FMO DATABASE

FMODB ID: YM6N2

Calculation Name: 2IMJ-A-Xray549

Preferred Name:

Target Type:

Ligand Name: acetate ion | 1,2-ethanediol

Ligand 3-letter code: ACT | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2IMJ

Chain ID: A

ChEMBL ID:

UniProt ID: Q4KBL6

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	158
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1773758.007765
FMO2-HF: Nuclear repulsion	1707887.363462
FMO2-HF: Total energy	-65870.644302
FMO2-MP2: Total energy	-66066.120053

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:5:ALA)

Summations of interaction energy for fragment #1(A:5: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.
-10.73	-9.221	-0.02	-0.662	-0.826	0.001

Interaction energy analysis for fragmet #1(A:5:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.863 / q_NPA : 0.918

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	7	VAL	0	0.082	0.041	3.845	-0.198	1.311	-0.020	-0.662	-0.826	0.001
4	A	8	ARG	1	0.862	0.949	6.875	30.395	30.395	0.000	0.000	0.000	0.000
5	A	9	PRO	0	0.047	0.036	10.253	1.042	1.042	0.000	0.000	0.000	0.000
6	A	10	PRO	0	0.042	0.005	13.427	-0.069	-0.069	0.000	0.000	0.000	0.000
7	A	11	LEU	0	-0.037	-0.012	10.775	-1.118	-1.118	0.000	0.000	0.000	0.000
8	A	12	PRO	0	-0.040	0.024	13.112	1.337	1.337	0.000	0.000	0.000	0.000
9	A	13	PRO	0	0.013	-0.002	15.902	-0.548	-0.548	0.000	0.000	0.000	0.000
10	A	14	PHE	0	-0.019	-0.016	15.594	0.056	0.056	0.000	0.000	0.000	0.000
11	A	15	THR	0	0.045	0.028	20.490	0.665	0.665	0.000	0.000	0.000	0.000
12	A	16	ARG	1	1.005	0.991	23.270	10.201	10.201	0.000	0.000	0.000	0.000
13	A	17	GLU	-1	-0.930	-0.956	24.509	-12.299	-12.299	0.000	0.000	0.000	0.000
14	A	18	SER	0	0.041	0.013	19.556	-0.442	-0.442	0.000	0.000	0.000	0.000
15	A	19	ALA	0	0.033	0.006	20.284	-0.707	-0.707	0.000	0.000	0.000	0.000
16	A	20	ILE	0	-0.005	-0.008	22.002	-0.151	-0.151	0.000	0.000	0.000	0.000
17	A	21	GLU	-1	-0.900	-0.947	19.441	-16.193	-16.193	0.000	0.000	0.000	0.000
18	A	22	LYS	1	0.786	0.892	12.741	22.285	22.285	0.000	0.000	0.000	0.000
19	A	23	ILE	0	-0.006	-0.004	19.008	-0.424	-0.424	0.000	0.000	0.000	0.000
20	A	24	ARG	1	0.829	0.904	21.738	12.282	12.282	0.000	0.000	0.000	0.000
21	A	25	LEU	0	0.013	0.014	16.513	-0.062	-0.062	0.000	0.000	0.000	0.000
22	A	26	ALA	0	-0.020	-0.002	17.898	-0.530	-0.530	0.000	0.000	0.000	0.000
23	A	27	GLU	-1	-0.818	-0.886	18.793	-11.809	-11.809	0.000	0.000	0.000	0.000
24	A	28	ASP	-1	-0.767	-0.872	20.529	-13.612	-13.612	0.000	0.000	0.000	0.000
