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. Author manuscript; available in PMC: 2016 Jan 1.
Published in final edited form as: J Biomol NMR. 2014 Nov 27;61(1):47–53. doi: 10.1007/s10858-014-9881-8

Fig. 3.

Fig. 3

Survey of the assignment results for 30 JCSG target proteins. Backbone assignments obtained automatically by UNIO-MATCH-2014, and final assignments after interactive validation using a 3D 15N-resolved [1H,1H]-NOESY spectrum are shown. (a) Histograms showing the percentages of residues assigned. Residues assigned completely and partially by UNIO-MATCH-2014 are represented by red and pink bars, respectively. Blue and cyan bars represent the corresponding results after interactive validation and extension of the backbone assignment with the use of 3D 15N-resolved and 13Cali-resolved [1H, 1H]- NOESY data. (b) Percentages of residues that were erroneously assigned by UNIO-MATCH-2014 are indicated with green bars (these are contained in the red and/or pink bars), and those that were left unassigned are represented by yellow bars. From left to right, the proteins are arranged according to molecular weights, showing that the assignment results are not correlated with the protein size over the range from 62 to 152 residues, but rather with the quality of the NMR spectra (see also the text).