Protein Science
— Electronic Supplementary Material
Isabelle Théret, Jos A. Cox, Joel Mispelter, and Constantin T. Craescu
Backbone dynamics of the regulatory domain of calcium vector protein,
studied by 15N relaxation at four fields, reveals unique
mobility characteristics of the intermotif linker
Protein Science,
July 2001,
Volume
10,
Number
7,
pp.
1393-1402
Supplemental Research Data
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MS Excel file
(57 KB; 4 worksheets)
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Table S1. Relaxation parameters (R1, R2 and
heteronuclear NOE) of C-CaVP at four magnetic fields.
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Portable Document Format (PDF) file
(Adobe Acrobat 4.0; 249 KB; 2 pages)
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Figure S1. Plot of 15N relaxation
parameters and the estimated uncertainties along the sequence in
Ca2+-saturated C-CaVP, measured in a Tris buffer (20 mM)
containing 100 mM KCl, 6 mM CaCl2, at pH 6.5 and 308 K.
The secondary structure elements and the calcium binding loops are
schematically shown at the bottom of the figure. 15N
relaxation measurements were done at 9.39 T, 11.74 T, 14.1 T and
18.7 T.
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