Two pentadehydropeptides with different configurations of the Δphe residues

Article abstract of DOI:10.1107/S0108270110003094

Comparison of the crystal structures of two pentadehydropeptides containing ΔPhe residues, namely (Z,Z)-N-(tert-butoxycarbonyl)-glycyl-α, Β-phenyl-alanyl-glycyl-α,Β-phenylalanylglycine (or Boc ⁰-Gly¹-Δ^ZPhe²-Gly ³-Δ^ZPhe⁴-Gly⁵-OH) methanol solvate, C₂₉H₃₃N₅O₈·CH ₄O, (I), and (E,E)-N-(tert-butoxycarbonyl)-glycyl-α,Β- phenyl-alanyl-glycyl-α,Β-phenylalanylglycine (or Boc ⁰-Gly¹-Δ^EPhe²-Gly ³-Δ^EPhe⁴-Gly⁵-OH), C ₂₉H₃₃N₅O₈, (II), indicates that the Δ^ZPhe residue is a more effective inducer of folded structures than the Δ^EPhe residue. The values of the torsion angles and Ψ show the presence of two type-III′ Β-turns at the Δ^ZPhe residues and one type-II Β-turn at the Δ^EPhe residue. All amino acids are linked trans to each other in both peptides. Β-Turns present in the peptides are stabilized by intra-molecular 4→1 hydrogen bonds. molecules in both structures form two-dimensional hydrogen-bond networks parallel to the (100) plane.

Full text of DOI:10.1107/S0108270110003094

organic compounds
Acta Crystallographica Section C
Crystal Structure
Communications
This paper follows previous research on the conformational
preferences of ÁPhe residues (Makowski et al., 2006, and
references therein). We present the structures of two penta-
dehydropeptides with two ÁPhe residues, viz. Boc0–Gly1–
ÁZPhe2–Gly3–ÁZPhe4–Gly5–OH, (I), and Boc0–Gly1–
ÁEPhe2–Gly3–ÁEPhe4–Gly5–OH, (II). The peptides differ
only in the configuration of the ÁPhe residues. Both peptides
crystallize in the same space group, P21/c, with one molecule in
the asymmetric unit. Additionally, peptide (I) cocrystallizes
with one molecule of methanol in the asymmetric unit. A
comparison of the crystal structures of both peptides will allow
evaluation of the impact of individual ÁPhe isomers on the
conformational preferences of the peptides. The atom label-
ling is the same in both structures.
ISSN 0108-2701
Two pentadehydropeptides with
different configurations of the DPhe
residues
Maciej Makowski,a Marek Lisowski,b* Anna Macia˛g,b
Maciej Wiktor,b Anna Szlachcicb and Tadeusz Lisb
aInstitute of Chemistry, University of Opole, 48 Oleska Street, 45-052 Opole, Poland,
and bFaculty of Chemistry, University of Wrocław, 14 Joliot-Curie Street, 50-383
Wrocław, Poland
Correspondence e-mail: mbl@wchuwr.pl
Received 16 December 2009
Accepted 25 January 2010
Online 3 February 2010
Comparison of the crystal structures of two pentadehydro-
peptides containing ÁPhe residues, namely (Z,Z)-N-(tert-
butoxycarbonyl)glycyl-ꢀ,ꢁ-phenylalanylglycyl-ꢀ,ꢁ-phenylalanyl-
glycine (or Boc0–Gly1–ÁZPhe2–Gly3–ÁZPhe4–Gly5–OH)
methanol solvate, C29H33N5O8ꢀCH4O, (I), and (E,E)-N-(tert-
butoxycarbonyl)glycyl-ꢀ,ꢁ-phenylalanylglycyl-ꢀ,ꢁ-phenyl-
alanylglycine (or Boc0–Gly1–ÁEPhe2–Gly3–ÁEPhe4–Gly5–
OH), C29H33N5O8, (II), indicates that the ÁZPhe residue is a
more effective inducer of folded structures than the ÁEPhe
residue. The values of the torsion angles ’ and show the
presence of two type-III0 ꢁ-turns at the ÁZPhe residues and
one type-II ꢁ-turn at the ÁEPhe residue. All amino acids are
linked trans to each other in both peptides. ꢁ-Turns present in
the peptides are stabilized by intramolecular 4!1 hydrogen
bonds. Molecules in both structures form two-dimensional
hydrogen-bond networks parallel to the (100) plane.
