FMO DATABASE

FMODB ID: G8K51

Calculation Name: 2EW5-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 4-{(1e)-3-oxo-3-[(2-phenylethyl)amino]prop-1-en-1-yl}-1,2-phenylene diacetate | cobalt (ii) ion

Ligand 3-letter code: Y12 | CO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EW5

Chain ID: A

ChEMBL ID:

UniProt ID: Q672W7

Base Structure: X-ray

Registration Date: 2025-10-04

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	166
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1747291.363331
FMO2-HF: Nuclear repulsion	1680567.987764
FMO2-HF: Total energy	-66723.375568
FMO2-MP2: Total energy	-66917.195252

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-311.568	-314.757	36.728	-19.044	-14.495	-0.222

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.685 / q_NPA : 0.818

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	4	LEU	0	-0.029	-0.017	3.721	3.351	4.724	0.002	-0.546	-0.830	0.000
29	A	30	GLN	0	-0.011	-0.010	3.095	7.469	8.035	0.012	-0.264	-0.315	-0.001
30	A	31	GLN	0	-0.014	-0.015	5.009	-6.000	-6.011	-0.001	-0.002	0.014	0.000
33	A	34	ASP	-1	-0.803	-0.886	1.739	-122.793	-125.118	16.678	-8.352	-6.000	-0.096
34	A	35	MET	0	-0.055	0.002	3.344	5.132	5.281	0.008	-0.046	-0.111	-0.001
36	A	37	GLU	-1	-0.853	-0.918	1.743	-124.482	-127.493	20.030	-9.824	-7.194	-0.124
37	A	38	THR	0	-0.002	-0.032	5.093	4.860	4.930	-0.001	-0.010	-0.059	0.000
4	A	5	GLU	-1	-0.961	-0.981	6.253	-20.292	-20.292	0.000	0.000	0.000	0.000
5	A	6	ILE	0	0.013	0.008	9.687	0.303	0.303	0.000	0.000	0.000	0.000
6	A	7	ILE	0	-0.032	-0.020	12.505	1.936	1.936	0.000	0.000	0.000	0.000
7	A	8	HIS	0	0.071	0.043	15.338	1.189	1.189	0.000	0.000	0.000	0.000
8	A	9	TYR	0	0.011	0.004	18.708	0.638	0.638	0.000	0.000	0.000	0.000
9	A	10	PRO	0	-0.038	-0.017	22.349	-0.025	-0.025	0.000	0.000	0.000	0.000
10	A	11	SER	0	0.019	-0.001	18.898	0.633	0.633	0.000	0.000	0.000	0.000
11	A	12	LYS	1	0.953	0.956	21.770	11.513	11.513	0.000	0.000	0.000	0.000
12	A	13	ILE	0	0.032	0.030	16.288	0.398	0.398	0.000	0.000	0.000	0.000
13	A	14	LEU	0	0.053	0.035	17.561	-0.093	-0.093	0.000	0.000	0.000	0.000
14	A	15	ARG	1	0.684	0.803	20.551	12.757	12.757	0.000	0.000	0.000	0.000
15	A	16	THR	0	-0.080	-0.043	19.961	0.691	0.691	0.000	0.000	0.000	0.000
16	A	17	ILE	0	-0.003	0.008	21.872	-0.250	-0.250	0.000	0.000	0.000	0.000
17	A	18	SER	0	-0.010	-0.009	17.854	0.099	0.099	0.000	0.000	0.000	0.000
18	A	19	LYS	1	0.877	0.931	20.175	14.039	14.039	0.000	0.000	0.000	0.000
19	A	20	GLU	-1	-0.911	-0.967	19.909	-13.226	-13.226	0.000	0.000	0.000	0.000
20	A	21	VAL	0	-0.032	-0.008	16.204	-0.065	-0.065	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.024	0.010	19.068	0.556	0.556	0.000	0.000	0.000	0.000
