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Files “parallhdg.pro" and “topallhdg.pro" for
NMR Structure Determination of Proteins (All Hydrogens)
The weighting among bonds, bond angles, planarity, and chirality
reflects the special requirements when using interproton distance
restraints. Special improper terms have been added to maintain
the trans- or cis-peptide bonds, chirality of all
tetrahedral centers, and planarity of peptide bonds and
aromatic rings. The peptide
bond conformation is described by an improper angle that constrains
the conformation to trans. The
patch CISP allows the user to switch a trans-
to a cis-peptide
bond. The patch LTOD allows the user to switch from L to D
amino acids. The peptide-bond linkages
(Section 3.7.3) are defined in “toph19.pep".
Subsections
Xplor-NIH 2025-03-21