FMO DATABASE

FMODB ID: ZZ7VN

Calculation Name: 2EIF-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EIF

Chain ID: A

ChEMBL ID:

UniProt ID: Q58625

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	133
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1027164.751141
FMO2-HF: Nuclear repulsion	976164.558073
FMO2-HF: Total energy	-51000.193069
FMO2-MP2: Total energy	-51146.303218

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:0:MET)

Summations of interaction energy for fragment #1(A:0: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.
-23.974	-22.467	0.016	-0.756	-0.768	-0.002

Interaction energy analysis for fragmet #1(A:0:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.833 / q_NPA : 0.904

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	2	ILE	0	0.004	0.012	3.678	-9.239	-7.732	0.016	-0.756	-0.768	-0.002
4	A	3	ILE	0	0.013	0.011	6.514	-0.169	-0.169	0.000	0.000	0.000	0.000
5	A	4	MET	0	0.033	0.020	8.487	1.290	1.290	0.000	0.000	0.000	0.000
6	A	5	PRO	0	0.021	0.011	11.529	0.812	0.812	0.000	0.000	0.000	0.000
7	A	6	GLY	0	0.093	0.042	14.786	0.363	0.363	0.000	0.000	0.000	0.000
8	A	7	THR	0	-0.032	-0.020	13.015	0.216	0.216	0.000	0.000	0.000	0.000
9	A	8	LYS	1	0.923	0.967	14.709	15.682	15.682	0.000	0.000	0.000	0.000
10	A	9	GLN	0	0.035	0.030	10.446	-1.112	-1.112	0.000	0.000	0.000	0.000
11	A	10	VAL	0	-0.031	-0.010	13.677	1.365	1.365	0.000	0.000	0.000	0.000
12	A	11	ASN	0	0.033	0.014	15.188	-2.107	-2.107	0.000	0.000	0.000	0.000
13	A	12	VAL	0	0.048	0.034	15.624	0.885	0.885	0.000	0.000	0.000	0.000
14	A	13	GLY	0	-0.021	-0.034	18.205	0.689	0.689	0.000	0.000	0.000	0.000
15	A	14	SER	0	-0.122	-0.065	19.955	0.572	0.572	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.002	0.020	18.365	0.272	0.272	0.000	0.000	0.000	0.000
17	A	16	LYS	1	0.945	0.964	22.414	11.628	11.628	0.000	0.000	0.000	0.000
18	A	17	VAL	0	0.036	0.009	25.451	-0.346	-0.346	0.000	0.000	0.000	0.000
19	A	18	GLY	0	0.033	0.023	27.745	0.287	0.287	0.000	0.000	0.000	0.000
20	A	19	GLN	0	-0.096	-0.037	20.890	0.306	0.306	0.000	0.000	0.000	0.000
21	A	20	TYR	0	0.050	0.015	21.877	-0.110	-0.110	0.000	0.000	0.000	0.000
22	A	21	VAL	0	-0.053	-0.038	16.842	-0.344	-0.344	0.000	0.000	0.000	0.000
23	A	22	MET	0	-0.008	0.017	14.040	0.902	0.902	0.000	0.000	0.000	0.000
24	A	23	ILE	0	-0.028	-0.022	15.098	-0.667	-0.667	0.000	0.000	0.000	0.000
25	A	24	ASP	-1	-0.833	-0.913	13.019	-19.241	-19.241	0.000	0.000	0.000	0.000
26	A	25	GLY	0	-0.013	-0.004	13.301	0.080	0.080	0.000	0.000	0.000	0.000
27	A	26	VAL	0	0.023	0.014	13.875	0.619	0.619	0.000	0.000	0.000	0.000