Comment
ꢀ,ꢁ-Dehydroamino acid residues contain a double bond
between the Cꢀ and Cꢁ atoms. Due to this structural feature
they have the capacity to induce ordered structures in
peptides. These structures depend on the type, content and
mutual location of Á-amino acid residues in the peptide
sequence. The conformation-stabilizing effect is very pro-
nounced in the case of the ÁPhe residue. The presence of one
or more ÁPhe residues results in the ꢁ-turn conformation in
All amino acids, in both structures, are linked trans to each
other. The deviations from ideal ! = 180ꢁ do not exceed 10ꢁ.
Blocking groups adopt transoidal conformations, as indicated
by the values of the !0 (N1—C5—O1—C1) and ’0 (C6—N1—
C5—O1) torsion angles (Tables 1 and 3). The Cꢀ—Cꢁ
distances (C8 C9 and C19 C20) are classical double-bond
lengths (Tables 1 and 3) and correspond well with the results
of other X-ray crystallographic studies of dehydropeptides
´
´
´
(Głowka et al., 1987; Ejsmont et al., 2001; Makowski et al.
2005).
Because of the unsaturated character of the Cꢀ—Cꢁ bond,
the side chains of the ÁPhe residues are much closer to the
main-chain atoms compared with their saturated counterparts.
This feature results in some geometric distortions character-
short peptides (Głowka et al., 1987; Głowka, 1988; Aubry et al.,
1984) and the 310 helical arrangement in longer peptides
(Rajashankar et al., 1992; Padmanabhan & Singh, 1993;
Rajashankar, Ramakumar, Jain & Chauhan, 1995; Raja-
shankar, Ramakumar, Mal et al., 1995; Jain et al., 1997). The
preferred values for the torsion angles ’ and fall predomi-
nantly into the regions of 80 and 0, 60 and 140, and 60 and 30ꢁ,
respectively, and their enantiomeric values (Singh & Kaur,
1996).
´
istic of dehydropeptide structures (Głowka et al., 1987).
Systematic shortening of the N—Cꢀ (N2—C8 and N4—C19),
Cꢀ—Cꢁ (C8—C16 and C19—C27) and Cꢁ—Cꢂ (C9—C10 and
Acta Cryst. (2010). C66, o119–o123
doi:10.1107/S0108270110003094
# 2010 International Union of Crystallography o119

organic compounds
Figure 1
The molecular structures of peptides (a) (I) and (b) (II), showing the atom-numbering schemes. Displacement ellipsoids are drawn at the 30%
probability level and H atoms are shown as small spheres of arbitrary radii. Hydrogen bonds are shown as dashed lines.
C20—C21) single bonds (Tables 1 and 3) is observed, which
may be caused by extended delocalization of the ꢃ electron
system. The values of the N2—C8—C16 [118.8 (2) and
114.67 (18)ꢁ for (I) and (II), respectively] and N4—C19—C27
[117.1 (2) and 114.04 (18)ꢁ for (I) and (II), respectively] bond
angles are smaller than the regular trigonal value of 120ꢁ,
which is clearly understandable owing to the steric inter-
actions between the main chain and the side chains of ÁPhe. It
is interesting that these effects influence analogous angles in
both peptides to the same extent, regardless of the location of
the aromatic rings.
planar. The ÁPhe2 residue side chain adopts a trans-
(ꢂ)gauche conformation, with torsion angles ꢄ2,1
=
ꢂ152.6 (3)ꢁ and ꢄ2,2 = 30.8 (5)ꢁ.
The presence of two ÁZPhe residues in (I) induces the
occurrence of two overlapping ꢁ-turns. The first is formed by
the ÁZPhe2 and Gly3 residues, with torsion angles ’2
=
50.4 (4)ꢁ and = 20.0 (4)ꢁ, and ’3 = 54.7 (4)ꢁ and =
2
3
26.7 (4)ꢁ, respectively. The second turn includes the Gly3 and
ÁZPhe4 residues, with torsion angles ’3 = 50.4 (4)ꢁ and =
3
20.0 (4)ꢁ, and ’4 = 68.7 (3)ꢁ and = 17.4 (4)ꢁ, respectively.
