Water polymers in L-alanyl-L-methionine hemihydrate

The side chains of L-alanyl-L-me­thionine hemihydrate, C₈H₁₆N₂O₃S·0.5H₂O, form hydro­phobic columns within a three-dimensional hydrogen-bond network that includes extended polymers of cocrystallized water mol­ecules and C^[alpha]-H...S interactions.

S1. Comment

The crystal structure of L-Val-L-Ala (VA; Görbitz & Gundersen, 1996) was the first example of nanotube formation by such a small molecule. Subsequently, the reteroanalogue L-Ala-L-Val (Görbitz, 2002) and a series of other dipeptides with L-Ala, L-Val and L-Ile residues (Görbitz, 2003a) were found to form structures very similar to VA, differing only in the way that side chains partly fill the channels along the hexagonal axes, which translates directly to pore size.

To investigate whether crystallization in the VA class is compatible with dipeptides incorporating unbranched side chains (apart from the methyl group of L-Ala), crystallization and structure determination have been carried out for L-Met-L-Ala (MA) and L-Ala-L-Met (AM). The structure of MA is indeed closely related to the VA-class, but with seven molecules in the asymmetric unit (Görbitz, 2003b).

The asymmetric unit of AM, with two peptide molecules and one water molecule, is shown in Fig. 1. There are no signs of any kind of disorder. Bond lengths and bond angles are normal. Peptide molecule A has an elongated main-chain conformation, in which the carboxylate group is coplanar with the N atom of the peptide bond (Table 1). The L-Met side chain has an unusual gauche+,trans,trans conformation for χ¹,χ² and χ³ (N2A—C4A—C5A—C6A, C4A—C5A—C6A—S1A and C5A—C6A—S1A—C7A, respectively), which has been found previously only for D-Ala-L-Met (in the racemate; Stenkamp & Jensen, 1974; Guillot et al., 2001), for one of the two side chains in cyclo(L-Met-L-Met) (Valle et al., 1990) and for N-formyl-L-Met (Chen & Parthasarathy, 1977).

The main chain of peptide molecule B differs from A mainly in the carboxylate orientation defined by N2B—C4B—C8B—O2B [−57.8 (2)°]. The side-chain gauche- rotamer for χ¹ (N2B—C4B—C5B—C6B) and the trans rotamer for χ³ (C5B—C6B—S1B—C7B) are both quite common, but the gauche+ orientation for χ² (C4B—C5B—C6B—S1B) is very rare, and the gauche-,gauche+,trans combination for χ¹,χ² and χ³ yields a conformation that has not been observed previously for amino acids or peptides in the Cambridge Structural Database (CSD; Allen & Motherwell, 2002).

The packing diagram in Fig. 2 shows that even though some features are shared, like the aggregation of side chains into hydrophobic columns, AM is clearly not a member of the VA class. As was also evident from the P2₁2₁2₁ space group, AM lacks hexagonal symmetry, and furthermore, the open channels at the center of each hydrophobic column are missing. In the VA class, these channels are either empty or filled non-stoichiometrically with solvent molecules that can be removed by drying with complete retention of the peptide scaffold (Görbitz & Gundersen, 1996; Görbitz, 2002). The cocrystallized solvent water molecules of AM are located close to the twofold screw axes parallel to the short 5.0809 (2) Å a axis; they form an integral part of the hydrogen-bond network and cannot be removed by drying without destroying the crystal. Hydrogen bonds between water molecules give rise to polymers along the a axis that are surrounded by peptide B molecules, as seen in Fig. 3. Similar columns, with carboxylate groups as acceptors for water H atoms rather than peptide carbonyl groups, have been found for L-Asp-Gly·H₂O (Eggleston et al., 1981), for L-Arg-L-Asp·2H₂O (Ramakrishnan & Viswamitra, 1988) and twice in the 1:1 complex L-His-L-Ser:Gly-L-Glu·6H₂O (Suresh & Vijayan, 1985). L-Pro-Gly (Narasimhan & Chacko, 1982) and L-Pro-Val (Narasimhan et al., 1982) have polymers in which water molecules do not accept amino H atoms.

