Molecular modelling of the specific

interactions involved in the amylose

complexation by fatty acids
M. C. Godet, V. Tran, M. M. Delage and A. Bul6on
Laboratoire de Physicochimie des Macromol~cules, INRA, BP 527, 44072 Nantes Cedex, France

(Received 30 July 1992; revised 30 September 1992)

Comprehensive modellin 9 o f a fatty acid molecule inside a Vn amylose helix is described. In a first step, the
dockin 9 o f an acetic acid molecule near the helix entry was performed. The low eneroy solutions were
propagated by an iterative procedure involving the sequential addition o f single CH 2 groups up to a C12
fatty acid followed by energy minimizations. The main result is the superposition o f the aliphatic and the
helix axes. For the low-energy complexes, the mean plane o f the aliphatic carbons has three potential
orientations. In each, the aliphatic hydrogens point towards the less crowded regions near the glycosidic
oxygens o f the amylose. The close packing is due to the related symmetries o f both the helix and aliphatic
chain. In a second step, the relative roles o f the aliphatic part and the polar group were studied separately.
For the aliphatic chain, a map based on the two major internal parameters (translation and rotation) along
the helix axis shows that the isolated docking solutions are related by a combination o f a 60 (360/6) rotation
and a translation o f p~6 (p = 0.804 nm corresponds to the pitch o f Vhrdrate amylose). The H5 91ucopyranose
atoms participate in close contacts and are responsible for steric conflicts in structures intermediate to the
stable docking solutions. The four possible low-eneroy arrangements o f the carboxylic group were added to
the calculated amylose/aliphatic structures. Two stable conformations o f the total fatty acid molecule were
determined. For both stable solutions, the polar group is located near the entrance of the helix cavity. Steric
and electrostatic repulsions prohibit the polar group from entering the cavity.
Keywords: Molecularmodelling;docking;amylose;fatty acid; complexation

Introduction
Amylose can interact strongly with a number of polar
and non-polar compounds, including lipids and emulsitiers ~-3. These complexes, when characterized by X-ray
diffraction, yield specific V-type diagrams. V amylose is
a generic name for crystalline amyloses obtained as
collapsed single helices co-crystallized with compounds
such as iodine, DMSO, alcohols and fatty acids.
Although complexing molecules are required for the
formation of the V-type single helical structure, they may
be present or not in the precipitated complexes. Some of
these structures (V A, VH, VDMSO, V~OD~NE) have been
determined by X-ray analysis on crystalline fibres 4-8 or
electron crystallography9. The chain conformation
consists in a left-handed, six residues 65 helix with a rise
per monomer between 0.132 and 0.136 nm. In some VA
and VH structures obtained by precipitation with
alcohols, only water molecules are present inside the
central cavity. The central cavity of the VDMsocomplexes v
is occupied by two DMSO molecules and approximately
three iodine molecules per turn are in the V~OOINE
complex 8.
Other studies using X-ray diffraction1, n.m.r, and
optical techniques 1~ and Raman spectroscopy 12 show
that similar inclusion complexes can also be formed with
fatty acids and monoglycerides. These complexes usually
yield a VHtype diffraction diagram 13, and several models
have been proposed for the inclusion of fatty acid in a
VH type amylose helix a2-~4. Nevertheless, no precise
0141-8130/93/010011-06
1993 Butterworth-HeinemannLimited

crystalline structure is available for a fatty acidamylose complex since it has not been possible up to
now to prepare crystalline fibres or single crystals suitable
for good X-ray or electron analysis.
Molecular modelling has appeared to be useful to
predict the structural features of macromolecular
carbohydrates. In recent works, some models of
amylopectin 15'16 derived from the double helical
structure of A- and B-amylose polymorphs t7'~8 have
been proposed. Molecular modelling has also been shown
to be an efficient tool to predict the interactions between
cyclodextrins and guest molecules a9-22. This paper
describes a systematic study of the positioning of a
patmitic acid molecule into an amylose single helix similar
to that constituting the VH structure proposed by
Rappenecker and Zugenmaier6.

Experimental
The coordinates of the Vn structure proposed by
Rapenecker and Zugenmaier6 were used for the
glucopyranose residue. The 65 VH amylose helix was then
propagated using the following values for the ~(1-4)
glycosidic linkage:
Oo5(O5-C1-O4-C4) = - 134.4
qJc5(C1-O4-C4-C5) = - 127.5
0(C1-O4 C 4 ) = 118.6

Int. J. Biol. Macromol., 1993, Vol. 15, February

11

Molecular modelling of amylose-fatty acid complexes." M. C. Godet et al.