28	A	27	PRO	0	0.029	0.024	17.684	-0.325	-0.325	0.000	0.000	0.000	0.000
29	A	28	CYS	0	-0.059	-0.024	19.335	0.932	0.932	0.000	0.000	0.000	0.000
30	A	29	GLU	-1	-0.857	-0.940	21.668	-11.554	-11.554	0.000	0.000	0.000	0.000
31	A	30	ILE	0	-0.066	-0.030	21.252	-0.036	-0.036	0.000	0.000	0.000	0.000
32	A	31	VAL	0	0.024	0.001	24.801	0.447	0.447	0.000	0.000	0.000	0.000
33	A	32	ASP	-1	-0.876	-0.933	26.345	-10.686	-10.686	0.000	0.000	0.000	0.000
34	A	33	ILE	0	-0.005	0.002	23.899	-0.690	-0.690	0.000	0.000	0.000	0.000
35	A	34	SER	0	0.003	0.007	25.512	0.452	0.452	0.000	0.000	0.000	0.000
36	A	35	VAL	0	-0.027	-0.012	24.904	-0.617	-0.617	0.000	0.000	0.000	0.000
37	A	36	SER	0	-0.039	-0.023	25.640	0.252	0.252	0.000	0.000	0.000	0.000
38	A	37	LYS	1	1.005	1.002	27.346	10.013	10.013	0.000	0.000	0.000	0.000
39	A	38	PRO	0	0.033	0.025	27.035	-0.462	-0.462	0.000	0.000	0.000	0.000
40	A	39	GLY	0	-0.020	-0.012	26.229	0.323	0.323	0.000	0.000	0.000	0.000
41	A	40	LYS	1	0.923	0.936	27.217	11.089	11.089	0.000	0.000	0.000	0.000
42	A	41	HIS	0	0.009	0.007	24.390	0.613	0.613	0.000	0.000	0.000	0.000
43	A	42	GLY	0	0.058	0.041	26.002	-0.260	-0.260	0.000	0.000	0.000	0.000
44	A	43	GLY	0	0.003	0.005	22.811	-0.051	-0.051	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.037	0.026	23.185	0.351	0.351	0.000	0.000	0.000	0.000
46	A	45	LYS	1	0.871	0.939	17.153	16.537	16.537	0.000	0.000	0.000	0.000
47	A	46	ALA	0	0.044	0.019	20.800	0.754	0.754	0.000	0.000	0.000	0.000
48	A	47	ARG	1	0.869	0.941	20.543	11.118	11.118	0.000	0.000	0.000	0.000
49	A	48	VAL	0	0.003	0.008	19.954	0.589	0.589	0.000	0.000	0.000	0.000
50	A	49	VAL	0	0.012	-0.004	21.166	-0.578	-0.578	0.000	0.000	0.000	0.000
51	A	50	GLY	0	0.043	0.006	22.995	0.279	0.279	0.000	0.000	0.000	0.000
52	A	51	ILE	0	-0.013	0.001	23.813	0.014	0.014	0.000	0.000	0.000	0.000
53	A	52	GLY	0	0.028	0.018	22.728	-0.265	-0.265	0.000	0.000	0.000	0.000
54	A	53	ILE	0	-0.035	-0.014	22.610	0.562	0.562	0.000	0.000	0.000	0.000
55	A	54	PHE	0	0.039	0.004	22.545	0.539	0.539	0.000	0.000	0.000	0.000
56	A	55	GLU	-1	-0.900	-0.945	22.457	-13.498	-13.498	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.916	0.954	25.719	10.735	10.735	0.000	0.000	0.000	0.000
58	A	57	VAL	0	0.009	0.018	22.405	0.255	0.255	0.000	0.000	0.000	0.000
59	A	58	LYS	1	0.883	0.938	24.356	12.107	12.107	0.000	0.000	0.000	0.000
60	A	59	LYS	1	0.851	0.916	17.619	16.690	16.690	0.000	0.000	0.000	0.000
61	A	60	GLU	-1	-0.848	-0.935	19.982	-12.355	-12.355	0.000	0.000	0.000	0.000
62	A	61	PHE	0	0.027	0.026	16.021	-0.900	-0.900	0.000	0.000	0.000	0.000
63	A	62	VAL	0	0.040	0.007	17.420	0.884	0.884	0.000	0.000	0.000	0.000
