FMO DATABASE

FMODB ID: 4GMYN

Calculation Name: 2EA9-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EA9

Chain ID: A

ChEMBL ID:

UniProt ID: P52141

Base Structure: X-ray

Registration Date: 2025-10-11

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	103
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-778770.147191
FMO2-HF: Nuclear repulsion	737726.637044
FMO2-HF: Total energy	-41043.510147
FMO2-MP2: Total energy	-41160.354993

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:8:MET)

Summations of interaction energy for fragment #1(A:8:MET)

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.
-40.532	-33.038	3.348	-3.841	-7.001	-0.04

Interaction energy analysis for fragmet #1(A:8:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.795 / q_NPA : 0.889

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	10	ASN	0	0.092	0.056	3.462	6.192	8.611	0.016	-0.992	-1.443	-0.003
4	A	11	THR	0	0.010	-0.012	2.597	-14.322	-11.401	1.933	-2.230	-2.624	-0.029
5	A	12	THR	0	0.019	-0.004	3.209	-1.564	-0.821	0.144	0.000	-0.888	-0.003
6	A	13	TRP	0	0.074	0.040	3.847	0.975	1.067	0.005	-0.007	-0.090	0.000
8	A	15	LEU	0	-0.061	-0.047	2.477	0.148	0.362	0.966	-0.181	-0.999	-0.002
33	A	40	ARG	1	0.805	0.915	2.750	46.362	47.467	0.284	-0.431	-0.957	-0.003
7	A	14	GLY	0	0.049	0.036	6.376	2.123	2.123	0.000	0.000	0.000	0.000
9	A	16	GLN	0	-0.026	-0.017	6.634	2.200	2.200	0.000	0.000	0.000	0.000
10	A	17	ARG	1	0.856	0.937	9.063	21.404	21.404	0.000	0.000	0.000	0.000
11	A	18	ASP	-1	-0.874	-0.936	11.820	-17.346	-17.346	0.000	0.000	0.000	0.000
12	A	19	ILE	0	0.000	0.007	14.631	-0.171	-0.171	0.000	0.000	0.000	0.000
13	A	20	THR	0	-0.052	-0.013	14.700	-1.824	-1.824	0.000	0.000	0.000	0.000
14	A	21	PRO	0	-0.025	-0.010	16.156	0.751	0.751	0.000	0.000	0.000	0.000
15	A	22	ARG	1	0.844	0.908	9.297	23.021	23.021	0.000	0.000	0.000	0.000
16	A	23	LEU	0	-0.014	-0.002	12.388	-1.325	-1.325	0.000	0.000	0.000	0.000
17	A	24	GLY	0	-0.015	0.006	9.431	1.012	1.012	0.000	0.000	0.000	0.000
18	A	25	ALA	0	0.009	-0.013	9.817	-1.306	-1.306	0.000	0.000	0.000	0.000
19	A	26	ARG	1	0.873	0.957	7.694	32.868	32.868	0.000	0.000	0.000	0.000
20	A	27	LEU	0	0.015	0.020	10.293	-1.257	-1.257	0.000	0.000	0.000	0.000
21	A	28	VAL	0	0.000	-0.010	12.775	-0.695	-0.695	0.000	0.000	0.000	0.000
22	A	29	GLN	0	-0.020	-0.020	14.871	0.305	0.305	0.000	0.000	0.000	0.000
23	A	30	GLU	-1	-0.888	-0.940	18.275	-15.216	-15.216	0.000	0.000	0.000	0.000
24	A	31	GLY	0	-0.028	-0.011	21.340	0.562	0.562	0.000	0.000	0.000	0.000
25	A	32	ASN	0	-0.010	-0.009	23.199	-0.506	-0.506	0.000	0.000	0.000	0.000
26	A	33	GLN	0	-0.012	0.005	22.745	0.123	0.123	0.000	0.000	0.000	0.000
27	A	34	LEU	0	-0.034	-0.022	17.547	-0.716	-0.716	0.000	0.000	0.000	0.000
