FMO DATABASE

FMODB ID: YR9Z2

Calculation Name: 2EGI-F-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EGI

Chain ID: F

ChEMBL ID:

UniProt ID: O67466

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	123
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1118616.770984
FMO2-HF: Nuclear repulsion	1067179.093762
FMO2-HF: Total energy	-51437.677222
FMO2-MP2: Total energy	-51587.845751

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:PRO)

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

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.
-66.709	-57.906	8.058	-6.838	-10.022	-0.069

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.841 / q_NPA : 0.911

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

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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	ILE	0	-0.011	0.000	2.331	-1.896	0.028	1.057	-0.941	-2.040	-0.005
4	A	5	TYR	0	-0.031	-0.036	5.058	3.865	3.894	-0.001	-0.004	-0.024	0.000
75	A	76	HIS	0	-0.051	-0.033	2.684	-9.564	-8.707	0.205	-0.273	-0.789	-0.001
76	A	77	LEU	0	-0.014	0.003	3.768	2.271	2.848	0.018	-0.187	-0.408	-0.001
77	A	78	ASN	0	0.017	-0.011	2.296	-41.796	-36.466	6.777	-5.381	-6.726	-0.062
78	A	79	LEU	0	0.011	0.010	3.920	6.873	6.959	0.002	-0.052	-0.035	0.000
5	A	6	ARG	1	0.904	0.943	8.123	29.160	29.160	0.000	0.000	0.000	0.000
6	A	7	ARG	1	0.715	0.811	11.127	17.830	17.830	0.000	0.000	0.000	0.000
7	A	8	ARG	1	0.878	0.919	14.389	13.850	13.850	0.000	0.000	0.000	0.000
8	A	9	VAL	0	-0.017	0.018	17.662	0.128	0.128	0.000	0.000	0.000	0.000
9	A	10	GLN	0	-0.023	-0.020	19.830	1.058	1.058	0.000	0.000	0.000	0.000
10	A	11	PHE	0	0.042	0.011	23.044	-0.031	-0.031	0.000	0.000	0.000	0.000
11	A	12	TYR	0	0.000	-0.001	22.557	0.214	0.214	0.000	0.000	0.000	0.000
12	A	13	GLU	-1	-0.767	-0.835	20.331	-14.910	-14.910	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.060	-0.035	23.197	-0.297	-0.297	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.824	-0.921	25.180	-10.936	-10.936	0.000	0.000	0.000	0.000
15	A	16	ALA	0	0.006	-0.006	28.050	0.020	0.020	0.000	0.000	0.000	0.000
16	A	17	GLN	0	-0.049	-0.014	26.938	0.220	0.220	0.000	0.000	0.000	0.000
17	A	18	GLY	0	-0.007	-0.003	27.849	-0.048	-0.048	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.059	-0.031	22.774	-0.372	-0.372	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.008	-0.007	18.827	0.336	0.336	0.000	0.000	0.000	0.000
20	A	21	HIS	0	0.077	0.074	21.706	-0.543	-0.543	0.000	0.000	0.000	0.000
21	A	22	HIS	0	0.026	-0.001	20.291	-0.592	-0.592	0.000	0.000	0.000	0.000
22	A	23	SER	0	-0.047	-0.040	19.665	-0.737	-0.737	0.000	0.000	0.000	0.000
23	A	24	ASN	0	0.003	-0.011	19.754	-0.486	-0.486	0.000	0.000	0.000	0.000
24	A	25	TYR	0	0.046	0.027	14.402	-0.533	-0.533	0.000	0.000	0.000	0.000
25	A	26	PHE	0	0.006	-0.008	14.750	-1.254	-1.254	0.000	0.000	0.000	0.000
26	A	27	ARG	1	0.929	0.979	16.133	12.822	12.822	0.000	0.000	0.000	0.000
27	A	28	TYR	0	-0.001	-0.024	13.305	-0.698	-0.698	0.000	0.000	0.000	0.000
28	A	29	PHE	0	0.002	-0.016	10.642	-1.570	-1.570	0.000	0.000	0.000	0.000
29	A	30	GLU	-1	-0.966	-0.978	12.103	-17.268	-17.268	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.765	-0.825	14.091	-18.350	-18.350	0.000	0.000	0.000	0.000
31	A	32	ALA	0	0.004	0.003	8.647	-0.741	-0.741	0.000	0.000	0.000	0.000
