Team:Washington/DataTable

From 2010.igem.org

(Difference between revisions)
Line 5: Line 5:
<head>
<head>
 +
<meta name="Excel Workbook Frameset">
<meta http-equiv=Content-Type content="text/html; charset=windows-1252">
<meta http-equiv=Content-Type content="text/html; charset=windows-1252">
<meta name=ProgId content=Excel.Sheet>
<meta name=ProgId content=Excel.Sheet>
<meta name=Generator content="Microsoft Excel 14">
<meta name=Generator content="Microsoft Excel 14">
<link rel=File-List href="MutantData%20Table_files/filelist.xml">
<link rel=File-List href="MutantData%20Table_files/filelist.xml">
-
<!--[if !mso]>
+
<title>Mutant&nbsp;Data&nbsp;Table</title>
-
<style>
+
<![if !supportTabStrip]>
-
v\:* {behavior:url(#default#VML);}
+
<link id="shLink" href="MutantData%20Table_files/sheet001.htm">
-
o\:* {behavior:url(#default#VML);}
+
-
x\:* {behavior:url(#default#VML);}
+
-
.shape {behavior:url(#default#VML);}
+
-
</style>
+
-
<![endif]-->
+
-
<style id="MutantData Table_13667_Styles">
+
-
<!--table
+
-
{mso-displayed-decimal-separator:"\.";
+
-
mso-displayed-thousand-separator:"\,";}
+
-
.font013667
+
-
{color:black;
+
-
font-size:11.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Calibri, sans-serif;
+
-
mso-font-charset:0;}
+
-
.font513667
+
-
{color:black;
+
-
font-size:9.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Tahoma, sans-serif;
+
-
mso-font-charset:0;}
+
-
.font613667
+
-
{color:black;
+
-
font-size:11.0pt;
+
-
font-weight:400;
+
-
font-style:italic;
+
-
text-decoration:none;
+
-
font-family:Calibri, sans-serif;
+
-
mso-font-charset:0;}
+
-
.xl6413667
+
-
{padding:0px;
+
-
mso-ignore:padding;
+
-
color:black;
+
-
font-size:11.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Calibri, sans-serif;
+
-
mso-font-charset:0;
+
-
mso-number-format:General;
+
-
text-align:center;
+
-
vertical-align:middle;
+
-
mso-background-source:auto;
+
-
mso-pattern:auto;
+
-
white-space:normal;
+
-
mso-text-control:shrinktofit;}
+
-
.xl6513667
+
-
{padding:0px;
+
-
mso-ignore:padding;
+
-
color:black;
+
-
font-size:11.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Calibri, sans-serif;
+
-
mso-font-charset:0;
+
-
mso-number-format:General;
+
-
text-align:left;
+
-
vertical-align:top;
+
-
mso-background-source:auto;
+
-
mso-pattern:auto;
+
-
white-space:normal;
+
-
mso-text-control:shrinktofit;}
+
-
.xl6613667
+
-
{padding:0px;
+
-
mso-ignore:padding;
+
-
color:black;
+
-
font-size:11.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Calibri, sans-serif;
+
-
mso-font-charset:0;
+
-
mso-number-format:General;
+
-
text-align:left;
+
-
vertical-align:top;
+
-
mso-background-source:auto;
+
-
mso-pattern:auto;
+
-
white-space:normal;}
+
-
.xl6713667
+
-
{padding:0px;
+
-
mso-ignore:padding;
+
-
color:windowtext;
+
-
font-size:10.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Verdana, sans-serif;
+
-
mso-font-charset:0;
+
-
mso-number-format:General;
+
-
text-align:left;
+
-
vertical-align:top;
+
-
mso-background-source:auto;
+
-
mso-pattern:auto;
+
-
white-space:normal;}
+
-
.xl6813667
+
-
{padding:0px;
+
-
mso-ignore:padding;
+
-
color:windowtext;
+
-
font-size:10.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Verdana, sans-serif;
+
-
mso-font-charset:0;
+
-
mso-number-format:"0\.000";
+
-
text-align:left;
+
-
vertical-align:top;
+
-
mso-background-source:auto;
+
-
mso-pattern:auto;
+
-
white-space:normal;}
+
-
.xl6913667
+
-
{padding:0px;
+
-
mso-ignore:padding;
+
-
color:black;
+
-
font-size:11.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Calibri, sans-serif;
+
-
mso-font-charset:0;
+
-
mso-number-format:"0\.000";
+
-
text-align:left;
+
-
vertical-align:top;
+
-
mso-background-source:auto;
+
-
mso-pattern:auto;
+
-
white-space:normal;}
+
-
.xl7013667
+
-
{padding:0px;
+
-
mso-ignore:padding;
+
-
color:black;
+
-
font-size:11.0pt;
+
-
font-weight:400;
+
-
font-style:normal;
+
-
text-decoration:none;
+
-
font-family:Calibri, sans-serif;
+
-
mso-font-charset:0;
+
-
mso-number-format:General;
+
-
text-align:left;
+
-
vertical-align:top;
+
-
background:white;
+
-
mso-pattern:black none;
+
-
white-space:normal;
+
-
mso-text-control:shrinktofit;}
+
-
-->
+
-
</style>
+
-
<title>Mutant Data Table</title>
+
-
</head>
+
-
<body>
+
<link id="shLink">
-
<!--[if !excel]>&nbsp;&nbsp;<![endif]-->
+
-
<!--The following information was generated by Microsoft Excel's Publish as Web
+
-
Page wizard.-->
+
-
<!--If the same item is republished from Excel, all information between the DIV
+
-
tags will be replaced.-->
+
-
<!----------------------------->
+
-
<!--START OF OUTPUT FROM EXCEL PUBLISH AS WEB PAGE WIZARD -->
+
-
<!----------------------------->
+
-
<div id="MutantData Table_13667" align=center x:publishsource="Excel">
+
<script language="JavaScript">
 +
<!--
 +
var c_lTabs=1;
-
<h1 style='color:black;font-family:Calibri;font-size:14.0pt;font-weight:800;
+
var c_rgszSh=new Array(c_lTabs);
-
font-style:normal'>Mutant Data Table</h1>
+
c_rgszSh[0] = "MutantData Table";
-
<table border=0 cellpadding=0 cellspacing=0 width=1021 class=xl6413667
 
