FMO DATABASE

FMODB ID: JR269

Calculation Name: 4L3R-A-Xray549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4L3R

Chain ID: A

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-12

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	143
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1308728.512051
FMO2-HF: Nuclear repulsion	1252935.607457
FMO2-HF: Total energy	-55792.904593
FMO2-MP2: Total energy	-55956.92067

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:30:ASP)

Summations of interaction energy for fragment #1(A:30:ASP)

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.
13.002	15.744	0.009	-0.937	-1.816	0

Interaction energy analysis for fragmet #1(A:30:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.070 / q_NPA : -0.043

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	32	VAL	0	-0.010	-0.010	3.487	2.317	4.196	-0.001	-0.689	-1.190	0.001
4	A	33	MET	0	0.050	0.018	3.219	3.768	4.631	0.010	-0.248	-0.626	-0.001
5	A	34	GLU	-1	-0.788	-0.868	5.274	-0.304	-0.304	0.000	0.000	0.000	0.000
6	A	35	ILE	0	-0.039	-0.020	7.009	1.812	1.812	0.000	0.000	0.000	0.000
7	A	36	PHE	0	-0.003	-0.009	8.250	0.864	0.864	0.000	0.000	0.000	0.000
8	A	37	ASN	0	-0.114	-0.051	8.477	0.991	0.991	0.000	0.000	0.000	0.000
9	A	38	ASP	-1	-0.904	-0.947	10.500	-0.912	-0.912	0.000	0.000	0.000	0.000
10	A	39	LYS	1	0.771	0.892	10.755	3.397	3.397	0.000	0.000	0.000	0.000
11	A	40	THR	0	-0.021	-0.012	15.590	-0.099	-0.099	0.000	0.000	0.000	0.000
12	A	41	TRP	0	-0.069	-0.032	11.957	0.240	0.240	0.000	0.000	0.000	0.000
13	A	42	LYS	1	0.812	0.902	18.358	0.974	0.974	0.000	0.000	0.000	0.000
14	A	43	LEU	0	-0.030	-0.013	21.597	-0.048	-0.048	0.000	0.000	0.000	0.000
15	A	44	SER	0	-0.049	-0.027	22.482	0.102	0.102	0.000	0.000	0.000	0.000
16	A	45	ARG	1	0.934	0.974	20.471	1.339	1.339	0.000	0.000	0.000	0.000
17	A	46	ILE	0	0.009	0.010	24.491	-0.109	-0.109	0.000	0.000	0.000	0.000
18	A	47	THR	0	-0.011	-0.010	25.235	0.094	0.094	0.000	0.000	0.000	0.000
19	A	48	THR	0	0.032	-0.004	26.306	-0.067	-0.067	0.000	0.000	0.000	0.000
20	A	49	GLU	-1	-0.894	-0.949	22.471	-1.148	-1.148	0.000	0.000	0.000	0.000
21	A	50	LYS	1	0.926	0.955	23.576	0.740	0.740	0.000	0.000	0.000	0.000
22	A	51	GLY	0	0.021	0.036	25.901	0.067	0.067	0.000	0.000	0.000	0.000
23	A	52	LYS	1	0.900	0.927	26.184	0.579	0.579	0.000	0.000	0.000	0.000
24	A	53	GLU	-1	-0.805	-0.874	29.000	-0.666	-0.666	0.000	0.000	0.000	0.000
25	A	54	GLN	0	0.002	0.009	28.427	0.000	0.000	0.000	0.000	0.000	0.000
26	A	55	PHE	0	0.022	-0.013	28.350	-0.068	-0.068	0.000	0.000	0.000	0.000
27	A	56	TYR	0	0.019	0.022	29.142	0.058	0.058	0.000	0.000	0.000	0.000
28	A	57	GLN	0	0.012	-0.001	32.042	0.021	0.021	0.000	0.000	0.000	0.000
29	A	58	GLY	0	0.043	0.013	35.687	-0.011	-0.011	0.000	0.000	0.000	0.000
