Supplementary Figure 3: Contact maps illustrating the EC-NMR process.

Residue-residue contact maps illustrating the process of EC-NMR hybrid method for structure determination. (A) A9CJD6_AGRTT5 (no experimental RDC data). (B) A9CJD6_AGRTT5 (2 simulated RDC alignment tensors). (C) Q6D6V0_ERWCT (2 experimental RDC alignment tensors). (D) Q9ZV63_ARATH (2 experimental RDC alignment tensors). (E) Q1LD49_RALME (1 experimental RDC alignment tensor). (F) Q1LD49_RALME (1 experimental RDC alignment tensor and 1 simulated RDC alignment tensor). (G) RASH_HUMAN (no experimental RDC data). (H) RASH_HUMAN (2 simulated RDC alignment tensor). (I) YIAD_ECOLI (2 experimental RDC alignment tensors). (J) P74712_SYNY3 (2 experimental RDC alignment tensors). (K) MALE_ECOLI (1 experimental RDC alignment tensor). (L) MALE_ECOLI (1 experimental RDC alignment and 1 simulated RDC alignment tensor). For each protein, the superimposed ribbon diagrams are shown above the first triangles. Green ribbon - final EC-NMR structure. Grey ribbon - reference X-ray crystal structures (G, H, J, K, L) or NMR structures (A, B, C, D, E, F, I). In the contact map, Grey contacts – contacts in the reference X-ray crystal structure (G, H, J, K, L) or NMR structure (A, B, C, D, E, F, I); Red contacts – initial EC residue-pair contacts; Blue contacts – contacts indicated by unambiguous NOESY peak assignments obtained by ASDP using only the sparse NMR data; Green contacts – final residue-pair contacts resulting from simultaneous analysis of EC and sparse NMR data; Orange contacts in the upper triangle of the middle panel – all ambiguous NOESY peak potential assignments obtained by ASDP in the first cycle prior to incorporating EC data; Orange contacts in the upper triangle of the right panel –final NOESY peak assignments obtained used in conventional NMR structure determinations done with essentially complete chemical shift data including sidechain resonance assignments. These orange contacts in right panels illustrate the contact information obtained for a fully protonated NMR sample with extensive sidechain assignments, which is available for some of the smaller proteins used to test the EC-NMR method. For P74712_SYNY3 (J) and MALE_ECOLI (K, L), all available NMR structures in the PDB were solved using sparse NMR data with limited sidechain resonance assignments, thus orange contacts in the upper triangle region of the right panel are not available.