-
style='border-collapse:collapse;table-layout:fixed;width:766pt'>
 
-
<col class=xl6413667 width=172 style='mso-width-source:userset;mso-width-alt:
 
-
6290;width:129pt'>
 
-
<col class=xl6413667 width=216 style='mso-width-source:userset;mso-width-alt:
 
-
7899;width:162pt'>
 
-
<col class=xl6413667 width=297 style='mso-width-source:userset;mso-width-alt:
 
-
10861;width:223pt'>
 
-
<col class=xl6413667 width=168 span=2 style='mso-width-source:userset;
 
-
mso-width-alt:6144;width:126pt'>
 
-
<tr height=26 style='mso-height-source:userset;height:20.1pt'>
 
-
  <td height=26 class=xl7013667 width=172 style='height:20.1pt;width:129pt'>Mutant
 
-
  Name</td>
 
-
  <td class=xl7013667 width=216 style='width:162pt'>Brief Description</td>
 
-
  <td class=xl7013667 width=297 style='width:223pt'>Features and Mutations</td>
 
-
  <td class=xl6613667 width=168 style='width:126pt'>Transpeptidation per DCP</td>
 
-
  <td class=xl6613667 width=168 style='width:126pt'>Hydrolysis per DCP</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>CapD</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A protein native to <font
 
-
  class="font613667">Bacillus anthracis </font><font class="font013667">which
 
-
  cleaves poly-D-&#947;-glutamate (PDGA) and anchors it to the bacterium's
 
-
  peptidoglycan</font></td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>No Signal Sequence, Triple
 
-
  band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.491</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.713</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>CapD_CP</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A circularly permuted CapD
 
-
  with a Foldit-designed linker</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Foldit created linker,
 
-
  Circular Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.000</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.000</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>CapD_CPNFDelta</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A circularly permuted CapD
 
-
  with deletion of floppy areas</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Foldit created linker,
 
-
  Circular Permutation, No Signal Sequence, Single band on protein agarose gel,
 
-
  Removed &quot;floppy&quot; section to compact protein</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.035</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.878</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>F24A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  24 on CapDCP from Phenylalanine to Alanine, Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.021</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.061</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24H</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  24 on CapDCP from Phenylalanine to Histidine, Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.108</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>1.205</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24H,
 
-
  L40R, T59D_M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24, 40, 59, and 61 on Foldit design from Phenylalanine to Histidine, Leucine
 
-
  to Arginine, Threonine to Asparagine, and Methionine to Serine, respectively.
 