30	A	59	LEU	0	-0.060	-0.001	30.463	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	60	TRP	0	-0.022	-0.027	32.750	-0.003	-0.003	0.000	0.000	0.000	0.000
32	A	61	SER	0	-0.014	-0.021	38.016	0.004	0.004	0.000	0.000	0.000	0.000
33	A	62	ASN	0	-0.002	-0.006	41.508	0.024	0.024	0.000	0.000	0.000	0.000
34	A	63	GLU	-1	-0.852	-0.927	41.364	-0.373	-0.373	0.000	0.000	0.000	0.000
35	A	64	ALA	0	0.009	0.008	41.490	-0.011	-0.011	0.000	0.000	0.000	0.000
36	A	65	GLU	-1	-0.826	-0.896	39.290	-0.479	-0.479	0.000	0.000	0.000	0.000
37	A	66	GLU	-1	-0.782	-0.865	36.127	-0.547	-0.547	0.000	0.000	0.000	0.000
38	A	67	LYS	1	0.942	0.963	36.899	0.354	0.354	0.000	0.000	0.000	0.000
39	A	68	ALA	0	0.000	0.000	38.288	-0.008	-0.008	0.000	0.000	0.000	0.000
40	A	69	SER	0	0.010	-0.033	33.629	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	70	ARG	1	0.792	0.863	32.661	0.534	0.534	0.000	0.000	0.000	0.000
42	A	71	GLU	-1	-0.892	-0.918	34.463	-0.454	-0.454	0.000	0.000	0.000	0.000
43	A	72	LEU	0	-0.038	-0.016	33.632	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	73	LEU	0	0.012	0.005	27.479	-0.029	-0.029	0.000	0.000	0.000	0.000
45	A	74	LYS	1	0.801	0.889	29.830	0.454	0.454	0.000	0.000	0.000	0.000
46	A	75	ILE	0	-0.012	0.016	31.246	0.008	0.008	0.000	0.000	0.000	0.000
47	A	76	THR	0	0.016	0.003	26.503	-0.046	-0.046	0.000	0.000	0.000	0.000
48	A	77	GLU	-1	-0.805	-0.916	26.455	-0.743	-0.743	0.000	0.000	0.000	0.000
49	A	78	ASN	0	-0.038	0.003	26.786	-0.068	-0.068	0.000	0.000	0.000	0.000
50	A	79	PHE	0	-0.026	-0.021	25.915	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	80	THR	0	-0.016	-0.008	22.308	-0.076	-0.076	0.000	0.000	0.000	0.000
52	A	81	LEU	0	-0.012	-0.006	16.848	0.044	0.044	0.000	0.000	0.000	0.000
53	A	82	ASN	0	-0.040	-0.024	16.641	0.056	0.056	0.000	0.000	0.000	0.000
54	A	83	PHE	0	0.051	0.029	11.742	0.030	0.030	0.000	0.000	0.000	0.000
55	A	84	ASN	0	-0.009	-0.015	13.551	0.119	0.119	0.000	0.000	0.000	0.000
56	A	85	CYS	0	-0.001	-0.007	11.889	-0.457	-0.457	0.000	0.000	0.000	0.000
57	A	86	ALA	0	0.041	0.031	14.548	0.216	0.216	0.000	0.000	0.000	0.000
58	A	87	ASP	-1	-0.915	-0.958	17.943	-0.870	-0.870	0.000	0.000	0.000	0.000
59	A	88	VAL	0	-0.035	-0.017	19.533	0.055	0.055	0.000	0.000	0.000	0.000
60	A	89	ASN	0	-0.066	-0.049	21.511	0.032	0.032	0.000	0.000	0.000	0.000
61	A	90	GLY	0	0.020	0.020	23.398	0.040	0.040	0.000	0.000	0.000	0.000
62	A	91	GLU	-1	-0.943	-0.961	18.326	-1.071	-1.071	0.000	0.000	0.000	0.000
63	A	92	VAL	0	-0.027	-0.013	14.645	-0.072	-0.072	0.000	0.000	0.000	0.000
64	A	93	THR	0	-0.007	0.009	14.621	-0.222	-0.222	0.000	0.000	0.000	0.000
65	A	94	GLY	0	0.023	-0.001	11.998	-0.055	-0.055	0.000	0.000	0.000	0.000
66	A	95	THR	0	-0.095	-0.065	12.982	0.029	0.029	0.000	0.000	0.000	0.000
67	A	96	VAL	0	0.008	-0.005	14.763	-0.287	-0.287	0.000	0.000	0.000	0.000
