FMO DATABASE

FMODB ID: MLR3Z

Calculation Name: 2E7D-A-Xray547

Preferred Name:

Target Type:

Ligand Name: acetate ion

Ligand 3-letter code: ACT

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2E7D

Chain ID: A

ChEMBL ID:

UniProt ID: Q931P4

Base Structure: X-ray

Registration Date: 2025-10-05

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-967509.446745
FMO2-HF: Nuclear repulsion	921220.841223
FMO2-HF: Total energy	-46288.605522
FMO2-MP2: Total energy	-46425.359105

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:9:ASP)

Summations of interaction energy for fragment #1(A:9:ASP)

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.
-10.744	-8.539	0.009	-0.929	-1.285	-0.002

Interaction energy analysis for fragmet #1(A:9:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.076 / q_NPA : -0.053

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	11	LEU	0	0.010	0.023	3.778	1.848	3.544	0.003	-0.631	-1.068	0.000
4	A	12	THR	0	0.010	0.001	3.549	-8.996	-8.595	0.007	-0.295	-0.113	-0.002
5	A	13	ASP	-1	-0.921	-0.964	5.372	-3.698	-3.590	-0.001	-0.003	-0.104	0.000
6	A	14	LEU	0	-0.045	-0.033	6.777	0.522	0.522	0.000	0.000	0.000	0.000
7	A	15	GLN	0	-0.006	0.013	10.120	0.212	0.212	0.000	0.000	0.000	0.000
8	A	16	GLU	-1	-0.880	-0.951	13.897	-2.547	-2.547	0.000	0.000	0.000	0.000
9	A	17	ALA	0	-0.031	-0.019	16.217	0.090	0.090	0.000	0.000	0.000	0.000
10	A	18	HIS	0	-0.058	-0.046	18.712	0.052	0.052	0.000	0.000	0.000	0.000
11	A	19	PHE	0	-0.005	0.000	19.251	0.013	0.013	0.000	0.000	0.000	0.000
12	A	20	VAL	0	-0.013	0.008	22.987	0.023	0.023	0.000	0.000	0.000	0.000
13	A	21	VAL	0	-0.063	-0.033	24.953	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	22	PHE	0	0.068	0.023	27.383	0.052	0.052	0.000	0.000	0.000	0.000
15	A	23	GLU	-1	-0.904	-0.961	31.038	-0.450	-0.450	0.000	0.000	0.000	0.000
16	A	24	SER	0	-0.106	-0.076	33.712	-0.024	-0.024	0.000	0.000	0.000	0.000
17	A	25	GLU	-1	-0.886	-0.917	35.017	-0.449	-0.449	0.000	0.000	0.000	0.000
18	A	26	GLU	-1	-0.832	-0.913	37.604	-0.452	-0.452	0.000	0.000	0.000	0.000
19	A	27	ASN	0	-0.098	-0.055	35.114	-0.060	-0.060	0.000	0.000	0.000	0.000
20	A	28	SER	0	0.032	0.029	35.569	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	29	GLU	-1	-0.934	-0.968	30.616	-0.665	-0.665	0.000	0.000	0.000	0.000
22	A	30	SER	0	0.009	0.001	30.354	0.051	0.051	0.000	0.000	0.000	0.000
23	A	31	VAL	0	0.021	-0.002	30.912	-0.025	-0.025	0.000	0.000	0.000	0.000
24	A	32	MET	0	-0.039	-0.015	27.365	0.012	0.012	0.000	0.000	0.000	0.000
25	A	33	ASP	-1	-0.758	-0.861	26.369	-0.892	-0.892	0.000	0.000	0.000	0.000
26	A	34	GLY	0	0.054	0.027	26.147	-0.039	-0.039	0.000	0.000	0.000	0.000
27	A	35	PHE	0	-0.065	-0.032	25.894	0.013	0.013	0.000	0.000	0.000	0.000
28	A	36	VAL	0	-0.013	-0.012	21.431	-0.035	-0.035	0.000	0.000	0.000	0.000
29	A	37	GLU	-1	-0.888	-0.937	16.631	-1.243	-1.243	0.000	0.000	0.000	0.000
30	A	38	HIS	1	0.809	0.907	20.534	0.902	0.902	0.000	0.000	0.000	0.000
31	A	39	PRO	0	0.022	0.018	17.639	0.121	0.121	0.000	0.000	0.000	0.000
32	A	40	PHE	0	-0.017	-0.001	17.193	-0.016	-0.016	0.000	0.000	0.000	0.000
