N-Acetyl-L-tyrosine methyl ester monohydrate at 293 and 123 K

The crystal structure of a protected L-tyrosine, namely N-acetyl-L-tyrosine methyl ester monohydrate, C₁₂H₁₅NO₄·H₂O, was determined at both 293 (2) and 123 (2) K. The structure exhibits a network of O—H...O and N—H...O hydrogen bonds, in which the water mol­ecule plays a crucial role as an acceptor of one and a donor of two hydrogen bonds. Mol­ecules of water and of the protected L-tyrosine form hydrogen-bonded layers perpendicular to [001]. C—H...π inter­actions are observed in the hydro­phobic regions of the structure. The structure is similar to that of N-acetyl-L-tyrosine ethyl ester monohydrate [Soriano-García (1993). Acta Cryst. C49, 96–97].

S1. Comment

The N-acetyl methyl ester of L-tyrosine was chosen from among amino acid residues that are responsible for binding the antiarrhythmics of class I and III in sodium and potassium channels, respectively (Tseng, 2001), and was used in some experiments performed to reveal the mutual chemical recognition of antiarrhythmic agents by amino acids. The crystal structure of teh title compound, L-AcYOMe·H₂O, (I), was determined to allow comparison with the structures of N-acetyl-L-tyrosine ethyl ester monohydrate (Pieret et al., 1972; Soriano-García, 1993), L-tyrosine and L-tyrosine hydrochloride (Frey et al., 1973). Charge density studies have also been performed on N-acetyl-L-tyrosine ethyl ester monohydrate (Dahaoui et al., 1999).

Compound (I) crystallizes in space group P2₁2₁2₁, and the contents of the asymmetric unit at 123 (2) K are shown in Fig. 1. Selected geometric parameters at 293 (2) K, (Ia), and at 123 (2) K, (Ib), are given in Tables 1 and 3, respectively. In relation to L-tyrosine itself, the protected amino acid offers different possibilities of intermolecular interactions, which are closer to the specific interactions of small peptides. Owing to the inactivation of the amino and carboxyl groups, the water molecule can participate in a network of hydrogen bonds as an acceptor of one H atom and a donor of two. Water molecules and L-AcYOMe molecules form layers parallel to ab at z = 1/2 (Fig. 2, and Tables 2 and 4). Each layer consists of alternating hydrophobic and hydrophilic areas. In the hydrophobic area, C—H···π interactions of type III in the classification by Malone et al. (1997) dominate [C5—H5···Cg1(x − 1/2, −y + 3/2, −z + 1), where Cg1 is the centre of gravity of the C4–C9 benzene ring], whereas in the hydrophilic area, mainly O—H···O hydrogen bonds exist. There are weak C3—H3A···O10(x + 1, y, z) interactions between hydrophobic and hydrophilic areas of the layers. The layers are linked by N—H···O hydrogen bonds, and between hydrophobic and hydrophilic areas of neighbouring layers there are weak C8—H8···O1(−x + 2, y + 1/2, −z + 3/2) interactions (Fig. 3, and Tables 2 and 4). There is no obvious difference in molecular geometry between 293 and 123 K, except for the apparent elongation of bond lengths at the lower temperature due to a reduction in librational effects as the atomic displacements decrease.

Table 5 presents a comparison of the torsion angles that characterize the backbone conformation of (I), N-acetyl-L-tyrosine ethyl ester (Soriano-García, 1993), and N-acetyl-L-tyrosine ethyl ester at room- and low-temperature (Dahaoui et al., 1999) with the conformation of the L-tyrosine residue in selected tripeptides and with the conformation of L-tyrosine itself and L-tyrosine hydrochloride (Frey et al., 1973). The values of the torsion angles ω, ϕ, ψ₁, ψ₂, χ₁ and χ₂, which are defined in accordance with the IUPAC–IUB Commission on Biochemical Nomenclature (1970), are similar for protected L-tyrosine; the observed differences in torsion angles are in the range 0.7–5.2°. For tripeptides LYL and VYV, the differences are of up to 25°, indicating that the conformation of the L-tyrosine residue is, in general, well preserved with small deviations caused by the N– and C-ends forming hydrogen bonds. However, in both LYL and VYV, the presence of relatively long hydrocarbon chains of L or V residues provides steric hindrance for such intermolecular interactions. In GYA, owing to a lack of hydrocarbon chains, the N– and C-ends are free to form hydrogen bonds. The moderate N—H···O hydrogen bonds could change the torsion angles of the L-tyrosine residue by 50°. In the cases of L-tyrosine and its hydrochloride, the most pronounced conformational differences arise because of specific patterns of hydrogen bonding.

