Synthesis, magnetic, Hirshfeld, and molecular docking investigations of a mononuclear Ni(II) complex with N-methyldiethanolamine

Figures & data

Table 1. Crystal data, data collection, and structure refinement parameters of [Ni(mdeaH₂)₂](PhCO₂)₂.

Compound	[Ni(mdeaH2)2](PhCO2)2
Formula	C24H36N2NiO8
Formula weight	539.26
Crystal System	monoclinic
Space Group	P21/c
a / Å	7.0027(5)
b / Å	8.4636(4)
c / Å	21.6219(15)
α/ °	90
β/ °	92.095(5)
γ/ °	90
V / Å	1280.63(14)
Z	2
T / K	180
F (000)	572
D c/ Mg m^-3	1.398
μ/ mm^−1(GaKα)	0.807
Data Measured	10017
Unique Data	4378
Rint	0.0227
Data with I ≥2σ(I)	3709
wR2(all data)	0.0987
S(all data)	1.053
R1[I ≥ 2σ(I)]	0.0340
Parameters/Restraints	167/0
Biggest diff. peak/hole/eÅ	+0.442/−0.569

Figure 1. Molecular structure of [Ni(mdeaH₂)₂](PhCO₂)₂. Color code: black, red, blue, turquoise, and white spheres represent C, O, N, Ni, and H, respectively.

Table 2. Selected bond lengths and angles of 1.

Bond lengths		Bond lengths
Atom	Distance/Å	Atom	Distance/Å
Ni(1)-O(1)	2.0750(10)	Ni(1)-O(2)'	2.0612(10)
Ni(1)-O(1)'	2.0750(10)	Ni(1)-N(1)	2.0976(12)
Ni(1)-O(2)	2.0612(10)	Ni(1)-N(1)'	2.0976(12)
Symmetry code: (') 1-x, -y,1-z
Bond angles		Bond angles
Atom	Angles/°	Atom	Angles/°
N(1)-Ni(1)-O(1)'	98.311	N(1)-Ni(1)-N(1)'	180
N(1)-Ni(1)-O(2)	84.259	O(1)-Ni(1)-O(1)'	180
N(1) -Ni(1)-O(1)	81.689	O(2) -Ni(1)-O(2)'	180
N(1) -Ni(1)-O(2)'	95.741	O(1)-Ni(1)-O(2)	92.927
N(1)'-Ni(1)-O(1)'	98.311	O(1) -Ni(1)-O(2)'	87.073
N(1)'-Ni(1)-O(2)	84.259	O(1)'-Ni(1)-O(2)'	92.927
N(1)' -Ni(1)-O(1)	81.689	O(1)'-Ni(1)-O(2)	87.073
N(1)' -Ni(1)-O(2)'	95.741
Symmetry code: (') 1-x, -y,1-z

Figure 2. Temperature dependence of χT products for 1 at 1000 Oe.

Figure 3. Field dependence of magnetization temperatures of 1.

Figure 4. Molecular Hirshfeld surfaces (a) d_norm, (b) shape index, (c) curvedness, (d) d_i and (e) d_e of 1.

Figure 5. Fingerprint plots of 1 showing the percentages of contact contributions to the total Hirshfeld surface area (a) all, (b) resolved into H–H/H–H interactions, (c) C–H interactions, (d) O–H and (e) C–C type of interactions.

Scheme 1. Schematic representation of [Ni(mdeaH₂)₂](PhCO₂)₂ (1).

Figure 6. Proteins (i) 6TOU, (ii) 7ZFM and (iii) 7WC0 are docked with 1.

Table 3. The binding energies, inhibition constant, amino acid residues, and bond distances linked with 1.

PDB ID	Binding energy (Kcal/mol)	Inhibition constant (μm)	Amino acid residues	Bond distance (Å)
6TOU	−4.4	7.43	TYR52	2.82879
			SER98	2.60095
			GLY100	2.66851
			TYR1094	1.97994
			TYR52	2.42093
7ZFM	−3.8	6.42	GLN102	2.38151
			THR100	2.28524
			SER98	3.53139
7WC0	−3.6	6.08	SER174	2.53636
			THR196	2.43413