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. Author manuscript; available in PMC: 2016 Apr 1.
Published in final edited form as: Proteins. 2015 Feb 7;83(4):735–745. doi: 10.1002/prot.24755

Table 3.

Summary data of six principal structural models of conformational states of LacY and XylE used in this study.

PDB ID Protein Conformation Resolution*
4OAA LacY Outward occluded 3.50
2Y5Y LacY Inward, affinity inactivator-occluded 3.38
2V8N LacY Inward open 3.60
4GBY XylE Outward occluded 2.81
4JA3 XylE Inward occluded 3.80
4JA4 XylE Inward open 4.20
*

) The magnitude of the TMS11 movement differs in panels b and d of Figure 1, being on the order of 4 Å for LacY, and 6 to 8 Å for XylE. The resolution limits are better on average for LacY, never reaching the 4 Å threshold, whereas for XylE in the inward open state, the resolution is only 4.2 Å.