68	A	97	SER	0	0.028	0.024	16.997	0.279	0.279	0.000	0.000	0.000	0.000
69	A	98	ALA	0	0.004	-0.008	19.567	-0.127	-0.127	0.000	0.000	0.000	0.000
70	A	99	HIS	1	0.822	0.904	22.210	0.963	0.963	0.000	0.000	0.000	0.000
71	A	100	ALA	0	0.004	0.013	25.761	-0.024	-0.024	0.000	0.000	0.000	0.000
72	A	101	VAL	0	-0.014	-0.006	28.019	0.023	0.023	0.000	0.000	0.000	0.000
73	A	102	LYS	1	0.896	0.933	31.585	0.570	0.570	0.000	0.000	0.000	0.000
74	A	103	ALA	0	-0.064	-0.020	29.965	0.011	0.011	0.000	0.000	0.000	0.000
75	A	104	ASN	0	0.004	-0.014	26.504	-0.059	-0.059	0.000	0.000	0.000	0.000
76	A	105	ILE	0	0.002	0.003	21.832	0.053	0.053	0.000	0.000	0.000	0.000
77	A	106	SER	0	-0.025	-0.022	22.626	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	107	ASP	-1	-0.826	-0.889	19.502	-1.404	-1.404	0.000	0.000	0.000	0.000
79	A	108	ALA	0	-0.039	-0.008	19.812	0.051	0.051	0.000	0.000	0.000	0.000
80	A	109	ILE	0	0.035	0.006	17.950	-0.202	-0.202	0.000	0.000	0.000	0.000
81	A	110	LEU	0	-0.001	0.011	11.222	0.013	0.013	0.000	0.000	0.000	0.000
82	A	111	LYS	1	0.917	0.958	13.541	2.116	2.116	0.000	0.000	0.000	0.000
83	A	112	ILE	0	0.033	0.002	8.493	0.126	0.126	0.000	0.000	0.000	0.000
84	A	113	ASP	-1	-0.819	-0.898	8.786	-5.084	-5.084	0.000	0.000	0.000	0.000
85	A	114	GLY	0	0.018	-0.006	5.040	-0.126	-0.126	0.000	0.000	0.000	0.000
86	A	115	LYS	1	0.883	0.946	6.083	2.659	2.659	0.000	0.000	0.000	0.000
87	A	116	GLU	-1	-0.868	-0.901	8.265	-2.053	-2.053	0.000	0.000	0.000	0.000
88	A	117	HIS	1	0.824	0.920	7.708	5.739	5.739	0.000	0.000	0.000	0.000
89	A	118	THR	0	0.000	-0.027	10.787	0.245	0.245	0.000	0.000	0.000	0.000
90	A	119	ILE	0	-0.020	-0.030	11.958	-0.676	-0.676	0.000	0.000	0.000	0.000
91	A	120	SER	0	-0.041	-0.006	14.245	0.366	0.366	0.000	0.000	0.000	0.000
92	A	121	ILE	0	0.057	0.026	16.221	-0.218	-0.218	0.000	0.000	0.000	0.000
93	A	122	SER	0	-0.005	0.001	18.547	0.228	0.228	0.000	0.000	0.000	0.000
94	A	123	GLY	0	0.027	-0.001	21.414	-0.031	-0.031	0.000	0.000	0.000	0.000
95	A	124	LYS	1	0.931	0.967	24.240	0.804	0.804	0.000	0.000	0.000	0.000
96	A	125	ALA	0	0.035	0.022	26.586	-0.034	-0.034	0.000	0.000	0.000	0.000
97	A	126	TYR	0	-0.006	0.008	28.067	0.065	0.065	0.000	0.000	0.000	0.000
98	A	127	GLY	0	0.046	0.025	30.470	-0.014	-0.014	0.000	0.000	0.000	0.000
99	A	128	SER	0	-0.023	-0.025	32.778	-0.029	-0.029	0.000	0.000	0.000	0.000
100	A	129	GLU	-1	-0.712	-0.847	31.519	-0.706	-0.706	0.000	0.000	0.000	0.000
101	A	130	SER	0	-0.045	-0.027	34.920	0.018	0.018	0.000	0.000	0.000	0.000
102	A	131	ASP	-1	-0.775	-0.875	33.873	-0.624	-0.624	0.000	0.000	0.000	0.000
103	A	132	LYS	1	0.862	0.913	34.461	0.465	0.465	0.000	0.000	0.000	0.000
104	A	133	LEU	0	0.044	0.038	29.194	-0.034	-0.034	0.000	0.000	0.000	0.000
105	A	134	ALA	0	-0.002	-0.006	29.823	-0.066	-0.066	0.000	0.000	0.000	0.000
106	A	135	LYS	1	0.887	0.946	29.556	0.532	0.532	0.000	0.000	0.000	0.000