33	A	41	TYR	0	0.030	0.017	12.514	-0.108	-0.108	0.000	0.000	0.000	0.000
34	A	42	THR	0	-0.031	-0.003	13.735	0.140	0.140	0.000	0.000	0.000	0.000
35	A	43	ALA	0	0.025	0.007	8.347	-0.481	-0.481	0.000	0.000	0.000	0.000
36	A	44	THR	0	-0.026	-0.013	8.362	1.313	1.313	0.000	0.000	0.000	0.000
37	A	45	LEU	0	0.049	0.023	7.675	-2.298	-2.298	0.000	0.000	0.000	0.000
38	A	46	ASN	0	-0.034	-0.032	8.432	0.481	0.481	0.000	0.000	0.000	0.000
39	A	47	GLY	0	0.015	0.010	10.236	0.664	0.664	0.000	0.000	0.000	0.000
40	A	48	GLN	0	-0.026	0.001	12.275	0.439	0.439	0.000	0.000	0.000	0.000
41	A	49	LYS	1	0.936	0.967	11.056	3.941	3.941	0.000	0.000	0.000	0.000
42	A	50	TYR	0	-0.009	-0.006	12.361	0.575	0.575	0.000	0.000	0.000	0.000
43	A	51	VAL	0	0.042	0.031	13.696	-0.354	-0.354	0.000	0.000	0.000	0.000
44	A	52	VAL	0	-0.055	-0.037	10.437	-0.041	-0.041	0.000	0.000	0.000	0.000
45	A	53	MET	0	0.019	0.022	13.781	0.156	0.156	0.000	0.000	0.000	0.000
46	A	54	LYS	1	0.856	0.910	14.585	1.021	1.021	0.000	0.000	0.000	0.000
47	A	55	THR	0	-0.011	-0.024	17.151	0.064	0.064	0.000	0.000	0.000	0.000
48	A	56	LYS	1	0.884	0.951	20.346	0.674	0.674	0.000	0.000	0.000	0.000
49	A	57	ASP	-1	-0.780	-0.906	23.234	-0.304	-0.304	0.000	0.000	0.000	0.000
50	A	58	ASP	-1	-0.780	-0.853	20.792	-0.549	-0.549	0.000	0.000	0.000	0.000
51	A	59	SER	0	-0.058	-0.030	23.308	0.019	0.019	0.000	0.000	0.000	0.000
52	A	60	TYR	0	0.012	0.023	26.300	0.035	0.035	0.000	0.000	0.000	0.000
53	A	61	TRP	0	-0.028	-0.020	24.127	-0.042	-0.042	0.000	0.000	0.000	0.000
54	A	62	LYS	1	0.792	0.885	26.253	0.283	0.283	0.000	0.000	0.000	0.000
55	A	63	ASP	-1	-0.807	-0.898	24.894	-0.491	-0.491	0.000	0.000	0.000	0.000
56	A	64	LEU	0	0.003	0.018	21.100	-0.010	-0.010	0.000	0.000	0.000	0.000
57	A	65	ILE	0	-0.060	-0.020	23.183	-0.041	-0.041	0.000	0.000	0.000	0.000
58	A	66	VAL	0	0.066	0.028	22.037	0.023	0.023	0.000	0.000	0.000	0.000
59	A	67	GLU	-1	-0.754	-0.860	24.655	-0.836	-0.836	0.000	0.000	0.000	0.000
60	A	68	GLY	0	0.015	0.021	26.914	0.019	0.019	0.000	0.000	0.000	0.000
61	A	69	LYS	1	0.819	0.889	22.503	0.737	0.737	0.000	0.000	0.000	0.000
62	A	70	ARG	1	0.828	0.886	21.194	0.476	0.476	0.000	0.000	0.000	0.000
63	A	71	VAL	0	0.013	0.025	18.265	-0.056	-0.056	0.000	0.000	0.000	0.000
64	A	72	THR	0	-0.011	-0.001	13.316	0.186	0.186	0.000	0.000	0.000	0.000
65	A	73	THR	0	-0.039	-0.024	14.457	-0.103	-0.103	0.000	0.000	0.000	0.000
66	A	74	VAL	0	0.002	-0.006	9.181	0.156	0.156	0.000	0.000	0.000	0.000
67	A	75	SER	0	-0.015	0.000	9.895	0.206	0.206	0.000	0.000	0.000	0.000
68	A	76	LYS	1	0.967	0.971	11.956	0.030	0.030	0.000	0.000	0.000	0.000
69	A	77	ASP	-1	-0.799	-0.877	15.064	0.071	0.071	0.000	0.000	0.000	0.000
70	A	78	PRO	0	0.012	-0.013	17.289	-0.053	-0.053	0.000	0.000	0.000	0.000
71	A	79	LYS	1	0.923	0.987	20.254	-0.116	-0.116	0.000	0.000	0.000	0.000
72	A	80	ASN	0	-0.083	-0.070	18.384	0.003	0.003	0.000	0.000	0.000	0.000
73	A	81	ASN	0	-0.013	0.006	21.499	-0.093	-0.093	0.000	0.000	0.000	0.000
74	A	82	SER	0	-0.022	-0.010	18.513	-0.101	-0.101	0.000	0.000	0.000	0.000
75	A	83	ARG	1	0.819	0.874	16.241	0.697	0.697	0.000	0.000	0.000	0.000
