H2O/5% D2O	0.02	6.0	ambient	298
18	3D CCH NOESY	0.5-1.3mM [U-99% 13C; U-99% 15N] NR3-1	95% H2O/5% D2O	0.02	6.0	ambient	298
19	2D 1H-1H NOESY	0.6-1mM NR3-2	95% H2O/5% D2O	0.02	6.0	ambient	298
20	filtered NOESY	1mM [U-99% 13C; U-99% 15N] NR3-3, 1mM NR3-4	95% H2O/5% D2O	0.02	6.0	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DMX	600
2	Bruker	DMX	750
3	Bruker	AVANCE	900

NMR Refinement
Method	Details	Software
simulated annealing		TopSpin

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	50
Conformers Submitted Total Number	21
Representative Model	1 (minimized average)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	TopSpin	1.3	Bruker Biospin
2	peak picking	Sparky	3.11	Goddard
3	chemical shift assignment	PASTA	0.1	Kessler, Gemmecker
4	data analysis	TALOS	9.4	Cornilescu, Delaglio, Bax
5	structure solution	X-PLOR NIH		Schwieters, Kuszewski, Tjandra, Clore
6	data analysis	ProcheckNMR		Laskowski, MacArthur
7	refinement	X-PLOR NIH		Schwieters, Kuszewski, Tjandra, Clore

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.

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2KHM

Structure of the C-terminal non-repetitive domain of the spider dragline silk protein ADF-3