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. Author manuscript; available in PMC: 2009 Jan 30.
Published in final edited form as: Biochemistry. 2008 Apr 15;47(18):5111–5126. doi: 10.1021/bi702537s

Table 4.

Interhelical Angles and Distances in S100A4a

interhelical angle (deg)
interhelical distance (Å)
1–2 1–3 1–4 2–3 2–4 3–4 1–1′ 4–4′ 1–1′ 4–4′
Ca2+-S100A4 139 ± 1 −118 ± 2 130 ± 2 102 ± 2 −32 ± 2 107 ± 2 −151 ± 1 145 ± 1 13.9 ± 0.5 10.1 ± 0.5
apo-S100A4b 119 ± 2 −55 ± 4 120 ± 2 151 ± 4f −45 ± 3 162 ± 4 −152 ± 4 153 ± 4 n/a n/a
Ca2+-S100A1c 132 ± 1 −102 ± 2 131 ± 2 125 ± 2 −29 ± 1 121 ± 2 −157 ± 3 152 ± 3 12.5 ± 0.2 11.1 ± 0.4
apo-S100A1d 120 ± 3 −45 ± 2 107 ± 2 148 ± 2 −46 ± 1 −150 ± 1 −165 ± 3 176 ± 2 n/a n/a
calbindine 129 ± 1 −116 ± 2 123 ± 2 111 ± 2 −31 ± 1 118 ± 2 n/a n/a n/a n/a
a

The helices in S100A4 are defined as follows: helix 1, Pro4-Ser20; helix 2, Lys31-Glu41; helix 3, Glu52-Leu62; helix 4, Phe72-Glu88.

b

From ref 23.

c

From ref 35.

d

From ref 77.

e

From ref 108.

f

In the orginal report (23), the interhelical angle for helices 2 and 3 in apo-S100A4 was mistakenly reported as a negative value.