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Table 2 Solvent accessibilities and Secondary structure analysis in the native and mutant proteins

From: In Silico profiling of deleterious amino acid substitutions of potential pathological importance in haemophlia A and haemophlia B

Mutation
Position
Solvent accessibility in the native and mutant proteins by GETAREA Secondary structure analysis by DSSP
  Changed from exposed to buried Changed from buried to exposed  
W274C Thr (2), Tyr(5) Leu(7), Val(63), His(76), Ala(81), Pro(93), Ser(116), Ala(119), Glu(129), Lys(146), Tyr(155), Lys(185), Leu(187), Ala(194), Lys(213), Leu (217), Ile(310), Leu(319), Leu(327), Gln(335), Glu(340), Lys(344), Pro(349), Lys(399), Thr(400), Leu(419), Tyr(426), Lys(431), Lys(441), Ala(449), Thr(454), Lys(485), Arg(509), Gly(539), Thr(549), Ser(553), Glu(559), Glu(576), Asp(579), Gln(585), Lys(589), Val(592), Phe(598), Arg(602), Leu(614), Asn(631), Tyr(639), Ser(647), Ala(654), His(679), Leu(689), Val(697), Asn(713), Arg(719), Ser(728), Lys(732) Trp(14), Leu(69), Gln(96), Val(99), Ser(138), Ser(176), Ser(179), Ile(405), Asn(299), Cys(329), Val(392), Arg(424), Tyr(473), Arg(503), Arg(546), Val(556), Pro(569), Gly(565), Asn(609), Gly(619), Ile(636), Trp(707) T → H: Pro(86), Gly(89), Leu(203), Thr(208), Ser(428), Lys(518), Gly(638), His(1735), Thr(1763), Lys(1932), Asn(1934), Met(1945), Glu(2200)
H → T:Lys(161), Lys(185), Leu(187), Leu(562), Asn(601), Glu(608), Arg(612), Ser(630), Asp(1865), Gly(2022)
T → S:Trp(87), Leu(517), Asn(637), Asn(1772)
W2065R Asp(1260), Gln(1336), Leu(1481), Ala(1610), Ile(1698), Tyr(1699), Arg(1708), Thr(1714), Glu(1723), Arg(1740), Gly(1769), Leu(1775), Ile(1782), Arg(1800), His(1867), Leu(1882), Trp(1908), Ala(1939), Asn(1941), Met(1945), Arg(1960), Ser(1968), Asn(1971), Phe(1982), Met(2007), Arg(2016), Ser(2082), Arg(2169) Asn(1460), Gln(1705), Gly(1779), Leu(1808), Val(1876), Glu(1884), Glu(1904), Met(1842), Ile(1901), Tyr(1909), Thr(2015), T → H:), His(1735), Thr(1763), Lys(1932), Asn(1934), Met(1945), Glu(2200)
H → T: Asp(1865), His(1867), Asp(2206)
T → S: Asn(1772)
W2248C Asp(1260), Gln(1336), Asn(1460), Leu(1481), Ala(1610), Ile(1698), Tyr(1699), Arg(1708), Thr(1714), Glu(1723), Arg(1740), Gly(1769), Leu(1775), Ile(1782), Arg(1800), His(1867), Val(1876), Leu(1882), Trp(1908), Ala(1939), Asn(1941), Met(1945), Arg(1960), Ser(1968), Asn(1971), Phe(1982), Met(2007), Arg(2016), Gly(2028), Ala (2070)Ser(2082), Arg(2169) Asn(1460), Gln(1705), Gly(1779), Leu(1808), Val(1876), Glu(1884), Glu(1904), Met(1842), Ile(1901), Tyr(1909), Thr(2015), Gly(2022), Ala(2070) T → H:), His(1735), Thr(1763), Lys(1932), Asn(1934), Met(1945), Glu(2200)
H → T: Asp(1865), Gly(2022)
  1. T-Turn, H-Helix, S-Strand