22	A	23	SER	0	-0.076	-0.051	16.911	0.623	0.623	0.000	0.000	0.000	0.000
23	A	24	PHE	0	0.005	0.003	16.337	-0.944	-0.944	0.000	0.000	0.000	0.000
24	A	25	ASP	-1	-0.816	-0.890	14.055	-20.672	-20.672	0.000	0.000	0.000	0.000
25	A	26	ALA	0	0.063	0.012	12.228	-1.133	-1.133	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.937	0.980	10.044	19.399	19.399	0.000	0.000	0.000	0.000
27	A	28	LEU	0	-0.009	-0.003	9.389	-2.994	-2.994	0.000	0.000	0.000	0.000
28	A	29	HIS	0	-0.026	-0.028	10.041	-2.260	-2.260	0.000	0.000	0.000	0.000
31	A	32	LEU	0	0.014	0.012	6.926	-1.322	-1.322	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.823	-0.905	5.226	-36.755	-36.755	0.000	0.000	0.000	0.000
35	A	36	TYR	0	0.017	-0.022	6.863	2.310	2.310	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.054	-0.006	7.098	4.834	4.834	0.000	0.000	0.000	0.000
39	A	40	ILE	0	-0.008	0.004	8.845	2.555	2.555	0.000	0.000	0.000	0.000
40	A	41	ALA	0	-0.036	-0.018	7.931	2.374	2.374	0.000	0.000	0.000	0.000
41	A	42	SER	0	-0.055	-0.021	9.853	2.162	2.162	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.969	-0.979	12.686	-16.714	-16.714	0.000	0.000	0.000	0.000
43	A	44	GLY	0	-0.002	0.009	13.505	1.588	1.588	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.012	-0.006	14.448	-0.626	-0.626	0.000	0.000	0.000	0.000
45	A	46	GLY	0	0.000	-0.010	15.817	0.496	0.496	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.010	0.003	9.899	-0.688	-0.688	0.000	0.000	0.000	0.000
47	A	48	ALA	0	0.060	0.025	13.609	-0.542	-0.542	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.008	-0.001	12.302	-0.880	-0.880	0.000	0.000	0.000	0.000
49	A	50	ILE	0	-0.021	-0.009	13.009	-1.096	-1.096	0.000	0.000	0.000	0.000
50	A	51	GLN	0	0.054	0.000	13.818	-0.061	-0.061	0.000	0.000	0.000	0.000
51	A	52	VAL	0	0.006	0.021	8.754	-0.666	-0.666	0.000	0.000	0.000	0.000
52	A	53	GLY	0	-0.004	-0.001	10.485	-0.966	-0.966	0.000	0.000	0.000	0.000
53	A	54	LEU	0	-0.023	-0.005	8.959	1.216	1.216	0.000	0.000	0.000	0.000
54	A	55	PRO	0	0.001	0.004	13.298	0.643	0.643	0.000	0.000	0.000	0.000
55	A	56	LEU	0	0.002	-0.001	13.165	1.194	1.194	0.000	0.000	0.000	0.000
56	A	57	ARG	1	0.820	0.893	16.810	13.488	13.488	0.000	0.000	0.000	0.000
57	A	58	MET	0	-0.007	-0.003	10.829	0.828	0.828	0.000	0.000	0.000	0.000
58	A	59	LEU	0	-0.015	0.000	14.377	-0.408	-0.408	0.000	0.000	0.000	0.000
59	A	60	ILE	0	-0.006	0.010	9.918	0.253	0.253	0.000	0.000	0.000	0.000
60	A	61	ILE	0	0.016	0.000	14.094	0.580	0.580	0.000	0.000	0.000	0.000
61	A	62	ASN	0	0.003	0.011	14.188	-1.369	-1.369	0.000	0.000	0.000	0.000
