Conformation and structure of bis­(glycyl-L-aspartic acid) oxalate 0.4-hydrate

The title bis­(glycyl-L-aspartic acid) oxalate complex {systematic name: bis­[2-(2-ammonio­acetamido)butane­dioic acid] oxalate 0.4-hydrate}, 2C₆H₁₁N₂O₅⁺·C₂O₄²⁻·4H₂O, crystallizes in a triclinic space group with the planar peptide unit in a trans conformation. The asymmetric unit consists of two glycyl-L-aspartic acid mol­ecules with positively charged amino groups and neutral carboxyl groups, and an oxalate dianion. The twist around the C—Cα bond indicates that both the peptide mol­ecules adopt extended conformations, while the twist around the N—Cα bond shows that one has a folded and the other a semi-extended state. The present complex can be described as an inclusion compound with the dipeptide mol­ecule as the host and the oxalate anion as the guest. The usual head-to-tail sequence of aggregation is not observed in this complex, as is also the case with the glycyl-L-aspartic acid dihydrate mol­ecule. The study of aggregation and inter­action patterns in binary systems is the first step towards understanding more complex phenomena. This further leads to results that are of general interest in bimolecular aggregation.

S1. Comment

X-ray analysis of complexes of amino acids and peptides among themselves as well as with relevant molecules helps in understanding the geometrical features of elementary patterns of these complexes (Vijayan, 1988). The aggregation pattern of biological molecules largely depends on the non-covalent interactions. In these complexes there is always an extensive network of hydrogen bonds. The aggregation pattern can divulge information relating to chemical evolution and the origin of life. In addition, structural and conformational studies of peptides that contain acidic residues have shown that these compounds are implicated in the binding of calcium and similar metals to proteins (Wasserman et al., 1977). It has been observed that these residues are involved in the complexation of calcium in all calcium proteins of known structure (Kretsinger & Nelson, 1976). Most of the calcium-specific site sequences contain glycine adjacent to one or more of the coordinating acid peptide residues (Potter et al., 1977). The acidic side chain of these peptides offers unique possibilities of hydrogen bonding, which may result in unusual conformational properties. The crystal structure of the peptide glycyl-L-aspartic acid has been determined using single-crystal X-ray diffraction (Eggleston & Hodgson, 1982: Pichon-Pesme et al., 2000). Oxalic acid is the simplest dicarboxylic acid and it can, in principle, exist in three ionization states, viz. singly charged (semi-oxalate), doubly charged (oxalate) and neutral (oxalic acid). Oxalic acid has also been complexed with the peptides glycyl glycine (Ejsmont et al., 2003), glycyl-L-histidine and L-histidyl-L-alanine (Manoj & Vijayan, 2000). We present here the crystal structure of a bis(glycyl-L-aspartic acid) oxalate complex, (I), solved using single-crystal X-ray diffraction. Using the Cambridge Structural Database (CSD; update 5.26 of November 2004; Allen, 2002) an analysis of geometry in the salts of the peptide and oxalic acid has been carried out.

A displacement ellipsoid representation of the complex is given in Fig. 1. The asymmetric unit consists of two glycyl-L-aspartic acid molecules with positively charged amino groups and neutral carboxyl groups, and an oxalate ion, which is doubly negatively charged. A comparison of the bond parameters of the peptide unit in the complex and in the pure structure showed that only the bond parameters involving the main chain COOH group differ, as a result of the zwitterionic nature of the pure glycyl-L-aspartic acid. The peptide plane is defined by atoms C1, C2, O1, N2 and H6 for the first molecule and C7, C8, O6, N4 and H17 for the second molecule of peptide. The maximum deviations from the least-squares plane through these atoms occur for C3 [−0.023 (3) Å] and C7 [0.022 (4) Å].

The torsion angles of the two molecules of (I) and that of glycyl-L-aspartic acid are compared in Table 3. The planarity of the peptide unit is defined by the torsion angle ω, which characterizes the rotation around the C—N peptide bond. An ω value of 180° corresponds to a planar peptide unit (trans conformation). In the present complex the deviation of ω (C1—C2—N2—C3 and C7—C8—N4—C9) for both the peptide residues is about 3°, and hence they adopt trans conformations. The full conformation of a peptide chain is described by two additional torsion angles, ψ and ϕ, which characterize the twist around the C—Cα and N—Cα bonds, respectively (Suresh & Vijayan, 1985; Vijayan, 1988). The ψ angle around C—C^α is also extended in the present structure, which is also true for pure glycyl-L-aspartic acid molecule. As a rough guide, the confirmation may be considered as extended if the magnitude of ϕ is between 60 and 180°; otherwise it may be considered folded. According to this guide, one of the peptide molecules (molecule 2) is in a folded state and the other (molecule 1) is in a semi-extended state in the complex, unlike the molecule of pure glycyl-L-aspartic acid, which is extended, having a value of −133.3°. The aspartic acid residue has ψ1 of around 60° with the side chain trans to the carboxyl group in both the peptide molecules, unlike the case in pure glycyl-L-aspartic acid, which has a side chain having a cis conformation to the carboxyl group.

