title: EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
abstract: For several of the proteins in the BioMagResBank larger than 200 residues, 60 % or fewer of the backbone resonances were assigned. But how reliable are those assignments? In contrast to complete assignments, where it is possible to check whether every triple-resonance Generalized Spin System (GSS) is assigned once and only once, with incomplete data one should compare all possible assignments and pick the best one. But that is not feasible: For example, for 200 residues and an incomplete set of 100 GSS, there are 1.6 × 10260 possible assignments. In "EZ-ASSIGN", the protein sequence is divided in smaller unique fragments. Combined with intelligent search approaches, an exhaustive comparison of all possible assignments is now feasible using a laptop computer. The program was tested with experimental data of a 388-residue domain of the Hsp70 chaperone protein DnaK and for a 351-residue domain of a type III secretion ATPase. EZ-ASSIGN reproduced the hand assignments. It did slightly better than the computer program PINE (Bahrami et al. in PLoS Comput Biol 5(3):e1000307, 2009) and significantly outperformed SAGA (Crippen et al. in J Biomol NMR 46:281-298, 2010), AUTOASSIGN (Zimmerman et al. in J Mol Biol 269:592-610, 1997), and IBIS (Hyberts and Wagner in J Biomol NMR 26:335-344, 2003). Next, EZ-ASSIGN was used to investigate how well NMR data of decreasing completeness can be assigned. We found that the program could confidently assign fragments in very incomplete data. Here, EZ-ASSIGN dramatically outperformed all the other assignment programs tested.
authors.forename: Erik R  P
authors.initials: ER
authors.lastname: Zuiderweg
authors.forename: Ireena
authors.initials: I
authors.lastname: Bagai
authors.forename: Paolo
authors.initials: P
authors.lastname: Rossi
authors.forename: Eric B
authors.initials: EB
authors.lastname: Bertelsen
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry; D000465:Algorithms; D000595:Amino Acid Sequence; D030562:Databases, Protein; D006801:Humans; D008292:Malate Synthase / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular; D011506:Proteins / Q000737:chemistry*; D016875:tau Proteins / Q000737:chemistry
chemical_list: D011506:Proteins; D016875:tau Proteins; D008292:Malate Synthase; D000251:Adenosine Triphosphatases
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