TABLE 1.

List of peptide sequences (with associated MPER residue variation) that were used for cocrystallization experiments with 2F5 Fab′

PeptideAmino acid sequenceVariation at position:X-ray diffraction dataa
Resolution range (Å)Rsym (%)Complete (%)Rwork (%)Rfree (%)PDB ID
1ELDKWASHXB2b12.0-2.003.5 (31.3)90.0 (93.3)23.225.82F5B
2ALDKWAS66212.0-2.103.3 (38.6)97.4 (96.9)22.123.61U8H
3ELAKWAS664
4ELEKWAS66450.0-2.246.0 (36.8)85.6 (83.2)22.823.81U8Q
5ELNKWAS664
6ELQKWAS664
7ELDAWAS665
8DLDRWAS662, 66517.0-2.608.8 (35.6)88.3 (88.0)22.324.91U8L
9ELDHWAS66580.0-2.245.6 (24.6)96.9 (100)21.023.91U95
10ELD(Orn)WAS66580.0-2.244.6 (11.8)91.3 (97.4)22.922.73IDJ
11ELD(Nrg)WAS66580.0-2.245.7 (31.3)93.2 (99.9)22.923.63IDM
12ELD(Paf)WAS66550.0-2.256.3 (23.6)97.4 (99.1)22.023.83IDN
13ELDEWAS665
14ELDKAAS666
15ELDKYAS66650.0-2.405.4 (36.4)99.2 (96.3)21.822.61U8M
16ELDKFAS66650.0-2.569.6 (37.1)92.2 (93.9)20.523.11U8N
17ELDKHAS66620.0-3.029.5 (34.7)94.8 (93.7)21.121.41U8O
18ELDKIAS666
19ELDKLAS666
20ELDK(Nle)AS666
21ALDKWQN662, 667, 66830.0-2.108.3 (39.2)99.9 (99.8)21.223.03IDI
22ALDKWD662, 66720.0-1.864.2 (29.9)98.5 (99.5)22.422.73IDG
23ELDKWNSL66750.0-2.6013.5 (35.2)95.8 (90.3)21.324.02PW1
24ELDKWKSL66750.0-2.5522.0 (39.0)99.0 (98.5)21.823.72PW2
25ELDKWAN66817.0-2.005.9 (39.9)97.1 (89.0)23.424.71U8I
26ELDKWAG66880.0-2.2413.6 (27.3)91.3 (96.5)22.923.81U8J
27ECDKWCS663, 66720.0-3.2312.6 (30.2)97.2 (97.8)21.222.21U8P
28E(Dap)DKWES663, 66780.0-2.2410.9 (24.8)94.0 (87.9)22.524.91U92
29EDDKW(Dap)S663, 66780.0-2.249.4 (20.0)91.4 (88.1)22.723.11U91
30EEDKW(Dap)S663, 66780.0-2.379.6 (34.5)92.0 (95.3)24.023.61U93
31E(Dap)DKWDS663, 667
32KLDNWAS662, 665
33ALDNWNN662, 665, 667, 668
  • a Collection and refinement statistics are given for each 2F5 Fab′-peptide complex that formed crystals along with the PDB identifier (ID). The absence of data indicates that no crystal complex was obtained. Values in parentheses are those for the highest-resolution bin.

  • b Reference sequence.