Figure 3.
Fig 3. X-ray crystal structures of 3ANK and 4ANK. (a)
Stereo representation showing the initial electron density map
of residues 37-40 of 4ANK, including the TPLH motif, contoured
at 1.5 . The figure was made
with O and rendered by using MOLRAY (43). (b) Overlay of 3ANK
(cyan) and 4ANK (orange) backbone structures. This figure and
all following structural representations were made with MOLMOL
(44). (c) Hydrogen bonding network in -hairpin/loop region of
4ANK. Each repeat is colored differently and hydrogen bonds are
represented by letters: a, D32(OD1) and N34(HN); b, D32(O) and
G35(HN); c, D32(OD1) and R36(HN); d, D32(HN) and R36(O); e,
R36(O) and H7(HNE2); f, A30(O) and H7(HNE2); g, A30(HN) and
D27(O); h, D27(OD1) and N29(HN); i, N29(OD1) and D60(HN); j,
N29(ND2) and G58(O); k, N34(O) and K66(HN); and l, R36(HNE) and
D65(OD2). Equivalent hydrogen bonds in adjacent repeats are
represented by the letter followed by ' or " and for all residue
numbers i > 33, the canonical ankyrin repeat position = i - 33.
(d) Comparison of intramolecular packing of ankyrin repeat
proteins based on the occluded surface area analysis. For each
protein, the average ray length of all residues was plotted
against the average occluded surface packing (OSP) value of all
buried residues with exposed surface area of <5%. The average
values of 152 high-resolution structures in PDB are shown by the
dashed lines on the graph (31).
. The figure was made
with O and rendered by using MOLRAY (43). (b) Overlay of 3ANK
(cyan) and 4ANK (orange) backbone structures. This figure and
all following structural representations were made with MOLMOL
(44). (c) Hydrogen bonding network in 
-hairpin/loop region of
4ANK. Each repeat is colored differently and hydrogen bonds are
represented by letters: a, D32(OD1) and N34(HN); b, D32(O) and
G35(HN); c, D32(OD1) and R36(HN); d, D32(HN) and R36(O); e,
R36(O) and H7(HNE2); f, A30(O) and H7(HNE2); g, A30(HN) and
D27(O); h, D27(OD1) and N29(HN); i, N29(OD1) and D60(HN); j,
N29(ND2) and G58(O); k, N34(O) and K66(HN); and l, R36(HNE) and
D65(OD2). Equivalent hydrogen bonds in adjacent repeats are
represented by the letter followed by ' or " and for all residue
numbers i > 33, the canonical ankyrin repeat position = i - 33.
(d) Comparison of intramolecular packing of ankyrin repeat
proteins based on the occluded surface area analysis. For each
protein, the average ray length of all residues was plotted
against the average occluded surface packing (OSP) value of all
buried residues with exposed surface area of <5%. The average
values of 152 high-resolution structures in PDB are shown by the
dashed lines on the graph (31).