FMO DATABASE

FMODB ID: L6MK9

Calculation Name: 2LF0-A-Other549

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2LF0

Chain ID: A

ChEMBL ID:

UniProt ID: A0A384

Base Structure: SolutionNMR

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	120
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-853754.727635
FMO2-HF: Nuclear repulsion	804807.651518
FMO2-HF: Total energy	-48947.076117
FMO2-MP2: Total energy	-49086.522574

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.
27.371	35.97	5.281	-5.777	-8.103	-0.06

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 : 0.844 / q_NPA : 0.921

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	-0.819	-0.927	2.424	-72.310	-63.984	5.282	-5.738	-7.870	-0.060
4	A	4	VAL	0	0.009	0.032	4.663	4.749	5.022	-0.001	-0.039	-0.233	0.000
5	A	5	GLU	-1	-0.842	-0.928	7.739	-23.192	-23.192	0.000	0.000	0.000	0.000
6	A	6	LYS	1	0.871	0.926	5.601	42.188	42.188	0.000	0.000	0.000	0.000
7	A	7	ASN	0	-0.037	-0.023	11.122	3.451	3.451	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.749	-0.855	11.780	-22.071	-22.071	0.000	0.000	0.000	0.000
9	A	9	ILE	0	0.014	0.001	12.337	1.322	1.322	0.000	0.000	0.000	0.000
10	A	10	LYS	1	0.911	0.961	14.995	19.868	19.868	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.853	0.911	15.270	19.575	19.575	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.017	0.007	16.677	0.766	0.766	0.000	0.000	0.000	0.000
13	A	13	SER	0	-0.024	-0.003	19.423	0.892	0.892	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.930	-0.961	21.135	-12.845	-12.845	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.936	0.976	22.785	11.741	11.741	0.000	0.000	0.000	0.000
16	A	16	LEU	0	0.018	0.008	24.221	0.517	0.517	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.899	-0.966	25.311	-10.932	-10.932	0.000	0.000	0.000	0.000
18	A	18	ALA	0	0.033	0.007	27.028	0.483	0.483	0.000	0.000	0.000	0.000
19	A	19	ILE	0	-0.047	-0.013	28.304	0.361	0.361	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.920	0.954	28.395	10.749	10.749	0.000	0.000	0.000	0.000
21	A	21	HIS	0	-0.024	0.003	31.248	0.120	0.120	0.000	0.000	0.000	0.000
22	A	22	GLN	0	0.017	0.005	32.900	0.216	0.216	0.000	0.000	0.000	0.000
23	A	23	GLN	0	-0.061	-0.064	33.901	0.006	0.006	0.000	0.000	0.000	0.000
24	A	24	ALA	0	-0.039	-0.007	35.827	0.179	0.179	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.944	-0.971	36.685	-8.443	-8.443	0.000	0.000	0.000	0.000
26	A	26	LEU	0	-0.070	-0.021	38.341	0.231	0.231	0.000	0.000	0.000	0.000
27	A	27	SER	0	0.042	0.013	40.601	-0.072	-0.072	0.000	0.000	0.000	0.000
28	A	28	LEU	0	-0.002	-0.015	42.346	0.053	0.053	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.049	-0.030	43.670	0.117	0.117	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.893	-0.939	44.908	-6.996	-6.996	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.015	0.014	42.658	0.046	0.046	0.000	0.000	0.000	0.000
32	A	32	ALA	0	-0.003	0.009	43.283	-0.179	-0.179	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.896	-0.966	43.804	-7.112	-7.112	0.000	0.000	0.000	0.000
34	A	34	LYS	1	0.944	0.977	36.856	8.211	8.211	0.000	0.000	0.000	0.000
35	A	35	TYR	0	-0.028	-0.013	38.057	-0.235	-0.235	0.000	0.000	0.000	0.000
