FMO DATABASE

FMODB ID: 24GGR

Calculation Name: 1EW3-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1EW3

Chain ID: A

ChEMBL ID:

UniProt ID: Q95182

Base Structure: X-ray

Registration Date: 2025-09-02

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	158
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1744633.476818
FMO2-HF: Nuclear repulsion	1679307.729873
FMO2-HF: Total energy	-65325.746945
FMO2-MP2: Total energy	-65517.922658

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:23:VAL)

Summations of interaction energy for fragment #1(A:23:VAL)

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.
-271.605	-269.128	16.439	-10.342	-8.574	-0.122

Interaction energy analysis for fragmet #1(A:23:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.773 / q_NPA : 0.869

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	25	ILE	0	0.032	0.035	3.848	3.787	5.450	-0.009	-0.663	-0.991	-0.002
92	A	114	PHE	0	-0.025	-0.029	4.452	-8.111	-7.891	-0.001	-0.093	-0.126	-0.001
93	A	115	GLU	-1	-0.854	-0.926	1.684	-123.826	-126.677	14.874	-7.335	-4.688	-0.099
94	A	116	ASN	0	0.004	0.003	4.897	6.735	6.820	-0.001	-0.005	-0.079	0.000
130	A	152	GLU	-1	-0.870	-0.927	2.319	-76.729	-73.795	1.570	-2.165	-2.339	-0.020
133	A	155	LYS	1	0.765	0.873	3.437	55.879	56.170	0.006	-0.057	-0.240	0.000
134	A	156	ILE	0	-0.041	-0.028	3.833	2.295	2.430	0.000	-0.024	-0.111	0.000
4	A	26	ARG	1	0.904	0.955	6.084	38.717	38.717	0.000	0.000	0.000	0.000
5	A	27	ASN	0	0.053	0.019	9.556	0.289	0.289	0.000	0.000	0.000	0.000
6	A	28	PHE	0	0.043	0.024	12.207	-0.384	-0.384	0.000	0.000	0.000	0.000
7	A	29	ASP	-1	-0.844	-0.892	13.820	-15.707	-15.707	0.000	0.000	0.000	0.000
8	A	30	ILE	0	0.028	-0.004	16.846	0.115	0.115	0.000	0.000	0.000	0.000
9	A	31	SER	0	-0.088	-0.056	19.446	0.641	0.641	0.000	0.000	0.000	0.000
10	A	32	LYS	1	0.804	0.893	14.064	21.787	21.787	0.000	0.000	0.000	0.000
11	A	33	ILE	0	-0.003	0.003	16.946	-0.423	-0.423	0.000	0.000	0.000	0.000
12	A	34	SER	0	-0.023	0.009	18.857	-0.033	-0.033	0.000	0.000	0.000	0.000
13	A	35	GLY	0	0.046	0.028	21.352	-0.426	-0.426	0.000	0.000	0.000	0.000
14	A	36	GLU	-1	-0.833	-0.905	22.068	-13.097	-13.097	0.000	0.000	0.000	0.000
15	A	37	TRP	0	-0.084	-0.037	13.357	-1.409	-1.409	0.000	0.000	0.000	0.000
16	A	38	TYR	0	0.061	0.040	17.542	0.843	0.843	0.000	0.000	0.000	0.000
17	A	39	SER	0	0.045	0.023	16.517	-1.278	-1.278	0.000	0.000	0.000	0.000
18	A	40	ILE	0	-0.058	-0.011	13.070	0.789	0.789	0.000	0.000	0.000	0.000
