Fig. 5: Robustness of MAUS assignments from different structural models.
From: Backbone-independent NMR resonance assignments of methyl probes in large proteins
a Top: flowchart showing the combined de novo structure modeling and methyl resonance assignment strategy using trRosetta (transform-restrained Rosetta) and MAUS, respectively. (bottom) Overlay of trRosetta model (wheat) and X-ray structure (PDB ID: 1DMB; pale cyan) of maltose-binding protein. Number of resonance assignment options identified by MAUS are indicated by colored spheres (violet: 1, green: 2, yellow: 3 and red: >3). b Top: structures of a designed homotrimeric protein27, in the open (solved by X-ray crystallography) and closed (solved by solution NMR) states showing inter-methyl distances corresponding to experimental NOEs identified in a 3D CM-CMHM NOESY spectrum, assigned manually27. Gray spheres show methyl residues participating in the NOE network. The dashed lines represent pairwise distances in the two models, also shown as bar plots (bottom) for the open (gray) and closed (golden) states. The dashed line in the bar plot highlights the 10 Å NOE upper distance limit used by MAUS. Using the unassigned NOE peaks, MAUS delivers a set of satisfying assignments when provided with a model of the closed, but not of the open structure as input.
