FMO DATABASE

FMODB ID: 3MZVL

Calculation Name: 2L2F-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2L2F

Chain ID: A

ChEMBL ID:

UniProt ID: I1RM03

Base Structure: SolutionNMR

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	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-774184.821356
FMO2-HF: Nuclear repulsion	732388.537118
FMO2-HF: Total energy	-41796.284237
FMO2-MP2: Total energy	-41916.218676

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.
-309.451	-302.925	1.221	-3.239	-4.51	-0.034

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 : 0.809 / 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	ASN	0	-0.051	-0.050	3.034	-1.055	2.053	0.145	-1.446	-1.807	-0.009
4	A	4	PHE	0	0.065	0.033	5.077	6.388	6.532	-0.001	-0.009	-0.134	0.000
95	A	95	GLU	-1	-1.005	-0.984	3.615	-46.563	-45.891	0.008	-0.281	-0.400	-0.002
96	A	96	ARG	1	0.794	0.882	3.093	22.438	23.989	0.097	-0.823	-0.825	-0.008
107	A	107	LEU	0	-0.118	-0.057	2.195	-6.099	-5.048	0.972	-0.680	-1.344	-0.015
5	A	5	HIS	1	0.842	0.923	5.962	34.548	34.548	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.928	-0.946	7.099	-30.897	-30.897	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.056	-0.024	9.440	2.024	2.024	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.008	-0.037	11.268	1.073	1.073	0.000	0.000	0.000	0.000
9	A	9	ASN	0	-0.005	-0.001	13.685	0.608	0.608	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.032	-0.031	16.682	-0.231	-0.231	0.000	0.000	0.000	0.000
11	A	11	ILE	0	0.007	0.013	12.300	-0.122	-0.122	0.000	0.000	0.000	0.000
12	A	12	TRP	0	-0.003	-0.010	15.608	0.611	0.611	0.000	0.000	0.000	0.000
13	A	13	LEU	0	-0.017	-0.013	16.844	-0.532	-0.532	0.000	0.000	0.000	0.000
14	A	14	GLU	-1	-0.891	-0.923	19.379	-12.238	-12.238	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.913	-0.975	22.678	-11.666	-11.666	0.000	0.000	0.000	0.000
16	A	16	GLY	0	0.047	0.039	21.458	0.029	0.029	0.000	0.000	0.000	0.000
17	A	17	HIS	1	0.822	0.905	19.764	13.038	13.038	0.000	0.000	0.000	0.000
18	A	18	ILE	0	0.026	0.020	19.163	-0.684	-0.684	0.000	0.000	0.000	0.000
19	A	19	LEU	0	0.014	0.016	12.507	0.204	0.204	0.000	0.000	0.000	0.000
20	A	20	HIS	1	0.827	0.875	17.237	15.477	15.477	0.000	0.000	0.000	0.000
21	A	21	ALA	0	0.026	0.014	13.889	-0.576	-0.576	0.000	0.000	0.000	0.000
22	A	22	GLU	-1	-0.846	-0.904	15.992	-14.976	-14.976	0.000	0.000	0.000	0.000
23	A	23	CYS	0	-0.076	0.005	13.305	-1.582	-1.582	0.000	0.000	0.000	0.000
24	A	24	GLY	0	0.045	0.034	14.423	1.262	1.262	0.000	0.000	0.000	0.000
25	A	25	ASN	0	-0.018	-0.025	14.131	-1.500	-1.500	0.000	0.000	0.000	0.000
26	A	26	GLY	0	0.007	-0.002	15.363	-0.845	-0.845	0.000	0.000	0.000	0.000
27	A	27	GLU	-1	-1.012	-0.997	16.617	-13.481	-13.481	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.047	-0.030	19.734	0.628	0.628	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.938	-0.954	20.674	-13.246	-13.246	0.000	0.000	0.000	0.000