4
The torsion angles indicate that these ꢁ-turns are of type III0
(Lewis et al., 1973). They are stabilized by 4!1 hydrogen
bonds between the NH group of ÁZPhe4 and the CO group of
Gly1, and between the NH group of Gly5 and the CO group of
ÁZPhe2 (Table 2). The two ꢁ-turns of type III0 in (I) are the
same as in the previously reported crystal structure of the
Boc0–Gly1–ÁZPhe2–Gly3–ÁZPhe4–Gly5–OMe pentapeptide,
which differs from (I) only in the methanolate group at the C
terminus (Makowski et al., 2007). The molecular structure of
peptide (I) is presented in Fig. 1(a) and its packing diagram is
shown in Fig. 2.
The situation is somewhat different in the case of (II). There
is only one ꢁ-turn at the ÁEPhe2 and Gly3 residues, stabilized
by a 4!1 hydrogen bond between the NH group of ÁEPhe4
and the CO group of Gly1 (Table 4). This ꢁ-turn is additionally
stabilized by a C—Hꢀ ꢀ ꢀꢃ interaction. The ’ and angles of
these residues are 33.2 (3) and ꢂ119.6 (2)ꢁ, and ꢂ83.2 (3) and
ꢂ5.3 (3)ꢁ, respectively. These values correspond well with a
type-II ꢁ-turn (Lewis et al., 1973). Deviations from the ideal
Another characteristic consequence of the short distance
between the aromatic rings and the peptide chain is a
considerable opening of the valence angles Cꢀ—Cꢁ—Cꢂ to
´
relax the steric strain (Głowka, 1988). This trend explains the
increased values of the Cꢀ—Cꢁ—Cꢂ bond angles for both
structures. These angles are the same in both ÁPhe residues in
each structure and agree to within one standard deviation
between (I) and (II). In the case of (I), these angles for
ÁZPhe2 and ÁZPhe4 are C8—C9—C10 = 131.4 (3)ꢁ and C19—
C20—C21 = 131.4 (3)ꢁ, respectively, and for ÁEPhe2 and
ÁEPhe4 of (II) they are C8—C9—C10 = 129.9 (2)ꢁ and C19—
C20—C21 = 129.9 (2)ꢁ, respectively. The torsion angles ꢄ2 =
ꢂ176.9 (2)ꢁ and ꢄ4 = ꢂ176.0 (2)ꢁ between N—Cꢀ and the
aromatic system, and ꢄ2,1 = ꢂ155.1 (3)ꢁ, ꢄ2,2 = 25.4 (4)ꢁ, ꢄ4,1
=
20.7 (4)ꢁ and ꢄ4,2 = ꢂ159.7 (2)ꢁ, indicate that in the case of (II)
the side chains of both ÁPhe residues are almost planar, while
for (I) the torsion angles ꢄ4 = 0.2 (5)ꢁ, ꢄ4,1 = ꢂ19.8 (5)ꢁ and
ꢄ4,2 = 162.9 (3)ꢁ show that only the side chain of ÁPhe4 is
ꢃ
o120 Makowski et al. C29H33N5O8ꢀCH4O and C29H33N5O8
Acta Cryst. (2010). C66, o119–o123

organic compounds
bond (Table 4). The formation of this bond requires a relo-
cation of the H atom. What is more, amide atom H2 of another
molecule of (II) in that hydrogen bond corresponds to the
position of the carboxyl H atom in (I). Therefore, we suspect
some competition between the O8—H8 covalent bond and the
1
N2—H2ꢀ ꢀ ꢀO8(1 ꢂ x, y ꢂ , 12 ꢂ z) hydrogen bond which results
2
in moving atom H8 to the alternative position.
Further information can be derived from a detailed analysis
of the packing diagrams of both molecules. The crystal
structure stabilizing effect compensates for the energy loss
resulting from the unusual position of the H atom in (II).