##AUTHOR: In the paragraph above, please define the residue symbols L, V, Y, A, G.

S2. Experimental

The protected amino acid was purchased from Bachem Chemical Company. Crystals suitable for X-ray structure determination were obtained by vapour diffusion at room temperature between heptane and an acetone solution containing N-acetyl-L-tyrosine ethyl ester and lidocaine in a molar ratio of 1:1. Lidocaine, which was used to provide the correct ionic strength of the solutions, was purchased from Sigma Chemical Company. The diffraction intensity measurements at 293 (2) and 123 (2) K were performed on two different crystals.

S3. Refinement

Owing to the absence of significant anomalous scattering, Friedel pairs were merged. The absolute configuration of the purchased materials was known. H atoms bonded to N and O atoms were located in difference Fourier maps and included in the refinement without constraints. For the sp²-bound methyl group (C11), the procedure for finding the H atom relied on locating the maximum electron density around the circle representing the locus of possible H-atom positions (Sheldrick, 1997). For this methyl group, C—H distances and C—C—H angles were kept fixed, while the torsion angles were allowed to refine with U_iso(H) set at 1.2U_eq(C11). H atoms attached to other C atoms were included with appropriate geometrical constraints and were treated as riding, with U_iso(H) values of 1.2U_eq of the parent atoms.

Computing details

For both compounds, data collection: COLLECT (Nonius, 1997); cell refinement: DENZO–SMN (Otwinowski & Minor, 1997); data reduction: DENZO and SCALEPACK (Otwinowski & Minor, 1997); program(s) used to solve structure: SIR92 (Altomare et al., 1994); program(s) used to refine structure: SHELXL97 (Sheldrick, 1997); molecular graphics: PLATON (Spek, 2003), ORTEP-3 for Windows (Farrugia, 1997) and Mercury (Version 1.4; Macrae et al., 2006); software used to prepare material for publication: SHELXL97.

Figures

	Fig. 1. The asymmetric unit of N-acetyl-L-tyrosine methyl ester monohydrate at 123 K, showing the atom numbering scheme. Displacement ellipsoids are drawn at the 50% probability level.
	Fig. 2. (a) The role of hydrogen bonds formed by water molecules in joining molecules of N-acetyl-L-tyrosine ethyl ester into layers; (b) a projection onto the (x, y, 1/2) layer, showing hydrophobic and hydrophilic areas alternating along [010].
	Fig. 3. The arrangement of layers in projection along [100].

(Ia) N-Acetyl-L-tyrosine methyl ester monohydrate

Crystal data

C12H15NO4·H2O	Dx = 1.271 Mg m^−3
Mr = 255.27	Mo Kα radiation, λ = 0.71073 Å
Orthorhombic, P212121	Cell parameters from 2095 reflections
a = 7.2117 (1) Å	θ = 1.0–30.0°
b = 12.9868 (3) Å	µ = 0.10 mm^−1
c = 14.2470 (4) Å	T = 293 K
V = 1334.33 (5) Å^3	Block, colourless
Z = 4	0.52 × 0.52 × 0.37 mm
F(000) = 544

Data collection

Nonius KappaCCD diffractometer	2223 independent reflections
Radiation source: fine-focus sealed tube	1847 reflections with I > 2σ(I)
Horizontally mounted graphite crystal monochromator	Rint = 0.020
Detector resolution: 9 pixels mm^-1	θmax = 30.0°, θmin = 3.2°
ϕ scans and ο scans to fill asymmetric unit	h = −10→10
Absorption correction: multi-scan (DENZO and SCALEPACK; Otwinowski & Minor, 1997)	k = −18→18
Tmin = 0.950, Tmax = 0.964	l = −19→20
8443 measured reflections

Refinement

Refinement on F^2	Secondary atom site location: difference Fourier map
Least-squares matrix: full	Hydrogen site location: difference Fourier map
R[F^2 > 2σ(F^2)] = 0.040	H atoms treated by a mixture of independent and constrained refinement
wR(F^2) = 0.101	w = 1/[σ^2(Fo^2) + (0.0462P)^2 + 0.235P] where P = (Fo^2 + 2Fc^2)/3
S = 1.01	(Δ/σ)max < 0.001
2223 reflections	Δρmax = 0.20 e Å^−3
181 parameters	Δρmin = −0.16 e Å^−3
0 restraints	Extinction correction: SHELXL97, Fc^*=kFc[1+0.001xFc^2λ^3/sin(2θ)]^-1/4
Primary atom site location: structure-invariant direct methods	Extinction coefficient: 0.094 (4)

