LINUS perturbs three consecutive residues at a time to generate a new conformation. Five move types constitute the move set: α-helix, β-strand, β-turn, PII, and coil. These moves are defined by the φ, ψ ranges in different mesostate bins. Specifically, the five move types are:

1. α-helix: All three residues are assigned backbone torsion angles within any of the following mesostate φ, ψ bins: 'Ee','Ee','Ee','De','Df','Ef'
2. β-strand: All three residues are assigned backbone torsion angles within any of the following mesostate φ, ψ bins: 'Ck','Ck','Ck','Cj','Cl','Bk','Bl','Dk','Dj'
3. PII: The central residue in the three moveset residues are set to PII and the first and third residue are set to coil. The PII residue is assigned backbone torsion angles within any of the following mesostate φ, ψ bins: 'Ek','El'. See below for mesostate definitions of the coil moveset.
4. Coil: For non-glycine, non-proline residues each of the three residues is assigned backbone torsion angles with values from the allowed region of φ, ψ space chosen at random.
5. β-turn: Either the first two residues or last two residues of the three residue segment are assigned to one of the following β-turn conformations, and the remaining residue is assigned a conformation from the sterically allowed region of φ, ψ space (i.e. coil). The backbone torsion angles for the two positions in turn conformations are chosen from within the following mesostate bin combinations.

   
              (('Ef'),('Df')),
              (('Ee'),('Ef')),
              (('Ef'),('Ef')),
              (('Ef'),('Dg')),
              (('Ee'),('Dg')),
              (('Ee'),('Ee')),
              (('Ef'),('Cg')),
              (('Ee'),('Df')),
              (('Ek'),('Jf')),
              (('Ek'),('Ig')),
              (('Ef'),('Ee')),
              (('Ek'),('Jg')),
              (('Ee'),('Cg')),
              (('Df'),('Df')),
              (('Ef'),('Cf')),
              (('Dg'),('Df')),
              (('Df'),('Dg')),
              (('Ih'),('Ig')),
              (('Ef'),('De')),
              (('Ek'),('Ih')),
              (('Dg'),('Cg')),
              (('Df'),('Cg')),
              (('Ib'),('Dg')),
              (('Df'),('Ee')),
              (('Fe'),('Ef')),
              (('Ib'),('Ef')),
              (('Df'),('Ef')),
              (('Ih'),('Jf')),
              (('Ih'),('Jg')),
              (('Ig'),('Ig')),
              (('Ef'),('Ch')),
              (('Dg'),('Ee')),
              (('Dg'),('Ef')),
              (('Ee'),('Eg')),
              (('Ih'),('Ih')),
              (('Ee'),('De')),
              (('Ig'),('Jg')),
              (('Ig'),('Jf')),
              (('Ib'),('Df')),
              (('Ic'),('Df')),
              (('Ic'),('Dg')),
              (('Dg'),('Dg')),
              (('Ig'),('Ih')),
   

The allowed region of φ, ψ space for glycine is appropriately expanded and for proline it is limited to two regions centered on helical or PII conformation. Additionally, the coil move for proline samples cis-peptide conformations.

In addition to the above default moves LINUS may read in a mesostate list or a probability mesostate list. These lists define allowed ranges of φ and ψ for each residue and moves are chosen from these ranges. Mesostates are defined here.

For each move, the peptide bond angle ω is set to 180° ± 5° and side chain chi angles angles (if any) are chosen at random from a list of sterically acceptable combinations. The ranges of acceptable torsion angles for residue rotamers are defined in chidict.py