NMR spectra were acquired at 318 K using an Agilent Varian VNMRS 500 MHz spectrometer equipped with a 5 mm HCN probe. This temperature was chosen to prevent interference from the resonance of residual HDO. The NMR chemical shifts were referenced with respect to the resonances of the anomeric CH-group (H-1) of α-D-mannose at 5.17 ( 1 H) and 96.8 ppm ( 13 C), these values from the NMR chemical shift database BioMagResBank 1 (www.bmrb.wisc.edu, entry no. bmse000018) were measured using a solution of α-D-mannose (0.5 mM) in 50 mM sodium phosphate buffer, equivalent to pH 7.4, in D2O at 298 K, referenced to sodium trimethylsilylpropane-sulfonate (DSS). Standard 2D experiments (DQF-COSY, z-TOCSY with 120 ms mixing time, NOESY with 500 ms mixing time, C-HSQC, and 13 C-HMBC, optimized for 8 Hz) were used for chemical shift assignments, using SPARKY 2 software. TOCSY and NOESY experiments were typically run using a spectral width of 4680 Hz in the indirect dimension, 512 increments, 32 scans, and a recycle delay of 2 s, resulting in roughly 22 h acquisition time. The 2D C-HSQC experiment was acquired with improved resolution in the indirect dimension using non-uniform sampling (NUS) of 400 (41%) out of a total of 974 increments. The experiment used a recycle delay of 2 s, 32 scans, and an indirect spectral width of 12066 Hz, giving a total acquisition time of 16 h. The NUS sampled C-HSQC experiment was reconstructed and processed using NMRPipe . The 1 JC-1,H-1 scalar coupling constants were determined from the C-satellites in a 1D 1 H spectrum.