Additionally, the position of atom H8 in (II) is stabilized by
the O8—H8ꢀ ꢀ ꢀO2(x, 12 ꢂ y, 21 + z) hydrogen bond. This unusual
position of the hydroxy H atom is rarely encountered. As
reported recently, it occurs when additional stabilization is
provided by other interactions (Videnova-Adrabinska et al.,
2007). In the discussed case, the H atom switches its orienta-
tion to approach the lone pair of another hydroxy O atom.
Figure 2
A packing diagram for peptide (I). Hydrogen bonds are represented by
dashed lines. Symmetry codes are as given in Table 2.
torsion angles for this ꢁ-turn (ꢂ60 and 120ꢁ, and 80 and 0ꢁ) are
not larger than 26ꢁ, compared with a maximum acceptable
deviation of 40ꢁ (Lewis et al., 1973). In addition, the C-term-
inal amino acid residues adopt a conformation similar to a
type-IV ꢁ-turn. The whole structure is stabilized by inter- and
intramolecular hydrogen bonds of various types, namely O—
Hꢀ ꢀ ꢀO, N—Hꢀ ꢀ ꢀO and C—Hꢀ ꢀ ꢀꢃ (Table 4). However, the
conformational constraints are not sufficient for a second
ꢁ-turn to be formed. The molecular structure of peptide (II) is
presented in Fig. 1(b).
A comparison of (I) and (II) reveals that a ÁZPhe residue is
a more effective inducer of folded structures than a ÁEPhe
residue. The insertion of two ÁZPhe residues in (I) gives rise
to the formation of two ꢁ-turns and the structure is stabilized
by two intramolecular 4!1 hydrogen bonds. In the case of
(II), there is only one ꢁ-turn stabilized by a hydrogen bond
and the resulting conformation is more distorted, and this is
reflected in the greater deviations from ideal dihedral angles
for the ꢁ-turns. The previously reported crystal structure of a
closely related peptide, viz. Boc–Gly–ÁZPhe–Gly–ÁEPhe–
Gly–OMe (Makowski et al., 2006), shows that in the case of a
ÁEPhe4 residue the formation of a second ꢁ-turn is hindered
and deviations from ideal values for the torsion angles ’ and
are increased. A type-II ꢁ-turn for the ÁZPhe2 and Gly3
residues, and a type-IV ꢁ-turn for Gly3 and ÁEPhe4, was
observed. The ÁEPhe4 residue in (II) does not induce a ꢁ-turn,
as in the case of Boc0–Gly1–ÁZPhe2–Gly3–ÁEPhe4–Gly5–
OMe. A ꢁ-turn at the ÁEPhe4 residue has been observed for
Boc0–Gly1–ÁZPhe2–Gly3–ÁEPhe4–Phe5-p-NAꢀEtOH (Mak-
owski et al., 2005), due to the presence of the additional
H-atom donor, p-nitroaniline (p-NA), which forms a hydrogen
bond with the CO group of Gly3.
Experimental
Both title compounds were obtained from their methyl esters. The
syntheses of the methyl esters of (I) and (II) have been described by
Latajka et al. (2008). For the preparation of (I), Boc–Gly–ÁZPhe–
Gly–ÁZPhe–Gly–OMe (0.059 g, 0.1 mmol) was dissolved in MeOH
(1.5 ml) and then H2O (0.1 ml) and 1 M NaOH (0.3 ml, 0.3 mmol)
were added. The reaction was carried out for 30 min at room
temperature. The reaction mixture was then acidified to pH 3 and
brine (ca 10 ml) was added. The mixture was extracted with EtOAc (5
ꢄ 3 ml). The acetate extracts were washed with 0.5 M HCl (2 ꢄ 2 ml)
and brine (2 ꢄ 2 ml) and dried over anhydrous MgSO4. After
removal of EtOAc in vacuo, Boc–Gly–ÁZPhe–Gly–ÁZPhe–Gly–OH
was crystallized from EtOAc with addition of hexane to the first
turbidity [yield 0.056 g, 97%; m.p. 474–477 K (decomposition)].