Special details

Geometry. All e.s.d.'s (except the e.s.d. in the dihedral angle between two l.s. planes) are estimated using the full covariance matrix. The cell e.s.d.'s are taken into account individually in the estimation of e.s.d.'s in distances, angles and torsion angles; correlations between e.s.d.'s in cell parameters are only used when they are defined by crystal symmetry. An approximate (isotropic) treatment of cell e.s.d.'s is used for estimating e.s.d.'s involving l.s. planes.

Fractional atomic coordinates and isotropic or equivalent isotropic displacement parameters (Ų)

	x	y	z	Uiso*/Ueq
N1	0.7140 (2)	0.48523 (12)	0.65541 (11)	0.0346 (3)
H1	0.794 (4)	0.4776 (19)	0.7018 (17)	0.051 (7)*
C1	0.7867 (3)	0.38301 (13)	0.51672 (12)	0.0357 (4)
O1	0.7839 (3)	0.30420 (10)	0.56035 (11)	0.0627 (5)
C2	0.7818 (3)	0.49014 (13)	0.55995 (12)	0.0318 (4)
H2	0.6984	0.5337	0.5229	0.038*
O2	0.7977 (2)	0.38843 (11)	0.42440 (10)	0.0485 (4)
C3	0.9779 (3)	0.53656 (14)	0.55704 (14)	0.0365 (4)
H3A	1.0595	0.4952	0.5958	0.044*
H3B	1.0240	0.5337	0.4931	0.044*
C4	0.9842 (3)	0.64710 (13)	0.59090 (12)	0.0335 (4)
C5	0.9006 (3)	0.72601 (14)	0.54091 (14)	0.0401 (4)
H5	0.8373	0.7107	0.4858	0.048*
C6	1.0781 (3)	0.67253 (15)	0.67263 (14)	0.0411 (5)
H6	1.1365	0.6209	0.7069	0.049*
C7	0.9094 (3)	0.82747 (14)	0.57132 (14)	0.0400 (4)
H7	0.8529	0.8794	0.5366	0.048*
C8	1.0864 (3)	0.77369 (15)	0.70432 (13)	0.0442 (5)
H8	1.1485	0.7892	0.7598	0.053*
C9	1.0023 (3)	0.85107 (13)	0.65342 (12)	0.0342 (4)
O9	1.0160 (2)	0.94996 (11)	0.68728 (11)	0.0459 (4)
H9	0.967 (5)	0.994 (2)	0.646 (2)	0.073 (9)*
C10	0.5350 (3)	0.46506 (15)	0.67405 (13)	0.0386 (4)
O10	0.4177 (2)	0.45931 (14)	0.61182 (11)	0.0530 (4)
C11	0.4865 (4)	0.4494 (2)	0.77528 (15)	0.0578 (6)
H11A	0.4050	0.5035	0.7956	0.069*
H11B	0.5975	0.4505	0.8124	0.069*
H11C	0.4257	0.3841	0.7827	0.069*
C12	0.8085 (5)	0.29253 (19)	0.37345 (17)	0.0668 (7)
H12A	0.8159	0.3065	0.3074	0.080*
H12B	0.7000	0.2521	0.3862	0.080*
H12C	0.9169	0.2553	0.3929	0.080*
O5	0.3430 (3)	0.41471 (13)	0.42768 (13)	0.0555 (5)
H5A	0.335 (5)	0.357 (3)	0.425 (2)	0.081 (11)*
H5B	0.369 (5)	0.436 (3)	0.493 (3)	0.102 (12)*

Atomic displacement parameters (Ų)