32	A	33	ARG	1	0.896	0.952	9.693	18.823	18.823	0.000	0.000	0.000	0.000
33	A	34	GLY	0	0.000	0.005	11.307	0.052	0.052	0.000	0.000	0.000	0.000
34	A	35	GLU	-1	-0.787	-0.870	11.477	-19.653	-19.653	0.000	0.000	0.000	0.000
35	A	36	PHE	0	-0.008	0.004	6.335	-0.759	-0.759	0.000	0.000	0.000	0.000
36	A	37	LEU	0	-0.005	-0.016	9.462	0.390	0.390	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.788	0.851	12.639	19.199	19.199	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.051	-0.024	10.217	0.444	0.444	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.841	0.918	8.324	29.619	29.619	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.004	0.024	12.660	1.044	1.044	0.000	0.000	0.000	0.000
41	A	42	PHE	0	-0.019	-0.010	14.713	1.633	1.633	0.000	0.000	0.000	0.000
42	A	43	PRO	0	0.032	0.021	16.239	-0.395	-0.395	0.000	0.000	0.000	0.000
43	A	44	TYR	0	0.062	-0.001	17.035	0.917	0.917	0.000	0.000	0.000	0.000
44	A	45	SER	0	-0.025	-0.008	18.665	0.452	0.452	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.900	0.930	20.839	14.716	14.716	0.000	0.000	0.000	0.000
46	A	47	MET	0	-0.031	0.002	17.559	0.122	0.122	0.000	0.000	0.000	0.000
47	A	48	ARG	1	0.937	0.986	21.717	13.589	13.589	0.000	0.000	0.000	0.000
48	A	49	ASP	-1	-0.943	-0.953	24.443	-10.722	-10.722	0.000	0.000	0.000	0.000
49	A	50	MET	0	-0.025	0.005	23.130	0.493	0.493	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.008	-0.002	26.550	0.100	0.100	0.000	0.000	0.000	0.000
51	A	52	LEU	0	-0.098	-0.061	21.816	0.191	0.191	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.890	-0.963	22.165	-12.143	-12.143	0.000	0.000	0.000	0.000
53	A	54	VAL	0	0.001	-0.013	16.178	-0.075	-0.075	0.000	0.000	0.000	0.000
54	A	55	VAL	0	-0.005	0.004	19.619	0.058	0.058	0.000	0.000	0.000	0.000
55	A	56	LEU	0	-0.031	-0.014	17.298	-0.594	-0.594	0.000	0.000	0.000	0.000
56	A	57	LEU	0	-0.025	-0.023	19.094	0.748	0.748	0.000	0.000	0.000	0.000
57	A	58	ASN	0	-0.026	-0.025	17.785	-0.087	-0.087	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.037	0.007	16.772	-0.954	-0.954	0.000	0.000	0.000	0.000
59	A	60	TYR	0	-0.060	-0.028	14.899	1.268	1.268	0.000	0.000	0.000	0.000
60	A	61	CYS	0	-0.022	-0.017	14.899	-1.736	-1.736	0.000	0.000	0.000	0.000
61	A	62	GLU	-1	-0.880	-0.905	14.932	-17.059	-17.059	0.000	0.000	0.000	0.000
62	A	63	TYR	0	-0.012	-0.031	15.308	-1.053	-1.053	0.000	0.000	0.000	0.000
63	A	64	LYS	1	0.954	0.981	16.227	17.388	17.388	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.933	0.959	17.417	15.885	15.885	0.000	0.000	0.000	0.000
65	A	66	PRO	0	0.003	0.013	17.841	-0.663	-0.663	0.000	0.000	0.000	0.000
66	A	67	LEU	0	-0.015	0.010	15.142	-0.318	-0.318	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.023	-0.010	19.207	0.579	0.579	0.000	0.000	0.000	0.000
68	A	69	TYR	0	0.040	-0.007	21.451	-0.316	-0.316	0.000	0.000	0.000	0.000
69	A	70	ASP	-1	-0.841	-0.898	22.172	-12.566	-12.566	0.000	0.000	0.000	0.000
70	A	71	ASP	-1	-0.756	-0.831	17.844	-15.147	-15.147	0.000	0.000	0.000	0.000
71	A	72	VAL	0	-0.004	-0.007	14.566	-0.260	-0.260	0.000	0.000	0.000	0.000
72	A	73	PHE	0	-0.040	-0.024	11.997	-0.136	-0.136	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.817	-0.897	7.611	-31.593	-31.593	0.000	0.000	0.000	0.000
74	A	75	VAL	0	-0.025	-0.020	7.494	0.690	0.690	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.856	-0.898	7.194	-37.121	-37.121	0.000	0.000	0.000	0.000