Elemental analysis calculated for C29H33N5O8: C 60.09, H 5.74,
N 12.08%; found: C 59.89, H 5.98, N 12.12%. Boc–Gly–ÁEPhe–Gly–
ÁEPhe–Gly–OH, (II), was obtained from its methyl ester in the same
way [yield 0.054 g, 94%; m.p. 474–477 K (decomposition)]. Elemental
analysis calculated for C29H33N5O8: C 60.09, H 5.74, N 12.08%; found:
C 60.33, H 5.87, N 11.89%. Finally, peptide (II) were recrystallized
from a solution in a mixture of MeOH and EtOAc.
Compound (I)
Crystal data
3
˚
C29H33N5O8ꢀCH4O
V = 3030.2 (17) A
Z = 4
Cu Kꢀ radiation
ꢅ = 0.84 mmꢂ1
T = 100 K
Mr = 611.65
Monoclinic, P21=c
˚
˚
a = 14.075 (4) A
b = 16.577 (5) A
˚
c = 14.041 (4) A
0.30 ꢄ 0.20 ꢄ 0.01 mm
ꢁ = 112.34 (3)ꢁ
Data collection
Oxford Xcalibur PX ꢆ-geometry
diffractometer with CCD area
detector
Absorption correction: analytical
[CrysAlis RED (Oxford
Diffraction, 2003); analytical
numeric absorption correction
using a multifaceted crystal
model based on the expressions
derived by Clark & Reid (1995)]
Tmin = 0.842, Tmax = 0.966
22848 measured reflections
5247 independent reflections
3735 reflections with I > 2ꢇ(I)
Rint = 0.099
The atypical location of the H atom of the C-terminal
carboxyl group, H8, merits further discussion. In (II) it is
directed to the opposite side compared with the analogous
atom in (I). The O8 atoms in both molecules take part in
hydrogen bonds. In the case of (II), atom H8 participates in
1
the intermolecular N2—H2ꢀ ꢀ ꢀO8(1 ꢂ x, y ꢂ , 12 ꢂ z) hydrogen
2
ꢃ
Acta Cryst. (2010). C66, o119–o123
Makowski et al. C29H33N5O8ꢀCH4O and C29H33N5O8 o121

organic compounds
Table 1
Selected geometric parameters (A, ) for (I).
Table 4
Hydrogen-bond geometry (A, ) for (II).
ꢁ
ꢁ
˚
˚
Cg1 is the centroid of the ring defined by atoms C21–C26.
N2—C8
C8—C9
C8—C16
C16—O4
C9—C10
1.428 (3)
1.339 (4)
1.508 (4)
1.248 (3)
1.471 (4)
N4—C19
C19—C20
C19—C27
C27—O6
C20—C21
1.433 (4)
1.336 (4)
1.493 (4)
1.244 (3)
1.465 (4)
D—Hꢀ ꢀ ꢀA
D—H
Hꢀ ꢀ ꢀA
Dꢀ ꢀ ꢀA
D—Hꢀ ꢀ ꢀA
N4—H4ꢀ ꢀ ꢀO3
0.88
0.84
0.88
0.88
0.88
0.88
0.98
0.99
2.07
1.76
2.12
1.93
2.01
1.99
2.87
2.81
2.867 (2)
2.602 (3)
2.926 (2)
2.782 (2)
2.886 (3)
2.721 (2)
3.851 (4)
3.647 (3)
150
177
152
163
178
139
176
142
O8—H8ꢀ ꢀ ꢀO2i
N2—H2ꢀ ꢀ ꢀO8ii
N1—H1ꢀ ꢀ ꢀO4iii
N5—H5ꢀ ꢀ ꢀO6iv
N3—H3ꢀ ꢀ ꢀO5iv
C2—H2Cꢀ ꢀ ꢀCg1
C28—H28Bꢀ ꢀ ꢀCg1iv
N2—C8—C16
C8—C9—C10
118.8 (2)
131.4 (3)
N4—C19—C27
C19—C20—C21
117.1 (2)
131.4 (3)
N1—C6—C7—N2
C6—C7—N2—C8
C7—N2—C8—C16
N2—C8—C16—N3
N2—C8—C9—C10
C8—C9—C10—C11
C8—C9—C10—C15
C8—C16—N3—C17
C16—N3—C17—C18
161.6 (2)
176.0 (3)
50.4 (4)
20.0 (4)
5.8 (5)
N3—C17—C18—N4
C17—C18—N4—C19
C18—N4—C19—C27
N4—C19—C27—N5
C19—C27—N5—C28
C27—N5—C28—C29
C6—N1—C5—O1
26.7 (4)
ꢂ175.6 (2)
68.7 (3)
17.4 (4)
177.7 (2)
73.0 (4)
1
2
1
2
1
2
1
2
Symmetry codes: (i) x; ꢂy þ ; z þ ; (ii) ꢂx þ 1; y ꢂ ; ꢂz þ ; (iii) ꢂx þ 1; ꢂy; ꢂz þ 1;
1
2
1
2
(iv) x; ꢂy þ ; z ꢂ .