19	A	41	PHE	0	-0.025	-0.026	10.971	0.372	0.372	0.000	0.000	0.000	0.000
20	A	42	LEU	0	0.038	0.040	15.244	0.001	0.001	0.000	0.000	0.000	0.000
21	A	43	ALA	0	-0.025	-0.023	15.067	-0.092	-0.092	0.000	0.000	0.000	0.000
22	A	44	SER	0	0.025	0.006	17.016	-0.269	-0.269	0.000	0.000	0.000	0.000
23	A	45	ASP	-1	-0.815	-0.895	19.703	-14.675	-14.675	0.000	0.000	0.000	0.000
24	A	46	VAL	0	0.018	0.021	21.544	0.633	0.633	0.000	0.000	0.000	0.000
25	A	47	LYS	1	0.874	0.960	21.848	13.304	13.304	0.000	0.000	0.000	0.000
26	A	48	GLU	-1	-0.867	-0.929	24.202	-10.427	-10.427	0.000	0.000	0.000	0.000
27	A	49	LYS	1	0.855	0.920	24.122	11.310	11.310	0.000	0.000	0.000	0.000
28	A	50	ILE	0	-0.033	-0.006	19.844	-0.132	-0.132	0.000	0.000	0.000	0.000
29	A	51	GLU	-1	-0.902	-0.950	23.635	-11.994	-11.994	0.000	0.000	0.000	0.000
30	A	52	GLU	-1	-0.836	-0.922	26.293	-11.185	-11.185	0.000	0.000	0.000	0.000
31	A	53	ASN	0	-0.005	-0.008	29.130	0.191	0.191	0.000	0.000	0.000	0.000
32	A	54	GLY	0	0.003	0.029	27.458	0.214	0.214	0.000	0.000	0.000	0.000
33	A	55	SER	0	-0.044	-0.062	27.381	-0.319	-0.319	0.000	0.000	0.000	0.000
34	A	56	MET	0	0.015	0.022	22.338	-0.073	-0.073	0.000	0.000	0.000	0.000
35	A	57	ARG	1	0.783	0.879	22.493	11.513	11.513	0.000	0.000	0.000	0.000
36	A	58	VAL	0	-0.029	0.006	21.867	0.554	0.554	0.000	0.000	0.000	0.000
37	A	59	PHE	0	-0.008	-0.035	21.323	-0.872	-0.872	0.000	0.000	0.000	0.000
38	A	60	VAL	0	-0.026	0.008	18.353	0.546	0.546	0.000	0.000	0.000	0.000
39	A	61	ASP	-1	-0.766	-0.882	21.589	-12.292	-12.292	0.000	0.000	0.000	0.000
40	A	62	VAL	0	0.020	0.006	22.598	-0.636	-0.636	0.000	0.000	0.000	0.000
41	A	63	ILE	0	0.006	0.009	18.708	0.235	0.235	0.000	0.000	0.000	0.000
42	A	64	ARG	1	0.855	0.920	22.940	11.025	11.025	0.000	0.000	0.000	0.000
43	A	65	ALA	0	0.036	0.022	24.409	-0.187	-0.187	0.000	0.000	0.000	0.000
44	A	66	LEU	0	-0.066	-0.033	25.792	0.522	0.522	0.000	0.000	0.000	0.000
45	A	67	ASP	-1	-0.909	-0.959	28.791	-9.703	-9.703	0.000	0.000	0.000	0.000
46	A	68	ASN	0	-0.053	-0.025	30.998	-0.067	-0.067	0.000	0.000	0.000	0.000
47	A	69	SER	0	-0.074	-0.039	26.020	-0.244	-0.244	0.000	0.000	0.000	0.000
48	A	70	SER	0	0.026	0.002	25.546	-0.438	-0.438	0.000	0.000	0.000	0.000
49	A	71	LEU	0	-0.030	-0.015	20.493	-0.009	-0.009	0.000	0.000	0.000	0.000
50	A	72	TYR	0	-0.059	-0.081	24.805	0.472	0.472	0.000	0.000	0.000	0.000
51	A	73	ALA	0	0.025	0.007	22.786	-0.476	-0.476	0.000	0.000	0.000	0.000
52	A	74	GLU	-1	-0.821	-0.859	24.826	-10.346	-10.346	0.000	0.000	0.000	0.000