It was no surprise to find that the structure of AM is completely different from the monoclinic structure of D,L-Ala-L,D-Met (Stenkamp & Jensen, 1974; Guillot et al., 2001), the difference being due to the different directions in which side chains are disposed relative to the main chain for L—L and D,L—L,D diastereomers (Görbitz & Etter, 1992).

The hydrogen-bond geometry is detailed in Table 2. A l l amino H atoms of molecule A are donated to molecule B carboxylate groups and vice verca (including a three-center interaction for H2B; Table 2), except for atom H1B, which is accepted by the water molecule. Neighboring molecules of type A or type B are connected by hydrogen bonds, with the >N—H peptide bond as the donor, and by a number of weak interactions with C^α—H donors (including C4B—H41B···S1B; Fig. 3). A search of the CSD revealed that C—H···S(L-Met) contacts are surprisingly ubiquitous, with H···S distances starting at 2.85 Å. The most common donor is, however, not C^α—H, as in AM, but the terminal methyl group of another L-Met side chain.

In summary, the hydrogen-bond network in AM incorporates two peptide molecules in the asymmetric unit, both with unusual L-Met side-chain conformations, together with a solvent water molecule that forms extended hydrogen-bonded polymers along the shortest crystallographic axis.

S2. Experimental

The title compound was obtained from BACHEM and used as received. Crystals were grown by slow diffusion of acetonitrile into an aqueous solution (30 µl) containing the peptide (approximately 1 mg).

S3. Refinement

Data were collected by measuring three sets of exposures (with the detector set at 2θ = 29°; crystal-to-detector distance = 5.00 cm). Coordinates for water H atoms, which were found in an electron density map, were refined; other H atoms were placed geometrically and treated in the refinement with constraints. Free rotation of amine and methyl groups was permitted. U_iso values for H atoms were set to 1.2U_eq of the carrier atom, or 1.5U_eq for water, methyl and amine groups. The Flack (1983) parameter [−0.04 (8)] confirmed the known absolute structure; Friedel pairs were not merged in the final refinements.

Computing details

Data collection: SMART (Bruker, 1998); cell refinement: SAINT (Bruker, 2001); data reduction: SAINT; program(s) used to solve structure: SHELXTL (Bruker, 2000); program(s) used to refine structure: SHELXTL; molecular graphics: SHELXTL; software used to prepare material for publication: SHELXTL.

Figures

	Fig. 1. : The asymmetric unit of L-Ala-L-Met, with peptide molecules A and B and a solvent water molecule. Displacement ellipsoids are shown at the 50% probability level and H atoms are shown as spheres of arbitrary size.
	Fig. 2. : The molecular packing and unit cell viewed along the a axis. Molecules in the asymmetric unit are identified by the suffixes A, B and W.
	Fig. 3. : A stereoview of the chains of water molecules, related by twofold screw symetry, along the a axis. Peptide B molecules surround the column. H atoms not involved in hydrogen bonds have been omitted for clarity. For peptide A molecules, only line drawings of the carboxylate groups are included.

L-Alanyl-L-methionine hemihydrate

Crystal data

C8H16N2O3S·0.5H2O	F(000) = 984
Mr = 229.31	Dx = 1.365 Mg m^−3
Orthorhombic, P212121	Mo Kα radiation, λ = 0.71073 Å
Hall symbol: P 2ac 2ab	Cell parameters from 5401 reflections
a = 5.0809 (2) Å	θ = 1.7–27.1°
b = 17.9228 (9) Å	µ = 0.28 mm^−1
c = 24.5005 (11) Å	T = 105 K
V = 2231.11 (17) Å^3	Needle, colourless
Z = 8	0.58 × 0.05 × 0.03 mm

Data collection

Siemens SMART CCD diffractometer	4661 independent reflections
Radiation source: fine-focus sealed tube	3741 reflections with I > 2σ(I)
Graphite monochromator	Rint = 0.099
Detector resolution: 8.3 pixels mm^-1	θmax = 27.1°, θmin = 1.7°
Sets of exposures each taken over 0.3° ω rotation scans	h = −6→6
Absorption correction: multi-scan SADABS (Sheldrick, 1996)	k = −21→21
Tmin = 0.829, Tmax = 0.992	l = −31→31
13921 measured reflections

