Table 1.

Protein structures used to evaluate the performance of PCS-ROSETTA

Targets	Protein Data Bank ID	Nresa	NMb	NPCSc	PCS-ROSETTA rund			CS-ROSETTA rune		RefCSf	RefPCSg
					rmsdh	Convegencei	Qj	rmsdh	Convergencei
Protein G (A)	3GfB1	56	3	158	0.61	0.92	0.06	0.80	0.88	33	34
Calbindin (B)	1KQV	75	11	1169	1.46	2.04	0.16	4.96	4.37	35	4
θ subunit (C)	2AE9	76	2	91	1.65	4.35	0.07	8.90	8.75	36	37
ArgNk (D)	1AOY	78	3	222	0.98	2.38	0.08	6.93	5.32	21	21
ArgNl (E)	1AOY	78	2	82	1.03	2.25	0.09	8.01	6.64	21	38
N-Calmodulin (F)	1SW8	79	2	125	2.34	1.85	0.09	4.69	3.68	39	39
Thioredoxin (G)	1XOA	108	1	90	2.58	2.64	0.23	4.98	6.06	40, 41	42
Parvalbumin (H)	1RJV	110	1	106	11.26	10.42	0.20	11.80	11.20	43	43
Calmodulin (I)	2K61	146	4	408	2.80	2.12	0.14	6.35	5.55	44	44
ε186m (J)	1J54	186	3	738	20.57	17.54	0.36	15.46	17.23	45	46

^aNumber of residues.

^bNumber of metal ions for which PCS data were measured.

^cTotal number of PCSs measured.

^dThe structures used to calculate the rmsd values were identified using the combined PCS score and ROSETTA full-atom energy on the whole protein sequence.

^eThe structures used to calculate the rmsd values were identified by the ROSETTA full-atom energy on the whole protein sequence.

^fReference to source of chemical shifts in diamagnetic state of the protein.

^gReference to source of PCS data of the protein.

^hC^α rmsd (with respect to the native structure) of the structure of lowest score, in angstroms. All C^α rmsd values were calculated using the core residues defined in Supplementary Table 1.

ⁱAverage C^α rmsd calculated between the lowest-score structure and the next four lowest-scoring structure, in angstroms. The rmsd values were calculated on the whole protein sequence.

^jQuality factor $Q=\text{rms}({\text{PCS}}_i^{\text{calc}}-{\text{PCS}}_i^{exp})/\text{rms}({\text{PCS}}_i^{exp})$ calculated on the structure of lowest PCS-ROSETTA score.

^kPCS measured with covalently attached dipicolinic acid tag.

^lPCS measured with non-covalently bound [Ln(DPA)₃]³⁻.

^mN-terminal 186 residues of the ε subunit of the E. coli polymerase III.