25	A	29	GLY	0	-0.040	-0.013	17.906	-0.149	-0.149	0.000	0.000	0.000	0.000
26	A	30	TRP	0	0.005	0.004	17.842	0.735	0.735	0.000	0.000	0.000	0.000
27	A	31	ASN	0	0.024	0.000	20.977	0.700	0.700	0.000	0.000	0.000	0.000
28	A	32	SER	0	-0.108	-0.069	19.869	0.336	0.336	0.000	0.000	0.000	0.000
29	A	33	ARG	1	0.871	0.938	22.262	12.609	12.609	0.000	0.000	0.000	0.000
30	A	34	ASP	-1	-0.819	-0.895	17.400	-17.962	-17.962	0.000	0.000	0.000	0.000
31	A	35	PRO	0	0.014	-0.013	17.582	-0.948	-0.948	0.000	0.000	0.000	0.000
32	A	36	GLU	-1	-0.857	-0.906	11.336	-26.295	-26.295	0.000	0.000	0.000	0.000
33	A	37	ARG	1	0.934	0.967	12.942	15.667	15.667	0.000	0.000	0.000	0.000
34	A	38	VAL	0	-0.017	-0.004	13.286	-1.241	-1.241	0.000	0.000	0.000	0.000
35	A	39	SER	0	0.007	0.007	12.592	-1.431	-1.431	0.000	0.000	0.000	0.000
36	A	40	LEU	0	-0.037	-0.022	7.691	-2.481	-2.481	0.000	0.000	0.000	0.000
37	A	41	ALA	0	-0.028	-0.015	8.590	-3.586	-3.586	0.000	0.000	0.000	0.000
38	A	42	TYR	0	0.023	0.015	10.461	0.858	0.858	0.000	0.000	0.000	0.000
39	A	43	THR	0	0.006	-0.006	7.985	-3.177	-3.177	0.000	0.000	0.000	0.000
40	A	44	LEU	0	0.000	-0.016	4.811	1.433	1.433	0.000	0.000	0.000	0.000
41	A	45	ASP	-1	-0.825	-0.894	8.696	-24.831	-24.831	0.000	0.000	0.000	0.000
42	A	46	THR	0	-0.039	0.006	11.747	2.468	2.468	0.000	0.000	0.000	0.000
43	A	47	GLN	0	-0.037	-0.014	13.446	2.296	2.296	0.000	0.000	0.000	0.000
44	A	48	TRP	0	-0.010	-0.023	15.121	0.947	0.947	0.000	0.000	0.000	0.000
45	A	49	ARG	1	0.734	0.802	19.568	11.969	11.969	0.000	0.000	0.000	0.000
46	A	50	ASN	0	0.031	0.020	22.670	-0.442	-0.442	0.000	0.000	0.000	0.000
47	A	51	ARG	1	0.813	0.869	24.601	10.565	10.565	0.000	0.000	0.000	0.000
48	A	52	ALA	0	0.027	0.015	28.311	-0.037	-0.037	0.000	0.000	0.000	0.000
49	A	53	GLU	-1	-0.847	-0.898	24.142	-12.585	-12.585	0.000	0.000	0.000	0.000
50	A	54	PHE	0	-0.005	-0.030	22.774	-0.176	-0.176	0.000	0.000	0.000	0.000
51	A	55	ALA	0	-0.024	0.008	17.926	0.066	0.066	0.000	0.000	0.000	0.000
52	A	56	HIS	1	0.859	0.912	17.480	15.121	15.121	0.000	0.000	0.000	0.000
53	A	57	ASN	0	0.069	0.035	13.225	-0.820	-0.820	0.000	0.000	0.000	0.000
54	A	58	ARG	1	0.863	0.918	5.882	39.475	39.475	0.000	0.000	0.000	0.000
55	A	59	GLU	-1	-0.930	-0.950	12.259	-18.398	-18.398	0.000	0.000	0.000	0.000
56	A	60	GLU	-1	-0.791	-0.910	14.732	-15.021	-15.021	0.000	0.000	0.000	0.000
57	A	61	ALA	0	-0.009	0.005	14.709	0.921	0.921	0.000	0.000	0.000	0.000
58	A	62	LYS	1	0.915	0.938	14.152	21.268	21.268	0.000	0.000	0.000	0.000