	U^11	U^22	U^33	U^12	U^13	U^23
N1	0.0345 (8)	0.0365 (7)	0.0329 (7)	−0.0012 (7)	−0.0016 (7)	−0.0013 (6)
C1	0.0384 (9)	0.0310 (8)	0.0377 (9)	0.0013 (8)	−0.0037 (8)	−0.0017 (7)
O1	0.1109 (15)	0.0289 (6)	0.0482 (8)	0.0039 (8)	−0.0003 (10)	0.0038 (6)
C2	0.0345 (9)	0.0269 (7)	0.0340 (8)	0.0012 (7)	−0.0015 (7)	0.0006 (6)
O2	0.0726 (10)	0.0369 (7)	0.0360 (7)	0.0030 (7)	−0.0008 (7)	−0.0047 (6)
C3	0.0341 (9)	0.0329 (8)	0.0425 (9)	0.0009 (8)	0.0025 (8)	−0.0033 (8)
C4	0.0323 (8)	0.0305 (8)	0.0376 (8)	−0.0026 (7)	0.0023 (7)	−0.0002 (7)
C5	0.0441 (10)	0.0379 (9)	0.0382 (9)	−0.0017 (8)	−0.0107 (8)	−0.0024 (8)
C6	0.0488 (11)	0.0344 (9)	0.0400 (9)	−0.0017 (8)	−0.0089 (9)	0.0064 (8)
C7	0.0430 (10)	0.0339 (9)	0.0431 (10)	0.0016 (8)	−0.0106 (9)	0.0032 (8)
C8	0.0561 (12)	0.0405 (10)	0.0361 (9)	−0.0080 (9)	−0.0114 (9)	0.0021 (8)
C9	0.0372 (9)	0.0314 (8)	0.0341 (8)	−0.0041 (7)	0.0006 (8)	−0.0020 (7)
O9	0.0595 (9)	0.0327 (7)	0.0454 (7)	−0.0025 (7)	−0.0109 (7)	−0.0049 (6)
C10	0.0391 (10)	0.0371 (9)	0.0397 (9)	−0.0006 (8)	0.0019 (8)	−0.0059 (8)
O10	0.0381 (8)	0.0717 (10)	0.0492 (8)	−0.0048 (8)	−0.0050 (7)	−0.0057 (8)
C11	0.0528 (13)	0.0792 (16)	0.0415 (10)	−0.0089 (13)	0.0104 (10)	−0.0077 (11)
C12	0.099 (2)	0.0503 (12)	0.0517 (13)	0.0063 (14)	−0.0051 (14)	−0.0207 (11)
O5	0.0784 (12)	0.0361 (8)	0.0519 (9)	−0.0045 (8)	0.0016 (9)	0.0004 (7)

Geometric parameters (Å, º)