36	A	36	ALA	0	0.038	0.013	38.144	-0.210	-0.210	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.819	-0.898	38.115	-7.852	-7.852	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.035	-0.009	33.723	-0.261	-0.261	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.770	-0.853	33.631	-8.908	-8.908	0.000	0.000	0.000	0.000
40	A	40	LYS	1	0.801	0.883	33.915	7.534	7.534	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.944	-0.963	31.248	-9.703	-9.703	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.798	0.898	29.468	8.838	8.838	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.057	0.030	28.976	-0.338	-0.338	0.000	0.000	0.000	0.000
44	A	44	THR	0	-0.040	-0.028	28.747	-0.095	-0.095	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.015	-0.008	24.364	-0.424	-0.424	0.000	0.000	0.000	0.000
46	A	46	GLU	-1	-0.935	-0.975	24.658	-10.640	-10.640	0.000	0.000	0.000	0.000
47	A	47	ALA	0	-0.001	-0.005	25.268	-0.314	-0.314	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.916	-0.945	22.235	-12.209	-12.209	0.000	0.000	0.000	0.000
49	A	49	ILE	0	-0.035	-0.036	20.385	-0.592	-0.592	0.000	0.000	0.000	0.000
50	A	50	ALA	0	-0.022	-0.006	20.729	-0.501	-0.501	0.000	0.000	0.000	0.000
51	A	51	ARG	1	0.892	0.938	22.829	10.841	10.841	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.004	-0.014	16.779	-0.370	-0.370	0.000	0.000	0.000	0.000
53	A	53	ARG	1	0.932	0.963	17.615	13.475	13.475	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.798	-0.874	19.510	-10.867	-10.867	0.000	0.000	0.000	0.000
55	A	55	VAL	0	0.019	0.014	16.946	-0.090	-0.090	0.000	0.000	0.000	0.000
56	A	56	HIS	0	-0.107	-0.068	13.023	-1.283	-1.283	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.029	-0.003	16.767	-0.065	-0.065	0.000	0.000	0.000	0.000
58	A	58	GLN	0	0.000	-0.005	19.502	-0.170	-0.170	0.000	0.000	0.000	0.000
59	A	59	LYS	1	0.860	0.914	15.382	13.638	13.638	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.001	0.026	15.031	-1.022	-1.022	0.000	0.000	0.000	0.000
61	A	61	SER	0	0.054	0.014	9.893	-1.084	-1.084	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.912	0.945	5.446	28.048	28.048	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.837	-0.909	7.443	-23.902	-23.902	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.076	0.039	10.812	0.864	0.864	0.000	0.000	0.000	0.000
65	A	65	GLN	0	0.098	0.049	14.125	0.567	0.567	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.838	0.909	9.133	21.547	21.547	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.037	-0.019	13.216	0.451	0.451	0.000	0.000	0.000	0.000
68	A	68	MET	0	0.002	0.004	16.347	0.571	0.571	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.888	0.958	16.886	14.346	14.346	0.000	0.000	0.000	0.000
70	A	70	MET	0	-0.060	-0.014	14.978	0.093	0.093	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.049	-0.011	19.758	0.292	0.292	0.000	0.000	0.000	0.000
72	A	72	PHE	0	0.054	0.029	22.071	0.436	0.436	0.000	0.000	0.000	0.000
73	A	73	GLN	0	-0.032	-0.033	21.615	-0.417	-0.417	0.000	0.000	0.000	0.000
74	A	74	ARG	1	0.864	0.938	23.055	11.087	11.087	0.000	0.000	0.000	0.000
75	A	75	ALA	0	0.059	0.039	23.451	-0.523	-0.523	0.000	0.000	0.000	0.000
76	A	76	ILE	0	-0.057	-0.032	22.414	0.335	0.335	0.000	0.000	0.000	0.000
77	A	77	THR	0	0.102	0.047	25.787	0.058	0.058	0.000	0.000	0.000	0.000