Comparison of the oxalate bond parameters for the three above-mentioned peptide–oxalate complexes shows that in all cases, with the exception of glycyl-L-histidine oxalate, the oxalate unit exists as doubly ionized oxalate anion. The stochiometery in the case of the present complex and bis(glycyl glycinium) oxalate is 2:1. The other two have 1:1 stochiometery. In all the complexes the oxalate ion is essentially planar, the O—C—C—O torsion angle having deviation of around 6° from planarity. Table 2 gives the hydrogen-bonding parameters in the present complex. The peptide molecule has a number of potential H-atom donors and acceptors in the structures. As observed previously (Eggleston & Hodgson, 1982) and in the present complex, intramolecular hydrogen bonding is absent. An arrangement in which the terminal amino group and the carboxylate group are brought into periodic hydrogen-bonded proximity is called a head-to-tail sequence. In the present complex, the terminal amine groups (i.e. N3/H12 and N1/H3) are hydrogen bonded to atoms O4 and O9 respectively, which are the main-chain alpha carboxyl O atoms. However, the arrangement is not the usual head-to-tail arrangement. Rather the two molecules are related by a pseudo-inversion center. It is also seen that the amine N atoms of each peptide molecule (N3—H14 and N1—H1) are hydrogen bonded to atoms O3 and O8, respectively, which are the side-chain carboxyl O atoms. Amine atoms H2 and H13 also form bifurcated hydrogen bonds to the oxalate O atoms (O13/O12 and O14/O11, respectively). The O-bound H atoms of the carboxyl groups of the main chain and the side chain act as hydrogen-bond donors to the oxalate O atom. Each oxalate O atom, in turn, acts as an acceptor of two hydrogen bonds (one to the amino N atom and the other to the OH group of the carboxyl group). Another interesting observation is that the peptide N atom forms a hydrogen bond to the peptide carbonyl (i.e. N2—H6···O1ⁱⁱⁱ and N4—H17···O6ⁱ; Table 2) of the same molecule but in different asymmetric unit resulting in an S5–4 (Vijayan, 1988) sequence. Adjacent molecules are parallel. A hydrogen bond between the peptide N atom and the peptide carbonyl group is also observed in the pure glycyl-L-aspartic acid, bis(glycyl-L-histidine) oxalate and glycyl-L-histidine–oxalic acid complexes, but the same is not true for the L-histidyl-L-alanine complex. Hence it can be said that this might be due to the fact that the glycyl residue occupying the amine terminal position does not cause steric hindrance to allow this type of hydrogen bond to be formed in these kind of complexes. Of course, a systematic study of complexes of oxalic acid with peptides involving a glycyl residue at the amine terminal position is required to prove this point. In terms of graph-set notation (Bernstein et al., 1995), the largest motif has the first-level graph set N1 = DDD, the binary level being R²₄ (22). The next level graph set is N1 = DD, the binary level being R²₁ (5) and C4. The dipeptide and oxalate molecules are arranged parallel to the ab plane. Fig. 2 shows the packing as viewed down the crystallographic a axis. It is observed that the dipeptide molecules are stacked in such a way that the oxalate molecules are enclosed in the voids created during stacking. The present complex can be described as an inclusion compound with the dipeptide molecule as the host and the oxalate as the guest.

S2. Experimental

Crystals of bis(glycyl-L-aspartic acid) oxalate were grown by slow evaporation from a saturated aqueous solution containing stoichiometric quantities of glycyl-L-aspartic acid and oxalic acid.

S3. Refinement

All H atoms were fixed using geometrical constraints and were considered as riding on the atoms to which they are attached, with C—H, N—H and O—H distances of 0.97–0.98, 0.86–0.89 and 0.82 Å, respectively. At this stage, the maximum difference density of 0.60 e Å⁻³ indicated the presence of a possible atom site. In addition, a check for solvent-accessible volume using PLATON (Spek, 2003) showed a void of 128 ų. An attempt to refine this peak as a water atom with full occupancy resulted in a high U_iso value. An alternative strategy, the SQUEEZE function of PLATON (van der Sluis & Spek, 1990: Spek, 2003) was used to eliminate the contribution of the electron density in the solvent region form the intensity data. PLATON total Potential Solvent Area Vol 29.4 ų [please clarify meaning of this] estimated that the cavity contained four electrons, which is equivalent to one partially occupied solvent water molecule. The PLATON suite was used to generate the reflection file and the refinement was carried out using this file.