62	A	63	LEU	0	0.022	0.012	16.309	-0.120	-0.120	0.000	0.000	0.000	0.000
63	A	64	PRO	0	0.009	0.002	19.067	-0.506	-0.506	0.000	0.000	0.000	0.000
64	A	65	GLN	0	-0.043	-0.035	20.461	0.966	0.966	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.953	-0.983	23.138	-10.889	-10.889	0.000	0.000	0.000	0.000
66	A	67	ASP	-1	-0.842	-0.913	22.602	-13.923	-13.923	0.000	0.000	0.000	0.000
67	A	68	GLY	0	-0.009	0.005	23.322	0.042	0.042	0.000	0.000	0.000	0.000
68	A	69	VAL	0	-0.075	-0.041	18.647	-0.634	-0.634	0.000	0.000	0.000	0.000
69	A	70	GLN	0	-0.066	-0.047	14.697	-0.035	-0.035	0.000	0.000	0.000	0.000
70	A	71	HIS	1	0.846	0.926	16.157	15.570	15.570	0.000	0.000	0.000	0.000
71	A	72	LYS	1	0.915	0.976	7.727	34.942	34.942	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.925	-0.980	13.878	-19.162	-19.162	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.842	-0.901	17.176	-15.063	-15.063	0.000	0.000	0.000	0.000
74	A	75	CYS	0	-0.095	-0.041	13.120	-0.446	-0.446	0.000	0.000	0.000	0.000
75	A	76	LEU	0	-0.021	0.000	15.468	0.222	0.222	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.776	-0.867	11.467	-26.707	-26.707	0.000	0.000	0.000	0.000
77	A	78	ILE	0	-0.048	-0.025	15.386	1.254	1.254	0.000	0.000	0.000	0.000
78	A	79	ILE	0	-0.008	-0.011	15.072	-0.641	-0.641	0.000	0.000	0.000	0.000
79	A	80	ASN	0	-0.010	-0.012	18.476	0.439	0.439	0.000	0.000	0.000	0.000
80	A	81	PRO	0	0.012	0.019	20.429	0.649	0.649	0.000	0.000	0.000	0.000
81	A	82	LYS	1	0.896	0.940	23.378	12.201	12.201	0.000	0.000	0.000	0.000
82	A	83	PHE	0	0.011	0.004	26.781	-0.095	-0.095	0.000	0.000	0.000	0.000
83	A	84	ILE	0	-0.028	-0.001	29.651	0.243	0.243	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.852	-0.935	32.446	-8.706	-8.706	0.000	0.000	0.000	0.000
85	A	86	THR	0	-0.055	-0.023	31.580	-0.313	-0.313	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.006	-0.003	34.170	0.312	0.312	0.000	0.000	0.000	0.000
87	A	88	GLY	0	0.020	0.006	35.690	-0.208	-0.208	0.000	0.000	0.000	0.000
88	A	89	SER	0	-0.114	-0.085	35.946	-0.203	-0.203	0.000	0.000	0.000	0.000
89	A	90	MET	0	0.014	0.023	31.514	0.107	0.107	0.000	0.000	0.000	0.000
90	A	91	MET	0	-0.014	0.009	33.830	-0.161	-0.161	0.000	0.000	0.000	0.000
91	A	92	TYR	0	0.044	0.008	26.278	0.090	0.090	0.000	0.000	0.000	0.000
92	A	93	LYS	1	0.893	0.964	28.572	10.284	10.284	0.000	0.000	0.000	0.000
93	A	94	GLU	-1	-0.734	-0.826	25.124	-12.847	-12.847	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.062	0.015	23.343	0.456	0.456	0.000	0.000	0.000	0.000
95	A	96	CYS	-1	-0.963	-0.848	19.523	-17.114	-17.114	0.000	0.000	0.000	0.000
96	A	97	LEU	0	0.077	0.045	13.107	0.244	0.244	0.000	0.000	0.000	0.000