Figure 1 A VH-amylose chain of 15 residues built from the

structure proposed by Rappenecker and Zugenmaier6 with the
glycosidic values as described in the text

A 15-residue amylose chain was built and used for

modelling (Figure 1). Except for some final refinements
using molecular mechanics, this helix was kept rigid. The
modelling was performed for dodecanoic (C12) acid but,
in the first step of the modelling, all intermediate lengths
between acetic and dodecanoic acids were used.
This study includes three steps:
(1) an initial search of the global docking solutions,
(2) the analysis of the aliphatic chain positions inside
the VH type helix,
(3) the analysis of the polar group contribution to the
complexation.
The calculations were carried out on Micro Vax 3100
and Silicon Graphics 4D35TG computers.
Initial search of docking solutions
In the model usually proposed for amylose-lipid
complexes 12, the aliphatic part of the lipid is inside the
helical cavity of amylose. The lipid has a trans
conformation and its carboxylic group is located at the
helix periphery. A complete docking search in one
procedure would require management of both the
positioning parameters for the fatty acid inside the helix
and the internal parameters accounting the flexibility of
the fatty acid. For simplification, this search was
performed in two steps:
(1) a systematic docking of an acetic acid molecule
(precursor of dodecanoic a c i d ) w i t h six positioning
parameters. Only low-energy solutions with the CH3
group pointing towards the helix cavity were kept for
the next steps,
(2) the iterative conversion of acetic acid into
dodecanoic C12 acid. This procedure was preferred to a
direct docking of the entire fatty acid molecule since the

12

Int. J. Biol. Macromol., 1993, Vol. 15, February

first step saves computer time by discarding a great

number of solutions. Furthermore, the second step
specifically takes into account the flexibility of the
aliphatic chain.
The acetic acid docking was performed with a
procedure derived from that used by Imberty et al. 21 and
Tran et al. 22 for lectin-carbohydrate interactions and
cyclodextrins complexations respectively. The procedure
involves the scanning of six positioning parameters
(respectively one distance, one angle and four dihedrals).
The corresponding construction with virtual bonds is
shown in Figure 2. The different ranges and increments
used for positioning parameters are described in Table 1.
After preliminary calculations, only a few values,
corresponding to the location of the carboxylic group at
the entry of the helical cavity, were chosen for the pl
parameter. The p2 parameter can only have values
between 150 and 180 for inclusion of the acetic acid tail
inside the helical cavity. This scanning step was carried
out using the SEARCH module 23 of the SYBYL package
which can only manage dihedrals. Therefore, each pair
of pl (distance) and p2 (angle) was treated separately
with complete scan of p3, p4, p5 and p6 parameters from
0 to 360 . The most improbable structures (in terms of
steric conflicts and total energy) were excluded. The
remaining structures were clustered into families with the
program PROXIM 22. The lowest energy structure inside
each family was selected as representative of the family.
Among the selected structures, only those with the
aliphatic end-group pointing towards the helix cavity
were kept and optimized using molecular mechanics as
described for the cyclodextrin/phenyl ethanol complexz2.
These structures were then converted by an interactive
procedure involving the sequential addition of single CH2
groups up to a C12 fatty acid. Each addition was followed
by energy minimizations using the MAXIMIN224
module of SYBYL. The amylose helix was kept rigid
during minimizations except for the final step (complete
C12 fatty acid).

pl
p2
p3
I)4
I)5
i)6

distance GH
angle OGH
dihedral around
dihedral around
dihedral around
dihedral around

OG
GH
HI
IJ

Figure 2 Internal positioning parameters for the initial

scanning of docking solutions
Table 1 Variation ranges for the six positioning parameter in
the scanning procedure (increments are in brackets)
pl (nm)
p2 ()
p3 ()
p4 ()
p5 ()
p6 ()

0.78 (0.02) 0.82

150 (0) 180
0 (20) 340
0 (20) 340
0 (20) 340
0 (20) 340

Molecular modelling of amylose fatty acid complexes: M. C. Godet et al.

Analysis of the aliphatic chain positions
From the results obtained in the former step, it was
assumed that the helix axes of the amylose and the fatty
acid chains are superimposed. Thus a search of eventual
intermediate structures was performed using translation
parallel to the helix axis and rotation around the central
axis of the complete aliphatic chain without any polar
end-group. Arbitrary atoms of amylose and aliphatic
chains were used to define the translation and the
rotation, since only the relative displacements are
interesting. These calculations were necessary to
determine if there was a continuity of solutions between
the discrete ones found in the docking step. An energy
map was calculated from rotation (0 to 180 every 5)
and translation (0 to 0.4nm every 0.02nm) of the
aliphatic chain inside the helix cavity. Finally, all internal
parameters were relaxed to analyse the possible
transitions among the calculated structures. These
calculations were performed using the DISCOVER
Consistent Valence Forcefield (CVFF) 25 from the
BIOSYM package. The different amylose atoms
responsible for the interaction with the included molecule
were also determined by distance measurements between
the atoms of the two moieties.