53	A	75	TYR	0	0.002	-0.021	20.088	-0.447	-0.447	0.000	0.000	0.000	0.000
54	A	76	GLN	0	-0.004	-0.017	25.575	0.082	0.082	0.000	0.000	0.000	0.000
55	A	77	THR	0	-0.051	-0.045	25.885	-0.386	-0.386	0.000	0.000	0.000	0.000
56	A	78	LYS	1	0.863	0.911	27.995	10.709	10.709	0.000	0.000	0.000	0.000
57	A	79	VAL	0	0.009	0.015	30.421	-0.068	-0.068	0.000	0.000	0.000	0.000
58	A	80	ASN	0	-0.048	-0.042	33.465	0.119	0.119	0.000	0.000	0.000	0.000
59	A	81	GLY	0	-0.022	-0.006	33.681	0.212	0.212	0.000	0.000	0.000	0.000
60	A	82	GLU	-1	-0.945	-0.969	34.275	-8.263	-8.263	0.000	0.000	0.000	0.000
61	A	83	CYS	0	-0.047	-0.016	24.899	-0.269	-0.269	0.000	0.000	0.000	0.000
62	A	84	THR	0	-0.003	-0.008	31.588	0.294	0.294	0.000	0.000	0.000	0.000
63	A	85	GLU	-1	-0.852	-0.925	29.691	-10.577	-10.577	0.000	0.000	0.000	0.000
64	A	86	PHE	0	-0.058	-0.025	27.484	0.432	0.432	0.000	0.000	0.000	0.000
65	A	87	PRO	0	0.002	0.014	28.637	-0.391	-0.391	0.000	0.000	0.000	0.000
66	A	88	MET	0	-0.022	-0.006	24.538	0.055	0.055	0.000	0.000	0.000	0.000
67	A	89	VAL	0	-0.015	-0.017	27.093	-0.026	-0.026	0.000	0.000	0.000	0.000
68	A	90	PHE	0	-0.016	-0.011	21.758	-0.061	-0.061	0.000	0.000	0.000	0.000
69	A	91	ASP	-1	-0.850	-0.901	25.073	-11.031	-11.031	0.000	0.000	0.000	0.000
70	A	92	LYS	1	0.890	0.935	22.460	13.440	13.440	0.000	0.000	0.000	0.000
71	A	93	THR	0	-0.051	-0.027	22.846	0.481	0.481	0.000	0.000	0.000	0.000
72	A	94	GLU	-1	-0.978	-1.003	24.905	-12.467	-12.467	0.000	0.000	0.000	0.000
73	A	95	GLU	-1	-0.835	-0.894	18.364	-16.684	-16.684	0.000	0.000	0.000	0.000
74	A	96	ASP	-1	-0.831	-0.904	19.175	-15.112	-15.112	0.000	0.000	0.000	0.000
75	A	97	GLY	0	-0.020	-0.014	16.693	-0.975	-0.975	0.000	0.000	0.000	0.000
76	A	98	VAL	0	-0.079	-0.034	17.220	-0.841	-0.841	0.000	0.000	0.000	0.000
77	A	99	TYR	0	0.029	0.019	18.965	0.925	0.925	0.000	0.000	0.000	0.000
78	A	100	SER	0	-0.035	-0.015	21.994	-0.073	-0.073	0.000	0.000	0.000	0.000
79	A	101	LEU	0	0.046	0.011	23.529	0.045	0.045	0.000	0.000	0.000	0.000
80	A	102	ASN	0	-0.035	-0.016	26.075	0.160	0.160	0.000	0.000	0.000	0.000
81	A	103	TYR	0	0.011	-0.024	26.429	0.374	0.374	0.000	0.000	0.000	0.000
82	A	104	ASP	-1	-0.792	-0.842	27.942	-11.187	-11.187	0.000	0.000	0.000	0.000
83	A	105	GLY	0	0.040	0.041	29.188	-0.130	-0.130	0.000	0.000	0.000	0.000
84	A	106	TYR	0	-0.004	-0.011	27.288	-0.047	-0.047	0.000	0.000	0.000	0.000
85	A	107	ASN	0	-0.002	-0.014	23.289	-0.394	-0.394	0.000	0.000	0.000	0.000
86	A	108	VAL	0	-0.022	-0.008	21.270	0.257	0.257	0.000	0.000	0.000	0.000