64	A	63	ALA	0	0.015	0.016	15.403	-0.870	-0.870	0.000	0.000	0.000	0.000
65	A	64	PRO	0	-0.014	-0.019	15.499	1.121	1.121	0.000	0.000	0.000	0.000
66	A	65	THR	0	0.045	0.033	17.532	-0.775	-0.775	0.000	0.000	0.000	0.000
67	A	66	SER	0	-0.005	0.003	18.394	-0.156	-0.156	0.000	0.000	0.000	0.000
68	A	67	SER	0	-0.078	-0.059	13.349	-1.010	-1.010	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.909	0.946	10.928	21.871	21.871	0.000	0.000	0.000	0.000
70	A	69	VAL	0	0.029	0.016	11.980	-1.180	-1.180	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.840	-0.923	9.965	-27.947	-27.947	0.000	0.000	0.000	0.000
72	A	71	VAL	0	-0.044	-0.020	13.336	1.064	1.064	0.000	0.000	0.000	0.000
73	A	72	PRO	0	0.054	0.025	16.881	-0.562	-0.562	0.000	0.000	0.000	0.000
74	A	73	ILE	0	-0.105	-0.057	18.278	0.631	0.631	0.000	0.000	0.000	0.000
75	A	74	ILE	0	-0.030	-0.018	20.722	-0.152	-0.152	0.000	0.000	0.000	0.000
76	A	75	ASP	-1	-0.828	-0.887	24.192	-11.062	-11.062	0.000	0.000	0.000	0.000
77	A	76	ARG	1	0.885	0.929	26.797	11.014	11.014	0.000	0.000	0.000	0.000
78	A	77	ARG	1	0.775	0.871	29.527	10.533	10.533	0.000	0.000	0.000	0.000
79	A	78	LYS	1	0.845	0.919	32.903	8.390	8.390	0.000	0.000	0.000	0.000
80	A	79	GLY	0	0.030	0.012	36.601	-0.097	-0.097	0.000	0.000	0.000	0.000
81	A	80	GLN	0	-0.047	-0.021	38.034	0.093	0.093	0.000	0.000	0.000	0.000
82	A	81	VAL	0	0.021	0.007	40.374	-0.147	-0.147	0.000	0.000	0.000	0.000
83	A	82	LEU	0	-0.048	-0.018	40.868	0.232	0.232	0.000	0.000	0.000	0.000
84	A	83	ALA	0	0.007	-0.007	42.117	0.228	0.228	0.000	0.000	0.000	0.000
85	A	84	ILE	0	0.014	0.004	41.017	-0.214	-0.214	0.000	0.000	0.000	0.000
86	A	85	MET	0	-0.070	-0.027	39.030	0.353	0.353	0.000	0.000	0.000	0.000
87	A	86	GLY	0	-0.010	-0.001	39.594	-0.203	-0.203	0.000	0.000	0.000	0.000
88	A	87	ASP	-1	-0.912	-0.964	34.572	-9.113	-9.113	0.000	0.000	0.000	0.000
89	A	88	MET	0	-0.025	-0.001	31.741	-0.369	-0.369	0.000	0.000	0.000	0.000
90	A	89	VAL	0	0.004	-0.009	36.629	0.334	0.334	0.000	0.000	0.000	0.000
91	A	90	GLN	0	-0.004	0.016	36.764	-0.068	-0.068	0.000	0.000	0.000	0.000
92	A	91	ILE	0	-0.014	-0.014	34.347	0.252	0.252	0.000	0.000	0.000	0.000
93	A	92	MET	0	0.002	0.010	37.794	-0.073	-0.073	0.000	0.000	0.000	0.000
94	A	93	ASP	-1	-0.704	-0.808	34.040	-9.502	-9.502	0.000	0.000	0.000	0.000
95	A	94	LEU	0	-0.009	-0.017	36.782	0.179	0.179	0.000	0.000	0.000	0.000
96	A	95	GLN	0	-0.071	-0.017	33.142	-0.069	-0.069	0.000	0.000	0.000	0.000
97	A	96	THR	0	-0.063	-0.086	32.887	0.225	0.225	0.000	0.000	0.000	0.000
98	A	97	TYR	0	-0.043	-0.020	36.355	0.180	0.180	0.000	0.000	0.000	0.000
99	A	98	GLU	-1	-0.895	-0.901	32.045	-10.029	-10.029	0.000	0.000	0.000	0.000