30	A	30	TYR	0	-0.043	-0.040	15.605	-1.249	-1.249	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.029	-0.008	18.082	1.011	1.011	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.957	-0.973	18.422	-14.631	-14.631	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.017	-0.020	16.448	0.584	0.584	0.000	0.000	0.000	0.000
34	A	34	THR	0	-0.031	-0.034	17.830	0.035	0.035	0.000	0.000	0.000	0.000
35	A	35	LEU	0	-0.022	-0.008	12.611	-0.607	-0.607	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.857	-0.921	16.721	-14.520	-14.520	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.022	-0.002	14.154	-0.981	-0.981	0.000	0.000	0.000	0.000
38	A	38	ASP	-1	-0.889	-0.963	17.105	-13.638	-13.638	0.000	0.000	0.000	0.000
39	A	39	TYR	0	-0.022	-0.009	17.412	0.713	0.713	0.000	0.000	0.000	0.000
40	A	40	TYR	0	-0.030	-0.014	13.154	-1.106	-1.106	0.000	0.000	0.000	0.000
41	A	41	ILE	0	-0.026	-0.004	12.825	-1.665	-1.665	0.000	0.000	0.000	0.000
42	A	42	GLY	0	0.016	0.021	15.749	1.127	1.127	0.000	0.000	0.000	0.000
43	A	43	ASN	0	-0.067	-0.056	17.711	-0.981	-0.981	0.000	0.000	0.000	0.000
44	A	44	ASP	-1	-0.944	-0.979	18.456	-14.935	-14.935	0.000	0.000	0.000	0.000
45	A	45	ASP	-1	-0.878	-0.954	20.122	-12.872	-12.872	0.000	0.000	0.000	0.000
46	A	46	GLY	0	0.027	0.023	22.430	0.051	0.051	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.006	-0.004	17.072	-0.350	-0.350	0.000	0.000	0.000	0.000
48	A	48	PHE	0	-0.007	-0.017	14.494	0.162	0.162	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.022	-0.002	14.234	-1.318	-1.318	0.000	0.000	0.000	0.000
50	A	50	TRP	0	-0.003	-0.025	8.661	-0.131	-0.131	0.000	0.000	0.000	0.000
51	A	51	GLY	0	-0.002	-0.001	12.182	-0.231	-0.231	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.042	-0.006	14.282	1.096	1.096	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.967	-0.983	17.514	-14.214	-14.214	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.054	-0.046	20.035	0.373	0.373	0.000	0.000	0.000	0.000
55	A	55	PHE	0	0.014	0.011	18.950	0.469	0.469	0.000	0.000	0.000	0.000
56	A	56	SER	0	0.028	0.011	21.281	0.556	0.556	0.000	0.000	0.000	0.000
57	A	57	GLY	0	-0.003	0.003	23.421	0.476	0.476	0.000	0.000	0.000	0.000
58	A	58	SER	0	-0.085	-0.045	24.905	0.481	0.481	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.032	0.038	23.072	-0.115	-0.115	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.063	-0.035	25.053	0.751	0.751	0.000	0.000	0.000	0.000
61	A	61	ASN	0	-0.101	-0.077	24.691	-0.765	-0.765	0.000	0.000	0.000	0.000
62	A	62	ILE	0	0.040	0.053	20.004	-0.270	-0.270	0.000	0.000	0.000	0.000
63	A	63	THR	0	-0.038	-0.023	20.774	0.259	0.259	0.000	0.000	0.000	0.000
64	A	64	LEU	0	-0.063	-0.017	13.550	-0.702	-0.702	0.000	0.000	0.000	0.000
65	A	65	ASP	-1	-0.863	-0.915	16.892	-14.075	-14.075	0.000	0.000	0.000	0.000
66	A	66	ILE	0	-0.051	-0.031	13.793	-1.074	-1.074	0.000	0.000	0.000	0.000
