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. 2010 Aug 20;285(43):32906–32918. doi: 10.1074/jbc.M110.151316

TABLE 3.

Pairwise conformational comparisons between the five H77_NS5b molecules in two crystal forms (X1 and X2) and the best-defined J4_NS5b molecule in crystal form O (J4*_O2_B; see the legend to Table 4)

The letters A, B, and C indicate the protein chain used for the analysis; several protein molecules present in each asymmetric unit (Table 2). 〈esd〉, average coordinate error for α carbons in Å. The values are the percentages of residues whose α carbons are not in significantly different positions given tolerance (ESCET lolim parameter) of 2.5 σ (5 σ; for the values in parentheses). Values larger than 98% indicate identical molecules within error (49). With a higher lolim, significant global differences (values smaller than 98%, in bold) are still observed between H77_NS5b and J4_NS5b, whereas no differences remain between H77_NS5b chains and crystal forms. The underlined value refers to the molecules and lolim parameter used for Fig. 2.

H77_X1_A H77_X1_B H77_X1_C H77_X2_A H77_X2_B J4*_O2_B
〈esd〉 (Å) 0.08 0.12 0.10 0.08 0.08 0.08
H77_X1_A 97.9 (99.9) 95.3 (99.9) 98.2 (100.0) 93.0 (99.7) 72.4 (94.9)
H77_X1_B 95.5 (99.7) 98.0 (99.9) 93.2 (99.4) 80.9 (97.4)
H77_X1_C 93.4 (99.8) 99.4 (100.0) 81.1 (97.6)
H77_X2_A 89.9 (99.2) 70.5 (93.3)
H77_X2_B 77.7 (96.5)
J4*_O2_B