-
  Foldit-created linker, Circular Permutation, No Signal Sequence, Single band
 
-
  on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.001</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.006</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24H,
 
-
  L40R, T59N_M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24, 40, 59, and 61 on Foldit design from Phenylalanine to Histidine, Leucine
 
-
  to Arginine, Threonine to Aspartic Acid, and Methionine to Serine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.058</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>1.050</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24H,
 
-
  L40R, T59S_M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24, 40, 59, and 61 on CapDCP from Phenylalanine to Histidine, Leucine to
 
-
  Arginine, Threonine to Serine, and Methionine to Serine, respectively.
 
-
  Foldit-created linker, Circular Permutation, No Signal Sequence, Single band
 
-
  on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.000</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.007</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>F24H,
 
-
  R356K</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24 and 356 on CapDCP from Phenylalanine to Histidine and Arginine to Lysine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.129</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.257</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24H,
 
-
  T59R</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24 and 59 on CapDCPfrom Phenylalanine to Histidine and Threonine to Arginine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.011</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.005</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>F24H,T59N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24 and 59 on CapDCP from Phenylalanine to Histidine and Threonine to
 
-
  Asparagine, respectively. Foldit-created linker, Circular Permutation, No
 
-
  Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.007</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.029</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24W</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  24 on CapDCP from Phenylalanine to Tryptophan. Foldit-created linker,
 
-
  Circular Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.006</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.044</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>F24Y</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  24 on CapDCP from Phenylalanine to Tyrosine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.593</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.887</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24Y,
 
-
  L40R</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24 and 40 on CapDCP from Phenylalanine to Tyrosine and Leucine to Arginine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.009</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>-0.013</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F24Y,
 
-
  L40R, T59N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24, 40, 59 on CapDCP from Phenylalanine to Tyrosine, Leucine to
 
-
  Arginine,<span style='mso-spacerun:yes'>  </span>and Threonine to Asparagine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.003</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.157</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>F24Y,R305K</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24 and 305 on CapDCP from Phenylalanine to Tyrosine and Arginine to Lysine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.002</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.233</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>F24Y,T59N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24 and 59 on CapDCP from Phenylalanine to Tyrosine and Threonine to
 
-
  Asparagine, respectively. Foldit-created linker, Circular Permutation, No
 
-
  Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.008</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.165</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>F24Y,T59N,R305K</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  24, 59, and 356 on CapDCP from Phenylalanine to Tyrosine, Threonine to
 
-
  Asparagine, and Arginine to Lysine, respectively. Foldit-created linker,
 
-
  Circular Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.002</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.127</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>F60W</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  60 on CapDCP from Phenylalanine to Tryptophan. Foldit-created linker,
 
-
  Circular Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.239</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.489</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>G79A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  79 on CapDCP from Glycine to Alanine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.040</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.511</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>I83T</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  83 on CapDCP from Isoleucine to Threonine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.009</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.006</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>I83V</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  83 on CapDCP from Isoleucine to Valine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.003</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.043</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>L40A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  40 on CapDCP from Leucine to Alanine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.150</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.413</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>L40R</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  40 on CapDCP from Leucine to Arginine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.157</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.527</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>L40S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  40 on CapDCP from Leucine to Serine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.166</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.577</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>L40W</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  40 on CapDCP from Leucine to Tryptophan. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.825</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.215</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>M61H</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  61 on CapDCP from Methionine to Histidine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.003</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.002</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>M61N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  61 on CapDCP from Methionine to Asparagine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.011</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.002</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  61 on CapDCP from Methionine to Serine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.262</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.485</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>N23K</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  23 on CapDCP from Asparagine to Lysine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.818</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.839</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>N23Q</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  23 on CapDCP from Asparagine to Glutamine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.165</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.646</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>S143K</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  143 on CapDCP from Serine to Lysine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.574</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.426</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>S22I,
 
-
  T59A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  22 and 59 on CapDCP from Serine to Isoleucine and Threonine to Alanine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.030</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.057</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>S22Q,
 
-
  T59Q</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  22 and 59 on CapDCP from Serine to Glutamine and Threonine to Glutamine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.012</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.085</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>S57H,
 
-
  M61H</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  57 and 61 on CapDCP from Serine to Histidine and Methionine to Histidine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.004</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.007</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T18L,
 
-
  T59Q, M61N, F452W</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  18, 59, 61, and 452 on CapDCP from Threonine to Leucine, Threonine to
 
