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. 2009 Nov 5;78(5):1311–1325. doi: 10.1002/prot.22651

Table I.

Real Protein Controls

PDB code Residues Chain Radius of gyration/Å Experimental method Resolution/Å Rosetta energy after relaxation
2jdi 10–81 D 10.39 XTAL 1.90 −150.74
2bwf 2–73 A 10.49 XTAL 1.15 −154.59
2as0 1–72 A 10.50 XTAL 1.80 −164.50
1osd 1–72 A 10.70 XTAL 2.00 −152.30
1ubq 1–72 A 10.71 XTAL 1.80 −166.36
1wm3 17–88 A 10.87 XTAL 1.20 −154.52
1hyp 6–77 A 10.88 XTAL 1.80 −115.45
1cc8 2–73 A 10.91 XTAL 1.02 −151.57
4ait 3–74 A 10.91 NMR n/a −122.73
1o8b 127–198 A 10.92 XTAL 1.25 −146.61
1lea 1–72 A 10.96 NMR n/a −153.41
1zyb 149–220 A 11.12 XTAL 2.00 −156.17
1v97 94–165 A 11.17 XTAL 1.94 −109.02
1vcc 1–72 A 11.30 XTAL 1.60 −161.37
1iyu 1–72 A 11.31 NMR n/a −139.04
1i27 445–516 A 11.81 XTAL 1.02 −150.68
1dzf 144–215 A 12.05 XTAL 1.90 −146.29

Rosetta energies of the wild-type sequences are given after idealization and one round of Rosetta relaxation.