Computing details

Data collection: SMART (Bruker, 2004); cell refinement: SAINT (Bruker, 2004); data reduction: SAINT; program(s) used to solve structure: SHELXS97 (Sheldrick, 1997); program(s) used to refine structure: SHELXL97 (Sheldrick, 1997); molecular graphics: ORTEP-3 (Farrugia, 1997); software used to prepare material for publication: SHELXL97.

Figures

	Fig. 1. An ellipsoid plot of bis(glycyl-L-aspartic acid) oxalate with the atom-numbering scheme and 50% probability displacement ellipsoids.
	Fig. 2. Packing diagram for the title salt viewed down the a axis.

bis[2-(2-ammonioacetamido)butanedioic acid] oxalate 0.4-hydrate

Crystal data

2C6H11N2O5^+·C2O4^2^−·0.4H2O	Z = 1
Mr = 477.56	F(000) = 246
Triclinic, P1	Dx = 1.519 Mg m^−3
Hall symbol: P 1	Mo Kα radiation, λ = 0.71073 Å
a = 4.8100 (8) Å	Cell parameters from 2081 reflections
b = 10.7760 (18) Å	θ = 2.0–26.4°
c = 10.8756 (18) Å	µ = 0.14 mm^−1
α = 69.325 (3)°	T = 300 K
β = 85.792 (3)°	Irregular, colourless
γ = 81.946 (3)°	0.24 × 0.19 × 0.13 mm
V = 522.03 (15) Å^3

Data collection

Bruker SMART CCD area-detector diffractometer	1732 reflections with I > 2σ(I)
Radiation source: fine-focus sealed tube	Rint = 0.028
Graphite monochromator	θmax = 26.4°, θmin = 2.0°
ϕ and ω scans	h = −6→5
5499 measured reflections	k = −13→13
2081 independent reflections	l = −13→13

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)] = 0.059	Hydrogen site location: constr
wR(F^2) = 0.133	H-atom parameters constrained
S = 1.11	w = 1/[σ^2(Fo^2) + (0.0749P)^2] where P = (Fo^2 + 2Fc^2)/3
2081 reflections	(Δ/σ)max < 0.001
297 parameters	Δρmax = 0.28 e Å^−3
3 restraints	Δρmin = −0.19 e Å^−3

Special details

Geometry. Bond distances, angles etc. have been calculated using the rounded fractional coordinates. All e.s.d.'s are estimated from the variances of the (full) variance-covariance matrix. The cell e.s.d.'s are taken into account in the estimation of distances, angles and torsion angles

Refinement. Refinement of F² against ALL reflections. The weighted R-factor wR and goodness of fit S are based on F², conventional R-factors R are based on F, with F set to zero for negative F². The threshold expression of F² > σ(F²) is used only for calculating R-factors(gt) etc. and is not relevant to the choice of reflections for refinement. R-factors based on F² are statistically about twice as large as those based on F, and R- factors based on ALL data will be even larger.