59	A	63	ALA	0	0.002	0.011	16.621	0.994	0.994	0.000	0.000	0.000	0.000
60	A	64	PHE	0	-0.019	-0.009	19.818	0.816	0.816	0.000	0.000	0.000	0.000
61	A	65	LEU	0	-0.029	-0.015	16.634	0.600	0.600	0.000	0.000	0.000	0.000
62	A	66	THR	0	-0.038	-0.038	19.810	0.454	0.454	0.000	0.000	0.000	0.000
63	A	67	ARG	1	0.859	0.918	22.186	13.779	13.779	0.000	0.000	0.000	0.000
64	A	68	LYS	1	0.796	0.909	23.172	12.823	12.823	0.000	0.000	0.000	0.000
65	A	69	TRP	0	0.001	-0.012	19.818	0.268	0.268	0.000	0.000	0.000	0.000
66	A	70	ALA	0	-0.004	0.021	26.043	0.267	0.267	0.000	0.000	0.000	0.000
67	A	71	LYS	1	0.866	0.941	28.060	9.585	9.585	0.000	0.000	0.000	0.000
68	A	72	GLU	-1	-0.822	-0.882	27.558	-11.131	-11.131	0.000	0.000	0.000	0.000
69	A	73	LEU	0	0.031	0.013	29.526	-0.310	-0.310	0.000	0.000	0.000	0.000
70	A	74	ASP	-1	-0.855	-0.931	31.738	-9.121	-9.121	0.000	0.000	0.000	0.000
71	A	75	TYR	0	-0.013	-0.005	24.316	0.046	0.046	0.000	0.000	0.000	0.000
72	A	76	ARG	1	0.815	0.925	28.727	9.477	9.477	0.000	0.000	0.000	0.000
73	A	77	LEU	0	-0.055	-0.030	23.815	0.139	0.139	0.000	0.000	0.000	0.000
74	A	78	ILE	0	0.014	0.025	27.949	-0.131	-0.131	0.000	0.000	0.000	0.000
75	A	79	LYS	1	0.821	0.894	21.175	14.045	14.045	0.000	0.000	0.000	0.000
76	A	80	GLU	-1	-0.793	-0.884	26.880	-9.704	-9.704	0.000	0.000	0.000	0.000
77	A	81	LEU	0	-0.017	-0.005	24.851	-0.182	-0.182	0.000	0.000	0.000	0.000
78	A	82	TRP	0	-0.046	-0.011	27.477	0.456	0.456	0.000	0.000	0.000	0.000
79	A	83	ALA	0	0.002	-0.013	27.412	0.324	0.324	0.000	0.000	0.000	0.000
80	A	84	PHE	0	0.019	0.004	23.049	-0.358	-0.358	0.000	0.000	0.000	0.000
81	A	85	THR	0	-0.051	-0.028	23.092	0.700	0.700	0.000	0.000	0.000	0.000
82	A	86	ASP	-1	-0.834	-0.910	20.641	-13.752	-13.752	0.000	0.000	0.000	0.000
83	A	87	ASN	0	0.016	-0.004	15.741	0.600	0.600	0.000	0.000	0.000	0.000
84	A	88	ARG	1	0.846	0.903	17.658	13.131	13.131	0.000	0.000	0.000	0.000
85	A	89	ILE	0	-0.006	-0.007	19.081	0.442	0.442	0.000	0.000	0.000	0.000
86	A	90	ALA	0	0.001	0.018	22.065	-0.195	-0.195	0.000	0.000	0.000	0.000
87	A	91	VAL	0	-0.002	-0.011	22.709	0.292	0.292	0.000	0.000	0.000	0.000
88	A	92	ARG	1	0.945	0.984	26.070	9.850	9.850	0.000	0.000	0.000	0.000
89	A	93	TYR	0	-0.020	-0.027	25.538	-0.351	-0.351	0.000	0.000	0.000	0.000
90	A	94	ALA	0	0.060	0.043	28.852	0.302	0.302	0.000	0.000	0.000	0.000
91	A	95	TYR	0	-0.044	-0.065	28.158	-0.400	-0.400	0.000	0.000	0.000	0.000
92	A	96	GLU	-1	-0.733	-0.831	30.471	-8.470	-8.470	0.000	0.000	0.000	0.000