87	A	109	PHE	0	0.011	0.007	17.333	-0.430	-0.430	0.000	0.000	0.000	0.000
88	A	110	ARG	1	0.800	0.890	13.206	20.397	20.397	0.000	0.000	0.000	0.000
89	A	111	ILE	0	0.031	0.018	14.091	-0.953	-0.953	0.000	0.000	0.000	0.000
90	A	112	SER	0	-0.055	-0.037	9.529	0.126	0.126	0.000	0.000	0.000	0.000
91	A	113	GLU	-1	-0.886	-0.938	8.991	-28.577	-28.577	0.000	0.000	0.000	0.000
95	A	117	ASP	-1	-0.787	-0.884	8.765	-23.369	-23.369	0.000	0.000	0.000	0.000
96	A	118	GLU	-1	-0.909	-0.947	11.682	-19.866	-19.866	0.000	0.000	0.000	0.000
97	A	119	HIS	0	-0.086	-0.060	8.420	0.685	0.685	0.000	0.000	0.000	0.000
98	A	120	ILE	0	0.009	0.007	9.999	-1.261	-1.261	0.000	0.000	0.000	0.000
99	A	121	ILE	0	-0.064	-0.020	7.670	-0.596	-0.596	0.000	0.000	0.000	0.000
100	A	122	LEU	0	0.023	0.016	10.204	0.473	0.473	0.000	0.000	0.000	0.000
101	A	123	TYR	0	-0.085	-0.067	12.859	-0.574	-0.574	0.000	0.000	0.000	0.000
102	A	124	LEU	0	0.032	0.010	14.509	0.498	0.498	0.000	0.000	0.000	0.000
103	A	125	VAL	0	-0.038	-0.012	18.338	-0.192	-0.192	0.000	0.000	0.000	0.000
104	A	126	ASN	0	0.010	-0.005	21.302	0.594	0.594	0.000	0.000	0.000	0.000
105	A	127	PHE	0	-0.068	-0.056	23.330	0.022	0.022	0.000	0.000	0.000	0.000
106	A	128	ASP	-1	-0.776	-0.890	27.651	-9.463	-9.463	0.000	0.000	0.000	0.000
107	A	129	LYS	1	0.745	0.859	30.143	8.572	8.572	0.000	0.000	0.000	0.000
108	A	130	ASP	-1	-0.897	-0.939	32.784	-8.779	-8.779	0.000	0.000	0.000	0.000
109	A	131	ARG	0	-0.068	-0.033	28.666	-0.108	-0.108	0.000	0.000	0.000	0.000
110	A	132	PRO	0	0.007	0.027	26.017	-0.205	-0.205	0.000	0.000	0.000	0.000
111	A	133	PHE	0	-0.010	-0.013	22.235	-0.045	-0.045	0.000	0.000	0.000	0.000
112	A	134	GLN	0	-0.020	0.002	17.682	-1.106	-1.106	0.000	0.000	0.000	0.000
113	A	135	LEU	0	0.019	0.003	18.074	0.204	0.204	0.000	0.000	0.000	0.000
114	A	136	PHE	0	-0.042	-0.035	11.064	-1.099	-1.099	0.000	0.000	0.000	0.000
115	A	137	GLU	-1	-0.786	-0.869	14.395	-15.761	-15.761	0.000	0.000	0.000	0.000
116	A	138	PHE	0	-0.032	-0.022	7.106	-1.871	-1.871	0.000	0.000	0.000	0.000
117	A	139	TYR	0	-0.006	-0.032	12.386	1.640	1.640	0.000	0.000	0.000	0.000
118	A	140	ALA	0	0.002	0.002	12.113	-2.432	-2.432	0.000	0.000	0.000	0.000
119	A	141	ARG	1	0.850	0.913	13.800	18.734	18.734	0.000	0.000	0.000	0.000
120	A	142	GLU	-1	-0.880	-0.920	15.424	-15.906	-15.906	0.000	0.000	0.000	0.000
121	A	143	PRO	0	0.000	-0.014	16.638	-0.544	-0.544	0.000	0.000	0.000	0.000
122	A	144	ASP	-1	-0.846	-0.915	15.860	-18.809	-18.809	0.000	0.000	0.000	0.000