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

	x	y	z	Uiso*/Ueq
O4	0.0104 (7)	0.4777 (4)	0.3705 (4)	0.0488 (14)
O8	0.3237 (9)	0.3465 (4)	0.1545 (4)	0.0510 (16)
O9	0.1254 (8)	0.5107 (3)	−0.0168 (3)	0.0446 (14)
O12	0.3319 (10)	0.8424 (4)	0.1311 (5)	0.0655 (16)
O13	0.7000 (9)	0.8660 (4)	−0.0103 (4)	0.0596 (16)
N1	0.2079 (9)	0.3927 (4)	0.6125 (4)	0.0378 (12)
N5	0.4292 (8)	0.5234 (4)	0.2696 (4)	0.0316 (14)
C2	0.4128 (12)	0.4195 (6)	0.5026 (5)	0.0431 (19)
C3	0.2647 (10)	0.4768 (5)	0.3739 (5)	0.0299 (17)
C6	0.3133 (10)	0.5768 (4)	0.1387 (4)	0.0268 (16)
C7	0.2577 (10)	0.4624 (5)	0.0941 (5)	0.0297 (17)
C10	0.4976 (11)	0.6692 (5)	0.0415 (5)	0.0343 (16)
C11	0.4956 (12)	0.8009 (5)	0.0618 (5)	0.0389 (17)
O17	1.2525 (8)	1.0291 (5)	0.4262 (4)	0.0607 (14)
O21	0.9577 (10)	1.1712 (4)	0.6203 (5)	0.0697 (18)
O22	1.2008 (8)	1.0048 (4)	0.7744 (4)	0.0521 (16)
O25	1.0426 (12)	0.6538 (5)	0.5892 (5)	0.083 (2)
O26	0.7376 (8)	0.6641 (4)	0.7483 (4)	0.0462 (12)
N14	1.0929 (9)	1.1014 (4)	0.1719 (4)	0.0385 (16)
N18	0.8189 (8)	0.9927 (4)	0.5108 (4)	0.0334 (14)
C15	0.8765 (13)	1.0801 (8)	0.2765 (6)	0.056 (2)
C16	1.0034 (11)	1.0304 (6)	0.4127 (5)	0.0421 (17)
C19	0.8926 (10)	0.9466 (5)	0.6496 (5)	0.0345 (17)
C20	1.0259 (11)	1.0540 (5)	0.6792 (6)	0.0389 (17)
C23	1.0769 (11)	0.8122 (5)	0.6907 (6)	0.0427 (17)
C24	0.9524 (12)	0.7022 (5)	0.6697 (5)	0.0407 (18)
O27	0.9036 (9)	0.3279 (4)	0.9456 (4)	0.0545 (16)
O28	0.6271 (8)	0.4250 (4)	0.7740 (4)	0.0453 (14)
O29	0.4371 (9)	0.1874 (4)	0.8223 (4)	0.0577 (14)
O30	0.6904 (10)	0.1015 (4)	0.9994 (4)	0.0590 (16)
C27	0.7228 (11)	0.3286 (5)	0.8712 (5)	0.0337 (16)
C28	0.6043 (10)	0.1932 (5)	0.9011 (5)	0.0320 (17)
H1A	0.09197	0.33874	0.60422	0.0561*
H1B	0.29750	0.35372	0.68790	0.0561*
H1C	0.10981	0.46920	0.61220	0.0561*
H2A	0.53017	0.33727	0.50696	0.0514*
H2B	0.53291	0.48216	0.50888	0.0514*
H5	0.60558	0.52221	0.27902	0.0381*
H6	0.13203	0.62915	0.14414	0.0319*
H9	0.07579	0.44930	−0.03446	0.0668*
H10A	0.43572	0.68651	−0.04660	0.0411*
H10B	0.68876	0.62497	0.04792	0.0411*
H13	0.69884	0.93695	0.00181	0.0897*
H14A	1.20442	1.15745	0.17949	0.0578*
H14B	1.01185	1.13594	0.09411	0.0578*
H14C	1.19416	1.02365	0.17852	0.0578*
H15A	0.76179	1.01519	0.27090	0.0676*
H15B	0.75576	1.16336	0.26421	0.0676*
H18	0.64690	0.99544	0.49228	0.0401*
H19	0.71716	0.93370	0.70172	0.0417*
H22	1.25466	1.06578	0.79121	0.0780*
H23A	1.25417	0.82330	0.64180	0.0514*
H23B	1.11704	0.78580	0.78316	0.0514*
H26	0.72258	0.58622	0.75844	0.0689*

Atomic displacement parameters (Ų)