N1—C10	1.344 (3)	C6—H6	0.9300
N1—C2	1.447 (2)	C7—C9	1.383 (3)
N1—H1	0.88 (3)	C7—H7	0.9300
C1—O1	1.198 (2)	C8—C9	1.379 (3)
C1—O2	1.320 (2)	C8—H8	0.9300
C1—C2	1.522 (2)	C9—O9	1.375 (2)
C2—C3	1.538 (3)	O9—H9	0.89 (3)
C2—H2	0.9800	C10—O10	1.228 (2)
O2—C12	1.444 (2)	C10—C11	1.498 (3)
C3—C4	1.515 (2)	C11—H11A	0.9600
C3—H3A	0.9700	C11—H11B	0.9600
C3—H3B	0.9700	C11—H11C	0.9600
C4—C5	1.386 (3)	C12—H12A	0.9600
C4—C6	1.387 (3)	C12—H12B	0.9600
C5—C7	1.388 (3)	C12—H12C	0.9600
C5—H5	0.9300	O5—H5A	0.75 (4)
C6—C8	1.391 (3)	O5—H5B	0.99 (4)
C10—N1—C2	121.3 (2)	C8—C6—H6	119.4
C10—N1—H1	117 (2)	C9—C7—C5	119.76 (17)
C2—N1—H1	119 (2)	C9—C7—H7	120.1
O1—C1—O2	124.4 (2)	C5—C7—H7	120.1
O1—C1—C2	124.9 (2)	C9—C8—C6	119.9 (2)
O2—C1—C2	110.9 (2)	C9—C8—H8	120.0
N1—C2—C1	110.4 (2)	C6—C8—H8	120.0
N1—C2—C3	110.7 (2)	O9—C9—C8	117.7 (2)
C1—C2—C3	109.1 (2)	O9—C9—C7	122.6 (2)
N1—C2—H2	108.9	C8—C9—C7	119.8 (2)
C1—C2—H2	108.9	C9—O9—H9	110 (2)
C3—C2—H2	108.9	O10—C10—N1	122.1 (2)
C1—O2—C12	117.3 (2)	O10—C10—C11	121.7 (2)
C4—C3—C2	113.0 (2)	N1—C10—C11	116.2 (2)
C4—C3—H3A	109.0	C10—C11—H11A	109.5
C2—C3—H3A	109.0	C10—C11—H11B	109.5
C4—C3—H3B	109.0	H11A—C11—H11B	109.5
C2—C3—H3B	109.0	C10—C11—H11C	109.5
H3A—C3—H3B	107.8	H11A—C11—H11C	109.5
C5—C4—C6	117.9 (2)	H11B—C11—H11C	109.5
C5—C4—C3	121.6 (2)	O2—C12—H12A	109.5
C6—C4—C3	120.5 (2)	O2—C12—H12B	109.5
C4—C5—C7	121.4 (2)	H12A—C12—H12B	109.5
C4—C5—H5	119.3	O2—C12—H12C	109.5
C7—C5—H5	119.3	H12A—C12—H12C	109.5
C4—C6—C8	121.2 (2)	H12B—C12—H12C	109.5
C4—C6—H6	119.4	H5A—O5—H5B	110 (3)
C10—N1—C2—C1	−71.3 (2)	C6—C4—C5—C7	−0.2 (3)
C10—N1—C2—C3	167.9 (2)	C3—C4—C5—C7	−178.9 (2)
O1—C1—C2—N1	−18.5 (3)	C5—C4—C6—C8	0.8 (3)
O2—C1—C2—N1	162.6 (2)	C3—C4—C6—C8	179.5 (2)
O1—C1—C2—C3	103.3 (2)	C4—C5—C7—C9	−0.3 (3)
O2—C1—C2—C3	−75.6 (2)	C4—C6—C8—C9	−0.9 (3)
O1—C1—O2—C12	−0.5 (4)	C6—C8—C9—O9	−179.4 (2)
C2—C1—O2—C12	178.4 (2)	C6—C8—C9—C7	0.3 (3)
N1—C2—C3—C4	−63.4 (2)	C5—C7—C9—O9	180.0 (2)
C1—C2—C3—C4	175.0 (2)	C5—C7—C9—C8	0.3 (3)
C2—C3—C4—C5	−67.4 (2)	C2—N1—C10—O10	−6.9 (3)
C2—C3—C4—C6	113.9 (2)	C2—N1—C10—C11	172.8 (2)

Hydrogen-bond geometry (Å, º)

D—H···A	D—H	H···A	D···A	D—H···A
O9—H9···O5^i	0.89 (3)	1.82 (3)	2.707 (2)	173 (3)
N1—H1···O9^ii	0.88 (3)	2.12 (3)	3.004 (2)	177 (2)
O5—H5A···O1^iii	0.75 (4)	2.14 (4)	2.880 (2)	170 (4)
O5—H5B···O10	0.99 (4)	1.76 (4)	2.740 (2)	174 (3)
C3—H3A···O10^iv	0.97	2.63	3.417 (3)	138
C8—H8···O1^v	0.93	2.62	3.503 (2)	160
C11—H11A···O5^vi	0.96	2.81	3.671 (3)	150
C12—H12C···O10^vii	0.96	2.79	3.371 (3)	120
C5—H5···Cg1^viii	0.93	2.94	3.73 (5)	144

Symmetry codes: (i) x+1/2, −y+3/2, −z+1; (ii) −x+2, y−1/2, −z+3/2; (iii) x−1/2, −y+1/2, −z+1; (iv) x+1, y, z; (v) −x+2, y+1/2, −z+3/2; (vi) −x+1/2, −y+1, z+1/2; (vii) x+1/2, −y+1/2, −z+1; (viii) x−1/2, −y+3/2, −z+1.

(Ib) N-Acetyl-L-tyrosine methyl ester monohydrate

Crystal data

C12H15NO4·H2O	Dx = 1.302 Mg m^−3
Mr = 255.27	Mo Kα radiation, λ = 0.71073 Å
Orthorhombic, P212121	Cell parameters from 2646 reflections
a = 7.1118 (2) Å	θ = 1.0–33.1°
b = 12.9364 (3) Å	µ = 0.10 mm^−1
c = 14.1538 (4) Å	T = 123 K
V = 1302.17 (6) Å^3	Block, colourless
Z = 4	0.40 × 0.37 × 0.25 mm
F(000) = 544