Contribution of the fatty acid polar group in the

complexation
The possible conformations of the carboxylic group
with regard to the alphatic chain were determined by
systematic rotation around the C2-C1 and C1-O bonds
(Figure 3) and calculation of the corresponding energy.
This systematic conformational search was performed on
an isolated fatty acid molecule with its aliphatic part in
a trans conformation. The complete fatty acid in the
different determined conformations was then progressively
inserted into the amylose helix with translations and
rotations calculated for the aliphatic chain positions (see
above). The insertion of the fatty acid was monitored by
reference to the C3 atom (third atom from the carboxylic
group) and its relative positions along the helix axis with
regard to the H5 atom of the amylose residues. After

each insertion step, the fatty acid was optimized by

molecular mechanics inside the amylose helix, using the
DISCOVER z5 force field from BIOSYM.

Results and discussion

Initial search of docking solutions
More than 4 million conformations were scanned.
Most of them are improbable for steric reasons and were
discarded by a combined criterion of VDW overlap and
energy cut-off. Only 370 solutions were selected, which
represent less than 0.01%. This drastic reduction could
be explained by the narrow form of the helix cavity.
Nevertheless, 370 selected solutions are more than could
be completely analysed. About 60 families were obtained
by use of the program PROXIM z2 with the standard
proximity distance criterion set to one. The lowest energy
structure inside each family was selected as representative
of the family. Among them, about 10 structures were
discarded because the aliphatic end-group points out of
the helix cavity. The remaining structures were displayed
and redundancies that resulted from the ranges (0-360 )
used for the p4, p5 and p6 parameters were eliminated.
Finally, 11 structures were kept for further refinement.
The progressive propagation of the acetic acid moiety
in each of these structures yielded five distinct structures.
This reduction was due to movements of the lengthened
aliphatic chain in order to accommodate the geometry
of the helix cavity. These involved the alignment of the
aliphatic chain with the helix axis, the translation of the
aliphatic chain and its relative rotation. The final
structures changed little after the generation of C8 acid.
As shown in Figure 4, the axes of both amylose helix
and fatty acid molecule coincide for all five structures.
Due to the helix symmetry, six conformations should be
found instead of five. This is due to the too restrained
range used for the parameter p 1 during the scanning step.
These six orientations are separated by 60 which
correspond to three equivalent mean planes for the
carbon atoms of the fatty acid moiety. With these
orientations, the fatty acid hydrogen atoms can point
towards the less crowded regions near the glycosidic
oxygens of the amylose. The intermolecular interactions
will be described further in detail.

(2)
I1

1)

C3
Figure 3 Dihedrals used for the systematic conformational
search of the propanoic acid

Figure 4 Representation of the three orientations of the

aliphatic chain inside the helix cavity. This view is obtained
perpendicular to the helix axis

Int. J. Biol. Macromol., 1993, Vol. 15, February

13

Molecular modelling of amylose-fatty acid complexes." M. C. Godet et al.

Analys& of the aliphatic chain contribution
The energy map calculated from rotation and
translation of the aliphatic chain inside the cavity of the
helix is shown in Figure 5 with eight contours every
1 kcal/mol above the minimum value. There is no
continuity between the low-energy solutions. The
structures determined previously (see above) are found
again, but this map shows that the different calculated
structures can be deduced by geometrical operations
directly related to the symmetry of the two moieties.
Along the helix axis, any structure can be deduced
from the nearest one by a 0.13 nm translation and a 60
rotation. The 60 rotation increment is related to the 6th
order symmetry of the amylose helix. The 0.13 nm
translation increment nearly corresponds to both the rise
per glucopyranose monomer (0.132 nm) and half the
Cx-Cx+ 2 distance in the aliphatic chain (0.252 nm). In
fact the general shape of contours are not identical since
these two values are not exactly the same but this does
not really perturb the complementary of these symmetries.
The analysis of all short intermolecular distances shows
that only the H 5 atoms of each glucopyranose residue
are involved in short van der Waals contacts with the
two nearest hydrogen atoms of the aliphatic chain.
Figure 6 represents schematically the short distances that
are observed in the calculated structures. In this plot, the
helical patten of the H5 atoms is projected onto a
cylinder, which is then cut parallel to its axis, unrolled
and duplicated. Thus the helix is represented by
successive oblique lines. The involved H5 atoms are
referenced by one letter A, B... O corresponding to the
glucopyranose residues of the helix (from the upper one
to the lower one). In the same map the aliphatic chain
trace is also drawn with respect to rotation as well as
translation (broken lines). The hydrogen atoms of the
aliphatic chain carbons are referenced by one number.
For example 31 and 32 represent respectively the H1 and
H2 hydrogen atoms linked to the carbon C3.