-
  Glutamine, Methionine to Asparagine, and Phenylalanine to Tryptophan,<span
 
-
  style='mso-spacerun:yes'>  </span>respectively. Foldit-created linker,
 
-
  Circular Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.020</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.028</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T18S_T20S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  18 and 20 on CapDCP from Threonine to Serine and Threonine to Serine,<span
 
-
  style='mso-spacerun:yes'>  </span>respectively. Foldit-created linker,
 
-
  Circular Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.617</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.186</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  20 on CapDCP from Threonine to Alanine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.011</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.021</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20C</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  20 on CapDCP from Threonine to Cystine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.090</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.142</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  20 on CapDCP from Threonine to Serine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.639</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.443</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40D</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 40 on CapDCP from Threonine to Serine and Leucine to Asparagine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.853</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.001</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40E</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 40 on CapDCP from Threonine to Serine and Leucine to Glutamic Acid,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.163</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.637</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40F</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 40 on CapDCP from Threonine to Serine and Leucine to Phenylalanine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.246</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.335</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40H</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 40 on CapDCP from Threonine to Serine and Leucine to Histidine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.001</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.012</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40K</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 40 on CapDCP from Threonine to Serine and Leucine to Lysine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.000</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.007</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40Q</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 40 on CapDCP from Threonine to Serine and Leucine to Glutamine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.126</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.478</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40R</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 40 on CapDCP from Threonine to Serine and Leucine to Arginine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.000</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.009</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40R, F60E</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 40, and 60 on CapDCP from Threonine to Serine, Leucine to Arginine, and
 
-
  Phenylalanine to Glutamic Acid, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.048</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.028</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40R, F60Q</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 40, and 60 on CapDCP from Threonine to Serine, Leucine to Arginine, and
 
-
  Phenylalanine to Glutamine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.002</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.007</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40R, N81E</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 40, and 60 on CapDCP from Threonine to Serine, Leucine to Arginine, and
 
-
  Phenylalanine to Glutamine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.001</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>-0.004</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40R, N81Q</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 40, and 81 on CapDCP from Threonine to Serine, Leucine to Arginine, and
 
-
  Asparagine to Glutamine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.422</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.321</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40R, T59K</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 40, and 59 on CapDCP from Threonine to Serine, Leucine to Arginine, and
 
-
  Threonine to Lysine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.048</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.033</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6713667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  L40R, T59K_M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 40, 59, and 61 on CapDCP from Threonine to Serine, Leucine to Arginine,
 
-
  Threonine to Lysine, and Methionine to Serine, respectively. Foldit-created
 
-
  linker, Circular Permutation, No Signal Sequence, Single band on protein agarose
 
-
  gel</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.010</td>
 
-
  <td class=xl6813667 width=168 style='width:126pt'>0.032</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,
 
-
  T59Q, M61T</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 59, and 61 on CapDCP from Threonine to Serine, Threonine to Glutamine,
 
-
  and Methionine to Threonine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.007</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.069</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Alanine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.005</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.045</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61C</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Cystine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.102</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.207</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61D</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Aspartic Acid,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.004</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.003</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61G</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Glycine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.004</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.029</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61L</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Leucine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.004</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.029</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Asparagine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.003</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.002</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Serine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.007</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.053</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61T</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Threonine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.038</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.363</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,M61V</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 61 on CapDCP from Threonine to Serine and Methionine to Valine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.004</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.039</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,T59N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 59 on CapDCP from Threonine to Serine and Threonine to Asparagine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.019</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.125</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S,T59S_M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 59, and 61 on CapDCP from Threonine to Serine, Threonine to Serine, and
 
-
  Methionine to Serine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.300</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.719</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S_F24H</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 24 on CapDCP from Threonine to Serine and Phenylalanine to Histidine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.008</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.097</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S_F24Y</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20 and 24 on CapDCP from Threonine to Serine and Phenylalanine to Tyrosine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.040</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.201</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T20S_F24Y,T59N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  20, 24, and 59 on CapDCP from Threonine to Serine, Phenylalanine to Tyrosine,
 
-
  and Threonine to Asparagine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.013</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.048</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T2A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue 2
 
-
  on CapDCP from Threonine to Alanine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.007</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.020</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T2C</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at destroying all activity with poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue 2
 
-
  on CapDCP from Threonine to Cystine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.001</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.005</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T2S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue 2
 
-
  on CapDCP from Threonine to Serine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.024</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.325</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T2S,T18S_T20S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  2, 18, and 20 on CapDCP from Threonine to Serine, Threonine to Serine, and
 
