sci-chemistry/panav/metadata.xml


1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30

<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE pkgmetadata SYSTEM "http://www.gentoo.org/dtd/metadata.dtd">
<pkgmetadata>
  <herd>sci-chemistry</herd>
  <maintainer>
    <email>jlec@gentoo.org</email>
  </maintainer>
  <longdescription>
It has been estimated that more than 20% of the proteins in the BMRB are 
improperly referenced and that about 1% of all chemical shift assignments are 
mis-assigned. These statistics also reflect the likelihood that any newly 
assigned protein will have shift assignment or shift referencing errors. The 
relatively high frequency of these errors continues to be a concern for the 
biomolecular NMR community. While several programs do exist to detect and/or 
correct chemical shift mis-referencing or chemical shift mis-assignments, most 
can only do one, or the other. The one program (SHIFTCOR) that is capable of 
handling both chemical shift mis-referencing and mis-assignments, requires the 
3D structure coordinates of the target protein. Given that chemical shift 
mis-assignments and chemical shift re-referencing issues should ideally be 
addressed prior to 3D structure determination, there is a clear need to develop 
a structure-independent approach. Here, we present a new structure-independent 
protocol, which is based on using residue-specific and secondary 
structure-specific chemical shift distributions calculated over 
small (3–6 residue) fragments to identify mis-assigned resonances. The method 
is also able to identify and re-reference mis-referenced chemical shift 
 assignments. Comparisons against existing re-referencing or mis-assignment 
 detection programs show that the method is as good or superior to existing 
 approaches.
</longdescription>
</pkgmetadata>