Refinement

Refinement on F^2	Secondary atom site location: difference Fourier map
Least-squares matrix: full	Hydrogen site location: inferred from neighbouring sites
R[F^2 > 2σ(F^2)] = 0.040	H atoms treated by a mixture of independent and constrained refinement
wR(F^2) = 0.090	w = 1/[σ^2(Fo^2) + (0.0356P)^2] where P = (Fo^2 + 2Fc^2)/3
S = 0.99	(Δ/σ)max = 0.001
4661 reflections	Δρmax = 0.29 e Å^−3
290 parameters	Δρmin = −0.35 e Å^−3
0 restraints	Absolute structure: Flack (1983)
Primary atom site location: structure-invariant direct methods	Absolute structure parameter: −0.04 (8)

Special details

Refinement. Refinement of F² against ALL reflections.

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

	x	y	z	Uiso*/Ueq
S1A	0.00812 (16)	0.42636 (4)	0.76208 (3)	0.02919 (18)
O1A	−0.2719 (4)	0.69891 (10)	0.65014 (6)	0.0191 (4)
O2A	0.4030 (4)	0.68803 (12)	0.78347 (6)	0.0304 (5)
O3A	0.1017 (4)	0.64020 (9)	0.83967 (6)	0.0250 (4)
N1A	−0.0406 (4)	0.72992 (10)	0.55620 (7)	0.0147 (5)
H1A	−0.015	0.7703	0.5356	0.022*
H2A	−0.209	0.7275	0.5662	0.022*
H3A	0.001	0.6892	0.5371	0.022*
N2A	0.1111 (5)	0.67829 (11)	0.69541 (7)	0.0165 (5)
H4A	0.271	0.67866	0.6934	0.020*
C1A	0.1286 (6)	0.73448 (13)	0.60562 (8)	0.0156 (5)
H11A	0.289	0.7044	0.5999	0.019*
C2A	0.2054 (6)	0.81481 (14)	0.61705 (9)	0.0247 (6)
H21A	0.300	0.8349	0.5859	0.037*
H22A	0.318	0.8167	0.6491	0.037*
H23A	0.048	0.8442	0.6235	0.037*
C3A	−0.0304 (5)	0.70142 (13)	0.65273 (8)	0.0141 (5)
C4A	−0.0143 (6)	0.65213 (13)	0.74612 (8)	0.0181 (5)
H41A	−0.176	0.6856	0.7540	0.022*
C5A	−0.1071 (5)	0.57157 (14)	0.74186 (9)	0.0196 (5)
H51A	−0.232	0.5672	0.7100	0.023*
H52A	−0.208	0.5585	0.7760	0.023*
C6A	0.1149 (6)	0.51502 (14)	0.73445 (10)	0.0223 (6)
H61A	0.270	0.5317	0.7531	0.027*
H62A	0.156	0.5098	0.6965	0.027*
C7A	0.2883 (6)	0.36853 (17)	0.74804 (12)	0.0369 (8)
H71A	0.256	0.3189	0.7612	0.055*
H72A	0.440	0.3886	0.7661	0.055*
H73A	0.319	0.3671	0.7094	0.055*
C8A	0.1842 (6)	0.66180 (15)	0.79313 (9)	0.0210 (6)
S1B	0.59102 (16)	0.59987 (4)	1.08894 (3)	0.03015 (19)
O1B	0.9833 (4)	0.60955 (9)	0.96639 (6)	0.0170 (4)
O2B	0.9721 (4)	0.34854 (9)	1.01264 (6)	0.0167 (4)
O3B	1.3731 (3)	0.39718 (9)	1.00395 (6)	0.0209 (4)
N1B	0.6177 (5)	0.64273 (11)	0.89371 (7)	0.0195 (5)
H1B	0.626	0.6827	0.9175	0.029*
H2B	0.480	0.6497	0.8695	0.029*
H3B	0.774	0.6393	0.8746	0.029*
N2B	0.8080 (4)	0.49850 (11)	0.99211 (7)	0.0144 (4)
H4B	0.680	0.4685	0.9883	0.017*
C1B	0.5739 (5)	0.57253 (13)	0.92526 (9)	0.0160 (5)
H11B	0.421	0.5784	0.9467	0.019*
C2B	0.5298 (6)	0.50791 (13)	0.88594 (9)	0.0223 (6)
H21B	0.390	0.5194	0.8624	0.033*
H22B	0.489	0.4647	0.9058	0.033*
H23B	0.683	0.4999	0.8654	0.033*
C3B	0.8082 (5)	0.56245 (13)	0.96325 (8)	0.0126 (5)
C4B	1.0208 (6)	0.47859 (13)	1.02985 (8)	0.0146 (5)
H41B	1.163	0.5162	1.0269	0.018*
C5B	0.9229 (6)	0.47606 (13)	1.08968 (9)	0.0210 (6)
H51B	0.758	0.4476	1.0910	0.025*
H52B	1.053	0.4492	1.1118	0.025*
C6B	0.8759 (6)	0.55269 (14)	1.11528 (9)	0.0208 (6)
H61B	1.026	0.5830	1.1091	0.025*
H62B	0.856	0.5469	1.1536	0.025*
C7B	0.6229 (7)	0.68536 (15)	1.12659 (10)	0.0375 (8)
H71B	0.478	0.7139	1.1213	0.056*
H72B	0.767	0.7105	1.1149	0.056*
H73B	0.640	0.6749	1.1627	0.056*
C8B	1.1306 (5)	0.40232 (13)	1.01375 (8)	0.0137 (5)
O1W	1.1342 (5)	0.73326 (11)	1.02722 (7)	0.0274 (5)
H1W	1.277 (7)	0.7356 (19)	1.0126 (13)	0.041*
H2W	1.097 (7)	0.6961 (17)	1.0185 (12)	0.041*

