FMO DATABASE

FMODB ID: 8QG5Y

Calculation Name: 2EF7-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2EF7

Chain ID: A

ChEMBL ID:

UniProt ID: Q96Y20

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1028803.492935
FMO2-HF: Nuclear repulsion	978938.823139
FMO2-HF: Total energy	-49864.669796
FMO2-MP2: Total energy	-50008.060008

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:1:MET)

Summations of interaction energy for fragment #1(A:1: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.
-112.565	-105.501	5.923	-5.031	-7.955	-0.054

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.793 / q_NPA : 0.896

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	3	GLU	-1	-0.932	-0.977	3.216	-39.543	-37.263	0.173	-1.168	-1.284	-0.005
4	A	4	GLU	-1	-0.779	-0.853	4.783	-30.482	-30.258	-0.001	-0.006	-0.217	0.000
126	A	126	MET	0	-0.115	-0.046	2.415	-4.402	-4.301	3.553	-0.936	-2.718	-0.006
127	A	127	PHE	-1	-0.982	-0.982	2.394	-48.267	-43.808	2.198	-2.921	-3.736	-0.043
5	A	5	ILE	0	-0.020	-0.014	7.108	1.881	1.881	0.000	0.000	0.000	0.000
6	A	6	VAL	0	-0.028	-0.036	10.947	0.779	0.779	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.836	0.906	13.810	16.929	16.929	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.891	-0.939	11.315	-18.630	-18.630	0.000	0.000	0.000	0.000
9	A	9	TYR	0	-0.068	-0.046	7.780	1.868	1.868	0.000	0.000	0.000	0.000
10	A	10	MET	0	-0.086	-0.032	13.937	1.234	1.234	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.970	0.997	17.420	11.771	11.771	0.000	0.000	0.000	0.000
12	A	12	THR	0	0.073	0.026	20.217	0.467	0.467	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.028	-0.029	22.689	0.060	0.060	0.000	0.000	0.000	0.000
14	A	14	VAL	0	-0.031	0.005	24.431	0.338	0.338	0.000	0.000	0.000	0.000
15	A	15	ILE	0	-0.004	-0.003	27.356	0.211	0.211	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.025	-0.014	30.803	-0.083	-0.083	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.000	0.000	32.607	0.222	0.222	0.000	0.000	0.000	0.000
18	A	18	THR	0	0.016	-0.012	35.764	-0.199	-0.199	0.000	0.000	0.000	0.000
19	A	19	LYS	1	0.867	0.910	37.848	8.005	8.005	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.861	-0.922	39.096	-7.269	-7.269	0.000	0.000	0.000	0.000
21	A	21	ALA	0	-0.008	0.010	40.076	0.193	0.193	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.960	0.979	42.133	6.462	6.462	0.000	0.000	0.000	0.000
23	A	23	LEU	0	0.008	0.014	42.764	-0.125	-0.125	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.017	-0.026	43.186	-0.088	-0.088	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.860	-0.925	43.261	-6.843	-6.843	0.000	0.000	0.000	0.000
26	A	26	ILE	0	-0.035	-0.017	37.805	-0.178	-0.178	0.000	0.000	0.000	0.000
27	A	27	ALA	0	0.029	0.010	39.170	-0.163	-0.163	0.000	0.000	0.000	0.000
28	A	28	LYS	1	0.918	0.991	40.775	6.750	6.750	0.000	0.000	0.000	0.000
29	A	29	VAL	0	0.004	0.000	36.239	-0.093	-0.093	0.000	0.000	0.000	0.000
30	A	30	MET	0	-0.038	-0.025	35.204	-0.161	-0.161	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.014	-0.009	36.697	-0.099	-0.099	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.935	-0.990	38.757	-7.283	-7.283	0.000	0.000	0.000	0.000
33	A	33	LYS	1	0.875	0.939	33.659	8.286	8.286	0.000	0.000	0.000	0.000
34	A	34	ASN	0	-0.015	0.011	33.321	-0.075	-0.075	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.053	-0.022	30.744	-0.339	-0.339	0.000	0.000	0.000	0.000
36	A	36	GLY	0	0.099	0.045	31.955	0.195	0.195	0.000	0.000	0.000	0.000