Data collection

Nonius KappaCCD diffractometer	2790 independent reflections
Radiation source: fine-focus sealed tube	2605 reflections with I > 2σ(I)
Horizontally mounted graphite crystal monochromator	Rint = 0.020
Detector resolution: 9 pixels mm^-1	θmax = 33.1°, θmin = 3.3°
ο scans at chi = 55 deg	h = −10→10
Absorption correction: multi-scan HKL DENZO and SCALEPACK (Otwinowski & Minor, 1997)	k = −19→19
Tmin = 0.961, Tmax = 0.975	l = −21→21
10167 measured reflections

Refinement

Refinement on F^2	Primary atom site location: structure-invariant direct methods
Least-squares matrix: full	Secondary atom site location: difference Fourier map
R[F^2 > 2σ(F^2)] = 0.032	Hydrogen site location: inferred from neighbouring sites
wR(F^2) = 0.084	H atoms treated by a mixture of independent and constrained refinement
S = 1.00	w = 1/[σ^2(Fo^2) + (0.0426P)^2 + 0.2619P] where P = (Fo^2 + 2Fc^2)/3
2790 reflections	(Δ/σ)max < 0.001
184 parameters	Δρmax = 0.31 e Å^−3
0 restraints	Δρmin = −0.18 e Å^−3

Special details

Geometry. All e.s.d.'s (except the e.s.d. in the dihedral angle between two l.s. planes) are estimated using the full covariance matrix. The cell e.s.d.'s are taken into account individually in the estimation of e.s.d.'s in distances, angles and torsion angles; correlations between e.s.d.'s in cell parameters are only used when they are defined by crystal symmetry. An approximate (isotropic) treatment of cell e.s.d.'s is used for estimating e.s.d.'s involving l.s. planes.

Fractional atomic coordinates and isotropic or equivalent isotropic displacement parameters (Ų)

	x	y	z	Uiso*/Ueq
N1	0.71157 (15)	0.48699 (7)	0.65787 (7)	0.01325 (17)
H1	0.794 (3)	0.4817 (15)	0.7039 (14)	0.028 (5)*
C1	0.77991 (17)	0.38398 (8)	0.51734 (8)	0.01321 (19)
O1	0.77403 (18)	0.30426 (6)	0.56186 (7)	0.0240 (2)
C2	0.77647 (16)	0.49188 (8)	0.56094 (8)	0.01177 (18)
H2	0.6892	0.5367	0.5237	0.014*
O2	0.79393 (15)	0.38950 (7)	0.42407 (6)	0.01828 (17)
C3	0.97621 (16)	0.53788 (8)	0.55674 (8)	0.01389 (19)
H3A	1.0611	0.4955	0.5964	0.017*
H3B	1.0226	0.5345	0.4909	0.017*
C4	0.98391 (16)	0.64882 (8)	0.59029 (8)	0.01260 (18)
C5	0.89806 (17)	0.72820 (8)	0.53906 (8)	0.0151 (2)
H5	0.8327	0.7121	0.4824	0.018*
C6	1.07879 (18)	0.67465 (8)	0.67320 (8)	0.0156 (2)
H6	1.1384	0.6217	0.7088	0.019*
C7	0.90651 (17)	0.83047 (8)	0.56958 (9)	0.0149 (2)
H7	0.8476	0.8835	0.5338	0.018*
C8	1.08802 (19)	0.77652 (8)	0.70499 (8)	0.0164 (2)
H8	1.1527	0.7926	0.7618	0.020*
C9	1.00179 (16)	0.85473 (8)	0.65288 (8)	0.01301 (18)
O9	1.01535 (14)	0.95384 (6)	0.68652 (6)	0.01733 (17)
H9	0.967 (4)	1.0001 (19)	0.6502 (18)	0.049 (7)*
C10	0.53053 (17)	0.46497 (8)	0.67793 (8)	0.0144 (2)
O10	0.40919 (13)	0.45748 (8)	0.61595 (7)	0.02064 (18)
C11	0.4846 (2)	0.44935 (11)	0.78070 (9)	0.0221 (2)
H11A	0.4006	0.5047	0.8021	0.027*
H11B	0.6008	0.4509	0.8179	0.027*
H11C	0.4225	0.3824	0.7891	0.027*
C12	0.8035 (2)	0.29199 (10)	0.37386 (10)	0.0257 (3)
H12A	0.8135	0.3052	0.3059	0.031*
H12B	0.6895	0.2517	0.3866	0.031*
H12C	0.9139	0.2531	0.3952	0.031*
O5	0.34119 (15)	0.41298 (7)	0.43062 (7)	0.02093 (19)
H5B	0.360 (4)	0.4303 (17)	0.4900 (19)	0.048 (7)*
H5A	0.330 (4)	0.352 (2)	0.4296 (19)	0.049 (7)*