180

,llll,,,,l,,,,l,,,,l,

"O
r"
O

tw

''''I''''I'
o

Translation

,
q

2
(nm)

Figure 5 Energy map calculated from relative translation and

rotation of the aliphatic chain inside the helix cavity

14

Int. J. Biol. Macromol., 1993, Vol. 15, February

0,0

60

120

180

Relative
240
l

rotation
300
360
I

(*)

0,26

0, s z-

71

~~~.~
62

e-,

._
o
_~

.....

I
'

.....
'

~0

""
Figure 6 Schematic representation of the location of the
aliphatic chain on the helical pattern of the H5 atoms for
glucopyranose residues. The oblique lines represent the
V-amylose helix. The broken zig-zag line represents the
aliphatic chain. The different short contact pairs are shown by
geometric figures
There are three types of short contacts.
(I) (E ... 21); (E ... 22)
(II) (F ... Zl); (F ... 41)
(III) (G ... 32); (G ... 52)
The previous expressions can be generalized to all
interactions between the amylose helix and the total fatty
acid as following:
(I) (x ... y l ) ; (x ... y2)
with(x,y) = (E,2),
(H,5), (K,8) and
(N,11),
(II) ( x . . . y l ) ; ( x . . . ( y + 2 ) l )
with(x,y)=(F,2),
(1,5) and (L,8),
(III) (x ... yZ); (x ... (y + 2)2) with (x,y) = (G,3),
(J,6) and (M,9)
The mean values for these three types of distances are
respectively 0.236, 0.238 and 0.233nm which are
compatible with the shortest hydrogen-hydrogen
distance without steric conflict. This close packing
typically shows the complementarity of the two
conformation symmetries. Each calculated structure is
isolated since any movement of the aliphatic chain
relative to the helix provokes steric conflicts as shown in
Figure 5. For instance, the first type of close contacts
(I) prevents any rotation while the types (II) and (III)
freeze any movement in translation as well as in screwing.

Role of the polar group

Four low-energy conformations named S1, S2, S3 and
$4 were determined by systematic rotation around the
C2-C1 and C1-O bonds (Figure3). The values of the
corresponding dihedrals {C3-C2-C 1-O } and { C2-C 1-OH} are (-80,0); (-80,180); (100,0) (100,180). The

Molecular modelling of amylose-fatty acid complexes: M. C. Godet et al.

Figure 7 Two final low energy conformations for the fatty

permitted around the determined structures. This is

confirmed by the molecular mechanics results obtained
with relaxation of all internal parameters and preliminary
molecular dynamics calculations. These results are
consistent with the Vh X-ray diffractograms observed
frequently for fatty acid amylose c o m p l e x e s 12'13'26-28. A
seven-residue helix (71) was calculated by Neszmelyi er
al. 29 for fatty acid-amylose complexes in solution. This
71 helix has also been proposed for complexes crystallized
at intermediate temperatures a. But these forms were
completely transformed into 65 helices by annealing at
90C which illustrates the higher stability of this form 3.
The very tight packing of the calculated structures and
the steric hindrance provoked by the H5 atoms of