28	A	35	HIS	0	-0.025	-0.002	17.010	-0.256	-0.256	0.000	0.000	0.000	0.000
29	A	36	TYR	0	0.003	-0.016	14.006	-1.651	-1.651	0.000	0.000	0.000	0.000
30	A	37	LEU	0	0.000	0.003	10.560	0.378	0.378	0.000	0.000	0.000	0.000
31	A	38	ALA	0	0.011	-0.001	11.047	-1.684	-1.684	0.000	0.000	0.000	0.000
32	A	39	ASP	-1	-0.892	-0.953	6.558	-42.683	-42.683	0.000	0.000	0.000	0.000
34	A	41	ALA	0	0.081	0.054	7.537	3.028	3.028	0.000	0.000	0.000	0.000
35	A	42	SER	0	-0.077	-0.056	6.800	-2.636	-2.636	0.000	0.000	0.000	0.000
36	A	43	ILE	0	0.039	0.031	8.951	2.231	2.231	0.000	0.000	0.000	0.000
37	A	44	THR	0	-0.049	-0.020	9.835	-2.511	-2.511	0.000	0.000	0.000	0.000
38	A	45	GLY	0	0.044	0.017	11.906	1.536	1.536	0.000	0.000	0.000	0.000
39	A	46	LYS	1	0.902	0.945	15.196	13.573	13.573	0.000	0.000	0.000	0.000
40	A	47	PHE	0	0.042	0.040	15.761	0.549	0.549	0.000	0.000	0.000	0.000
41	A	48	SER	0	-0.048	-0.067	20.064	0.183	0.183	0.000	0.000	0.000	0.000
42	A	49	ASP	-1	-0.861	-0.946	23.383	-12.922	-12.922	0.000	0.000	0.000	0.000
43	A	50	ALA	0	-0.019	-0.006	24.941	0.126	0.126	0.000	0.000	0.000	0.000
44	A	51	GLU	-1	-0.795	-0.869	22.603	-13.183	-13.183	0.000	0.000	0.000	0.000
45	A	52	CYS	0	-0.022	-0.002	21.007	-0.325	-0.325	0.000	0.000	0.000	0.000
46	A	53	PRO	0	0.057	0.031	22.196	-0.155	-0.155	0.000	0.000	0.000	0.000
47	A	54	LYS	1	0.828	0.906	24.730	11.464	11.464	0.000	0.000	0.000	0.000
48	A	55	LEU	0	0.022	0.010	17.299	0.061	0.061	0.000	0.000	0.000	0.000
49	A	56	ASP	-1	-0.886	-0.957	20.300	-15.462	-15.462	0.000	0.000	0.000	0.000
50	A	57	VAL	0	-0.068	-0.027	21.929	0.163	0.163	0.000	0.000	0.000	0.000
51	A	58	VAL	0	-0.027	-0.009	21.599	0.162	0.162	0.000	0.000	0.000	0.000
52	A	59	PHE	0	0.010	0.015	15.180	-0.205	-0.205	0.000	0.000	0.000	0.000
53	A	60	PRO	0	0.015	0.004	20.526	-0.201	-0.201	0.000	0.000	0.000	0.000
54	A	61	HIS	0	0.004	0.019	22.450	0.356	0.356	0.000	0.000	0.000	0.000
55	A	62	PHE	0	0.057	0.016	19.998	0.156	0.156	0.000	0.000	0.000	0.000
56	A	63	ILE	0	-0.015	-0.001	17.194	-0.111	-0.111	0.000	0.000	0.000	0.000
57	A	64	SER	0	-0.017	-0.014	20.940	0.357	0.357	0.000	0.000	0.000	0.000
58	A	65	GLN	0	-0.015	-0.028	23.442	0.170	0.170	0.000	0.000	0.000	0.000
59	A	66	ILE	0	0.005	0.004	17.867	0.168	0.168	0.000	0.000	0.000	0.000
60	A	67	GLU	-1	-0.835	-0.921	21.878	-13.320	-13.320	0.000	0.000	0.000	0.000
61	A	68	SER	0	-0.050	-0.011	23.740	0.481	0.481	0.000	0.000	0.000	0.000
62	A	69	MET	0	0.013	0.002	23.455	0.067	0.067	0.000	0.000	0.000	0.000
63	A	70	LEU	0	-0.050	-0.019	19.864	0.056	0.056	0.000	0.000	0.000	0.000
64	A	71	THR	0	-0.086	-0.047	24.155	0.281	0.281	0.000	0.000	0.000	0.000
65	A	72	THR	0	-0.078	-0.075	27.823	0.252	0.252	0.000	0.000	0.000	0.000
66	A	73	GLY	0	-0.023	0.004	26.482	0.316	0.316	0.000	0.000	0.000	0.000
