Table 3.

Accuracy of beta-barrel modeling from cryo-EM experimental maps at medium resolutions.

EMD_PDB IDa	Res.b	#Det./#Obs. Strdc	2-w Dist.d	#Det./#Obs. AAe
1657_4V5H_AH4	5.8 Å	6/6	1.94	25/30
1780_4V7E_AH4	5.5 Å	5/5	1.88	24/28
1829_4V5H_AH4	5.6 Å	8/6	2.11	25/30
1849_4V6K_AE6	8.25 Å	7/6	2.34	24/40
1849_4V6K_AC6		6/5	1.90	26/31
1849_4V6K_AG2		6/6	2.74	31/52
5030_4V68_AF8	6.4 Å	4/5	1.72	24/32
5036_4V69_AD5	6.7 Å	5/5	1.73	23/29
Average			2.05	202/272 = 74.26%
Standard deviation			0.35

^aEMDB_PDB_Sheet ID.

^bResolution of the cryo-EM density map.

^cThe number of β-traces detected in the best of the fifteen possible sets/the number of β-strands in the β-sheet of the PDB structure.

^dThe 2-way distance (in Å) between the observed β-traces and the modeled β-traces for the best of the fifteen possible sets.

^eThe number of detected/the total number of amino acids in the β-barrel.