Atomic displacement parameters (Ų)

	U^11	U^22	U^33	U^12	U^13	U^23
N1	0.0143 (4)	0.0153 (4)	0.0102 (4)	−0.0004 (3)	−0.0009 (3)	−0.0006 (3)
C1	0.0150 (4)	0.0122 (4)	0.0125 (4)	0.0004 (4)	−0.0014 (4)	−0.0008 (3)
O1	0.0430 (6)	0.0115 (3)	0.0176 (4)	0.0017 (4)	0.0005 (4)	0.0014 (3)
C2	0.0140 (4)	0.0106 (4)	0.0107 (4)	0.0002 (3)	−0.0003 (4)	−0.0002 (3)
O2	0.0281 (4)	0.0149 (3)	0.0118 (3)	0.0013 (3)	−0.0008 (4)	−0.0020 (3)
C3	0.0139 (4)	0.0125 (4)	0.0152 (4)	0.0000 (4)	0.0010 (4)	−0.0014 (3)
C4	0.0135 (4)	0.0120 (4)	0.0123 (4)	−0.0012 (4)	0.0007 (4)	0.0000 (3)
C5	0.0171 (5)	0.0144 (4)	0.0139 (5)	−0.0003 (4)	−0.0043 (4)	−0.0012 (4)
C6	0.0197 (5)	0.0133 (4)	0.0137 (5)	−0.0008 (4)	−0.0031 (4)	0.0022 (3)
C7	0.0168 (5)	0.0136 (4)	0.0144 (5)	0.0008 (4)	−0.0032 (4)	0.0000 (4)
C8	0.0227 (5)	0.0143 (4)	0.0122 (4)	−0.0020 (4)	−0.0042 (4)	0.0008 (3)
C9	0.0146 (4)	0.0124 (4)	0.0121 (4)	−0.0016 (4)	0.0002 (4)	−0.0006 (3)
O9	0.0240 (4)	0.0120 (3)	0.0161 (4)	−0.0002 (3)	−0.0051 (4)	−0.0020 (3)
C10	0.0154 (5)	0.0138 (4)	0.0141 (4)	0.0001 (4)	0.0014 (4)	−0.0027 (4)
O10	0.0159 (4)	0.0283 (4)	0.0177 (4)	−0.0017 (4)	−0.0020 (3)	−0.0022 (4)
C11	0.0210 (5)	0.0321 (6)	0.0133 (5)	−0.0034 (5)	0.0039 (5)	−0.0021 (5)
C12	0.0393 (8)	0.0202 (5)	0.0175 (5)	0.0029 (5)	−0.0019 (6)	−0.0081 (4)
O5	0.0320 (5)	0.0137 (4)	0.0171 (4)	−0.0025 (3)	0.0009 (4)	−0.0002 (3)

Geometric parameters (Å, º)

