Table 3.

The results of RDC-guided docking using PATIDOCK for the SINGLE dataset based on experimental RDC data.

Protein	PDBa	RMSDb	RMSD2c	Δcd	RMSDRDCe	Time(s)f	#Sol.g
B1 domain of protein G	3gb1	0.92	2.14	2.02	1.17	2.20	8
B3 domain of protein G	2oed	1.68	4.30	4.28	1.20	2.08	8
Cyanovirin-N	2ezm	1.92	5.02	5.02	3.99	2.56	10
Gα interacting protein	1cmz	2.72	7.04	6.75	1.40	2.63	8
Ubiquitin	1d3z	1.79	3.77	3.76	1.29	2.66	9
Hen lysozyme	1e8l	1.60	3.29	3.29	7.20	3.19	8
Oxidized putidaredoxin	1yjj	2.51	5.40	5.32	4.53	2.94	9
Mean		1.88	4.42	4.35	2.97	2.61	8.43

^aThe RCSB Protein Data Bank code for protein coordinates. First model from the ensemble of NMR structures was used for all calculations.

^bThe backbone RMSD (in Å) between the original complex structure and the predicted complex. The structures are optimally rotated and centered using the center of mass.³⁹

^cThe backbone RMSD (in Å) between the coordinates of atoms of the second domain for the original and the predicted complex.

^dThe distance (in Å) between the original and the predicted center of the second domain. The center is computed as the average of the positions of all the atoms in the domain.

^eThe RMSD (in Hz) between the experimental and the predicted RDC values at the best predicted minimizer.

^fThe elapsed time (in seconds) required for docking of all four orientations.

^gThe number of possible solutions, all of which have a very similar predicted alignment tensor.