37	A	37	SER	0	-0.083	-0.062	30.166	-0.067	-0.067	0.000	0.000	0.000	0.000
38	A	38	VAL	0	0.013	0.016	31.535	-0.109	-0.109	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.000	0.004	27.383	0.046	0.046	0.000	0.000	0.000	0.000
40	A	40	VAL	0	0.002	0.004	31.060	0.215	0.215	0.000	0.000	0.000	0.000
41	A	41	VAL	0	-0.011	-0.015	31.078	-0.266	-0.266	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.807	-0.897	33.775	-7.951	-7.951	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.036	0.019	34.462	-0.210	-0.210	0.000	0.000	0.000	0.000
44	A	44	ASN	0	-0.038	-0.036	31.243	-0.089	-0.089	0.000	0.000	0.000	0.000
45	A	45	LYS	1	0.927	0.992	29.883	9.558	9.558	0.000	0.000	0.000	0.000
46	A	46	PRO	0	-0.016	-0.012	26.777	0.341	0.341	0.000	0.000	0.000	0.000
47	A	47	VAL	0	0.014	0.007	30.086	-0.028	-0.028	0.000	0.000	0.000	0.000
48	A	48	GLY	0	0.054	0.019	31.896	0.192	0.192	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.067	-0.007	28.480	-0.201	-0.201	0.000	0.000	0.000	0.000
50	A	50	ILE	0	0.014	0.027	32.111	0.223	0.223	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.010	-0.029	32.061	-0.100	-0.100	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.872	-0.942	34.667	-8.158	-8.158	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.932	0.960	36.162	8.485	8.485	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.787	-0.885	35.488	-8.327	-8.327	0.000	0.000	0.000	0.000
55	A	55	ILE	0	0.058	0.032	38.785	0.196	0.196	0.000	0.000	0.000	0.000
56	A	56	VAL	0	0.009	0.003	41.080	0.198	0.198	0.000	0.000	0.000	0.000
57	A	57	LYS	1	0.839	0.925	37.608	8.183	8.183	0.000	0.000	0.000	0.000
58	A	58	ALA	0	0.018	0.009	42.828	0.147	0.147	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.029	0.016	44.530	0.159	0.159	0.000	0.000	0.000	0.000
60	A	60	GLY	0	-0.010	-0.003	46.265	0.159	0.159	0.000	0.000	0.000	0.000
61	A	61	LYS	1	0.840	0.917	45.639	6.727	6.727	0.000	0.000	0.000	0.000
62	A	62	GLY	0	0.013	0.014	48.706	0.067	0.067	0.000	0.000	0.000	0.000
63	A	63	LYS	1	0.815	0.919	46.253	6.568	6.568	0.000	0.000	0.000	0.000
64	A	64	SER	0	0.012	-0.014	49.059	-0.039	-0.039	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.042	0.021	48.103	-0.160	-0.160	0.000	0.000	0.000	0.000
66	A	66	GLU	-1	-0.861	-0.917	47.416	-6.180	-6.180	0.000	0.000	0.000	0.000
67	A	67	THR	0	-0.070	-0.040	45.019	-0.019	-0.019	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.890	0.935	43.539	6.805	6.805	0.000	0.000	0.000	0.000
69	A	69	ALA	0	0.039	0.014	38.378	-0.032	-0.032	0.000	0.000	0.000	0.000
70	A	70	GLU	-1	-0.854	-0.941	39.356	-7.508	-7.508	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.896	-0.942	40.386	-6.661	-6.661	0.000	0.000	0.000	0.000
72	A	72	PHE	0	-0.079	-0.044	40.067	0.076	0.076	0.000	0.000	0.000	0.000
73	A	73	MET	0	-0.034	0.009	35.646	-0.142	-0.142	0.000	0.000	0.000	0.000
74	A	74	THR	0	-0.030	-0.006	32.241	0.107	0.107	0.000	0.000	0.000	0.000
75	A	75	ALA	0	-0.005	-0.003	33.124	-0.268	-0.268	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.030	-0.035	28.051	-0.168	-0.168	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.039	0.021	29.756	0.045	0.045	0.000	0.000	0.000	0.000
78	A	78	ILE	0	-0.053	-0.008	23.926	-0.289	-0.289	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.023	-0.013	23.616	-0.096	-0.096	0.000	0.000	0.000	0.000
80	A	80	ILE	0	0.017	0.009	17.202	-0.208	-0.208	0.000	0.000	0.000	0.000
81	A	81	ARG	1	0.963	0.988	19.161	14.274	14.274	0.000	0.000	0.000	0.000