ꢂ152.6 (3)
30.8 (5)
ꢂ170.5 (2)
54.7 (4)
ꢂ179.9 (2)
Refinement
N1—C5—O1—C1
ꢂ171.3 (2)
R[F2 > 2ꢇ(F2)] = 0.070
wR(F2) = 0.205
S = 1.03
404 parameters
H-atom parameteꢂrs3 constrained
˚
Áꢈmax = 0.42 e A
ꢂ3
˚
5247 reflections
Áꢈmin = ꢂ0.39 e A
Table 2
Hydrogen-bond geometry (A, ) for (I).
Compound (II)
ꢁ
˚
Crystal data
Cg1 is the centroid of the ring defined by atoms C21–C26.
3
˚
V = 3010 (2) A
Z = 4
C29H33N5O8
Mr = 579.60
D—Hꢀ ꢀ ꢀA
D—H
Hꢀ ꢀ ꢀA
Dꢀ ꢀ ꢀA
D—Hꢀ ꢀ ꢀA
Monoclinic, P21=c
Cu Kꢀ radiation
ꢅ = 0.79 mmꢂ1
T = 100 K
0.38 ꢄ 0.25 ꢄ 0.04 mm
O8—H8ꢀ ꢀ ꢀO2i
N1—H1ꢀ ꢀ ꢀO6ii
N4—H4ꢀ ꢀ ꢀO3
N5—H5ꢀ ꢀ ꢀO4
O9—H9Mꢀ ꢀ ꢀO6
N1—H1ꢀ ꢀ ꢀO3
N4—H4ꢀ ꢀ ꢀN3
N5—H5ꢀ ꢀ ꢀN4
C20—H20ꢀ ꢀ ꢀO3ii
C9—H9ꢀ ꢀ ꢀO4
C3—H3Aꢀ ꢀ ꢀO2
C4—H4Aꢀ ꢀ ꢀO2
C3—H3Bꢀ ꢀ ꢀCg1iii
0.84
0.88
0.88
0.88
0.84
0.88
0.88
0.88
0.95
0.95
0.98
0.98
0.98
1.75
2.25
1.99
2.08
1.87
2.38
2.42
2.43
2.45
2.40
2.43
2.43
2.94
2.587 (3)
2.903 (3)
2.860 (3)
2.927 (3)
2.703 (3)
2.691 (3)
2.769 (3)
2.788 (3)
3.246 (4)
2.786 (4)
2.982 (4)
2.993 (4)
3.735 (4)
172
131
168
162
173
101
104
105
141
104
115
116
138
˚
a = 13.520 (6) A
˚
b = 22.9220 (11) A
˚
c = 9.795 (5) A
ꢁ = 97.41 (5)ꢁ
Data collection
Oxford Xcalibur PX ꢆ-geometry
diffractometer with CCD area
detector
Absorption correction: analytical
(CrysAlis RED; Oxford
Diffraction, 2003)
Tmin = 0.760, Tmax = 0.970
24796 measured reflections
5975 independent reflections
3955 reflections with I > 2ꢇ(I)
Rint = 0.065
1
2
1
2
Symmetry codes: (i) ꢂx þ 1; y ꢂ ; ꢂz þ ; (ii) ꢂx þ 1; ꢂy þ 1; ꢂz þ 1; (iii) x ꢂ 1,
3
2
1
2
ꢂy þ ; z ꢂ .