-
  Threonine to Serine, respectively. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.144</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.250</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T2S,T18S_T20S,T59S_M61S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  2, 18, 20, 59, and 61 on CapDCP from Threonine to Serine, Threonine to
 
-
  Serine, Threonine to Serine, Threonine to Serine and Threonine to Serine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.003</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.022</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T2S,T20S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  2 and 20 on CapDCP from Threonine to Serine and Threonine to Serine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.106</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.089</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T2V</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at destroying all activity with poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue 2
 
-
  on CapDCP from Threonine to Valine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59H_M61A</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  59 and 61 on CapDCP from Threonine to Histidine and Methionine to Alanine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59H_M61T</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  59 and 61 on CapDCP from Threonine to Histidine and Methionine to Threonine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59M</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  59 on CapDCP from Threonine to Methionine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.008</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.008</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59N</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  59 on CapDCP from Threonine to Asparagine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.232</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.868</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59Q</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  59 on CapDCP from Threonine to Glutamine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.000</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59Q,
 
-
  M61Q, F452W</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  59, 61, and 452 on CapDCP from Threonine to Glutamine, Threonine to
 
-
  Glutamine, and Phenylalanine to Tryptophan, respectively. Foldit-created
 
-
  linker, Circular Permutation, No Signal Sequence, Single band on protein
 
-
  agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>-0.014</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.037</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59S</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residue
 
-
  59 on CapDCP from Threonine to Serine. Foldit-created linker, Circular
 
-
  Permutation, No Signal Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>3.525</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>1.047</td>
 
-
</tr>
 
-
<tr height=93 style='mso-height-source:userset;height:69.95pt'>
 
-
  <td height=93 class=xl6613667 width=172 style='height:69.95pt;width:129pt'>T59S,
 
-
  M61H</td>
 
-
  <td class=xl6513667 width=216 style='width:162pt'>A mutated CapDCP protein
 
-
  aimed at increasing hydrolysis and decreasing transpeptidation of
 
-
  poly-D-gamma-glutamate.</td>
 
-
  <td class=xl6513667 width=297 style='width:223pt'>Point mutation at residues
 
-
  59 and 61 on CapDCP from Threonine to Serine and Methionine to Histidine,
 
-
  respectively. Foldit-created linker, Circular Permutation, No Signal
 
-
  Sequence, Single band on protein agarose gel</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.013</td>
 
-
  <td class=xl6913667 width=168 style='width:126pt'>0.051</td>
 
-
</tr>
 
-
<![if supportMisalignedColumns]>
 
-
<tr height=0 style='display:none'>
 
-
  <td width=172 style='width:129pt'></td>
 
-
  <td width=216 style='width:162pt'></td>
 
-
  <td width=297 style='width:223pt'></td>
 
-
  <td width=168 style='width:126pt'></td>
 
-
  <td width=168 style='width:126pt'></td>
 
-
</tr>
 
-
<![endif]>
 
-
</table>
 
-
</div>
 
 +
var c_rgszClr=new Array(8);
 +
c_rgszClr[0]="window";
 +
c_rgszClr[1]="buttonface";
 +
c_rgszClr[2]="windowframe";
 +
c_rgszClr[3]="windowtext";
 +
c_rgszClr[4]="threedlightshadow";
 +
c_rgszClr[5]="threedhighlight";
 +
c_rgszClr[6]="threeddarkshadow";
 +
c_rgszClr[7]="threedshadow";
-
<!----------------------------->
+
var g_iShCur;
-
<!--END OF OUTPUT FROM EXCEL PUBLISH AS WEB PAGE WIZARD-->
+
var g_rglTabX=new Array(c_lTabs);
-
<!----------------------------->
+
 
-
</body>
+
function fnGetIEVer()
 +
{
 +
var ua=window.navigator.userAgent
 +
var msie=ua.indexOf("MSIE")
 +
if (msie>0 && window.navigator.platform=="Win32")
 +
  return parseInt(ua.substring(msie+5,ua.indexOf(".", msie)));
 +
else
 +
  return 0;
 +
}
 +
 
 +
function fnBuildFrameset()
 +
{
 +
var szHTML="<frameset rows=\"*,18\" border=0 width=0 frameborder=no framespacing=0>"+
 +
  "<frame src=\""+document.all.item("shLink")[0].href+"\" name=\"frSheet\" noresize>"+
 +
  "<frameset cols=\"54,*\" border=0 width=0 frameborder=no framespacing=0>"+
 +
  "<frame src=\"\" name=\"frScroll\" marginwidth=0 marginheight=0 scrolling=no>"+
 +
  "<frame src=\"\" name=\"frTabs\" marginwidth=0 marginheight=0 scrolling=no>"+
 +
  "</frameset></frameset><plaintext>";
 +
 