	U^11	U^22	U^33	U^12	U^13	U^23
O4	0.027 (2)	0.075 (3)	0.039 (2)	−0.0149 (19)	−0.0008 (17)	−0.010 (2)
O8	0.064 (3)	0.032 (2)	0.057 (3)	−0.0070 (19)	−0.025 (2)	−0.0103 (19)
O9	0.067 (3)	0.0296 (19)	0.041 (2)	−0.0147 (18)	−0.0257 (19)	−0.0088 (17)
O12	0.082 (3)	0.044 (2)	0.083 (3)	−0.024 (2)	0.022 (3)	−0.036 (2)
O13	0.071 (3)	0.044 (2)	0.071 (3)	−0.034 (2)	0.004 (2)	−0.020 (2)
N1	0.043 (2)	0.037 (2)	0.036 (2)	−0.0133 (19)	−0.005 (2)	−0.012 (2)
N5	0.019 (2)	0.046 (3)	0.033 (2)	−0.0090 (18)	−0.0089 (18)	−0.014 (2)
C2	0.036 (3)	0.059 (4)	0.030 (3)	−0.009 (3)	−0.005 (2)	−0.008 (3)
C3	0.026 (3)	0.031 (3)	0.031 (3)	−0.006 (2)	−0.005 (2)	−0.007 (2)
C6	0.028 (3)	0.023 (2)	0.029 (3)	−0.0042 (19)	−0.0081 (19)	−0.0066 (19)
C7	0.031 (3)	0.025 (3)	0.035 (3)	−0.013 (2)	−0.001 (2)	−0.009 (2)
C10	0.042 (3)	0.032 (3)	0.029 (2)	−0.010 (2)	−0.010 (2)	−0.007 (2)
C11	0.052 (3)	0.030 (3)	0.035 (3)	−0.014 (2)	−0.018 (3)	−0.005 (2)
O17	0.031 (2)	0.092 (3)	0.043 (2)	−0.027 (2)	−0.0127 (18)	0.006 (2)
O21	0.087 (3)	0.028 (2)	0.096 (4)	−0.008 (2)	−0.046 (3)	−0.015 (2)
O22	0.059 (3)	0.040 (2)	0.065 (3)	−0.0190 (19)	−0.026 (2)	−0.018 (2)
O25	0.131 (5)	0.050 (3)	0.079 (3)	−0.036 (3)	0.045 (3)	−0.035 (3)
O26	0.055 (2)	0.038 (2)	0.055 (2)	−0.0221 (19)	0.001 (2)	−0.0221 (19)
N14	0.044 (3)	0.033 (2)	0.037 (3)	−0.0081 (19)	−0.016 (2)	−0.006 (2)
N18	0.023 (2)	0.036 (2)	0.036 (3)	−0.0096 (17)	−0.0092 (19)	−0.0023 (19)
C15	0.037 (3)	0.078 (4)	0.046 (4)	−0.017 (3)	−0.011 (3)	−0.007 (3)
C16	0.033 (3)	0.049 (3)	0.041 (3)	−0.014 (2)	−0.012 (3)	−0.006 (3)
C19	0.024 (3)	0.035 (3)	0.050 (3)	−0.009 (2)	−0.008 (2)	−0.018 (2)
C20	0.034 (3)	0.041 (3)	0.051 (3)	−0.010 (2)	−0.009 (2)	−0.024 (3)
C23	0.040 (3)	0.035 (3)	0.054 (3)	−0.011 (2)	−0.013 (2)	−0.012 (2)
C24	0.063 (4)	0.016 (2)	0.040 (3)	−0.004 (2)	0.002 (3)	−0.007 (2)
O27	0.072 (3)	0.036 (2)	0.061 (3)	−0.025 (2)	−0.037 (2)	−0.010 (2)
O28	0.065 (3)	0.035 (2)	0.038 (2)	−0.0283 (19)	−0.0119 (19)	−0.0047 (19)
O29	0.081 (3)	0.041 (2)	0.054 (2)	−0.034 (2)	−0.028 (2)	−0.005 (2)
O30	0.087 (3)	0.031 (2)	0.056 (3)	−0.027 (2)	−0.037 (2)	0.003 (2)
C27	0.043 (3)	0.027 (2)	0.036 (3)	−0.014 (2)	0.003 (2)	−0.014 (2)
C28	0.041 (3)	0.034 (3)	0.029 (3)	−0.021 (2)	−0.009 (2)	−0.013 (2)

Geometric parameters (Å, º)