97	A	98	SER	0	0.030	-0.021	16.987	-0.479	-0.479	0.000	0.000	0.000	0.000
98	A	99	VAL	0	-0.097	-0.058	18.570	0.863	0.863	0.000	0.000	0.000	0.000
99	A	100	PRO	0	0.057	0.045	18.788	0.508	0.508	0.000	0.000	0.000	0.000
100	A	101	GLY	0	0.020	0.009	20.880	0.501	0.501	0.000	0.000	0.000	0.000
101	A	102	PHE	0	-0.046	-0.013	24.036	0.813	0.813	0.000	0.000	0.000	0.000
102	A	103	TYR	0	0.054	0.014	21.981	-0.240	-0.240	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.893	-0.950	27.491	-9.222	-9.222	0.000	0.000	0.000	0.000
104	A	105	GLU	-1	-0.979	-0.990	29.515	-9.592	-9.592	0.000	0.000	0.000	0.000
105	A	106	VAL	0	-0.039	-0.019	28.685	0.208	0.208	0.000	0.000	0.000	0.000
106	A	107	GLU	-1	-0.864	-0.913	31.521	-8.709	-8.709	0.000	0.000	0.000	0.000
107	A	108	ARG	1	0.741	0.821	25.979	11.617	11.617	0.000	0.000	0.000	0.000
108	A	109	PHE	0	0.025	0.018	31.519	0.301	0.301	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.865	-0.927	31.579	-9.037	-9.037	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.869	0.930	32.376	8.960	8.960	0.000	0.000	0.000	0.000
111	A	112	VAL	0	-0.009	-0.017	27.710	0.102	0.102	0.000	0.000	0.000	0.000
112	A	113	LYS	1	0.810	0.910	29.605	9.332	9.332	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.029	-0.005	24.291	0.139	0.139	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.888	-0.946	26.785	-10.855	-10.855	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.008	-0.017	20.270	-0.413	-0.413	0.000	0.000	0.000	0.000
116	A	117	GLN	0	-0.004	-0.004	20.587	0.368	0.368	0.000	0.000	0.000	0.000
117	A	118	ASN	0	0.065	0.010	17.846	-0.762	-0.762	0.000	0.000	0.000	0.000
118	A	119	ARG	1	0.827	0.854	9.184	29.483	29.483	0.000	0.000	0.000	0.000
119	A	120	PHE	0	-0.039	-0.021	15.610	-0.415	-0.415	0.000	0.000	0.000	0.000
120	A	121	ALA	0	-0.009	0.007	18.575	0.876	0.876	0.000	0.000	0.000	0.000
121	A	122	GLU	-1	-0.823	-0.875	20.823	-13.276	-13.276	0.000	0.000	0.000	0.000
122	A	123	VAL	0	0.025	0.004	22.518	-0.485	-0.485	0.000	0.000	0.000	0.000
123	A	124	LYS	1	0.798	0.897	22.170	13.808	13.808	0.000	0.000	0.000	0.000
124	A	125	VAL	0	0.031	0.011	25.361	0.023	0.023	0.000	0.000	0.000	0.000
125	A	126	LEU	0	-0.023	-0.001	23.418	-0.013	-0.013	0.000	0.000	0.000	0.000
126	A	127	GLU	-1	-0.852	-0.926	27.128	-9.327	-9.327	0.000	0.000	0.000	0.000
127	A	128	ALA	0	0.013	0.003	26.745	-0.263	-0.263	0.000	0.000	0.000	0.000
128	A	129	SER	0	0.017	-0.006	28.816	0.419	0.419	0.000	0.000	0.000	0.000
129	A	130	GLU	-1	-0.873	-0.941	28.714	-10.558	-10.558	0.000	0.000	0.000	0.000
130	A	131	LEU	0	0.018	0.015	23.519	-0.191	-0.191	0.000	0.000	0.000	0.000
131	A	132	LEU	0	0.043	0.026	22.606	-0.529	-0.529	0.000	0.000	0.000	0.000