100	A	99	THR	0	-0.022	-0.020	36.452	0.110	0.110	0.000	0.000	0.000	0.000
101	A	100	LEU	0	-0.035	-0.016	31.389	-0.208	-0.208	0.000	0.000	0.000	0.000
102	A	101	GLU	-1	-0.846	-0.932	32.869	-8.567	-8.567	0.000	0.000	0.000	0.000
103	A	102	LEU	0	-0.038	-0.019	31.424	-0.456	-0.456	0.000	0.000	0.000	0.000
104	A	103	PRO	0	0.018	-0.002	30.281	0.278	0.278	0.000	0.000	0.000	0.000
105	A	104	ILE	0	-0.025	0.002	33.575	0.028	0.028	0.000	0.000	0.000	0.000
106	A	105	PRO	0	-0.058	-0.017	35.021	-0.203	-0.203	0.000	0.000	0.000	0.000
107	A	106	GLU	-1	-0.970	-0.996	32.989	-9.656	-9.656	0.000	0.000	0.000	0.000
108	A	107	GLY	0	-0.026	0.007	37.117	0.219	0.219	0.000	0.000	0.000	0.000
109	A	108	ILE	0	0.015	-0.010	39.615	-0.098	-0.098	0.000	0.000	0.000	0.000
110	A	109	GLU	-1	-0.914	-0.968	41.956	-7.593	-7.593	0.000	0.000	0.000	0.000
111	A	110	GLY	0	0.024	0.012	44.469	-0.069	-0.069	0.000	0.000	0.000	0.000
112	A	111	LEU	0	-0.052	-0.013	39.858	-0.082	-0.082	0.000	0.000	0.000	0.000
113	A	112	GLU	-1	-0.939	-0.974	43.779	-6.576	-6.576	0.000	0.000	0.000	0.000
114	A	113	PRO	0	-0.027	-0.027	45.398	-0.087	-0.087	0.000	0.000	0.000	0.000
115	A	114	GLY	0	-0.014	0.003	45.596	0.171	0.171	0.000	0.000	0.000	0.000
116	A	115	GLY	0	0.030	0.024	45.174	0.035	0.035	0.000	0.000	0.000	0.000
117	A	116	GLU	-1	-0.915	-0.964	40.783	-7.949	-7.949	0.000	0.000	0.000	0.000
118	A	117	VAL	0	0.020	0.003	37.227	0.010	0.010	0.000	0.000	0.000	0.000
119	A	118	GLU	-1	-0.842	-0.904	34.860	-8.683	-8.683	0.000	0.000	0.000	0.000
120	A	119	TYR	0	-0.057	-0.059	30.692	-0.208	-0.208	0.000	0.000	0.000	0.000
121	A	120	ILE	0	-0.023	-0.020	26.511	-0.109	-0.109	0.000	0.000	0.000	0.000
122	A	121	GLU	-1	-0.842	-0.917	22.676	-14.193	-14.193	0.000	0.000	0.000	0.000
123	A	122	ALA	0	-0.005	-0.018	21.584	-0.099	-0.099	0.000	0.000	0.000	0.000
124	A	123	VAL	0	-0.067	-0.036	16.741	-0.201	-0.201	0.000	0.000	0.000	0.000
125	A	124	GLY	0	-0.001	0.010	19.290	-0.543	-0.543	0.000	0.000	0.000	0.000
126	A	125	GLN	0	-0.060	-0.023	20.206	0.924	0.924	0.000	0.000	0.000	0.000
127	A	126	TYR	0	0.095	0.029	24.075	-0.117	-0.117	0.000	0.000	0.000	0.000
128	A	127	LYS	1	0.856	0.941	27.563	11.009	11.009	0.000	0.000	0.000	0.000
129	A	128	ILE	0	0.089	0.049	30.340	-0.058	-0.058	0.000	0.000	0.000	0.000
130	A	129	THR	0	-0.162	-0.101	30.791	-0.206	-0.206	0.000	0.000	0.000	0.000
131	A	130	ARG	1	0.818	0.883	33.753	8.111	8.111	0.000	0.000	0.000	0.000
132	A	131	VAL	0	0.027	0.028	37.466	-0.129	-0.129	0.000	0.000	0.000	0.000
133	A	132	ILE	-1	-0.832	-0.882	40.772	-7.772	-7.772	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:MET)