Structural relaxation and binding energy calculations of FK506 binding protein complexes using the large-scale DFT code CONQUEST

24th IUPAP Conference on Computational Physics

物理学;计算机科学

Otsuka, T.^1 ; Okimoto, N.^1 ; Taiji, M.^1 ; Bowler, D.R.^2 ; Miyazaki, T.^3

Quantitative Biology Center (QBiC), RIKEN, 1-6-5 Minatojima-Minamimachi, Kobe, Chuo-ku, Hyoho, 650-0047, Japan^1

Department of Physics and Astronomy, University College London, Gower St, London, WC1E 6BT, United Kingdom^2

Computational Materials Science Center, National Institute for Materials Science (NIMS), 1-2-1 Sengen, Tsukuba, Ibaraki, 305-0047, Japan^3

关键词: DFT codes;    Energy calculation;    FK506-binding proteins;    Geometry relaxation;    Ligand molecules;    Protein-ligand complexes;   

Others  :  https://iopscience.iop.org/article/10.1088/1742-6596/454/1/012057/pdf
DOI  :  10.1088/1742-6596/454/1/012057

学科分类：计算机科学（综合）

来源: IOP

【 摘 要 】

We have performed structural relaxation and calculated binding energy of protein-ligand complex systems, FK506 binding protein (FKBP) and some ligand molecules, using a large-scale density functional theory (DFT) code CONQUEST. Detailed comparison of the calculated binding energies of FKBP with various ligand molecules is reported including the effects of the full geometry relaxation.