107	A	136	VAL	0	0.014	0.018	28.278	-0.040	-0.040	0.000	0.000	0.000	0.000
108	A	137	PHE	0	0.013	0.006	23.065	-0.057	-0.057	0.000	0.000	0.000	0.000
109	A	138	ILE	0	0.008	-0.004	24.968	-0.087	-0.087	0.000	0.000	0.000	0.000
110	A	139	SER	0	-0.035	-0.030	25.631	-0.043	-0.043	0.000	0.000	0.000	0.000
111	A	140	GLY	0	0.015	0.001	24.724	-0.031	-0.031	0.000	0.000	0.000	0.000
112	A	141	LEU	0	-0.030	-0.025	19.720	-0.117	-0.117	0.000	0.000	0.000	0.000
113	A	142	PHE	0	-0.014	-0.005	20.651	-0.122	-0.122	0.000	0.000	0.000	0.000
114	A	143	ASN	0	-0.039	0.001	22.644	-0.018	-0.018	0.000	0.000	0.000	0.000
115	A	144	VAL	0	-0.038	-0.020	17.383	0.036	0.036	0.000	0.000	0.000	0.000
116	A	145	PHE	0	-0.024	-0.015	18.312	0.054	0.054	0.000	0.000	0.000	0.000
117	A	146	LYS	1	0.876	0.952	14.945	1.387	1.387	0.000	0.000	0.000	0.000
118	A	147	TYR	0	-0.008	-0.008	7.137	0.232	0.232	0.000	0.000	0.000	0.000
119	A	148	GLU	-1	-0.848	-0.897	11.998	-2.040	-2.040	0.000	0.000	0.000	0.000
120	A	149	GLY	0	-0.007	-0.018	11.806	0.203	0.203	0.000	0.000	0.000	0.000
121	A	150	ASP	-1	-0.820	-0.882	9.906	-2.146	-2.146	0.000	0.000	0.000	0.000
122	A	151	VAL	0	0.018	0.009	9.441	-0.316	-0.316	0.000	0.000	0.000	0.000
123	A	152	HIS	1	0.836	0.915	11.290	1.206	1.206	0.000	0.000	0.000	0.000
124	A	153	ASN	0	-0.050	-0.029	14.338	0.260	0.260	0.000	0.000	0.000	0.000
125	A	154	LEU	0	0.030	0.023	12.428	-0.390	-0.390	0.000	0.000	0.000	0.000
126	A	155	THR	0	-0.043	-0.023	15.259	0.452	0.452	0.000	0.000	0.000	0.000
127	A	156	LEU	0	0.026	0.012	14.699	-0.259	-0.259	0.000	0.000	0.000	0.000
128	A	157	TYR	0	-0.056	-0.066	17.119	0.356	0.356	0.000	0.000	0.000	0.000
129	A	158	PHE	0	0.005	0.003	19.503	-0.092	-0.092	0.000	0.000	0.000	0.000
130	A	159	LYS	1	0.951	0.973	22.302	1.156	1.156	0.000	0.000	0.000	0.000
131	A	160	ASP	-1	-0.815	-0.895	25.525	-0.815	-0.815	0.000	0.000	0.000	0.000
132	A	161	GLY	0	0.045	0.041	29.009	0.050	0.050	0.000	0.000	0.000	0.000
133	A	162	ASN	0	-0.031	-0.022	30.008	-0.058	-0.058	0.000	0.000	0.000	0.000
134	A	163	THR	0	-0.051	-0.032	29.600	0.009	0.009	0.000	0.000	0.000	0.000
135	A	164	THR	0	0.014	0.009	23.118	-0.051	-0.051	0.000	0.000	0.000	0.000
136	A	165	LYS	1	0.800	0.886	24.859	0.879	0.879	0.000	0.000	0.000	0.000
137	A	166	VAL	0	-0.008	0.003	20.637	-0.112	-0.112	0.000	0.000	0.000	0.000
138	A	167	MET	0	-0.026	0.002	20.578	0.163	0.163	0.000	0.000	0.000	0.000
139	A	168	GLY	0	-0.019	-0.004	19.943	-0.181	-0.181	0.000	0.000	0.000	0.000
140	A	169	PHE	0	0.019	-0.013	17.853	0.168	0.168	0.000	0.000	0.000	0.000
141	A	170	THR	0	-0.016	-0.012	18.375	-0.031	-0.031	0.000	0.000	0.000	0.000
142	A	171	ALA	0	0.039	0.028	15.555	-0.014	-0.014	0.000	0.000	0.000	0.000
143	A	172	ARG	0	0.102	0.060	16.922	-0.415	-0.415	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:30:ASP)