Atomic displacement parameters (Ų)

	U^11	U^22	U^33	U^12	U^13	U^23
S1A	0.0327 (4)	0.0212 (4)	0.0337 (3)	−0.0013 (4)	0.0087 (3)	0.0074 (3)
O1A	0.0184 (11)	0.0238 (10)	0.0150 (8)	−0.0002 (9)	0.0003 (7)	0.0033 (7)
O2A	0.0210 (11)	0.0481 (14)	0.0221 (9)	0.0003 (11)	−0.0032 (9)	−0.0079 (8)
O3A	0.0389 (12)	0.0223 (10)	0.0137 (8)	0.0070 (10)	−0.0032 (8)	0.0020 (7)
N1A	0.0192 (13)	0.0126 (10)	0.0123 (8)	−0.0007 (9)	−0.0001 (8)	−0.0002 (7)
N2A	0.0152 (11)	0.0202 (12)	0.0142 (9)	0.0010 (10)	−0.0008 (9)	0.0031 (7)
C1A	0.0180 (14)	0.0157 (14)	0.0132 (11)	0.0012 (12)	−0.0005 (10)	0.0009 (8)
C2A	0.0365 (17)	0.0203 (15)	0.0173 (12)	−0.0084 (13)	−0.0050 (12)	−0.0009 (10)
C3A	0.0185 (15)	0.0121 (12)	0.0116 (10)	0.0001 (12)	0.0008 (10)	−0.0015 (8)
C4A	0.0205 (14)	0.0218 (14)	0.0120 (10)	0.0016 (12)	0.0020 (10)	0.0015 (9)
C5A	0.0223 (14)	0.0222 (14)	0.0142 (10)	−0.0026 (13)	0.0017 (11)	0.0024 (9)
C6A	0.0277 (15)	0.0169 (14)	0.0224 (12)	−0.0025 (13)	0.0020 (12)	0.0026 (9)
C7A	0.0339 (19)	0.0259 (17)	0.0510 (18)	0.0056 (15)	0.0010 (15)	0.0081 (13)
C8A	0.0271 (18)	0.0189 (15)	0.0170 (12)	0.0111 (13)	−0.0029 (11)	−0.0033 (9)
S1B	0.0330 (4)	0.0281 (4)	0.0294 (3)	0.0123 (3)	−0.0062 (3)	−0.0128 (3)
O1B	0.0204 (10)	0.0126 (9)	0.0179 (8)	−0.0042 (9)	−0.0029 (7)	0.0018 (6)
O2B	0.0183 (10)	0.0125 (9)	0.0191 (8)	−0.0020 (8)	0.0015 (7)	−0.0016 (6)
O3B	0.0173 (10)	0.0153 (9)	0.0301 (9)	0.0001 (8)	0.0034 (8)	0.0038 (7)
N1B	0.0313 (13)	0.0108 (11)	0.0163 (9)	0.0038 (11)	−0.0100 (9)	−0.0005 (7)
N2B	0.0170 (11)	0.0113 (11)	0.0150 (9)	−0.0028 (9)	−0.0020 (8)	0.0014 (7)
C1B	0.0196 (14)	0.0122 (13)	0.0161 (10)	0.0007 (11)	−0.0009 (10)	−0.0011 (8)
C2B	0.0330 (17)	0.0135 (13)	0.0203 (11)	−0.0019 (13)	−0.0092 (12)	−0.0002 (9)
C3B	0.0145 (13)	0.0121 (13)	0.0112 (10)	0.0029 (11)	0.0039 (9)	−0.0035 (8)
C4B	0.0193 (14)	0.0088 (12)	0.0158 (11)	−0.0008 (12)	−0.0011 (10)	0.0007 (8)
C5B	0.0334 (17)	0.0154 (13)	0.0143 (10)	0.0059 (12)	−0.0033 (11)	0.0003 (9)
C6B	0.0264 (16)	0.0183 (14)	0.0176 (11)	0.0019 (13)	−0.0019 (11)	−0.0058 (9)
C7B	0.060 (2)	0.0214 (16)	0.0316 (14)	0.0095 (17)	0.0069 (16)	−0.0077 (11)
C8B	0.0186 (14)	0.0158 (13)	0.0067 (9)	−0.0006 (12)	−0.0021 (9)	0.0025 (8)
O1W	0.0311 (13)	0.0187 (11)	0.0324 (10)	−0.0056 (10)	0.0036 (9)	−0.0092 (8)

Geometric parameters (Å, º)