93	A	97	TRP	0	-0.046	-0.033	31.278	-0.309	-0.309	0.000	0.000	0.000	0.000
94	A	98	HIS	1	0.813	0.877	33.376	9.149	9.149	0.000	0.000	0.000	0.000
95	A	99	ASP	-1	-0.751	-0.865	34.398	-8.567	-8.567	0.000	0.000	0.000	0.000
96	A	100	ASP	-1	-0.845	-0.925	35.924	-8.729	-8.729	0.000	0.000	0.000	0.000
97	A	101	SER	0	-0.057	-0.021	37.504	0.232	0.232	0.000	0.000	0.000	0.000
98	A	102	GLY	0	-0.023	0.001	39.623	0.219	0.219	0.000	0.000	0.000	0.000
99	A	103	ASN	0	-0.096	-0.056	39.432	0.272	0.272	0.000	0.000	0.000	0.000
100	A	104	TRP	0	0.021	-0.002	35.533	-0.334	-0.334	0.000	0.000	0.000	0.000
101	A	105	PHE	0	-0.002	-0.008	35.199	0.227	0.227	0.000	0.000	0.000	0.000
102	A	106	ARG	1	0.848	0.928	34.658	8.307	8.307	0.000	0.000	0.000	0.000
103	A	107	SER	0	-0.018	-0.028	31.106	0.181	0.181	0.000	0.000	0.000	0.000
104	A	108	TYR	0	-0.052	-0.059	31.705	-0.264	-0.264	0.000	0.000	0.000	0.000
105	A	109	GLY	0	0.008	-0.008	28.645	0.004	0.004	0.000	0.000	0.000	0.000
106	A	110	ASN	0	-0.010	0.000	28.509	0.069	0.069	0.000	0.000	0.000	0.000
107	A	111	GLU	-1	-0.764	-0.870	21.958	-14.391	-14.391	0.000	0.000	0.000	0.000
108	A	112	ASN	0	-0.021	-0.002	23.418	0.146	0.146	0.000	0.000	0.000	0.000
109	A	113	TRP	0	-0.020	-0.031	18.162	-0.535	-0.535	0.000	0.000	0.000	0.000
110	A	114	GLU	-1	-0.752	-0.839	16.975	-15.237	-15.237	0.000	0.000	0.000	0.000
111	A	115	PHE	0	-0.031	-0.023	13.038	-0.748	-0.748	0.000	0.000	0.000	0.000
112	A	116	ASP	-1	-0.756	-0.875	7.839	-33.145	-33.145	0.000	0.000	0.000	0.000
113	A	117	GLU	-1	-0.843	-0.936	10.002	-24.886	-24.886	0.000	0.000	0.000	0.000
114	A	118	GLN	0	-0.071	-0.030	5.032	1.067	1.067	0.000	0.000	0.000	0.000
115	A	119	GLY	0	0.010	0.010	8.161	-0.847	-0.847	0.000	0.000	0.000	0.000
116	A	120	LEU	0	-0.023	-0.010	5.315	0.132	0.132	0.000	0.000	0.000	0.000
117	A	121	MET	0	-0.034	-0.003	9.932	2.049	2.049	0.000	0.000	0.000	0.000
118	A	122	ALA	0	0.050	0.024	12.429	-0.764	-0.764	0.000	0.000	0.000	0.000
119	A	123	ARG	1	0.818	0.874	13.446	16.302	16.302	0.000	0.000	0.000	0.000
120	A	124	ARG	1	0.823	0.901	17.086	14.844	14.844	0.000	0.000	0.000	0.000
121	A	125	PHE	0	-0.026	-0.011	19.338	0.272	0.272	0.000	0.000	0.000	0.000
122	A	126	ALA	0	0.001	0.004	23.134	0.148	0.148	0.000	0.000	0.000	0.000
123	A	127	CYS	-1	-0.743	-0.799	25.044	-10.951	-10.951	0.000	0.000	0.000	0.000
124	A	128	ILE	0	-0.029	-0.027	25.942	0.030	0.030	0.000	0.000	0.000	0.000
125	A	129	ASN	0	-0.020	-0.006	30.344	0.293	0.293	0.000	0.000	0.000	0.000
