Supplementary Figure 10: Evaluation of structure quality statistics for reference X-ray crystal and NMR spectroscopy structures, and EC-NMR structures.
From: Protein structure determination by combining sparse NMR data with evolutionary couplings
The ensembles of EC-NMR structures described in the main text were assessed using NMR DP scores16,25 and structural quality metrics of the Protein Structure Validation Software Suite (PSVS). The reference structures and EC-NMR structures assessed include (A) RASH, (B) P74712, and (C) Maltose Binding Protein (MBP) generated by X-ray crystallography (X-ray, the reference structures), EC’s alone (EC), sparse NMR data alone (sparse NMR), the EC-NMR method using only available experimental data (EC-NMR), and EC-NMR supplemented with additional RDC data as described in the On Line Methods (EC-NMR*). PSVS structure quality Z scores < -6 were set to -6. According to the criteria outlined in the text (and Supplementary Figure 9), the X-ray reference structures and the EC-NMR structures are all classified as “reliable” structures (DP > ~ 0.73; structure quality Z scores > -2), while the EC alone structures are classified as “less accurate” structures. Structures determined with sparse NMR data alone (sparse NMR) have marginal structure quality scores, which are improved in the more accurate EC-NMR structures.