S1A—C7A	1.794 (3)	S1B—C6B	1.796 (3)
S1A—C6A	1.810 (3)	O1B—C3B	1.229 (3)
O1A—C3A	1.229 (3)	O2B—C8B	1.256 (3)
O2A—C8A	1.230 (3)	O3B—C8B	1.259 (3)
O3A—C8A	1.275 (3)	N1B—C1B	1.493 (3)
N1A—C1A	1.487 (3)	N1B—H1B	0.9230
N1A—H1A	0.8920	N1B—H2B	0.9230
N1A—H2A	0.8920	N1B—H3B	0.9230
N1A—H3A	0.8920	N2B—C3B	1.347 (3)
N2A—C3A	1.335 (3)	N2B—C4B	1.467 (3)
N2A—C4A	1.473 (3)	N2B—H4B	0.8501
N2A—H4A	0.8128	C1B—C3B	1.522 (3)
C1A—C2A	1.518 (3)	C1B—C2B	1.523 (3)
C1A—C3A	1.528 (3)	C1B—H11B	0.9427
C1A—H11A	0.9870	C2B—H21B	0.9374
C2A—H21A	0.9699	C2B—H22B	0.9374
C2A—H22A	0.9699	C2B—H23B	0.9374
C2A—H23A	0.9699	C4B—C8B	1.528 (3)
C4A—C5A	1.523 (3)	C4B—C5B	1.549 (3)
C4A—C8A	1.540 (3)	C4B—H41B	0.9884
C4A—H41A	1.0369	C5B—C6B	1.529 (3)
C5A—C6A	1.527 (4)	C5B—H51B	0.9803
C5A—H51A	1.0100	C5B—H52B	0.9803
C5A—H52A	1.0100	C6B—H61B	0.9493
C6A—H61A	0.9569	C6B—H62B	0.9493
C6A—H62A	0.9569	C7B—H71B	0.9072
C7A—H71A	0.9603	C7B—H72B	0.9072
C7A—H72A	0.9603	C7B—H73B	0.9072
C7A—H73A	0.9603	O1W—H1W	0.81 (3)
S1B—C7B	1.796 (3)	O1W—H2W	0.72 (3)
C7A—S1A—C6A	101.40 (14)	C1B—N1B—H1B	109.5
C1A—N1A—H1A	109.5	C1B—N1B—H2B	109.5
C1A—N1A—H2A	109.5	H1B—N1B—H2B	109.5
H1A—N1A—H2A	109.5	C1B—N1B—H3B	109.5
C1A—N1A—H3A	109.5	H1B—N1B—H3B	109.5
H1A—N1A—H3A	109.5	H2B—N1B—H3B	109.5
H2A—N1A—H3A	109.5	C3B—N2B—C4B	122.5 (2)
C3A—N2A—C4A	121.8 (2)	C3B—N2B—H4B	118.7
C3A—N2A—H4A	119.1	C4B—N2B—H4B	118.7
C4A—N2A—H4A	119.1	N1B—C1B—C3B	107.5 (2)
N1A—C1A—C2A	110.56 (19)	N1B—C1B—C2B	109.58 (17)
N1A—C1A—C3A	106.7 (2)	C3B—C1B—C2B	114.3 (2)
C2A—C1A—C3A	111.37 (19)	N1B—C1B—H11B	108.5
N1A—C1A—H11A	109.4	C3B—C1B—H11B	108.5
C2A—C1A—H11A	109.4	C2B—C1B—H11B	108.5
C3A—C1A—H11A	109.4	C1B—C2B—H21B	109.5
C1A—C2A—H21A	109.5	C1B—C2B—H22B	109.5
C1A—C2A—H22A	109.5	H21B—C2B—H22B	109.5
H21A—C2A—H22A	109.5	C1B—C2B—H23B	109.5
C1A—C2A—H23A	109.5	H21B—C2B—H23B	109.5
H21A—C2A—H23A	109.5	H22B—C2B—H23B	109.5
H22A—C2A—H23A	109.5	O1B—C3B—N2B	123.5 (2)
O1A—C3A—N2A	124.5 (2)	O1B—C3B—C1B	121.5 (2)
O1A—C3A—C1A	120.2 (2)	N2B—C3B—C1B	115.0 (2)