O4—C3	1.225 (6)	N18—C19	1.467 (7)
O8—C7	1.197 (7)	N18—C16	1.322 (7)
O9—C7	1.307 (6)	N14—H14A	0.8899
O12—C11	1.200 (7)	N14—H14C	0.8903
O13—C11	1.329 (7)	N14—H14B	0.8897
O9—H9	0.8199	N18—H18	0.8598
O13—H13	0.8196	C2—C3	1.504 (7)
O17—C16	1.215 (7)	C6—C10	1.504 (7)
O21—C20	1.207 (8)	C6—C7	1.536 (7)
O22—C20	1.295 (7)	C10—C11	1.510 (8)
O25—C24	1.196 (8)	C2—H2A	0.9697
O26—C24	1.307 (7)	C2—H2B	0.9706
O22—H22	0.8197	C6—H6	0.9799
O26—H26	0.8199	C10—H10A	0.9703
O27—C27	1.228 (7)	C10—H10B	0.9698
O28—C27	1.253 (7)	C15—C16	1.528 (8)
O29—C28	1.240 (7)	C19—C23	1.525 (8)
O30—C28	1.223 (7)	C19—C20	1.535 (8)
N1—C2	1.465 (7)	C23—C24	1.492 (8)
N5—C6	1.455 (6)	C15—H15A	0.9698
N5—C3	1.320 (6)	C15—H15B	0.9700
N1—H1C	0.8897	C19—H19	0.9797
N1—H1A	0.8901	C23—H23A	0.9702
N1—H1B	0.8902	C23—H23B	0.9698
N5—H5	0.8598	C27—C28	1.559 (8)
N14—C15	1.463 (8)
O4···N1	2.663 (6)	N14···O30^iv	2.793 (6)
O4···N5^i	2.991 (5)	N14···O8^vi	2.947 (6)
O4···C2^i	3.160 (7)	N14···O12^v	3.035 (7)
O4···C7	3.201 (7)	N14···O17	2.733 (6)
O8···N14^ii	2.947 (6)	N14···O27^iv	2.882 (6)
O8···C3	3.146 (7)	N18···O21	2.767 (6)
O8···O27^iii	3.224 (6)	N18···O17^i	2.870 (6)
O8···N5	2.740 (6)	C2···O28	3.220 (7)
O9···O26^iii	3.097 (5)	C2···O4^v	3.160 (7)
O9···O27^iii	2.531 (6)	C2···O25^i	3.257 (9)
O9···C24^iii	3.397 (6)	C3···O8	3.146 (7)
O9···C10^i	3.388 (7)	C7···O4	3.201 (7)
O12···N5	3.210 (7)	C7···O27^iii	3.218 (7)
O12···N14^i	3.035 (7)	C10···O9^v	3.388 (7)
O13···C28^iv	3.284 (7)	C10···O26^xii	3.327 (7)
O13···O30^iv	2.571 (6)	C11···O22^iii	3.396 (7)
O17···C23	3.146 (7)	C11···O30^iv	3.322 (7)
O17···N14	2.733 (6)	C15···O17^i	3.328 (7)
O17···C15^v	3.328 (7)	C15···O30^iv	3.128 (8)
O17···O21	3.170 (7)	C16···O21	3.115 (8)
O17···C20	2.972 (7)	C20···O17	2.972 (7)
O17···N18^v	2.870 (6)	C20···O29^vi	3.351 (7)
O21···N18	2.767 (6)	C23···O26^v	3.347 (7)
O21···C16	3.115 (8)	C23···O17	3.146 (7)
O21···N1^vi	2.793 (7)	C24···O28	3.364 (7)
O21···O17	3.170 (7)	C24···O9^viii	3.397 (6)
O21···O29^vii	3.235 (7)	C27···O26	3.392 (7)
O22···C11^viii	3.396 (7)	C28···O13^x	3.284 (7)
O22···O29^vi	2.622 (6)	C7···H10B^i	3.0079
O25···N1^v	2.741 (7)	C11···H5	3.0997
O25···C2^v	3.257 (9)	C16···H23A	2.8989
O26···C23^i	3.347 (7)	C20···H1A^vi	2.9409
O26···C10^ix	3.327 (7)	C24···H1C^v	2.7884
O26···C27	3.392 (7)	C27···H9^viii	2.7284
O26···O28	2.618 (6)	C27···H14B^x	2.8727
O26···O9^viii	3.097 (5)	C27···H1B	2.8800
O27···N14^x	2.882 (6)	C27···H26	2.6088
O27···O8^viii	3.224 (6)	C28···H13^x	2.5724
O27···O30	2.636 (6)	C28···H1B	2.7388
O27···C7^viii	3.218 (7)	C28···H22^ii	2.8710
O27···O9^viii	2.531 (6)	C28···H14B^x	2.8249
O28···C2	3.220 (7)	H1A···O29	2.8511
O28···N1	2.902 (6)	H1A···O21^ii	1.9479
O28···N1^v	3.233 (6)	H1A···C20^ii	2.9409
O28···O26	2.618 (6)	H1A···O4	2.4802
O28···O29	2.702 (6)	H1B···C27	2.8800
O28···C24	3.364 (7)	H1B···C28	2.7388
O29···N1	2.727 (6)	H1B···O29	1.9382
O29···O28	2.702 (6)	H1B···O28	2.2466
O29···O21^xi	3.235 (7)	H1C···C24^i	2.7884
O29···O22^ii	2.622 (6)	H1C···O25^i	1.8986
O29···C20^ii	3.351 (7)	H1C···O28^i	2.7987
O30···O13^x	2.571 (6)	H1C···O4	2.6737
O30···N14^x	2.793 (6)	H2A···O21^xi	2.5950
O30···O27	2.636 (6)	H2B···O28	2.7853
O30···C11^x	3.322 (7)	H2B···O4^v	2.6561
O30···C15^x	3.128 (8)	H2B···H5	2.3896
O4···H6	2.5071	H5···H2B	2.3896
O4···H1A	2.4802	H5···C11	3.0997
O4···H1C	2.6737	H5···H10B	2.3905
O4···H2B^i	2.6561	H5···O4^v	2.1673
O4···H5^i	2.1673	H6···H10B^i	2.4557
O8···H14A^ii	2.1135	H6···O12	2.5679
O8···H15B^xi	2.6813	H6···O4	2.5071
O9···H10B^i	2.4684	H9···O27^iii	1.7247
O9···H10A	2.4920	H9···C27^iii	2.7284
O12···H14C^i	2.1950	H10A···H23B^iii	2.3410
O12···H6	2.5679	H10A···O9	2.4920
O17···H23A	2.5966	H10A···O26^xii	2.6361
O17···H15A^v	2.8887	H10B···H6^v	2.4557
O17···H18^v	2.0174	H10B···H5	2.3905
O17···H14A	2.5586	H10B···O9^v	2.4684
