<p><b>Copyright information:</b></p><p>Taken from "Solution structure of the second bromodomain of Brd2 and its specific interaction with acetylated histone tails"</p><p>http://www.biomedcentral.com/1472-6807/7/57</p><p>BMC Structural Biology 2007;7():57-57.</p><p>Published online 12 Sep 2007</p><p>PMCID:PMC2065866.</p><p></p>representation of the average, energy-minimized structure with the secondary structure elements highlighted. The helix nomenclature follows that of hsP/CAF bromodomain [9]. () Contact surface emphasized surface hydrophobic potential (left) and surface electrostatic potential (right) at the acetyl-lysine binding site. Yellow denotes hydrophobic potential; red negative potential; and blue positive potential. () A clear view of showing the conserved or type conserved side chains lined the hydrophobic cavity, and denoting the negative-charged collar formed by residues D330, D338, D341, D385 and D387. A, B, C and D were produced with MOLMOL or PyMOL