N1—C10	1.349 (2)	C6—H6	0.9500
N1—C2	1.449 (2)	C7—C9	1.396 (2)
N1—H1	0.88 (2)	C7—H7	0.9500
C1—O1	1.209 (1)	C8—C9	1.394 (2)
C1—O2	1.326 (1)	C8—H8	0.9500
C1—C2	1.526 (1)	C9—O9	1.371 (1)
C2—C3	1.541 (2)	O9—H9	0.86 (3)
C2—H2	1.0000	C10—O10	1.234 (2)
O2—C12	1.449 (1)	C10—C11	1.504 (2)
C3—C4	1.513 (2)	C11—H11A	0.9800
C3—H3A	0.9900	C11—H11B	0.9800
C3—H3B	0.9900	C11—H11C	0.9800
C4—C6	1.394 (2)	C12—H12A	0.9800
C4—C5	1.398 (2)	C12—H12B	0.9800
C5—C7	1.393 (2)	C12—H12C	0.9800
C5—H5	0.9500	O5—H5B	0.88 (3)
C6—C8	1.394 (2)	O5—H5A	0.79 (3)
C10—N1—C2	120.8 (1)	C4—C6—H6	119.3
C10—N1—H1	118 (1)	C5—C7—C9	119.8 (1)
C2—N1—H1	120 (1)	C5—C7—H7	120.1
O1—C1—O2	124.6 (1)	C9—C7—H7	120.1
O1—C1—C2	124.7 (1)	C9—C8—C6	119.6 (1)
O2—C1—C2	110.8 (1)	C9—C8—H8	120.2
N1—C2—C1	110.4 (1)	C6—C8—H8	120.2
N1—C2—C3	110.3 (1)	O9—C9—C8	117.7 (1)
C1—C2—C3	108.8 (1)	O9—C9—C7	122.5 (1)
N1—C2—H2	109.1	C8—C9—C7	119.8 (1)
C1—C2—H2	109.1	C9—O9—H9	114 (2)
C3—C2—H2	109.1	O10—C10—N1	122.3 (1)
C1—O2—C12	116.4 (1)	O10—C10—C11	121.7 (1)
C4—C3—C2	112.8 (1)	N1—C10—C11	116.0 (1)
C4—C3—H3A	109.0	C10—C11—H11A	109.5
C2—C3—H3A	109.0	C10—C11—H11B	109.5
C4—C3—H3B	109.0	H11A—C11—H11B	109.5
C2—C3—H3B	109.0	C10—C11—H11C	109.5
H3A—C3—H3B	107.8	H11A—C11—H11C	109.5
C6—C4—C5	118.2 (1)	H11B—C11—H11C	109.5
C6—C4—C3	120.6 (1)	O2—C12—H12A	109.5
C5—C4—C3	121.2 (1)	O2—C12—H12B	109.5
C7—C5—C4	121.2 (1)	H12A—C12—H12B	109.5
C7—C5—H5	119.4	O2—C12—H12C	109.5
C4—C5—H5	119.4	H12A—C12—H12C	109.5
C8—C6—C4	121.4 (1)	H12B—C12—H12C	109.5
C8—C6—H6	119.3	H5A—O5—H5B	107 (2)
C10—N1—C2—C1	−70.3 (1)	C6—C4—C5—C7	0.0 (2)
C10—N1—C2—C3	169.4 (1)	C3—C4—C5—C7	−179.5 (1)
O1—C1—C2—N1	−16.5 (2)	C5—C4—C6—C8	0.3 (2)
O2—C1—C2—N1	164.8 (1)	C3—C4—C6—C8	179.7 (1)
O1—C1—C2—C3	104.7 (1)	C4—C5—C7—C9	−0.2 (2)
O2—C1—C2—C3	−74.1 (1)	C4—C6—C8—C9	−0.4 (2)
O1—C1—O2—C12	−0.3 (2)	C6—C8—C9—O9	−179.6 (1)
C2—C1—O2—C12	178.5 (1)	C6—C8—C9—C7	0.2 (2)
N1—C2—C3—C4	−64.0 (1)	C5—C7—C9—O9	179.9 (1)
C1—C2—C3—C4	174.8 (1)	C5—C7—C9—C8	0.1 (2)
C2—C3—C4—C6	112.9 (1)	C2—N1—C10—O10	−6.8 (2)
C2—C3—C4—C5	−67.6 (1)	C2—N1—C10—C11	172.9 (1)

Hydrogen-bond geometry (Å, º)

D—H···A	D—H	H···A	D···A	D—H···A
O9—H9···O5^i	0.86 (3)	1.83 (3)	2.693 (1)	173 (3)
N1—H1···O9^ii	0.88 (2)	2.09 (2)	2.968 (1)	174 (2)
O5—H5A···O1^iii	0.79 (3)	2.07 (3)	2.853 (1)	173 (3)
O5—H5B···O10	0.88 (3)	1.85 (3)	2.729 (1)	176 (2)
C3—H3A···O10^iv	0.99	2.54	3.356 (2)	140
C8—H8···O1^v	0.95	2.55	3.462 (2)	160
C11—H11A···O5^vi	0.98	2.72	3.612 (2)	151
C12—H12C···O10^vii	0.98	2.73	3.317 (2)	119
C5—H5···Cg1^viii	0.95	2.84	3.65 (4)	144

Symmetry codes: (i) x+1/2, −y+3/2, −z+1; (ii) −x+2, y−1/2, −z+3/2; (iii) x−1/2, −y+1/2, −z+1; (iv) x+1, y, z; (v) −x+2, y+1/2, −z+3/2; (vi) −x+1/2, −y+1, z+1/2; (vii) x+1/2, −y+1/2, −z+1; (viii) x−1/2, −y+3/2, −z+1.