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. Author manuscript; available in PMC: 2018 Jul 24.
Published in final edited form as: J Magn Reson. 2014 Dec 4;251:65–70. doi: 10.1016/j.jmr.2014.11.011

Table 2.

Feature comparison among the three 1H–15N HSQC spectra collected on a 26 kDa 15N-labeled protein.

Type Pulse program Cross-peak sign Averaged S/Na Experimental timeb

NH NH2 Separation
Standard Bruker hsqcfpf3gpphwg + + No 32.4 3 h 18 min
Standard multiplicity-edited hsqcfpf3gpphwg with an extra 1/1JNH period after t1 + No 24.6 3 h 21 min
Semi-CT The 1JNH-active version in Fig. 1A + Yes 27.1 3 h 12 min
a

A total of 137 isolated cross-peaks were picked on all spectra and peak S/N were calculated using Sparky (T.D. Goddard and D.G. Kneller, University of California, San Francisco). The averaged S/N are shown.

b

The sample is a 0.1 mM 15N-labeled retroviral capsid protein (26 kDa). All HSQC spectra were collected on a Bruker 500 MHz spectrometer equipped with a room-temperature probe.