Refinement
R[F2 > 2ꢇ(F2)] = 0.053
wR(F2) = 0.140
S = 1.00
383 parameters
H-atom parameteꢂrs3 constrained
˚
Áꢈmax = 0.40 e A
ꢂ3
˚
5975 reflections
Áꢈmin = ꢂ0.35 e A
Table 3
Selected geometric parameters (A, ) for (II).
ꢁ
˚
H atoms bonded to C atoms were placed in geometrically opti-
mized positions and treated as riding, with C—H = 0.95 (aromatic),
˚
0.98 (methyl) or 0.99 A (methylene). H atoms belonging to the amide
O4—C16
O6—C27
N2—C8
N4—C19
C8—C9
1.229 (3)
1.228 (3)
1.422 (3)
1.408 (3)
1.324 (3)
C8—C16
C9—C10
C19—C20
C19—C27
C20—C21
1.500 (3)
1.472 (3)
1.338 (3)
1.512 (3)
1.462 (3)
and hydroxy groups were initially located in difference Fourier maps
and in the final refinement their positions were geometrically opti-
˚
˚
mized and treated as riding, with N—H = 0.88 A and O—H = 0.84 A.
For all H atoms except the methyl groups of (II), Uiso(H) =
1.2Ueq(C,N,O). For the methyl groups of (II), Uiso(H) = 1.5Ueq(C).
For both compounds, data collection: CrysAlis CCD (Oxford
Diffraction, 2003); cell refinement: CrysAlis RED (Oxford Diffrac-
tion, 2003); data reduction: CrysAlis RED; program(s) used to solve
structure: SHELXS97 (Sheldrick, 2008); program(s) used to refine
structure: SHELXL97 (Sheldrick, 2008). Molecular graphics: XP in
SHELXTL (Sheldrick, 2008) for (I); Mercury (Macrae et al., 2006)
and SHELXTL for (II). For both compounds, software used to
prepare material for publication: SHELXL97.
N2—C8—C16
C8—C9—C10
114.67 (18)
129.9 (2)
N4—C19—C27
C19—C20—C21
114.04 (18)
129.9 (2)
C1—O1—C5—N1
C6—N1—C5—O1
C8—N2—C7—C6
N1—C6—C7—N2
C7—N2—C8—C16
C17—N3—C16—C8
N2—C8—C16—N3
N2—C8—C9—C10
C8—C9—C10—C15
179.64 (19)
ꢂ170.52 (18)
176.33 (19)
ꢂ163.93 (18)
33.2 (3)
ꢂ175.0 (2)
ꢂ119.6 (2)
ꢂ176.9 (2)
25.4 (4)
C8—C9—C10—C11
C16—N3—C17—C18
ꢂ155.1 (3)
ꢂ83.2 (3)
C19—N4—C18—C17 ꢂ172.19 (19)
N3—C17—C18—N4
C18—N4—C19—C27
ꢂ5.3 (3)
35.8 (3)
C28—N5—C27—C19 ꢂ174.9 (2)
N4—C19—C27—N5
C27—N5—C28—C29
55.4 (3)
122.3 (2)
ꢃ
o122 Makowski et al. C29H33N5O8ꢀCH4O and C29H33N5O8
Acta Cryst. (2010). C66, o119–o123

organic compounds
Macrae, C. F., Edgington, P. R., McCabe, P., Pidcock, E., Shields, G. P., Taylor,
R., Towler, M. & van de Streek, J. (2006). J. Appl. Cryst. 39, 453–457.
Makowski, M., Brzuszkiewicz, A., Lisowski, M. & Lis, T. (2005). Acta Cryst.
C61, o424–o426.
Supplementary data for this paper are available from the IUCr electronic
archives (Reference: SK3358). Services for accessing these data are
described at the back of the journal.
Makowski, M., Lisowski, M., Macia˛g, A. & Lis, T. (2006). Acta Cryst. E62,
o807–o810.
Makowski, M., Lisowski, M., Mikołajczyk, I. & Lis, T. (2007). Acta Cryst. E63,
o989–o991.
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ꢃ
Acta Cryst. (2010). C66, o119–o123
Makowski et al. C29H33N5O8ꢀCH4O and C29H33N5O8 o123