O17···H14C	2.7505	H10B···C7^v	3.0079
O21···H2A^vii	2.5950	H13···C28^iv	2.5724
O21···H1A^vi	1.9479	H13···O30^iv	1.7589
O22···H19^v	2.6433	H13···O29^iv	2.8928
O22···H23A	2.7870	H14A···O8^vi	2.1135
O22···H23B	2.4172	H14A···O27^iv	2.9041
O25···H1C^v	1.8986	H14A···O17	2.5586
O26···H10A^ix	2.6361	H14B···O30^iv	2.0625
O26···H23A^i	2.7506	H14B···O27^iv	2.1497
O26···H19	2.7558	H14B···C28^iv	2.8249
O27···H14A^x	2.9041	H14B···C27^iv	2.8727
O27···H14B^x	2.1497	H14C···O12^v	2.1950
O27···H26	2.8688	H14C···O17	2.7505
O27···H9^viii	1.7247	H15A···H18	2.3713
O28···H26	1.8062	H15A···O30^iv	2.7967
O28···H1B	2.2466	H15A···O17^i	2.8887
O28···H2B	2.7853	H15B···O8^vii	2.6813
O28···H1C^v	2.7987	H15B···H18	2.5703
O29···H1B	1.9382	H18···O17^i	2.0174
O29···H13^x	2.8928	H18···H15A	2.3713
O29···H1A	2.8511	H18···H15B	2.5703
O29···H22^ii	1.8113	H19···O22^i	2.6433
O30···H15A^x	2.7967	H19···O26	2.7558
O30···H14B^x	2.0625	H22···O29^vi	1.8113
O30···H13^x	1.7589	H22···C28^vi	2.8710
N1···O21^ii	2.793 (7)	H23A···O17	2.5966
N1···O4	2.663 (6)	H23A···O22	2.7870
N1···O25^i	2.741 (7)	H23A···O26^v	2.7506
N1···O28^i	3.233 (6)	H23A···C16	2.8989
N1···O28	2.902 (6)	H23B···O22	2.4172
N1···O29	2.727 (6)	H23B···H10A^viii	2.3410
N5···O4^v	2.991 (5)	H26···O27	2.8688
N5···O8	2.740 (6)	H26···O28	1.8062
N5···O12	3.210 (7)	H26···C27	2.6088
C7—O9—H9	109.48	C7—C6—H6	107.55
C11—O13—H13	109.48	N5—C6—H6	107.52
C20—O22—H22	109.49	C10—C6—H6	107.52
C24—O26—H26	109.46	C6—C10—H10B	108.86
C3—N5—C6	120.3 (4)	C11—C10—H10A	108.84
C2—N1—H1A	109.44	C11—C10—H10B	108.87
C2—N1—H1B	109.48	H10A—C10—H10B	107.69
C2—N1—H1C	109.51	C6—C10—H10A	108.82
H1A—N1—H1B	109.43	N14—C15—C16	111.9 (5)
H1A—N1—H1C	109.49	O17—C16—C15	121.4 (5)
H1B—N1—H1C	109.48	O17—C16—N18	124.5 (5)
C3—N5—H5	119.89	N18—C16—C15	114.1 (5)
C6—N5—H5	119.84	N18—C19—C23	111.9 (4)
C16—N18—C19	123.3 (4)	N18—C19—C20	110.6 (4)
C15—N14—H14C	109.44	C20—C19—C23	112.4 (4)
H14B—N14—H14C	109.47	O22—C20—C19	113.1 (5)
H14A—N14—H14B	109.51	O21—C20—C19	120.8 (5)
C15—N14—H14B	109.47	O21—C20—O22	126.0 (6)
C15—N14—H14A	109.48	C19—C23—C24	114.8 (5)
H14A—N14—H14C	109.46	O25—C24—O26	123.8 (6)
C19—N18—H18	118.35	O25—C24—C23	122.9 (6)
C16—N18—H18	118.32	O26—C24—C23	113.3 (5)
N1—C2—C3	110.3 (4)	N14—C15—H15A	109.26
N5—C3—C2	114.9 (4)	N14—C15—H15B	109.23
O4—C3—C2	120.6 (5)	C16—C15—H15A	109.22
O4—C3—N5	124.5 (5)	C16—C15—H15B	109.20
N5—C6—C7	110.3 (4)	H15A—C15—H15B	107.94
C7—C6—C10	111.9 (4)	N18—C19—H19	107.21
N5—C6—C10	111.8 (4)	C20—C19—H19	107.26
O9—C7—C6	110.0 (4)	C23—C19—H19	107.21
O8—C7—O9	125.9 (5)	C19—C23—H23A	108.57
O8—C7—C6	124.1 (5)	C19—C23—H23B	108.57
C6—C10—C11	113.6 (4)	C24—C23—H23A	108.55
O12—C11—C10	125.4 (5)	C24—C23—H23B	108.60
O13—C11—C10	110.0 (5)	H23A—C23—H23B	107.55
O12—C11—O13	124.6 (5)	O27—C27—O28	127.3 (5)
N1—C2—H2A	109.62	O27—C27—C28	115.7 (5)
C3—C2—H2B	109.59	O28—C27—C28	117.1 (5)
N1—C2—H2B	109.54	O29—C28—O30	126.1 (5)
C3—C2—H2A	109.66	O29—C28—C27	117.4 (5)
H2A—C2—H2B	108.11	O30—C28—C27	116.4 (5)
C6—N5—C3—C2	177.6 (5)	C6—C10—C11—O13	168.3 (4)
C3—N5—C6—C10	158.4 (5)	C6—C10—C11—O12	−12.7 (8)
C3—N5—C6—C7	−76.3 (6)	N14—C15—C16—O17	9.8 (10)
C6—N5—C3—O4	−2.1 (8)	N14—C15—C16—N18	−171.4 (6)
C19—N18—C16—C15	−177.5 (6)	N18—C19—C20—O22	−151.3 (5)
C19—N18—C16—O17	1.2 (10)	C23—C19—C20—O21	157.5 (5)
C16—N18—C19—C20	57.7 (7)	N18—C19—C20—O21	31.6 (7)
C16—N18—C19—C23	−68.4 (7)	N18—C19—C23—C24	−57.5 (6)
N1—C2—C3—O4	−10.2 (8)	C23—C19—C20—O22	−25.4 (7)
N1—C2—C3—N5	170.1 (5)	C20—C19—C23—C24	177.4 (5)
C10—C6—C7—O9	−61.8 (5)	C19—C23—C24—O25	111.2 (7)
C10—C6—C7—O8	119.2 (6)	C19—C23—C24—O26	−69.2 (6)
N5—C6—C7—O8	−5.9 (7)	O27—C27—C28—O29	−174.7 (5)
C7—C6—C10—C11	164.7 (4)	O27—C27—C28—O30	3.9 (7)
N5—C6—C7—O9	173.0 (4)	O28—C27—C28—O29	4.5 (7)
N5—C6—C10—C11	−71.0 (5)	O28—C27—C28—O30	−177.0 (5)

