Backbone and side chain H， N and C assignments of a putative peptidyl prolyl cis-trans isomerase FKBP12 from Mycobacterium tuberculosis.

FK506 Binding Proteins (FKBPs) are a family of highly conserved and important proteins that possess a peptidyl cis-trans isomerase (PPIases) domain. Human FKBP12 is a prototype of this family and it is involved in many diseases due to its interaction with the immunosuppressive drugs FK506 and rapamycin. They inhibit calcineurin and mTOR complex， respectively， leading to parasite death by inhibiting cell proliferation through cytokinesis blockade being an important target to find new drugs. Tuberculosis is a disease that causes important impacts on public health worldwide. In this context， MtFKBP12 is a putative peptidyl prolyl cis-trans isomerase from Mycobacterium tuberculosis and here we report the NMR chemical shift assignment for H， N and C nuclei in the backbone and side chains of the MtFKBP12. This lays the foundation for further structural studies， backbone dynamics， mapping of interactions and drug screening and development. We have found through the NMR spectrum that the protein is well folded with narrow peaks and almost none overlap in N-HSQC. Prediction of secondary structure using Talos-N server showed great similarity with other proteins from this family.