Table 1.

Accuracy of CS-ROSETTA structures for 16 proteins used during optimization

Protein namePDB IDNα/Nβ*Nres Ncs rmsdbb § , Årmsdall , Å
GB3 2OED 14/26563320.691.40
CspA 1MJC 0/33704051.572.19
Calbindin 4ICB 47/0754351.202.01
Ubiquitin 1D3Z 18/25764260.751.35
XcR50 1TTZ 28/16763521.532.30
DinI 1GHH 36/21814631.762.29
HPr 1POH 29/23854191.011.79
MrR16 1YWX 23/35885141.522.28
TM1112 1O5U 10/52895241.512.22
PHS018 2GLW 20/41925311.282.08
HR2106 2HZ5 37/25964701.652.42
TM1442 1SBO 41/231106471.091.88
Vc0424 1NXI 55/251146791.722.51
Spo0F 1SRR 55/251215901.242.02
Profilin 1PRQ 41/411255951.712.34
Apo_lfabp 1LFO 15/701296881.642.18
  • Additional information in SI Table 3.

  • *Number of residues in α-helix and β-strand.

  • Number of total residues. N- and C-terminal flexible tails are excluded from RMSD calculation (see SI Table 3).

  • Total number of CS-ROSETTA input chemical shifts.

  • §rmsd (Cα, C′, and N) of the lowest-energy model to the experimental structure.

  • rmsd (all non-H atoms) of the lowest-energy model to the experimental structure.

  • Protein HR2106 is a homodimer, only the monomer conformation is calculated and analyzed in this work.