TASSER‐based refinement of NMR structures

The TASSER structure prediction algorithm is employed to investigate whether NMR structures can be moved closer to their corresponding X‐ray counterparts by automatic refinement procedures. The benchmark protein dataset includes 61 nonhomologous proteins whose structures have been determined by both NMR and X‐ray experiments. Interestingly, by starting from NMR structures, the majority (79%) of TASSER refined models show a structural shift toward their X‐ray structures. On average, the TASSER refined models have a root‐mean‐square‐deviation (RMSD) from the X‐ray structure of 1.785 Å (1.556 Å) over the entire chain (aligned region), while the average RMSD between NMR and X‐ray structures (RMSDNMR_X‐ray) is 2.080 Å (1.731 Å). For all proteins having a RMSDNMR_X‐ray >2 Å, the TASSER refined structures show consistent improvement. However, for the 34 proteins with a RMSDNMR_X‐ray <2 Å, there are only 21 cases (60%) where the TASSER model is closer to the X‐ray structure than NMR, which may be due to the inherent resolution of TASSER. We also compare the TASSER models with 12 NMR models in the RECOORD database that have been recalculated recently by Nederveen et al. from original NMR restraints using the newest molecular dynamics tools. In 8 of 12 cases, TASSER models show a smaller RMSD to X‐ray structures; in 3 of 12 cases, where RMSDNMR_X‐ray <1 Å, RECOORD does better than TASSER. These results suggest that TASSER can be a useful tool to improve the quality of NMR structures. Proteins 2006. © 2006 Wiley‐Liss, Inc.