67	A	74	GLU	-1	-0.894	-0.917	26.014	-10.686	-10.686	0.000	0.000	0.000	0.000
68	A	75	LEU	0	0.004	0.011	18.744	-0.325	-0.325	0.000	0.000	0.000	0.000
69	A	76	ASN	0	0.063	0.028	21.699	-0.061	-0.061	0.000	0.000	0.000	0.000
70	A	77	PRO	0	0.050	0.011	19.667	-0.505	-0.505	0.000	0.000	0.000	0.000
71	A	78	ARG	1	0.930	0.953	19.191	10.997	10.997	0.000	0.000	0.000	0.000
72	A	79	HIS	0	-0.060	-0.027	20.046	0.400	0.400	0.000	0.000	0.000	0.000
73	A	80	ALA	0	-0.024	-0.007	16.072	-0.399	-0.399	0.000	0.000	0.000	0.000
74	A	81	GLN	0	-0.047	-0.041	17.603	0.788	0.788	0.000	0.000	0.000	0.000
75	A	82	CYS	0	-0.052	-0.005	16.319	-0.232	-0.232	0.000	0.000	0.000	0.000
76	A	83	VAL	0	0.017	0.019	18.078	0.749	0.749	0.000	0.000	0.000	0.000
77	A	84	THR	0	-0.007	-0.014	19.355	-0.595	-0.595	0.000	0.000	0.000	0.000
78	A	85	LEU	0	-0.021	0.001	20.836	0.599	0.599	0.000	0.000	0.000	0.000
79	A	86	TYR	0	0.033	-0.003	22.502	-0.333	-0.333	0.000	0.000	0.000	0.000
80	A	87	HIS	0	0.019	0.000	24.757	-0.006	-0.006	0.000	0.000	0.000	0.000
81	A	88	ASN	0	-0.036	-0.025	25.511	-0.187	-0.187	0.000	0.000	0.000	0.000
82	A	89	GLY	0	0.014	0.012	26.991	-0.048	-0.048	0.000	0.000	0.000	0.000
83	A	90	PHE	0	-0.010	0.012	20.685	-0.246	-0.246	0.000	0.000	0.000	0.000
84	A	91	THR	0	0.068	0.036	20.164	0.660	0.660	0.000	0.000	0.000	0.000
85	A	92	CYS	0	-0.055	-0.010	17.981	-1.048	-1.048	0.000	0.000	0.000	0.000
86	A	93	GLU	-1	-0.792	-0.847	15.325	-16.222	-16.222	0.000	0.000	0.000	0.000
87	A	94	ALA	0	0.037	-0.002	15.340	-1.156	-1.156	0.000	0.000	0.000	0.000
88	A	95	ASP	-1	-0.713	-0.868	13.889	-15.584	-15.584	0.000	0.000	0.000	0.000
89	A	96	THR	0	0.008	0.017	14.078	-1.335	-1.335	0.000	0.000	0.000	0.000
90	A	97	LEU	0	-0.102	-0.056	10.187	-1.135	-1.135	0.000	0.000	0.000	0.000
91	A	98	GLY	0	0.009	0.015	14.285	-0.040	-0.040	0.000	0.000	0.000	0.000
92	A	99	SER	0	-0.056	-0.042	13.130	0.065	0.065	0.000	0.000	0.000	0.000
93	A	100	CYS	0	-0.075	-0.036	15.159	-0.012	-0.012	0.000	0.000	0.000	0.000
94	A	101	GLY	0	0.047	0.026	16.080	0.450	0.450	0.000	0.000	0.000	0.000
95	A	102	TYR	0	-0.066	-0.027	10.699	-1.772	-1.772	0.000	0.000	0.000	0.000
96	A	103	VAL	0	0.041	0.026	13.796	0.953	0.953	0.000	0.000	0.000	0.000
97	A	104	TYR	0	-0.083	-0.038	7.538	-3.290	-3.290	0.000	0.000	0.000	0.000
98	A	105	ILE	0	0.044	0.011	11.471	1.547	1.547	0.000	0.000	0.000	0.000
99	A	106	ALA	0	-0.046	-0.034	11.551	-2.097	-2.097	0.000	0.000	0.000	0.000
100	A	107	VAL	0	0.019	0.019	13.403	1.186	1.186	0.000	0.000	0.000	0.000
101	A	108	TYR	0	-0.031	-0.054	15.799	-0.712	-0.712	0.000	0.000	0.000	0.000
102	A	109	PRO	0	-0.013	0.005	18.361	0.436	0.436	0.000	0.000	0.000	0.000
103	A	110	THR	-1	-0.939	-0.987	21.797	-11.943	-11.943	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:MET)