N2A—C3A—C1A	115.3 (2)	N2B—C4B—C8B	108.91 (18)
N2A—C4A—C5A	112.21 (18)	N2B—C4B—C5B	111.5 (2)
N2A—C4A—C8A	108.2 (2)	C8B—C4B—C5B	109.60 (18)
C5A—C4A—C8A	111.14 (19)	N2B—C4B—H41B	108.9
N2A—C4A—H41A	108.4	C8B—C4B—H41B	108.9
C5A—C4A—H41A	108.4	C5B—C4B—H41B	108.9
C8A—C4A—H41A	108.4	C6B—C5B—C4B	114.3 (2)
C4A—C5A—C6A	114.1 (2)	C6B—C5B—H51B	108.7
C4A—C5A—H51A	108.7	C4B—C5B—H51B	108.7
C6A—C5A—H51A	108.7	C6B—C5B—H52B	108.7
C4A—C5A—H52A	108.7	C4B—C5B—H52B	108.7
C6A—C5A—H52A	108.7	H51B—C5B—H52B	107.6
H51A—C5A—H52A	107.6	C5B—C6B—S1B	113.66 (19)
C5A—C6A—S1A	108.47 (18)	C5B—C6B—H61B	108.8
C5A—C6A—H61A	110.0	S1B—C6B—H61B	108.8
S1A—C6A—H61A	110.0	C5B—C6B—H62B	108.8
C5A—C6A—H62A	110.0	S1B—C6B—H62B	108.8
S1A—C6A—H62A	110.0	H61B—C6B—H62B	107.7
H61A—C6A—H62A	108.4	S1B—C7B—H71B	109.5
S1A—C7A—H71A	109.5	S1B—C7B—H72B	109.5
S1A—C7A—H72A	109.5	H71B—C7B—H72B	109.5
H71A—C7A—H72A	109.5	S1B—C7B—H73B	109.5
S1A—C7A—H73A	109.5	H71B—C7B—H73B	109.5
H71A—C7A—H73A	109.5	H72B—C7B—H73B	109.5
H72A—C7A—H73A	109.5	O2B—C8B—O3B	124.5 (2)
O2A—C8A—O3A	125.8 (2)	O2B—C8B—C4B	117.3 (2)
O2A—C8A—C4A	119.4 (2)	O3B—C8B—C4B	118.2 (2)
O3A—C8A—C4A	114.8 (2)	H1W—O1W—H2W	99 (4)
C7B—S1B—C6B	98.30 (14)
N1A—C1A—C3A—N2A	159.11 (19)	N1B—C1B—C3B—N2B	−175.58 (19)
C1A—C3A—N2A—C4A	173.8 (2)	C1B—C3B—N2B—C4B	178.65 (19)
C3A—N2A—C4A—C8A	−156.2 (2)	C3B—N2B—C4B—C8B	−124.4 (2)
N2A—C4A—C8A—O2A	0.2 (3)	N2B—C4B—C8B—O2B	−57.8 (2)
N2A—C4A—C5A—C6A	64.5 (3)	N2B—C4B—C5B—C6B	−74.5 (3)
C4A—C5A—C6A—S1A	152.83 (15)	C4B—C5B—C6B—S1B	71.8 (3)
C5A—C6A—S1A—C7A	178.66 (17)	C5B—C6B—S1B—C7B	−177.3 (2)
C4A—N2A—C3A—O1A	−4.7 (4)	C4B—N2B—C3B—O1B	−0.8 (3)
N1A—C1A—C3A—O1A	−22.4 (3)	N1B—C1B—C3B—O1B	3.8 (3)
C2A—C1A—C3A—O1A	98.4 (3)	C2B—C1B—C3B—O1B	125.7 (2)
C2A—C1A—C3A—N2A	−80.1 (3)	C2B—C1B—C3B—N2B	−53.7 (3)
C3A—N2A—C4A—C5A	80.9 (3)	C3B—N2B—C4B—C5B	114.5 (2)
C8A—C4A—C5A—C6A	−56.7 (3)	C8B—C4B—C5B—C6B	164.8 (2)
C5A—C4A—C8A—O2A	123.8 (3)	C5B—C4B—C8B—O2B	64.4 (3)
N2A—C4A—C8A—O3A	−179.1 (2)	N2B—C4B—C8B—O3B	124.0 (2)
C5A—C4A—C8A—O3A	−55.5 (3)	C5B—C4B—C8B—O3B	−113.7 (2)