126	A	130	ASP	-1	-0.764	-0.814	33.164	-9.785	-9.785	0.000	0.000	0.000	0.000
127	A	131	MET	0	-0.001	0.012	35.824	0.279	0.279	0.000	0.000	0.000	0.000
128	A	132	PRO	0	0.006	0.001	38.683	-0.102	-0.102	0.000	0.000	0.000	0.000
129	A	133	ILE	0	-0.051	-0.018	38.222	0.159	0.159	0.000	0.000	0.000	0.000
130	A	134	LYS	1	0.941	0.961	42.006	6.692	6.692	0.000	0.000	0.000	0.000
131	A	135	ALA	0	0.031	0.013	41.573	-0.097	-0.097	0.000	0.000	0.000	0.000
132	A	136	GLN	0	0.007	-0.016	42.133	-0.211	-0.211	0.000	0.000	0.000	0.000
133	A	137	GLU	-1	-0.776	-0.864	42.462	-7.234	-7.234	0.000	0.000	0.000	0.000
134	A	138	ARG	1	0.836	0.932	36.513	8.409	8.409	0.000	0.000	0.000	0.000
135	A	139	LYS	1	0.907	0.956	37.156	8.274	8.274	0.000	0.000	0.000	0.000
136	A	140	PHE	0	-0.049	-0.018	31.945	-0.121	-0.121	0.000	0.000	0.000	0.000
137	A	141	HIS	0	-0.014	-0.029	35.224	-0.068	-0.068	0.000	0.000	0.000	0.000
138	A	142	TRP	0	0.000	0.021	28.599	0.331	0.331	0.000	0.000	0.000	0.000
139	A	143	PRO	0	0.041	0.006	31.646	-0.026	-0.026	0.000	0.000	0.000	0.000
140	A	144	LEU	0	-0.026	0.001	28.898	-0.271	-0.271	0.000	0.000	0.000	0.000
141	A	145	GLY	0	0.015	-0.009	25.733	-0.274	-0.274	0.000	0.000	0.000	0.000
142	A	146	ARG	1	0.711	0.818	23.519	12.791	12.791	0.000	0.000	0.000	0.000
143	A	147	ARG	1	0.836	0.916	25.803	11.359	11.359	0.000	0.000	0.000	0.000
144	A	148	PRO	0	0.048	0.019	28.137	-0.367	-0.367	0.000	0.000	0.000	0.000
145	A	149	ASP	-1	-0.820	-0.886	27.890	-11.770	-11.770	0.000	0.000	0.000	0.000
146	A	150	ASP	-1	-0.867	-0.928	30.625	-9.430	-9.430	0.000	0.000	0.000	0.000
147	A	151	HIS	0	-0.066	-0.031	32.321	0.416	0.416	0.000	0.000	0.000	0.000
148	A	152	PRO	0	0.049	0.031	32.948	-0.298	-0.298	0.000	0.000	0.000	0.000
149	A	153	GLY	0	0.016	0.003	32.064	-0.279	-0.279	0.000	0.000	0.000	0.000
150	A	154	LEU	0	-0.028	-0.024	30.861	0.262	0.262	0.000	0.000	0.000	0.000
151	A	155	SER	0	-0.033	-0.050	33.559	0.322	0.322	0.000	0.000	0.000	0.000
152	A	156	GLU	-1	-0.947	-0.973	35.866	-8.796	-8.796	0.000	0.000	0.000	0.000
153	A	157	LEU	0	-0.029	-0.004	35.038	0.248	0.248	0.000	0.000	0.000	0.000
154	A	158	GLY	0	0.004	0.010	38.465	0.223	0.223	0.000	0.000	0.000	0.000
155	A	159	LEU	0	-0.031	-0.012	38.649	-0.222	-0.222	0.000	0.000	0.000	0.000
156	A	160	GLU	-1	-0.898	-0.965	35.465	-8.806	-8.806	0.000	0.000	0.000	0.000
157	A	161	HIS	0	-0.045	-0.020	39.677	-0.152	-0.152	0.000	0.000	0.000	0.000
158	A	162	HIS	0	-0.002	0.002	42.405	0.338	0.338	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:5:ALA)