 +
with (document) {
 +
  open("text/html","replace");
 +
  write(szHTML);
 +
  close();
 +
}
 +
 
 +
fnBuildTabStrip();
 +
}
 +
 
 +
function fnBuildTabStrip()
 +
{
 +
var szHTML=
 +
  "<html><head><style>.clScroll {font:8pt Courier New;color:"+c_rgszClr[6]+";cursor:default;line-height:10pt;}"+
 +
  ".clScroll2 {font:10pt Arial;color:"+c_rgszClr[6]+";cursor:default;line-height:11pt;}</style></head>"+
 +
  "<body onclick=\"event.returnValue=false;\" ondragstart=\"event.returnValue=false;\" onselectstart=\"event.returnValue=false;\" bgcolor="+c_rgszClr[4]+" topmargin=0 leftmargin=0><table cellpadding=0 cellspacing=0 width=100%>"+
 +
  "<tr><td colspan=6 height=1 bgcolor="+c_rgszClr[2]+"></td></tr>"+
 +
  "<tr><td style=\"font:1pt\">&nbsp;<td>"+
 +
  "<td valign=top id=tdScroll class=\"clScroll\" onclick=\"parent.fnFastScrollTabs(0);\" onmouseover=\"parent.fnMouseOverScroll(0);\" onmouseout=\"parent.fnMouseOutScroll(0);\"><a>&#171;</a></td>"+
 +
  "<td valign=top id=tdScroll class=\"clScroll2\" onclick=\"parent.fnScrollTabs(0);\" ondblclick=\"parent.fnScrollTabs(0);\" onmouseover=\"parent.fnMouseOverScroll(1);\" onmouseout=\"parent.fnMouseOutScroll(1);\"><a>&lt</a></td>"+
 +
  "<td valign=top id=tdScroll class=\"clScroll2\" onclick=\"parent.fnScrollTabs(1);\" ondblclick=\"parent.fnScrollTabs(1);\" onmouseover=\"parent.fnMouseOverScroll(2);\" onmouseout=\"parent.fnMouseOutScroll(2);\"><a>&gt</a></td>"+
 +
  "<td valign=top id=tdScroll class=\"clScroll\" onclick=\"parent.fnFastScrollTabs(1);\" onmouseover=\"parent.fnMouseOverScroll(3);\" onmouseout=\"parent.fnMouseOutScroll(3);\"><a>&#187;</a></td>"+
 +
  "<td style=\"font:1pt\">&nbsp;<td></tr></table></body></html>";
 +
 
 +
with (frames['frScroll'].document) {
 +
  open("text/html","replace");
 +
  write(szHTML);
 +
  close();
 +
}
 +
 
 +
szHTML =
 +
  "<html><head>"+
 +
  "<style>A:link,A:visited,A:active {text-decoration:none;"+"color:"+c_rgszClr[3]+";}"+
 +
  ".clTab {cursor:hand;background:"+c_rgszClr[1]+";font:9pt Arial;padding-left:3px;padding-right:3px;text-align:center;}"+
 +
  ".clBorder {background:"+c_rgszClr[2]+";font:1pt;}"+
 +
  "</style></head><body onload=\"parent.fnInit();\" onselectstart=\"event.returnValue=false;\" ondragstart=\"event.returnValue=false;\" bgcolor="+c_rgszClr[4]+
 +
  " topmargin=0 leftmargin=0><table id=tbTabs cellpadding=0 cellspacing=0>";
 +
 
