Skip to main content
. Author manuscript; available in PMC: 2013 Apr 1.
Published in final edited form as: J Biomol NMR. 2012 Feb 14;52(4):315–327. doi: 10.1007/s10858-012-9611-z

Table 1.

Acquisition and processing parameters of the experiments shown.

a) 3D 15N-dispersed NOESY: The spectrum was recorded on 0.8 mM sample of the M50 protein (19.4 kDa), sampling density 6% (2,400 of 40,000 complex points), measured on a Bruker Avance 800. FM reconstruction (500 iterations) on a Cuda computer using 4 Nvidia GPU cards was achieved in 1.5 days. IST reconstruction on a 128 cpu cluster was obtained in 3 min.
Dimension Spectral width (Hz) Number of complex points Maximal evolution time (ms)
F1 1H 9,606.148 400 41.62
F2 15N 2,000.00 100 50.00
F3 1H 9,765.6 1024 104.8
b) 4D 13C dispersed methyl-methyl NOESY (150 ms mixing time): The spectrum was recorded on a 1 mM sample of the Med25 complex with the transactivation domain of VP16 (28 kDa), sampling density 14.5%. Recorded on a Bruker Avance 750 with four scans per FID and a total measuring time of 7.5 days. FM reconstruction on one cube took 13 hrs on a Cuda computer using 4 Nvidia GPU cards. IST reconstruction of one cube on a single 32 Xeon cpu required 30 min, and all 339 cubes were reconstructed in 1.5 hrs on a cluster of 128 cpus.
Dimension Spectral width (Hz) Number of complex points Maximal evolution time (ms)
F1 1H 1,650 28 17
F2 13C 3,300 44 13
F3 13C 3,300 96 29
F4 1H 10,000 768 77
c) High-resolution 4D 13C dispersed methyl-methyl NOESY (120 ms mixing time): The spectrum was recorded on a 0.9 mM sample of a 10 kDa protein G construct containing the B1 domain with a sampling density of 0.8% (10,906 of 1,350,000 complex points), measured on a Bruker AMX 500 with four scans per FID and a total measuring time of 5 days. IST reconstruction was achieved in one day on a cluster of 128 cpus.
Dimension Spectral width (Hz) Number of complex points Maximal evolution time (ms)
F1 1H 500.1 60 118
F2 13C 1,257.6 150 118.4
F3 13C 1,257.6 150 118.8
F4 1H 6666.7 1024 154