Fig. 3: Performance of MAUS on simulated ILV data graphs from larger proteins.
From: Backbone-independent NMR resonance assignments of methyl probes in large proteins
a Top: target size distribution (in terms of number of methyl groups from Ile, Leu, and Val residues) of 63 proteins with high-resolution PDB structures of sizes up to 116 kDa (352 methyls; PDB ID: 5WTI) (top). For each target, a data graph H was simulated by removing edges from the corresponding structure graph G (defined as all methyl connectivities up to 10 Å present in the 3D structure) until a degree connectivity (defined as 2 × number of edges/number of nodes) in the range of 3.5–4.2 was reached, corresponding to 1.75–2.1 simulated NOEs/methyl. Bottom: bar plot showing the distribution of degree connectivities among all simulated data graphs. b Scatter plot showing run time (in minutes) taken by MAUS to perform exhaustive enumeration of the possible methyl assignment options for each H into G mapping case. Colors indicate % of methyls with up to three assignment options, according to the scale on the right.