 +
var iCellCount=(c_lTabs+1)*2;
 +
 
 +
var i;
 +
for (i=0;i<iCellCount;i+=2)
 +
  szHTML+="<col width=1><col>";
 +
 
 +
var iRow;
 +
for (iRow=0;iRow<6;iRow++) {
 +
 
 +
  szHTML+="<tr>";
 +
 
 +
  if (iRow==5)
 +
  szHTML+="<td colspan="+iCellCount+"></td>";
 +
  else {
 +
  if (iRow==0) {
 +
    for(i=0;i<iCellCount;i++)
 +
    szHTML+="<td height=1 class=\"clBorder\"></td>";
 +
  } else if (iRow==1) {
 +
    for(i=0;i<c_lTabs;i++) {
 +
    szHTML+="<td height=1 nowrap class=\"clBorder\">&nbsp;</td>";
 +
    szHTML+=
 +
      "<td id=tdTab height=1 nowrap class=\"clTab\" onmouseover=\"parent.fnMouseOverTab("+i+");\" onmouseout=\"parent.fnMouseOutTab("+i+");\">"+
 +
      "<a href=\""+document.all.item("shLink")[i].href+"\" target=\"frSheet\" id=aTab>&nbsp;"+c_rgszSh[i]+"&nbsp;</a></td>";
 +
    }
 +
    szHTML+="<td id=tdTab height=1 nowrap class=\"clBorder\"><a id=aTab>&nbsp;</a></td><td width=100%></td>";
 +
  } else if (iRow==2) {
 +
    for (i=0;i<c_lTabs;i++)
 +
    szHTML+="<td height=1></td><td height=1 class=\"clBorder\"></td>";
 +
    szHTML+="<td height=1></td><td height=1></td>";
 +
  } else if (iRow==3) {
 +
    for (i=0;i<iCellCount;i++)
 +
    szHTML+="<td height=1></td>";
 +
  } else if (iRow==4) {
 +
    for (i=0;i<c_lTabs;i++)
 +
    szHTML+="<td height=1 width=1></td><td height=1></td>";
 +
    szHTML+="<td height=1 width=1></td><td></td>";
 +
  }
 +
  }
 +
  szHTML+="</tr>";
 +
}
 +
 
 +
szHTML+="</table></body></html>";
 +
with (frames['frTabs'].document) {
 +
  open("text/html","replace");
 +
  charset=document.charset;
 +
  write(szHTML);
 +
  close();
 +
}
 +
}
 +
 
 +
function fnInit()
 +
{
 +
g_rglTabX[0]=0;
 +
var i;
 +
for (i=1;i<=c_lTabs;i++)
 +
  with (frames['frTabs'].document.all.tbTabs.rows[1].cells[fnTabToCol(i-1)])
 +
  g_rglTabX[i]=offsetLeft+offsetWidth-6;
 +
}
 +
 
 +
function fnTabToCol(iTab)
 +
{
 +
return 2*iTab+1;
 +
}
 +
 
 +
function fnNextTab(fDir)
 +
{
 +
var iNextTab=-1;
 +
var i;
 +
 
 +
with (frames['frTabs'].document.body) {
 +
  if (fDir==0) {
 +
  if (scrollLeft>0) {
 +
    for (i=0;i<c_lTabs&&g_rglTabX[i]<scrollLeft;i++);
 +
    if (i<c_lTabs)
 +
    iNextTab=i-1;
 +
  }
 +
  } else {
 +
  if (g_rglTabX[c_lTabs]+6>offsetWidth+scrollLeft) {
 +
    for (i=0;i<c_lTabs&&g_rglTabX[i]<=scrollLeft;i++);
 +
    if (i<c_lTabs)
 +
    iNextTab=i;
 +
  }
 +
  }
 +
}
 +
return iNextTab;
 +
}
 +
 
 +
function fnScrollTabs(fDir)
 +
{
 +
var iNextTab=fnNextTab(fDir);
 +
 
 +
if (iNextTab>=0) {
 +
  frames['frTabs'].scroll(g_rglTabX[iNextTab],0);
 +
  return true;
 +
} else
 +
  return false;
 +
}
 +
 
 +
function fnFastScrollTabs(fDir)
 +
{
 +
if (c_lTabs>16)
 +
  frames['frTabs'].scroll(g_rglTabX[fDir?c_lTabs-1:0],0);
 +
else
 +
  if (fnScrollTabs(fDir)>0) window.setTimeout("fnFastScrollTabs("+fDir+");",5);
 +
}
 +
 
 +
function fnSetTabProps(iTab,fActive)
 +
{
 +
var iCol=fnTabToCol(iTab);
 +
var i;
 +
 