glucopyranose residues could explain why these complexes are formed only at high temperatures, when the
flexibility of the two moieties is high enough to lead to
inclusion. As it is not possible to conclude from the classic
powder X-ray diffraction diagrams of complexed
amyloses if the complexing molecule occupies the centre
of the helix or some void between the helices, some further
molecular modelling calculations should be performed
in order to check this last hypothesis.

acid/V-amylose complex
References

insertion steps of the fatty acid are defined by the different

interactions of type I between atoms 31 and 32 of the
fatty acid and the residues of amylose. The starting point
for insertion corresponds to interactions (A...31);
(A...32); in this case, the polar group is completely
outside of the helix. For this position and the following
one ((B...31); (B...32)), all four conformations yielded
similar intermolecular energies. For the third position
((C...31); (C...32)), only conformations $3 and $4
yielded a decrease of about 3 kcal/mol while S1 and $2
conformations were discarded for steric conflicts. The
resulting structures (third position and conformations $3
and $4) were minimized with relaxation of all internal
parameters of both molecules. This confirmed the
stability of these structures; there was no displacement
of the fatty acid along the axis and no significant variation
in the conformation of the polar group. These two
structures are shown in Fioure 7, the corresponding
coordinates are given in the Appendix. Further insertion
of the fatty acid led to steric conflicts. Subsequent
minimizations caused large modifications of the polar
group conformation and can only partially remove bad
contacts.
In this last stage, the branching of the Polar group has
permitted selection of one specific position of ihe aliphatic
moiety. Furthermore, the polar group plays a role similar
to a 'cork' during the helicoidal driving in of the aliphatic
chain.

1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25

Conclusions

26

This study shows that the inclusion model for the fatty
acid amylose complexes is acceptable in terms of both
steric hindrance and interaction energy. The geometries
of the 65 amylose helix and the fatty acid carbon chain
are so complementary that very little movement is

27
28
29
30

Rundle, R. E. and Edwards, F. C. J. Am. Chem. Soc. 1943, 65,

2200
Bear, R. S. J. Am. Chem. Soc. 1944, 66, 2122
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Rappenecker, G. and Zugenmaier, P. Carbohydr. Res. 1981, 89,
11
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Int. J. Biol. Macromol., 1993, Vol. 15, February

15

Molecular modelling of amylose-fatty acid complexes." M. C. Godet

iX
,A- nr rn e o du.
amylose"
CI(A)
C3(A)
C5(A)
Of(A)
O3(A)
OS(A)
HI(A)
H3(A)
HS(A)
H62(A)
C2(B)
C4(B)
C6(B)
O2(B)
O5(B)
HI(B)
H3(B)
MS(B)
H62(B)
C2(C)
C4(C)
C6(C)
O2(C)
O5(C)
HI(C)
H3(C)
H5(C)
H62(C)
C2(D)
C4(D)
C6(D)
O2(D)
O5(D)
