| Summary: | We describe an alternate approach to protein structure determination that
relies on experimental NMR chemical shifts, plus sparse NOEs if available. The
newly introduced alignment method, POMONA, directly exploits the powerful
bioinformatics algorithms previously developed for sequence-based homology
modeling, but does not require significant sequence similarity. Protein
templates, generated by POMONA, are subsequently used as input for chemical
shift based Rosetta comparative modeling (CS-RosettaCM) to generate reliable
full atom models.
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