2L8V

Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	2D 1H-15N HSQC	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
2	2D 1H-13C HSQC aliphatic	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
3	2D 1H-13C HSQC aromatic	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
4	2D 1H-15N HSQC	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 10 mM DTT	100% D2O	0.1	7.5	ambient	298
5	2D 1H-13C HSQC-CT	1.3 mM [U-5% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 5 mM DTT, 0.02 % sodium azide	90% H2O/10% D2O	0.1	7.5	ambient	298
6	3D 1H-15N NOESY	1.3 mM [U-5% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 5 mM DTT, 0.02 % sodium azide	90% H2O/10% D2O	0.1	7.5	ambient	298
7	3D 1H-13C NOESY-aliph	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
8	3D HNCO	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
9	3D HNCACB	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
10	3D CBCA(CO)NH	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
11	3D HN(CO)CA	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
12	3D HBHA(CO)NH	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
13	3D H(CCO)NH	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
14	3D C(CCO)NH	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
15	3D HCCH-COSY	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
16	3D HCCH-TOCSY	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298
17	3D CCH-TOCSY	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 10 mM DTT	100% D2O	0.1	7.5	ambient	298
18	4D CC-NOESY	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 10 mM DTT	100% D2O	0.1	7.5	ambient	298
19	2D 1H-13C NOESY-aromatic	1.3 mM [U-100% 13C; U-100% 15N] protein, 10 mM Tris-HCl, 100 mM sodium chloride, 5 mM calcium chloride, 0.02 % sodium azide, 5 mM DTT	90% H2O/10% D2O	0.1	7.5	ambient	298

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

NMR Refinement
Method	Details	Software
simulated annealing	CNS water refinement	NMRPipe

NMR Ensemble Information
Conformer Selection Criteria	structures with the lowest energy
Conformers Calculated Total Number	125
Conformers Submitted Total Number	20
Representative Model	1 (lowest energy)

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	processing	NMRPipe	2008	Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
2	collection	VNMR	6.1C	Varian
3	collection	TopSpin	2.1.4	Bruker Biospin
4	data analysis	AutoStructure	2.2.1	Huang, Tejero, Powers and Montelione
5	structure solution	X-PLOR NIH	2.25	Schwieters, Kuszewski, Tjandra and Clore
6	refinement	CNS	1.2	Brunger, Adams, Clore, Gros, Nilges and Read
7	data analysis	Sparky	3.113	Goddard
8	refinement	PSVS	1.4	Bhattacharya and Montelione
9	chemical shift assignment	AutoAssign	2.30	Zimmerman, Moseley, Kulikowski and Montelione
10	structure solution	PdbStat	5.1	(PdbStat)-Roberto Tejero and Gaetano T. Montelione
11	chemical shift autoassignment	PINE Server	1.0	Bahrami, Markley, Assadi, and Eghbalnia
12	structure solution	CYANA	2.1	Guntert, Mumenthaler and Wuthrich

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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2L8V

Solution NMR structure of the phycobilisome linker polypeptide domain of CpcC (20-153) from Thermosynechococcus elongatus, Northeast Structural Genomics Consortium Target TeR219A