123	A	145	VAL	0	-0.004	0.002	10.845	-0.629	-0.629	0.000	0.000	0.000	0.000
124	A	146	SER	0	-0.004	-0.018	10.231	0.461	0.461	0.000	0.000	0.000	0.000
125	A	147	PRO	0	0.020	-0.010	10.709	-1.738	-1.738	0.000	0.000	0.000	0.000
126	A	148	GLU	-1	-0.846	-0.916	7.035	-29.394	-29.394	0.000	0.000	0.000	0.000
127	A	149	ILE	0	-0.003	0.008	5.707	-6.854	-6.854	0.000	0.000	0.000	0.000
128	A	150	LYS	1	0.797	0.901	7.370	19.672	19.672	0.000	0.000	0.000	0.000
129	A	151	GLU	-1	-0.917	-0.966	8.585	-25.102	-25.102	0.000	0.000	0.000	0.000
131	A	153	PHE	0	0.060	0.034	5.608	-0.131	-0.131	0.000	0.000	0.000	0.000
132	A	154	VAL	0	0.042	0.021	7.785	2.129	2.129	0.000	0.000	0.000	0.000
135	A	157	VAL	0	0.007	0.015	8.070	2.401	2.401	0.000	0.000	0.000	0.000
136	A	158	GLN	0	0.028	0.015	11.801	3.230	3.230	0.000	0.000	0.000	0.000
137	A	159	LYS	1	0.894	0.959	7.805	32.629	32.629	0.000	0.000	0.000	0.000
138	A	160	ARG	1	0.840	0.917	11.771	20.049	20.049	0.000	0.000	0.000	0.000
139	A	161	GLY	0	-0.018	-0.006	13.984	1.275	1.275	0.000	0.000	0.000	0.000
140	A	162	ILE	0	-0.020	0.006	15.674	1.010	1.010	0.000	0.000	0.000	0.000
141	A	163	VAL	0	0.000	0.000	15.959	-1.185	-1.185	0.000	0.000	0.000	0.000
142	A	164	LYS	1	0.954	0.952	14.182	20.680	20.680	0.000	0.000	0.000	0.000
143	A	165	GLU	-1	-0.860	-0.936	17.813	-15.138	-15.138	0.000	0.000	0.000	0.000
144	A	166	ASN	0	-0.089	-0.059	19.654	0.954	0.954	0.000	0.000	0.000	0.000
145	A	167	ILE	0	0.008	0.004	13.512	-0.509	-0.509	0.000	0.000	0.000	0.000
146	A	168	ILE	0	-0.015	-0.004	17.442	0.754	0.754	0.000	0.000	0.000	0.000
147	A	169	ASP	-1	-0.786	-0.873	16.723	-19.064	-19.064	0.000	0.000	0.000	0.000
148	A	170	LEU	0	0.018	0.001	17.473	1.054	1.054	0.000	0.000	0.000	0.000
149	A	171	THR	0	-0.080	-0.069	16.939	0.855	0.855	0.000	0.000	0.000	0.000
150	A	172	LYS	1	0.823	0.919	18.963	16.557	16.557	0.000	0.000	0.000	0.000
151	A	173	ILE	0	-0.015	0.001	22.558	0.626	0.626	0.000	0.000	0.000	0.000
152	A	174	ASP	-1	-0.846	-0.913	24.480	-11.084	-11.084	0.000	0.000	0.000	0.000
153	A	175	ARG	1	0.812	0.903	18.490	15.809	15.809	0.000	0.000	0.000	0.000
154	A	177	PHE	0	0.005	-0.014	21.574	0.085	0.085	0.000	0.000	0.000	0.000
155	A	178	GLN	0	-0.054	-0.041	27.543	0.078	0.078	0.000	0.000	0.000	0.000
156	A	179	LEU	0	-0.042	-0.016	30.251	0.287	0.287	0.000	0.000	0.000	0.000
157	A	180	ARG	1	0.750	0.893	22.185	13.385	13.385	0.000	0.000	0.000	0.000
158	A	181	GLY	-1	-0.968	-0.961	28.971	-9.822	-9.822	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:23:VAL)