67	A	67	GLU	-1	-0.917	-0.961	13.080	-17.054	-17.054	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.001	-0.005	12.506	-1.498	-1.498	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.969	-0.993	13.630	-15.924	-15.924	0.000	0.000	0.000	0.000
70	A	70	ASP	-1	-0.940	-0.967	9.071	-25.484	-25.484	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.057	-0.031	10.919	-1.231	-1.231	0.000	0.000	0.000	0.000
72	A	72	ILE	0	0.002	0.011	7.261	-1.660	-1.660	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.010	0.006	9.134	1.768	1.768	0.000	0.000	0.000	0.000
74	A	74	VAL	0	-0.028	-0.020	10.881	-1.961	-1.961	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.012	-0.001	12.941	1.472	1.472	0.000	0.000	0.000	0.000
76	A	76	ARG	1	0.889	0.932	15.410	16.299	16.299	0.000	0.000	0.000	0.000
77	A	77	ALA	0	0.049	0.019	18.475	0.350	0.350	0.000	0.000	0.000	0.000
78	A	78	GLU	-1	-0.865	-0.888	21.568	-11.291	-11.291	0.000	0.000	0.000	0.000
79	A	79	LEU	0	-0.047	-0.019	19.105	0.104	0.104	0.000	0.000	0.000	0.000
80	A	80	ASN	0	-0.046	-0.042	23.706	0.601	0.601	0.000	0.000	0.000	0.000
81	A	81	PRO	0	0.051	0.050	25.077	-0.319	-0.319	0.000	0.000	0.000	0.000
82	A	82	MET	0	-0.089	-0.047	26.014	0.397	0.397	0.000	0.000	0.000	0.000
83	A	83	ASP	-1	-0.931	-0.964	28.258	-10.150	-10.150	0.000	0.000	0.000	0.000
84	A	84	GLY	0	-0.085	-0.040	29.813	0.435	0.435	0.000	0.000	0.000	0.000
85	A	85	ASP	-1	-0.944	-0.988	30.089	-9.544	-9.544	0.000	0.000	0.000	0.000
86	A	86	PRO	0	-0.052	-0.014	27.388	-0.307	-0.307	0.000	0.000	0.000	0.000
87	A	87	VAL	0	0.010	0.004	22.915	0.244	0.244	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.969	-0.980	22.014	-12.852	-12.852	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.003	0.022	18.152	-0.343	-0.343	0.000	0.000	0.000	0.000
90	A	90	ASN	0	-0.030	-0.047	14.245	0.697	0.697	0.000	0.000	0.000	0.000
91	A	91	VAL	0	0.029	0.018	10.518	-0.659	-0.659	0.000	0.000	0.000	0.000
92	A	92	ASN	0	0.053	0.035	5.711	1.091	1.091	0.000	0.000	0.000	0.000
93	A	93	LEU	0	0.083	0.031	8.331	-2.797	-2.797	0.000	0.000	0.000	0.000
94	A	94	SER	0	0.013	-0.016	5.235	-1.562	-1.562	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.022	0.042	5.564	3.488	3.488	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.008	-0.014	6.367	-7.318	-7.318	0.000	0.000	0.000	0.000
99	A	99	ASN	0	-0.010	-0.017	7.618	1.101	1.101	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.917	-0.947	10.176	-25.225	-25.225	0.000	0.000	0.000	0.000
101	A	101	CYS	0	-0.004	-0.017	12.256	2.113	2.113	0.000	0.000	0.000	0.000
102	A	102	GLY	0	0.043	0.025	14.032	1.391	1.391	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.030	0.006	15.073	1.063	1.063	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.009	-0.006	11.750	-2.068	-2.068	0.000	0.000	0.000	0.000
105	A	105	ILE	0	-0.033	-0.003	8.269	1.069	1.069	0.000	0.000	0.000	0.000
106	A	106	PHE	0	0.048	0.016	9.135	-2.167	-2.167	0.000	0.000	0.000	0.000
108	A	108	ALA	-1	-0.838	-0.906	6.699	-31.469	-31.469	0.000	0.000	0.000	0.000

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