Hydrogen-bond geometry (Å, º)

D—H···A	D—H	H···A	D···A	D—H···A
N1A—H1A···O2B^i	0.89	1.85	2.736 (2)	175
N1A—H2A···O2B^ii	0.89	2.32	2.815 (3)	115
N1A—H3A···O3B^iii	0.89	1.86	2.748 (2)	172
N2A—H4A···O1A^iv	0.81	2.58	3.346 (3)	158
C1A—H11A···O1A^iv	0.99	2.55	3.300 (3)	132
C4A—H41A···O2A^v	1.04	2.26	3.165 (4)	145
N1B—H1B···O1W^vi	0.92	2.03	2.950 (3)	177
N1B—H2B···O3A	0.92	2.07	2.937 (3)	157
N1B—H2B···O2A	0.92	2.25	3.024 (2)	141
N1B—H3B···O3A^iv	0.92	1.87	2.793 (3)	175
N2B—H4B···O3B^v	0.85	2.05	2.875 (3)	163
C1B—H11B···O1B^v	0.94	2.34	3.234 (3)	157
C4B—H41B···S1B^iv	0.99	3.05	3.901 (3)	145
O1W—H1W···O1W^vii	0.81 (3)	2.14 (3)	2.931 (2)	167 (3)
O1W—H2W···O1B	0.72 (3)	2.09 (3)	2.779 (3)	159 (3)

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