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Normal-mode analyses showed no conformational deformability in the interacting interface of the complexes. The fluorescence proximity assay presented a higher number of detected spots in the HSP70 ATP treatment, corroborating with the computational result. The interacting energy of the complexes showed that the most favored docking situation occurs between HSP70 ATP-bound and RAGE in its monomeric state. This interaction was detected and visualized by a proximity fluorescence-based assay in A549 cells and further analyzed by normal mode analyses of the docking complexes. Putative models for HSP70 complexation to the receptor for advanced glycation endproducts (RAGEs), considering both ADP-and ATP-bound states of HSP70, were obtained through molecular docking and interaction energy calculations. However, the specific characteristics of HSP70 binding are still unknown, and all HSP70 receptors have not yet been described. This leads to activation of nuclear factor-kappa B (NF-KB), release of proinflammatory cytokines, enhancement of the phagocytic activity of innate immune cells, and stimulation of antigenspecific responses. Extracellular heat shock protein 70 (HSP70) is recognized by receptors on the plasma membrane, such as Tolllike receptor 4 (TLR4), TLR2, CD 14, and CD40.