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. Author manuscript; available in PMC: 2014 Aug 1.
Published in final edited form as: J Biomol NMR. 2013 Jul 30;56(4):337–351. doi: 10.1007/s10858-013-9753-7

Table 4.

Backbone (N, Cα, C) RMSD and GDT-TS scores comparing structures of NESG target proteins ZR18 and PfR193A generated with the standard NESG CYANA-CNSw protocol, with the same structures refined with rCS-Rosetta following restraint conversion using PDBStat. These ensembles of NMR conformers are compared with the corresponding X-ray crystal structure coordinates.

Number of Residuesa rCS-Rosetta vs. CNSw RMSD / GDT-TS /GDT-HA rCS-Rosetta vs. X-ray RMSD / GDT-TS /GDT-HA CNSw vs. X-rayb RMSD / GDT-TS /GDT-HA
ZR18 91 1.18 Å / 0.86 / 0.68 0.98 Å / 0.94 / 0.79 1.40 Å / 0.82 / 0.62
PfR193A 114 0.42 Å / 0.97 / 0.86 0.57 Å / 0.99 / 0.93 0.64 Å / 0.99 / 0.89
a

Well-defined residues were determined by PDBStat using the FindCore [35] method.

b

For target ZR18, the PDB_id of the reference X-ray crystal structure is 2ffm. For target PfR193A, the PDB_id of the reference X-ray crystal structure is 2idu.