Table 1

The Interaction energy (between ABA and receptors) and the Distance (between ABA C8′ and Fe) before and after MD simulation
AGI CYPs Interaction Energy (−kcal/mol) Distance (Å) Key binding residues
I M MDS a I M MDS b
AT4G19230.1 CYP707A1 137.279 251.118 272.081 4.174 5.349 4.889 K78, F88, F243 and L312
AT4G19230.2 CYP707A1 216.912 317.753 386.842 3.761 4.401 3.731 K78, F88, F243 and L312
AT2G29090.1 CYP707A2 95.382 315.168 323.671 3.620 4.159 3.804 K78, F88, F249 and L319
AT5G45340.1 CYP707A3 −10.400 281.497 317.584 3.121 3.203 3.574 K78, F88, F243 and L312
AT5G45340.2 CYP707A3 57.678 287.923 320.166 3.445 3.841 4.072 K78, F88, F243 and L312
AT3G19270.1 CYP707A4 166.980 335.875 333.591 4.267 3.399 3.275 Y74, K78, F88, F248 and I318
AT2G45510.1 CYP704A2 −41.931 81.447 108.988 4.315 4.782 6.800 T255

CYP707A1 and CYP707A3 have splicing isoforms. “I”: the initial docking complex; “M”: the complex after three steps of “Minimization”; “MDS a”: the average interaction energy of the conformations following MD simulation; “MDS b”: the last conformation following MD simulation.

Zhang et al.

Zhang et al. BMC Bioinformatics 2012 13:332   doi:10.1186/1471-2105-13-332

Open Data