Using NMR for allosterics of an Enzyme:
Stevens, S.Y., Sanker, S., Kent, C. and Zuiderweg, E.R.P. Delineation of the allosteric mechanism for a cytidylyltransferase  exhibiting negative cooperativity, Nature Structural Biology 8, 947-952 (2001)  
 

High Resolution Structure of a Hsp70 Chaperone based on 4500 NOEs:
Morshauser, R.C., Hu, W., Wang, H., Pang, Y., Flynn, G.C. and Zuiderweg, E.R.P. High resolution solution structure of the 18 kda substrate binding domain of the mammalian chaperone protein hsc70. J. Mol. Biol, 289, 1387-1403 (1999)

Structure of a 21 kDa DnaK Chaperone based on 1100 NOEs:
Wang, H., Pang, Y, Kurochkin, A.V.,  Hu, W., Flynn, G.C, and Zuiderweg, E.R.P.  The solution  structure of the 21 kDa chaperone protein DnaK substrate binding domain:  a preview of  chaperone - protein interaction.  Biochemistry  37 , 7929-7940 (1998)

An early structure of a larger protein: 19 kDa Stromelysin
Van Doren, S.W., Kurochkin, A.V., Hu, W., Ye, Q.Z., Johnson, L.L., Hupe, D.J. and Zuiderweg, E.R.P. Solution structure of the catalytic domain of human stromelysin  complexed with a hydrophobic inhibitor. Protein Science 4, 2487-2498 (1995)