  Residual Dipolar Couplings (RDCs) acquired by Nuclear Magnetic Resonance
(NMR) spectroscopy can be an indispensable source of information in
investigation of molecular structures and dynamics. Here we present a complete
strategy for structure calculation and reconstruction of discrete state
dynamics from RDC data. Our method utilizes the previously presented REDCRAFT
software package and its dynamic-profile analysis to complete the task of
fragmented structure determination and identification of the onset of dynamics
from RDC data. Fragmented structure determination was used to demonstrate
successful structure calculation of static and dynamic domains for several
models of dynamics. We provide a mechanism of producing an ensemble of
conformations for the dynamical regions that describe any observed order tensor
discrepancies between the static and dynamic domains within a protein. In
addition, the presented method is capable of approximating relative occupancy
of each conformational state. The developed methodology has been evaluated on
simulated RDC data with 1Hz of error from an 83 residue {\alpha} protein (PDBID
1A1Z), and a 213 residue {\alpha}/\b{eta} protein DGCR8 (PDBID 2YT4). Using
1A1Z, various models of arc and complex two and three discrete-state dynamics
were simulated. MD simulation was used to generate a 2-state dynamics for
DGCR8. In both instances our method reproduced structure of the protein
including the conformational ensemble to within less than 2{\AA}. Based on our
investigations, arc motions with more than 30{\deg} of rotation are recognized
as internal dynamics and are reconstructed with sufficient accuracy.
Furthermore, states with relative occupancies above 20% are consistently
recognized and reconstructed successfully. Arc motions with magnitude of
15{\deg} or relative occupancy of less than 10% are consistently unrecognizable
as dynamical regions.