 +
if (iTab>=0) {
 +
  with (frames['frTabs'].document.all) {
 +
  with (tbTabs) {
 +
    for (i=0;i<=4;i++) {
 +
    with (rows[i]) {
 +
      if (i==0)
 +
      cells[iCol].style.background=c_rgszClr[fActive?0:2];
 +
      else if (i>0 && i<4) {
 +
      if (fActive) {
 +
        cells[iCol-1].style.background=c_rgszClr[2];
 +
        cells[iCol].style.background=c_rgszClr[0];
 +
        cells[iCol+1].style.background=c_rgszClr[2];
 +
      } else {
 +
        if (i==1) {
 +
        cells[iCol-1].style.background=c_rgszClr[2];
 +
        cells[iCol].style.background=c_rgszClr[1];
 +
        cells[iCol+1].style.background=c_rgszClr[2];
 +
        } else {
 +
        cells[iCol-1].style.background=c_rgszClr[4];
 +
        cells[iCol].style.background=c_rgszClr[(i==2)?2:4];
 +
        cells[iCol+1].style.background=c_rgszClr[4];
 +
        }
 +
      }
 +
      } else
 +
      cells[iCol].style.background=c_rgszClr[fActive?2:4];
 +
    }
 +
    }
 +
  }
 +
  with (aTab[iTab].style) {
 +
    cursor=(fActive?"default":"hand");
 +
    color=c_rgszClr[3];
 +
  }
 +
  }
 +
}
 +
}
 +
 
 +
function fnMouseOverScroll(iCtl)
 +
{
 +
frames['frScroll'].document.all.tdScroll[iCtl].style.color=c_rgszClr[7];
 +
}
 +
 
 +
function fnMouseOutScroll(iCtl)
 +
{
 +
frames['frScroll'].document.all.tdScroll[iCtl].style.color=c_rgszClr[6];
 +
}
 +
 
 +
function fnMouseOverTab(iTab)
 +
{
 +
if (iTab!=g_iShCur) {
 +
  var iCol=fnTabToCol(iTab);
 +
  with (frames['frTabs'].document.all) {
 +
  tdTab[iTab].style.background=c_rgszClr[5];
 +
  }
 +
}
 +
}
 +
 
 +
function fnMouseOutTab(iTab)
 +
{
 +
if (iTab>=0) {
 +
  var elFrom=frames['frTabs'].event.srcElement;
 +
  var elTo=frames['frTabs'].event.toElement;
 +
 
 +
  if ((!elTo) ||
 +
  (elFrom.tagName==elTo.tagName) ||
 +
  (elTo.tagName=="A" && elTo.parentElement!=elFrom) ||
 +
  (elFrom.tagName=="A" && elFrom.parentElement!=elTo)) {
 +
 
 +
  if (iTab!=g_iShCur) {
 +
    with (frames['frTabs'].document.all) {
 +
    tdTab[iTab].style.background=c_rgszClr[1];
 +
    }
 +
  }
 +
  }
 +
}
 +
}
 +
 
 +
function fnSetActiveSheet(iSh)
 +
{
 +
if (iSh!=g_iShCur) {
 +
  fnSetTabProps(g_iShCur,false);
 +
  fnSetTabProps(iSh,true);
 +
  g_iShCur=iSh;
 +
}
 +
}
 +
 
 +
window.g_iIEVer=fnGetIEVer();
 +
if (window.g_iIEVer>=4)
 +
  fnBuildFrameset();
 +
//-->
 +
</script>
 +
<![endif]><!--[if gte mso 9]><xml>
 +
<x:ExcelWorkbook>
 +
  <x:ExcelWorksheets>
 +
  <x:ExcelWorksheet>
 +
    <x:Name>MutantData Table</x:Name>
 +
    <x:WorksheetSource HRef="MutantData%20Table_files/sheet001.htm"/>
 +
  </x:ExcelWorksheet>
 +
  </x:ExcelWorksheets>
 +
  <x:Stylesheet HRef="MutantData%20Table_files/stylesheet.css"/>
 +
  <x:WindowHeight>8250</x:WindowHeight>
 +
  <x:WindowWidth>8595</x:WindowWidth>
 +
  <x:WindowTopX>360</x:WindowTopX>
 +
  <x:WindowTopY>75</x:WindowTopY>
 +
  <x:ProtectStructure>False</x:ProtectStructure>
 +
  <x:ProtectWindows>False</x:ProtectWindows>
 +
</x:ExcelWorkbook>
 +
</xml><![endif]-->
 +
</head>
 +
<frameset rows="*,39" border=0 width=0 frameborder=no framespacing=0>
 +
<frame src="MutantData%20Table_files/sheet001.htm" name="frSheet">
 +
<frame src="MutantData%20Table_files/tabstrip.htm" name="frTabs" marginwidth=0 marginheight=0>
 +
<noframes>
 +
  <body>
 +
  <p>This page uses frames, but your browser doesn't support them.</p>
 +
  </body>
 +
</noframes>
 +
</frameset>
</html>
</html>

Revision as of 20:26, 25 October 2010

Mutant Data Table