Modeling Beta-Traces for Beta-Barrels from Cryo-EM Density Maps

Table 2

Accuracy of large size beta-barrel (more than fifteen strands) modeling from simulated density maps at 10 Å resolution.

PDB	#Det./#Obs.	2-w	#Det./#Obs.
2GUF_D23	21/22	2.03	230/296
2HDI_D23	22/22	1.93	226/296
2J1N_AA18	16/16	1.77	146/181
2MPR_A19	19/19	2.49	134/224
2POR_S117	12/16	2.53	94/178
2QDZ_C17	16/16	1.32	177/198
2YNK_AC20	20/18	2.26	133/194
3CSL_C23	23/22	2.59	171/300
3EMN_A20	20/19	1.83	135/183
3PRN_A17	15/17	1.67	131/162
3SYB_A19	19/18	2.12	155/220
4C00_AE17	17/16	2.37	121/202
4GEY_A18	19/16	2.33	116/189
4K3C_C18	18/16	2.43	126/193
Average		2.12	2095/3016 = 69.46%
Standard deviation		0.38

_Sheet ID.
number of β-traces in the best of the fifteen possible sets/the number of β-strands in the β-sheet of the PDB structure.
2-way distance (in Å) between the observed β-traces and the modeled β-traces for the best of the fifteen possible sets.
number of detected/the total number of amino acids in the β-barrel.