78	A	78	LYS	1	1.022	0.978	28.701	8.838	8.838	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.951	0.990	30.230	8.235	8.235	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.820	-0.916	26.789	-10.366	-10.366	0.000	0.000	0.000	0.000
81	A	81	GLN	0	-0.093	-0.062	25.212	-0.403	-0.403	0.000	0.000	0.000	0.000
82	A	82	ALA	0	0.009	0.021	26.098	-0.304	-0.304	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.850	-0.922	27.992	-10.037	-10.037	0.000	0.000	0.000	0.000
84	A	84	MET	0	0.002	0.017	21.964	-0.631	-0.631	0.000	0.000	0.000	0.000
85	A	85	GLY	0	0.006	0.006	22.838	-0.497	-0.497	0.000	0.000	0.000	0.000
86	A	86	LYS	1	0.888	0.937	24.036	9.706	9.706	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.026	0.016	22.972	-0.028	-0.028	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.946	0.966	17.955	14.981	14.981	0.000	0.000	0.000	0.000
89	A	89	LYS	1	0.912	0.963	20.452	10.710	10.710	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.038	-0.035	22.208	0.136	0.136	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.003	0.023	20.747	0.178	0.178	0.000	0.000	0.000	0.000
92	A	92	ARG	1	0.886	0.946	19.658	13.111	13.111	0.000	0.000	0.000	0.000
93	A	93	GLY	0	0.020	0.020	16.629	-0.479	-0.479	0.000	0.000	0.000	0.000
94	A	94	LEU	0	-0.036	-0.006	17.250	0.080	0.080	0.000	0.000	0.000	0.000
95	A	95	VAL	0	-0.036	-0.012	13.111	-0.905	-0.905	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.010	-0.028	15.199	0.917	0.917	0.000	0.000	0.000	0.000
97	A	97	VAL	0	-0.008	0.003	14.726	-1.091	-1.091	0.000	0.000	0.000	0.000
98	A	98	HIS	0	0.049	0.022	17.015	0.525	0.525	0.000	0.000	0.000	0.000
99	A	99	PRO	0	0.081	0.068	19.148	-0.624	-0.624	0.000	0.000	0.000	0.000
100	A	100	MET	0	0.038	0.012	21.809	0.073	0.073	0.000	0.000	0.000	0.000
101	A	101	THR	0	-0.037	-0.024	16.533	-0.403	-0.403	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.034	0.008	15.980	0.373	0.373	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.004	0.001	12.293	0.187	0.187	0.000	0.000	0.000	0.000
104	A	104	GLY	0	0.009	0.006	15.976	0.375	0.375	0.000	0.000	0.000	0.000
105	A	105	ARG	1	0.883	0.935	19.142	13.303	13.303	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.935	-0.956	17.942	-13.106	-13.106	0.000	0.000	0.000	0.000
107	A	107	MET	0	-0.098	-0.054	16.570	-0.197	-0.197	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.036	0.031	19.991	0.366	0.366	0.000	0.000	0.000	0.000
109	A	109	LEU	0	-0.089	-0.043	19.217	0.289	0.289	0.000	0.000	0.000	0.000
110	A	110	GLU	-1	-0.895	-0.952	23.242	-9.876	-9.876	0.000	0.000	0.000	0.000
111	A	111	GLU	-1	-0.852	-0.921	25.173	-10.565	-10.565	0.000	0.000	0.000	0.000
112	A	112	MET	0	-0.085	-0.053	20.561	-0.575	-0.575	0.000	0.000	0.000	0.000
113	A	113	THR	0	0.003	0.007	20.182	0.508	0.508	0.000	0.000	0.000	0.000
114	A	114	GLY	0	-0.006	-0.012	19.016	-0.738	-0.738	0.000	0.000	0.000	0.000
115	A	115	PHE	0	0.045	0.003	17.288	0.475	0.475	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.014	-0.006	17.566	-0.704	-0.704	0.000	0.000	0.000	0.000
117	A	117	LYS	1	0.966	0.971	16.905	13.352	13.352	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.011	-0.005	19.540	0.367	0.367	0.000	0.000	0.000	0.000
119	A	119	THR	0	0.018	0.007	22.185	-0.141	-0.141	0.000	0.000	0.000	0.000
120	A	120	PHE	-1	-0.860	-0.920	22.015	-10.679	-10.679	0.000	0.000	0.000	0.000

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