The recurrent coiled-coil domain in proteins consists of multiple helices that intertwine to form a superhelix. Superhelical formation is driven primarily by the packing of hydrophobic residues that pattern each helix making up the coil. An examination of the sequences forming naturally occurring coiled-coils reveals a high degree of variation, yet all the sequences ultimately fold into left-handed superhelical structures. We have developed a coarse grained atomistic folding model for coiled-coil formation that only requires a hydrophobic-polar pattern for the input sequence[1] and are able to generate coiled-coil structures that have a low root mean square distance(RMSD) to known structures. We have considered different parameters in our energy function and tried to optimize them to get lowest RMSD. Besides correctly predicting structure from sequence, we have applied the model to study both the thermodynamic and mechanical stability to sequence mutations for the selected coiled coils. The model provides insights into key sequence characteristics that aid both stability and the kinetics of coil formation. [1] S.Sadeghi & E.Emberly ; Phys. Rev. E.80, 061909 (2009).