82	A	82	GLU	-1	-0.776	-0.900	17.554	-15.788	-15.788	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.905	-0.950	14.842	-18.357	-18.357	0.000	0.000	0.000	0.000
84	A	84	SER	0	-0.079	-0.053	13.919	-0.869	-0.869	0.000	0.000	0.000	0.000
85	A	85	PRO	0	0.056	0.036	9.962	0.334	0.334	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.008	0.007	8.757	2.565	2.565	0.000	0.000	0.000	0.000
87	A	87	THR	0	0.013	-0.001	8.610	2.689	2.689	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.030	0.019	11.343	1.653	1.653	0.000	0.000	0.000	0.000
89	A	89	ALA	0	0.016	0.006	14.081	1.570	1.570	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.011	0.008	12.721	1.398	1.398	0.000	0.000	0.000	0.000
91	A	91	ALA	0	-0.026	-0.016	15.288	1.129	1.129	0.000	0.000	0.000	0.000
92	A	92	LEU	0	0.021	0.013	17.264	1.032	1.032	0.000	0.000	0.000	0.000
93	A	93	MET	0	-0.028	-0.015	17.399	0.776	0.776	0.000	0.000	0.000	0.000
94	A	94	ARG	1	0.914	0.954	16.253	17.432	17.432	0.000	0.000	0.000	0.000
95	A	95	GLN	0	-0.039	-0.002	20.773	0.149	0.149	0.000	0.000	0.000	0.000
96	A	96	PHE	0	-0.003	-0.015	23.153	0.648	0.648	0.000	0.000	0.000	0.000
97	A	97	ASN	0	-0.052	-0.013	24.002	0.163	0.163	0.000	0.000	0.000	0.000
98	A	98	ILE	0	-0.013	0.008	22.712	0.428	0.428	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.934	0.949	21.449	10.916	10.916	0.000	0.000	0.000	0.000
100	A	100	HIS	0	0.027	0.003	20.912	-0.682	-0.682	0.000	0.000	0.000	0.000
101	A	101	LEU	0	0.021	0.024	18.630	0.341	0.341	0.000	0.000	0.000	0.000
102	A	102	PRO	0	-0.009	-0.004	21.496	-0.284	-0.284	0.000	0.000	0.000	0.000
103	A	103	VAL	0	0.012	0.016	18.814	-0.200	-0.200	0.000	0.000	0.000	0.000
104	A	104	VAL	0	-0.010	-0.007	21.575	0.636	0.636	0.000	0.000	0.000	0.000
105	A	105	ASP	-1	-0.702	-0.856	21.763	-12.453	-12.453	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.865	-0.932	22.527	-12.419	-12.419	0.000	0.000	0.000	0.000
107	A	107	LYS	1	0.814	0.896	24.021	11.857	11.857	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.009	0.003	26.192	0.484	0.484	0.000	0.000	0.000	0.000
109	A	109	ASN	0	-0.081	-0.063	27.265	0.613	0.613	0.000	0.000	0.000	0.000
110	A	110	LEU	0	0.006	-0.005	25.323	-0.483	-0.483	0.000	0.000	0.000	0.000
111	A	111	LYS	1	0.852	0.942	22.294	12.298	12.298	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.054	0.009	21.841	0.049	0.049	0.000	0.000	0.000	0.000
113	A	113	ILE	0	-0.093	-0.032	21.652	0.299	0.299	0.000	0.000	0.000	0.000
114	A	114	ILE	0	0.029	0.035	14.283	-0.248	-0.248	0.000	0.000	0.000	0.000
115	A	115	SER	0	-0.026	-0.048	18.031	0.506	0.506	0.000	0.000	0.000	0.000
116	A	116	ILE	0	0.028	-0.016	15.906	-0.747	-0.747	0.000	0.000	0.000	0.000
117	A	117	ARG	1	0.901	0.946	15.544	13.747	13.747	0.000	0.000	0.000	0.000
118	A	118	ASP	-1	-0.742	-0.818	14.518	-16.172	-16.172	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.015	-0.003	11.679	-1.079	-1.079	0.000	0.000	0.000	0.000
120	A	120	THR	0	-0.032	-0.031	10.615	-0.910	-0.910	0.000	0.000	0.000	0.000
121	A	121	ARG	1	0.853	0.937	10.308	17.422	17.422	0.000	0.000	0.000	0.000
122	A	122	ALA	0	0.067	0.032	8.122	-0.809	-0.809	0.000	0.000	0.000	0.000
123	A	123	ILE	0	-0.101	-0.047	6.091	-3.284	-3.284	0.000	0.000	0.000	0.000
124	A	124	ASP	-1	-0.939	-0.986	5.829	-23.242	-23.242	0.000	0.000	0.000	0.000
125	A	125	ASP	-1	-0.879	-0.949	7.503	-22.497	-22.497	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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