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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

    

-

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BMC Structural Biology

ISSN: 1472-6807

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