Skip to main content

Table 1 The mean contact distance between residues in ChaK1 (first column) and annexin (first row).

From: Conformational preference of ChaK1 binding peptides: a molecular dynamics study

 

Met2

Val3

Ser4

Ala5

Phe6

Lys8

Trp11

ATP

Gly1619

   

0.84(33.1%)

0.69(93.6%)

  

0.65(100%)

Gly1620

  

0.63(98.9%)

0.58(99.9%)

0.53(100%)

  

0.62(100%)

Leu1621

  

0.61(100%)

0.66(97.3%)

0.66(97.3%)

  

0.79(67.5%)

Arg1622

       

0.53(100%)

Lys1646

       

0.68(100%)

Glu1651

    

0.92(24.36%)

0.92(31%)

  

Glu1718

       

0.87(20%)

Lys1727

 

0.74(83.7%)

0.79(55.8%)

     

Asn1730

0.64(100%)

0.60(100%)

0.86(12.3%)

     

Asn1731

0.44(100%)

0.71(99.9%)

0.85(7.7%)

     

Asn1732

0.55(100%)

0.83(34.1%)

      

Asp1765

  

0.77(86.6%)

     

Gln1767

  

0.77(90.9%)

     

Ala1794

0.83(20%)

       

Asn1795

0.47(100%)

     

1.0(10.1%)

 

Leu1796

0.77(72.1%)

       

Gly1797

0.79(60%)

       
  1. The contact was considered only when the distance between center mass of residues was shorter than 1.0 nm. The probability of occurrence of the interaction was calculated and shown in the parenthesis. The numbers highlighted in bold are identified as hydrogen bonding interactions and italic labels are salt bridges.