HI(D)
H3(D)
HS(D)
H62(D)
C2(E)
C4(E)
C6(E)
O2(E)
O5(E)
HI(E)
H3(E)
HS(E~
H62(E)
C2(F)
C4(F)
C6(F)
O2(F)

5.040
3.492
3.551
4.030
3.392
4.853
6.067
2.710
2.777
3.787
4.404
4.434
3.738
4.113
3.682
3.594
3.296
2.459
3.069
-0.628
1.097
0.101
-1.030
-1.285
-2.598
0.867
-0.427
-0.829
-5.111
-3.565
-3.805
-5.220
-5.149
-6.308
-2.939
-3.082
-4.081
-4.626
-4.648
-3.939
-4.368
-3.869
-3.793
-3.509
-2.672
-3.273
0.336
-1.288
-0.312
0.731
os(F~
1.085
HI(F)
2.358
H3(F)
-0.709
H5(F)
0.227
H62(F)
0.624
C2(G)
4.829
C4(G)
3.213
C6(G)
3.461
O2(G}
4.974
O5(G)
4.814
HI(G)
6.019
H3(G)
2.658
H5(G)
2.751
H62(G)
3.719
C2(H)
4.355
C4(H)
4.381
C6(H)
3.689
O2(H)
4.087
O5(H)
3.621
HI(H)
3.527
H3(H)
3.231
HS(H)
2.416
H62(H)
3.016
C2(I)
-0.625
C4(I)
1.023
C6(I)
0.104
O2(I)
-1.040
O5(I)
-1.341
HI(I)
-2.635
H3(1)
0.419
H5(I)
-0.482
H62(I) -0.806
C2(J)
-5.123
C4(J)
-3.492
C6(J)
-3.710
O2(J)
-5.276
O5(J)
-5.088
HI(J)
-6.315

16

H3(J)

-2.951 -11.276

-2.091

H4(J)

-4.172

-9.096

-3.889

H62(J)
C2(K)
c4(K~
C6(K)
02(K)
05(K)
HI(K)
H3(K)
H5(K)
H62(K)
C2(L)
C4(L)
C6(L)
02(5)
05(5)
HI(L)
H3(L)
H5(5)
H62(L)
C2(M)
C4(S)
C6(M)
O2(S)
O5(S)
HI(M)
H3(M)
H5(M)
H62(M)
C2(N)
Cl(N)
C6(N)
O2(N)
O5(N)
HI(N)
H3(N)
HS(N)
H62(N)
C2(O)
C4(O)
C6(O)
02(0)
05(0)
HOI(O)
H2(O)
H4(O)
~61(O)

-3.015
-3.955
-4.673
-4.677
-3.960
-4.414
-3.916
-3.847
-3.540
-2.700
-3.284
0.290
-1.338
-0.404
0.690
1.034
2.312
-0.737
0.174
0.506
4.791
3.172
3.422
4.934
4.780
5.987
2.619
2.705
3.670
4.318
4.335
3.639
4.054
3.569
3.495
3.170
2.356
2.970
-0.656
0.988
0.066
-1.045
-1.376
-2.481
-0.424
1.360
0.822

-1.049
-1.184
3.329
1.456
2.144
3.635
3.757
5.189
1.476
2.065
2.819
5.652
4.734
4.512
5.574
5.234
5.875
3.737
3.335
4.257
2.508
3.473
2.550
2.115
1.663
0.870
2.443
1.468
1.638
-2.979
-1.074
-1.727
-3.323
-3.364
-4.825
-1.137
-1.663
-2.394
-5.318
-4.370
-4.080
-5.265
-4.844
-2.958
-6.368
-5.368
-3.331

a61(J)
CI(K)
C3(K)
CS(K~
Of(K)
O3(K)
06(K)
H2(K)
H4(K)
H61(K)
CI(L)
C3(L)
CS(L)
OI(L)
03(5)
O6(L)
H2(L)
H4(5)
H61(L)
CI(M)
C3(M)
C5(M)
OI(M)
O3(M)
O6(M)
H2(M)
H4(M)
H61(M)
CI(N)
C3(N)
C5(N)
OI(N)
O3(N)
O6(N)
H2(N)
H4(N)
H61(N)
C1(O)
C3(0)
C5(O)
O1(O)
03(0)
06(0)
HI(O)
H3(O)
H5(O)
H62(O}

-2.684
-3.680
-4.538
-3.749
-2.329
-5.523
-5.316
-5.703
-5.731
-3.679
1.453
-0.956
-0.108
1.785
-2.058
-0.854
0.047
-1.716
-1.170
4.962
3.403
3.478
3.944
3.277
4.311
5.581
3.852
2.396
3.330
4.176
3.409
1.982
5.141
4.999
5.350
5.390
3.365
-1.811
0.598
-0.231
-2.148
1.692
0.529
-2.671
0.381
-0.512
-0.846

-8.731
-11.634
-12.288
-9.912
-11.987
-13.036
-8.018
-12.282
-10.482
-8.106
-13,001
-13.660
-11.270
-13.344
-14.422
-9.443
-13.664
-11.873
-9.465
-14.333
-15.010
-12.617
-14.684
-15.781
-10,784
-15.001
-13.224
-10.816
-15.634
-16.334
-13.942
-15.991
-17,121
-12.096
-16.297
-14.544
-12.150
-16.959
-17.640
-15.257
-17.335
-18.396
-13.400
-17.071
-18,000
-15.472
-13.188

-2.378
4.102
1.807
2.341
3.705
1.099
2.386
3.649
1.629
1.120
5.188
4.770
4.391
3.818
5.256
5.821
6.705
5.737
3.779
1.272
3.151
2.239
0.301
4.343
3.610
