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Table 4 RMSDs (Å) for Cα atoms based on multiple structural alignment [24] of the experimental structures and the end-point structures from the MD simulations.

From: A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding

  Pex5p(C)-apo1 (current) Pex5p(C)-apo2 Pex5p(C)-SCP2 MD with Sr MD w/o Sr
Pex5p(C)-apo1 (current) - 2.03 2.39 1.77 2.12
Pex5p(C)-apo2   - 2.31 2.28 2.61
Pex5p(C)-SCP2    - 2.46 2.09
MD with Sr     - 2.66
MD w/o Sr      -