Molecular dynamics simulations of STAT5 proteins.

<p><b>(A)</b> The root mean square deviations (RMSDs) from the initial coordinates computed on the Cα atoms for trajectories <b>1</b> (solid lines) and <b>2</b> (dashed lines) of MD simulations. The non-phosphorylated and phosphorylated (p-) states of proteins are distinguished by color: STAT5a and p-STAT5a are in blue and in yellow (top panel<i>)</i>, STAT5b and p-STAT5b are in green and in magenta, respectively (bottom panel). <b>(B)</b> The root mean square fluctuations (RMSFs) computed on the Cα atoms over the simulation time of STAT5a (STAT5a is in blue and p-STAT5a is in yellow) were compared to those of STAT5b (STAT5b is in green and p-STAT5b is in magenta). <b>Insert:</b> The average conformation for STAT5a is presented as tubes. The tube size is proportional to the by-residue atomic fluctuations computed on the Cα atoms. The high fluctuation regions are specified by color ranged from red to yellow and numbered from 1 to 7.