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. Author manuscript; available in PMC: 2008 Oct 19.
Published in final edited form as: J Mol Biol. 2007 Aug 15;373(2):367–381. doi: 10.1016/j.jmb.2007.07.069

Table 3.

Interface accessible surface area (ASA) of complex between C-peptide and dimeric SurA-P1. Parameters were computed as described for Table 2. Values in the table are averages of two values for the two complexes in the crystallographic asymmetric unit. For SurA-P1, only values >5% in at least one subunit are shown. Values between 0 and 5% are represented as “--”.

SurA-P1 residue % interface ASA in complex,subunits A/C % interface ASA in complex,subunits B/D Interface ASA (A2)subunits A/C Interface ASA (A2)subunits B/D
Glu185 6.8 -- 37.3 --
Gln224 5.9 6.7 32.5 37.2
Met231 18.5 12.4 101.7 66.8
Trp233 6.0 7.6 33.0 40.6
Arg235 -- 5.5 -- 29.3
Glu238 12.6 12.2 68.8 65.2
Pro240 7.3 9.5 40.1 50.9
Gly262 -- 5.9 -- 31.8
Val263 9.7 9.9 53.3 52.9

C-peptide % interface ASA in complex,subunits A/C % interface ASA in complex,subunits B/D Interface ASA (A2)subunits A/C Interface ASA (A2)subunits B/D

Asn1 7.4 10.3 48.9 65.3
Phe2 20.5 -- 135.8 --
Thr3 5.8 11.1 38.3 70.5
Leu4 -- 13.2 -- 83.4
Lys5 9.7 -- 64.2 --
Phe6 16.0 -- 105.9 --
Trp7 -- 24.2 -- 153.8
Asp8 3.0 4.1 20.0 25.9
Ile9 15.4 -- 102.3 --
Phe10 15.6 10.5 103.6 66.9
Arg11 -- 12.3 -- 78.1
Lys12 6.4 14.2 42.7 90.1