Symmetry codes: (i) x−1, y, z; (ii) x−1, y−1, z; (iii) x−1, y, z−1; (iv) x, y+1, z−1; (v) x+1, y, z; (vi) x+1, y+1, z; (vii) x, y+1, z; (viii) x+1, y, z+1; (ix) x, y, z+1; (x) x, y−1, z+1; (xi) x, y−1, z; (xii) x, y, z−1.

Hydrogen-bond geometry (Å, º)

D—H···A	D—H	H···A	D···A	D—H···A
N1—H1A···O21^ii	0.89	1.95	2.793 (7)	158
N1—H1B···O28	0.89	2.25	2.902 (6)	130
N1—H1B···O29	0.89	1.94	2.727 (6)	147
N1—H1C···O25^i	0.89	1.90	2.741 (7)	157
N5—H5···O4^v	0.86	2.170	2.991 (5)	160
O9—H9···O27^iii	0.82	1.72	2.531 (6)	167
O13—H13···O30^iv	0.82	1.76	2.571 (6)	170
N14—H14A···O8^vi	0.89	2.11	2.947 (6)	156
N14—H14B···O27^iv	0.89	2.15	2.882 (6)	139
N14—H14B···O30^iv	0.89	2.06	2.793 (6)	139
N14—H14C···O12^v	0.89	2.20	3.035 (7)	157
N18—H18···O17^i	0.86	2.02	2.870 (6)	171
O22—H22···O29^vi	0.82	1.81	2.622 (6)	170
O26—H26···O28	0.82	1.81	2.618 (6)	170
C2—H2A···O21^xi	0.97	2.59	3.432 (8)	145
C10—H10B···O9^v	0.97	2.47	3.388 (7)	158

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