Experiment: 2JU4

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	0.05 mM [U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
2	2D 1H-1H TOCSY	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
3	3D CBCA(CO)NH	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
4	3D HNCACB	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
5	2D 1H-1H TOCSY	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
6	3D HBHA(CO)NH	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
7	3D H(CCO)NH	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
8	3D C(CO)NH	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
9	3D HNCO	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
10	3D HNHA	0.09 mM [U-100% 13C; U-100% 15N] PDEgamma	90% H2O/10% D2O	0	4	ambient	298
11	2D 1H-15N HSQC	0.05 mM [U-15N] PROXYL-PDEgamma	90% H2O/10% D2O	0	4	ambient	298
12	2D 1H-15N HSQC	0.05 mM [U-100% 15N] PROXYL-PDEgamma, 5 mM Ascorbic Acid	93% H2O/7% D2O	0	4	ambient	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DMX	600
2	Bruker	DMX	750
3	Varian	INOVA	600

NMR Refinement
Method	Details	Software
molecular dynamics, simulated annealing	There are 10272 close contacts in this entry. The deposited structures were calculated using the combined distance restraints derived from ten single PDEgamma mutants (in each mutant a native residue was replaced by the 3-maleimido-PROXYL-cysteine residue). As a result, the deposited structures contain 10 mutated residues which do not coexist in the process of NMR structure determination. To avoid the artificial steric hinderance between individual spin groups, the Van der Waals contacts involving the 2,2,5,5-tetramethyl-1-pyrrolidinyloxy group (but not the maleimide group) are turned off in the structure calculation.	NMRPipe

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	200
Conformers Submitted Total Number	100
Representative Model	1 (fewest violations)

Additional NMR Experimental Information
Details	This protein is intrinsically disordered. Because the structures are largely disordered in solution, they contain several different conformational population. Therefore all the structures can not be superimposed.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	NMRPipe	2.4	Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
2	collection	VNMR		Varian
3	processing	Sparky	2.112	Goddard
4	refinement	XPLOR-NIH	2.11.2	Schwieters, Kuszewski, Tjandra and 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.