76	A	84	THR	0	0.023	0.022	11.310	-0.130	-0.130	0.000	0.000	0.000	0.000
77	A	85	LEU	0	-0.046	-0.032	13.766	0.131	0.131	0.000	0.000	0.000	0.000
78	A	86	ILE	0	0.030	0.015	11.334	-0.214	-0.214	0.000	0.000	0.000	0.000
79	A	87	PHE	0	0.022	0.005	14.945	0.296	0.296	0.000	0.000	0.000	0.000
80	A	88	PRO	0	0.003	-0.002	16.677	-0.227	-0.227	0.000	0.000	0.000	0.000
81	A	89	TYR	0	0.009	0.001	16.822	0.143	0.143	0.000	0.000	0.000	0.000
82	A	90	ILE	0	0.000	-0.001	18.461	-0.036	-0.036	0.000	0.000	0.000	0.000
83	A	91	PRO	0	-0.027	-0.033	19.357	0.047	0.047	0.000	0.000	0.000	0.000
84	A	92	ASP	-1	-0.886	-0.936	21.788	-1.118	-1.118	0.000	0.000	0.000	0.000
85	A	93	LYS	1	0.787	0.892	24.217	1.057	1.057	0.000	0.000	0.000	0.000
86	A	94	ALA	0	0.080	0.045	25.010	-0.072	-0.072	0.000	0.000	0.000	0.000
87	A	95	VAL	0	0.014	0.007	27.163	-0.008	-0.008	0.000	0.000	0.000	0.000
88	A	96	TYR	0	-0.013	-0.002	21.657	-0.039	-0.039	0.000	0.000	0.000	0.000
89	A	97	ASN	0	-0.025	-0.013	26.314	0.050	0.050	0.000	0.000	0.000	0.000
90	A	98	ALA	0	-0.011	-0.012	25.814	-0.051	-0.051	0.000	0.000	0.000	0.000
91	A	99	ILE	0	-0.043	-0.010	27.733	0.058	0.058	0.000	0.000	0.000	0.000
92	A	100	VAL	0	0.031	0.020	26.469	-0.033	-0.033	0.000	0.000	0.000	0.000
93	A	101	LYS	1	0.885	0.945	27.831	0.442	0.442	0.000	0.000	0.000	0.000
94	A	102	VAL	0	0.033	0.025	28.266	-0.026	-0.026	0.000	0.000	0.000	0.000
95	A	103	VAL	0	-0.040	-0.025	29.434	0.028	0.028	0.000	0.000	0.000	0.000
96	A	104	VAL	0	0.027	0.014	31.717	-0.001	-0.001	0.000	0.000	0.000	0.000
97	A	105	ALA	0	0.041	0.012	33.232	0.013	0.013	0.000	0.000	0.000	0.000
98	A	106	ASN	0	-0.039	-0.023	35.091	0.006	0.006	0.000	0.000	0.000	0.000
99	A	107	ILE	0	-0.013	-0.004	37.661	0.011	0.011	0.000	0.000	0.000	0.000
100	A	108	GLY	0	-0.013	0.004	38.752	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	109	TYR	0	-0.009	0.007	35.036	-0.011	-0.011	0.000	0.000	0.000	0.000
102	A	110	GLU	-1	-0.819	-0.914	33.543	-0.225	-0.225	0.000	0.000	0.000	0.000
103	A	111	GLY	0	0.017	0.017	33.839	0.010	0.010	0.000	0.000	0.000	0.000
104	A	112	GLN	0	-0.070	-0.052	32.287	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	113	TYR	0	0.035	0.020	31.293	0.015	0.015	0.000	0.000	0.000	0.000
106	A	114	HIS	0	0.005	0.002	31.233	-0.015	-0.015	0.000	0.000	0.000	0.000
107	A	115	VAL	0	-0.011	-0.011	27.946	0.022	0.022	0.000	0.000	0.000	0.000
108	A	116	ARG	1	0.853	0.926	29.417	0.562	0.562	0.000	0.000	0.000	0.000
109	A	117	ILE	0	-0.012	-0.007	22.655	-0.006	-0.006	0.000	0.000	0.000	0.000
110	A	118	ILE	0	-0.004	-0.007	25.796	-0.038	-0.038	0.000	0.000	0.000	0.000
111	A	119	ASN	0	0.001	-0.008	22.002	-0.033	-0.033	0.000	0.000	0.000	0.000
112	A	120	GLN	0	0.001	-0.026	24.656	0.011	0.011	0.000	0.000	0.000	0.000
113	A	121	ASP	-1	-0.853	-0.900	22.373	-1.315	-1.315	0.000	0.000	0.000	0.000
114	A	122	ILE	0	-0.109	-0.040	23.793	0.007	0.007	0.000	0.000	0.000	0.000
115	A	123	ASN	0	-0.085	-0.043	27.264	0.003	0.003	0.000	0.000	0.000	0.000
116	A	124	THR	-1	-0.884	-0.939	30.994	-0.685	-0.685	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:9:ASP)