3.244
4.301
2.827
-3.735
-1.453
-1.943
-3.342
-0.759
-1.966
-3.290
-1.251
-0.699
-4.829
-4.439
-3.990
-3.472
-4.948
-5.378
-5.517
-3.413
-2.940
-3.826

1.364
2.839
0.475
-0.278
-0.859
0.588
1.332
-0.870
0.589
1.304
-0.956
0.673
1.295
-0.750
0.745
1.452
-0.753
0.848
0.243

Oll
O12
H21
C3
H32
H4I
C5
H52
H61
C7
H72
H81
C9
H92
H101
C11
HI12
H121
H123

-0.756
-2.130
1.074
-0.005
0.811
0.993
-0.058
0.773
0.886
-0.116
-1.046
-0.945
-0.156
0.691
0.778
-0.192
-1.106
-1.034
0.743

1.652
2.157
1.441
0.092
0.048
-1.194
-2.446
-2.472
-3.716
-5.007
-5.005
-6.216
-7.558
-7.596
-8.823
-10.102
-10.171
-11.307
-11,336

2.695
0.923
1.047
-0.272
-1.018
1.166
-0.276
-1.006
1.201
-0.228
-0.831
1.377
-0.137
-0.847
1.368
-0.071
-0.688
1.515
1.439

Oll
O12
H21
C3
H32
H41
C5
H52
H61
C7
H72
H81
C9
H92
HI01
Cll
Hl12
HI21
H123

-0.833
-2.117
1.035
-0.047
0.761
0.985
-0.074
0.746
0.904
-0.i00
-1.038
-0.891
-0.104
0.735
0.867
-0.102
-1.021
-0.905
0.871

1.413
2.259
1.415
0.061
0.027
-1.212
-2.478
-2.498
-3.727
-5.038
-5.050
-6.252
-7.591
-7.620
-8.832
-10.134
-10.218
-11.341
-11.344

2.681
0.982
1.030
-0.282
-1.036
1.140
-0.282
-1.025
1.190
-0.222
-0.810
1.398
-0.120
-0.841
1.381
-0.039
-0.646
1.565
1.466

HS(J)

chain
1.818
1.131
3.534
1.483
0.363
3.201
1.697
0.774
3.349
5.610
-0.392
1.333
3.742
-1.747
1.920
0.427
-0.522
2.033
4.311
-1.825
0.026
2.397
-3.072
0.537
-0.985
-1.894
0.674
2.942
-3.071
-1.270
1.095
-4.439
-0.788
-2.351
-3.115
-0.637
1.642
-4.462
-2.705
-0.313
-5.826
-2.173
-3.706
-4.561
-2.031
0.212
-5.840
-4.082
-1.683
-7.202
-3.550
-5.080
-5.935
-3.388
-1.132
-7.188
-5.455
-3.058
-8.545
-4.891
-6.402
-7.299
-4.768
-2.499
-8.494
-6.776
-4.376
-9.849
-6.192
-7.694
-8.624
-6.097
-3.804
-9.794
-8.078
-5.681
-11.152
-7.498
-8.998
-9.939
-7.394
-5.100
-11.141
-9.409
-7.031
-12.501
-8.856
-10.372

1.328
3.217
2.303
0.347
4.413
1.723
0.929
2.520
1.530
1.696
-2.930
-1.026
-1.697
-3.252
-3.315
-4.774
-1,066
-1.620
-2.369
-4.916
-4.319
-4.024
-5.468
-4.789
-5.390
-3.328
-2.897
-3,779
-2.058
-3.004
-1.997
-I.693
-1.159
-0.396
-2.025
-0.982
-1.076
3.398
1.535
2.247
3.700
3.836
5.253
1.535
2.135
2.932
5.712
4.798
4.564
5.638
5.288
5.922
3.809
3.398
4.359
2.555
3.526
2.590
2.162
1.710
0.920
2.507
1.519
1.673
-2.929
-I.027
-1.683
-3.258
-3.319
-4.770
-1.072
-1.625
-2.347
-5.258
-4.312
-4.034
-5.202
-4.792
-5.459
-3.355
-2.897
-3.802
-2.134
-3.069
-2.105
-1.760
-1.251
-0.489

C2(A)
C4(A)
C6(A)
O2(A)
O4(A)
O6(A)
H2(A)
H4(A)
H61(A)
CI(B)
C3(B)
C5(B)
OI(B)
O3(B)
O6(B)
H2(B)
H4(B)
H61(B)
CI(C)
3(C)
C5(C)
OI(C)
03(C)
06(C)
H2(C)
H4(C)
H61(C)
CI(D)
C3(D)
C5(D)
Ol(n)
O3(D)
O6(D)
H2(D)
H4(D)
H61(D)
CI(E)
C3(E)
C5(E)
OI(E)
O3(E)
O6(E)
H2(E)
H4(E)
H61(E)
CI(F)
C3(F)
C5(F)
OI(F)
O3(F)
o6(v)
H2(F)
H4(F)
H61(F)
CI(G)
C3(G)
C5(G)
01(G)
03(G)
O6(G)
H2(G}
H4(G)
H61(G)
CI(H)
C3(H)
C5(H)
OI(H)
O3(H)
O6(H)
H2(H)
HI(H)
H61(H)
CI(I)
C3(I)
C5(I)
Ol(I)
O3(I)
O6(I)
H2(I)
H4(I)
H61(I)
CI(J)
C3(J)
C5(J)
Ol(J)
O3(J)
O6(J)
H2(J)

4.879
3.242
3.526
5.025
1.882
4.428
5.675
3.903
