Nuclear Magnetic Resonance (NMR) spectroscopy has been extensively used in elucidating protein structures and dynamics. The introduction of multi-dimensional NMR techniques significantly relieves resolution problems in peak assignments and gives additional information other than chemical shift. Various types of data from multi-dimensional NMR experiments are used in protein structure determination, such as the Nuclear Overhauser Effect (NOE), J-coupling (indirect dipole–dipole coupling), Residual Dipo- lar Coupling (RDC), Pseudo-Contact Shift (PCS), and so on.