132	A	133	ALA	0	0.010	0.011	24.626	-0.366	-0.366	0.000	0.000	0.000	0.000
133	A	134	VAL	0	-0.022	0.000	25.534	-0.114	-0.114	0.000	0.000	0.000	0.000
134	A	135	ALA	0	0.018	0.015	20.933	-0.225	-0.225	0.000	0.000	0.000	0.000
135	A	136	ILE	0	0.016	-0.001	21.837	-0.461	-0.461	0.000	0.000	0.000	0.000
136	A	137	GLN	0	-0.064	-0.055	23.112	0.187	0.187	0.000	0.000	0.000	0.000
137	A	138	HIS	1	0.782	0.836	20.065	15.163	15.163	0.000	0.000	0.000	0.000
138	A	139	GLU	-1	-0.828	-0.940	17.469	-18.083	-18.083	0.000	0.000	0.000	0.000
139	A	140	ILE	0	-0.025	-0.019	20.024	-0.270	-0.270	0.000	0.000	0.000	0.000
140	A	141	ASP	-1	-0.843	-0.888	22.500	-11.665	-11.665	0.000	0.000	0.000	0.000
141	A	142	HIS	0	0.064	0.008	18.818	0.395	0.395	0.000	0.000	0.000	0.000
142	A	143	LEU	0	-0.060	-0.010	17.573	-0.063	-0.063	0.000	0.000	0.000	0.000
143	A	144	ASN	0	-0.017	-0.012	20.893	0.186	0.186	0.000	0.000	0.000	0.000
144	A	145	GLY	0	0.020	0.037	22.724	0.560	0.560	0.000	0.000	0.000	0.000
145	A	146	VAL	0	-0.064	-0.033	23.887	0.522	0.522	0.000	0.000	0.000	0.000
146	A	147	LEU	0	0.044	0.010	21.773	-0.594	-0.594	0.000	0.000	0.000	0.000
147	A	148	PHE	0	0.041	0.014	23.425	0.550	0.550	0.000	0.000	0.000	0.000
148	A	149	VAL	0	0.008	-0.002	26.023	0.505	0.505	0.000	0.000	0.000	0.000
149	A	150	ASP	-1	-0.786	-0.851	27.607	-11.382	-11.382	0.000	0.000	0.000	0.000
150	A	151	LYS	1	0.824	0.907	28.270	11.594	11.594	0.000	0.000	0.000	0.000
151	A	152	LEU	0	-0.022	0.018	30.211	0.299	0.299	0.000	0.000	0.000	0.000
152	A	153	SER	0	0.045	0.018	33.420	0.197	0.197	0.000	0.000	0.000	0.000
153	A	154	ILE	0	0.010	-0.014	37.007	-0.116	-0.116	0.000	0.000	0.000	0.000
154	A	155	LEU	0	0.018	0.004	38.772	-0.092	-0.092	0.000	0.000	0.000	0.000
155	A	156	LYS	1	0.917	0.954	34.423	9.088	9.088	0.000	0.000	0.000	0.000
156	A	157	ARG	1	1.002	1.009	33.391	8.771	8.771	0.000	0.000	0.000	0.000
157	A	158	LYS	1	0.739	0.859	34.919	8.503	8.503	0.000	0.000	0.000	0.000
158	A	159	LYS	1	0.815	0.912	32.427	10.019	10.019	0.000	0.000	0.000	0.000
159	A	160	PHE	0	0.044	0.024	27.060	-0.028	-0.028	0.000	0.000	0.000	0.000
160	A	161	GLU	-1	-0.787	-0.896	31.700	-9.068	-9.068	0.000	0.000	0.000	0.000
161	A	162	LYS	1	0.806	0.900	33.720	9.180	9.180	0.000	0.000	0.000	0.000
162	A	163	GLU	-1	-0.732	-0.886	30.385	-9.999	-9.999	0.000	0.000	0.000	0.000
163	A	164	LEU	0	-0.052	-0.009	28.267	-0.225	-0.225	0.000	0.000	0.000	0.000
164	A	165	LYS	1	0.888	0.925	29.903	8.730	8.730	0.000	0.000	0.000	0.000
165	A	166	GLU	-1	-0.992	-0.979	31.522	-9.030	-9.030	0.000	0.000	0.000	0.000
166	A	167	LEU	-1	-0.961	-0.952	24.447	-11.224	-11.224	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)