2.506
3.431
4.290
3.513
2.077
5.284
5.090
5.436
5.488
3.468
-I.779
0.816
-0.148
-2.192
1.837
0.553
-0.389
1.448
0.844
-5.289
-3.739
-3.862
-4.259
-3.609
-4.669
-5.921
-4.245
-2.771
-3.629
-4.505
-3.720
-2.277
-5.496
-5.292
-5.651
-5.700
-3.661
1.498
-0.918
-0.055
1.827
-2.014
-0.806
0.108
-1.660
-1.033
4.993
3.444
3.514
3.980
3.338
1.345
5.625
3,895
2.436
3.366
4.230
3.462
2.016
5.215
5.045
5.384
5.436
3.417
-1.773
0.632
-0.195
-2.107
1.717
0.590
-0.391
1.396
0.853
-5.286
-3.737
-3.780
-4.276
-3.641
-4.595
-5.914

0.900
2.630
5.042
-0.457
2.804
5.379
1.146
2.919
5.360
0.542
-0.167
2.235
0.239
-0.936
4.105
-0.162
1.636
4.042
-0.818
-1.501
0.883
-1.006
-2.169
2.786
-1.408
0.349
2.709
-2.189
-2.788
-0.420
-2.522
-3.543
1.482
-2.829
-0.966
1.404
-3.565
-4.213
-1.825
-3.898
-4.968
0.051
-4.212
-2.403
-0.004
-4.940
-5.590
-3.196
-5.279
-6.350
-1.323
-5.592
-3.789
-1.351
-6.275
-6.956
-4.561
-6.616
-7.730
-2.708
-6.942
-5.163
-2.746
-7.575
-8,274
-5.877
-7.919
-9.048
-4.022
-8.246
-6.479
-4.085
-8.881
-9.578
-7.184
-9.243
-10.342
-5.335
-9.536
-7.771
-5.388
-10.247
-10.911
-8.534
-10.619
-11.655
-6.671
-10.881

2.561
3.535
2.608
2.166
3.929
3.656
3.289
4.376
2.891
-3.684
-1.403
-1.897
-3.293
-0.727
-1.952
-3.260
-1,194
-0.669
-4.662
-4.362
-3.941
-3.302
-5.128
-5.316
-5.928
-5.322
-3.269
-0.800
-2.718
-1.739
0.162
-3.922
-3.059
-2.773
-3.826
-2.238
4.166
1.876
2.423
3.770
1.182
2.494
3.732
1.720
1.225
5.237
4.841
4.449
3.869
5.346
5.849
6.766
5.801
3.795
1.320
3.208
2.291
0.343
4.400
3.650
3.283
4.351
2.857
-3.680
-i.401
-i.901
-3.285
-0.720
-1.929
-3.254
-1.198
-0.654
-4.771
-4.382
-3.941
-3.409
-4.902
-5.325
-6.309
-5.312
-3.279
-0.884
-2.782
-1.818
0.084
-3.995
-3.161
-2.863

Int. J. Biol. M a c r o m o l . , 1993, Vol. 15, F e b r u a r y

et al.

first lipid
C1
HI1
C2
H22
H31
C4
H42
HS1
C6
H62
H71
C8
H82
H91
C10
H102
Hill
C12
H122

-8.755
-6.473
-12.531
-10.786
-8.408
-13.891
-10.243
-11.769
-12.638
-10.131
-7.853
-13.905
-12.160
-9.772
-15.264
-11.612
-13.141
-13.997
-11.456
-9.201
-15.243
-13.512
-11.119
-16.599
-12.946
-14.463
-15,347
-12.811
-10.548
-16.549
-14.839
-12.443
-17.900
-14.250
-15.749
-16.676
-14.149
-11.871
-17.864
-16.142
-13.755
-19.230
-15.568
-16.507
-17.601
-15.832
-13.462

docking

-1.045
1.785
0.159
1.407
0.130
1.420
0.246
2.221
-0.940
0.097
0.050
-1.172
-0.765
-1.155
-0.991
-2.417
-0.029
-3.713
-0.874
-3.681
0.709
-5.037
-0.091
-6.256
0.822
-6.219
-1.074
-7.560
-0.136
-8.812
-0.983
-8.788
0.673 -10.195
-0.172 -11.337
-0.213 -12.242

second lipid docking

C1
Hll
C2
H22
H31
C4
H42
HSI
C6
H62
H71
C8
H82
H91
CI0
HI02
Hl11
C12
H122

-1.075
1.740
-1.574
1.673
0.084
1.388
0.186
2.193
-0.987
0.061
0.033
-1.202
-0.769
-1.193
-1.016
-2.462
-0.017
-3.740
-0.854
-3.715
0.714
-5.059
-0.047
-6.283
0.874
-6.262
-i.029
-7.609
-0.054
-8.838
-0.894
-8.824
0.758 -10.218
-0.052 -11.362
-0.087 -12.272

1.377
3.231
0.466
-0.285
-0.862
0.575
1.333
-0.862
0.588
1.313
-0.962
0.682
1.293
-0.724
0.769
1.486
-0.729
0.887
0.288