80	A	81	GLU	-1	-0.817	-0.888	9.892	-16.246	-16.246	0.000	0.000	0.000	0.000
81	A	82	LEU	0	0.046	0.004	12.693	-0.670	-0.670	0.000	0.000	0.000	0.000
82	A	83	SER	0	0.000	0.015	14.544	0.978	0.978	0.000	0.000	0.000	0.000
83	A	84	ARG	1	0.947	0.963	18.331	11.922	11.922	0.000	0.000	0.000	0.000
84	A	85	PHE	0	-0.003	-0.014	20.976	0.302	0.302	0.000	0.000	0.000	0.000
85	A	86	THR	0	-0.057	-0.042	17.887	0.542	0.542	0.000	0.000	0.000	0.000
86	A	87	PHE	0	0.033	0.019	12.399	-0.159	-0.159	0.000	0.000	0.000	0.000
87	A	88	THR	0	-0.006	-0.003	11.914	1.253	1.253	0.000	0.000	0.000	0.000
88	A	89	PHE	0	-0.003	0.013	7.535	-1.357	-1.357	0.000	0.000	0.000	0.000
89	A	90	SER	0	-0.042	-0.054	7.010	2.152	2.152	0.000	0.000	0.000	0.000
90	A	91	TYR	0	-0.005	-0.027	6.334	-4.212	-4.212	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.041	-0.014	6.004	3.874	3.874	0.000	0.000	0.000	0.000
92	A	93	VAL	0	-0.010	0.008	7.111	-2.047	-2.047	0.000	0.000	0.000	0.000
93	A	94	PHE	0	0.013	-0.009	5.625	1.039	1.039	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.859	0.900	10.478	15.564	15.564	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.918	-0.962	13.953	-16.624	-16.624	0.000	0.000	0.000	0.000
96	A	97	ASP	-1	-0.892	-0.936	10.652	-23.242	-23.242	0.000	0.000	0.000	0.000
97	A	98	ILE	0	-0.065	-0.030	11.223	-0.510	-0.510	0.000	0.000	0.000	0.000
98	A	99	ALA	0	-0.032	-0.014	10.385	-0.455	-0.455	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.048	-0.026	11.755	1.478	1.478	0.000	0.000	0.000	0.000
100	A	101	ALA	0	0.024	0.007	12.401	1.463	1.463	0.000	0.000	0.000	0.000
101	A	102	LYS	1	0.918	0.979	10.299	22.477	22.477	0.000	0.000	0.000	0.000
102	A	103	ALA	0	0.048	0.021	10.335	1.955	1.955	0.000	0.000	0.000	0.000
103	A	104	ASN	0	-0.037	-0.020	10.431	-1.706	-1.706	0.000	0.000	0.000	0.000
104	A	105	THR	0	0.044	0.024	12.286	1.054	1.054	0.000	0.000	0.000	0.000
105	A	106	LYS	1	0.851	0.949	13.271	15.159	15.159	0.000	0.000	0.000	0.000
106	A	107	HIS	0	0.037	0.022	13.634	-0.019	-0.019	0.000	0.000	0.000	0.000
107	A	108	CYS	0	-0.011	0.000	17.231	0.150	0.150	0.000	0.000	0.000	0.000
108	A	109	MET	0	0.033	0.028	17.333	-0.163	-0.163	0.000	0.000	0.000	0.000
109	A	110	VAL	0	0.014	0.000	21.239	0.588	0.588	0.000	0.000	0.000	0.000
110	A	111	LYS	1	0.900	0.958	24.717	11.170	11.170	0.000	0.000	0.000	0.000
111	A	112	ASN	0	-0.031	-0.025	26.925	0.142	0.142	0.000	0.000	0.000	0.000
112	A	113	GLY	0	0.046	0.031	29.206	0.360	0.360	0.000	0.000	0.000	0.000
113	A	114	LYS	1	0.937	0.969	29.517	9.379	9.379	0.000	0.000	0.000	0.000
114	A	115	ILE	0	0.026	0.022	24.051	-0.303	-0.303	0.000	0.000	0.000	0.000
115	A	116	VAL	0	-0.038	-0.026	23.884	0.439	0.439	0.000	0.000	0.000	0.000
116	A	117	SER	0	-0.002	0.001	23.387	-0.337	-0.337	0.000	0.000	0.000	0.000
117	A	118	ILE	0	0.001	-0.001	16.687	0.340	0.340	0.000	0.000	0.000	0.000
118	A	119	PRO	0	-0.014	-0.008	20.604	0.158	0.158	0.000	0.000	0.000	0.000
119	A	120	LYS	1	0.890	0.934	19.040	15.495	15.495	0.000	0.000	0.000	0.000
120	A	121	GLU	-1	-0.852	-0.903	19.000	-14.917	-14.917	0.000	0.000	0.000	0.000
121	A	122	VAL	0	0.002	-0.006	15.723	-0.595	-0.595	0.000	0.000	0.000	0.000
122	A	123	LEU	0	-0.043	-0.025	15.386	-0.678	-0.678	0.000	0.000	0.000	0.000
123	A	124	GLU	-2	-1.714	-1.833	11.817	-42.977	-42.977	0.000	0.000	0.000	0.000

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