FMO DATABASE

FMODB ID: 3K2ML

Calculation Name: 2J4T-A-Xray547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2J4T

Chain ID: A

ChEMBL ID:

UniProt ID: Q3TMQ6

Base Structure: X-ray

Registration Date: 2025-10-04

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	116
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1054756.262554
FMO2-HF: Nuclear repulsion	1004779.63742
FMO2-HF: Total energy	-49976.625134
FMO2-MP2: Total energy	-50118.535063

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:2:ASN)

Summations of interaction energy for fragment #1(A:2:ASN)

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.
44.603	56.14	16.119	-12.39	-15.262	-0.078

Interaction energy analysis for fragmet #1(A:2:ASN)

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 : 0.912

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

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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	4	ARG	1	0.874	0.933	2.261	26.298	29.559	2.333	-2.189	-3.405	0.019
4	A	5	TYR	-1	-0.851	-0.932	2.317	-44.816	-42.096	1.425	-1.559	-2.586	0.006
5	A	6	GLU	-1	-0.839	-0.923	1.876	-107.631	-104.657	9.339	-7.232	-5.080	-0.091
6	A	7	LYS	1	0.854	0.928	5.077	37.634	37.765	-0.001	-0.007	-0.122	0.000
52	A	53	ARG	1	0.940	0.962	4.510	39.991	40.049	-0.001	-0.003	-0.054	0.000
102	A	106	GLU	-1	-0.768	-0.870	4.403	-26.455	-26.388	-0.001	-0.005	-0.061	0.000
103	A	107	ASP	-1	-0.865	-0.935	4.424	-36.633	-36.520	-0.001	-0.013	-0.098	0.000
105	A	109	TRP	0	-0.045	-0.026	2.619	-11.048	-8.969	3.028	-1.373	-3.734	-0.012
106	A	110	PRO	0	0.020	0.004	4.912	1.981	2.019	-0.001	-0.005	-0.032	0.000
107	A	111	VAL	0	-0.050	-0.022	4.619	-4.460	-4.364	-0.001	-0.004	-0.090	0.000
7	A	8	PHE	0	0.024	0.026	7.327	3.685	3.685	0.000	0.000	0.000	0.000
8	A	9	LEU	0	-0.023	-0.023	6.162	4.544	4.544	0.000	0.000	0.000	0.000
9	A	10	ARG	1	0.883	0.950	8.250	33.518	33.518	0.000	0.000	0.000	0.000
10	A	11	GLN	0	0.058	0.023	10.915	2.924	2.924	0.000	0.000	0.000	0.000
11	A	12	HIS	1	0.881	0.955	12.310	21.988	21.988	0.000	0.000	0.000	0.000
12	A	13	TYR	0	-0.035	-0.038	11.591	-0.003	-0.003	0.000	0.000	0.000	0.000
13	A	14	ASP	-1	-0.760	-0.866	13.632	-17.242	-17.242	0.000	0.000	0.000	0.000
14	A	15	ALA	0	-0.001	0.014	15.184	0.932	0.932	0.000	0.000	0.000	0.000
15	A	16	LYS	1	0.941	0.960	16.798	15.225	15.225	0.000	0.000	0.000	0.000
16	A	17	PRO	0	0.032	0.047	20.313	0.219	0.219	0.000	0.000	0.000	0.000
17	A	18	GLN	0	0.017	-0.008	21.967	0.173	0.173	0.000	0.000	0.000	0.000
18	A	19	GLY	0	0.025	0.032	25.345	-0.108	-0.108	0.000	0.000	0.000	0.000
19	A	20	ARG	1	0.767	0.847	24.054	13.044	13.044	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.854	-0.934	26.277	-10.648	-10.648	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.750	-0.897	27.395	-10.589	-10.589	0.000	0.000	0.000	0.000
22	A	23	ARG	1	1.005	1.014	27.897	9.804	9.804	0.000	0.000	0.000	0.000
23	A	24	TYR	0	-0.056	-0.053	20.141	-0.281	-0.281	0.000	0.000	0.000	0.000
24	A	25	CYS	0	-0.039	-0.013	22.492	-0.124	-0.124	0.000	0.000	0.000	0.000
25	A	26	GLU	-1	-0.854	-0.923	23.391	-11.168	-11.168	0.000	0.000	0.000	0.000
26	A	27	SER	0	-0.069	-0.041	23.875	-0.195	-0.195	0.000	0.000	0.000	0.000
27	A	28	MET	0	-0.019	-0.006	17.380	-0.609	-0.609	0.000	0.000	0.000	0.000
28	A	29	MET	0	-0.014	0.004	19.016	-1.326	-1.326	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.970	0.991	20.041	11.730	11.730	0.000	0.000	0.000	0.000
30	A	31	GLU	-1	-0.916	-0.943	16.998	-18.037	-18.037	0.000	0.000	0.000	0.000
31	A	32	ARG	1	0.747	0.848	13.708	19.625	19.625	0.000	0.000	0.000	0.000
32	A	33	LYS	1	0.894	0.946	14.487	18.477	18.477	0.000	0.000	0.000	0.000
33	A	34	LEU	0	-0.016	-0.008	15.888	-0.394	-0.394	0.000	0.000	0.000	0.000
34	A	35	THR	0	0.035	0.011	19.338	0.446	0.446	0.000	0.000	0.000	0.000
35	A	36	SER	0	-0.054	-0.007	20.567	0.550	0.550	0.000	0.000	0.000	0.000
36	A	37	PRO	0	0.032	0.009	21.213	-0.466	-0.466	0.000	0.000	0.000	0.000
37	A	38	CYS	0	-0.019	0.008	22.477	-0.315	-0.315	0.000	0.000	0.000	0.000
38	A	39	LYS	1	0.830	0.925	15.953	17.802	17.802	0.000	0.000	0.000	0.000
39	A	40	ASP	-1	-0.770	-0.850	22.101	-11.285	-11.285	0.000	0.000	0.000	0.000
40	A	41	VAL	0	0.037	0.018	22.382	0.355	0.355	0.000	0.000	0.000	0.000
41	A	42	ASN	0	-0.037	-0.022	17.168	-1.273	-1.273	0.000	0.000	0.000	0.000
42	A	43	THR	0	0.017	0.004	19.136	0.664	0.664	0.000	0.000	0.000	0.000
43	A	44	PHE	0	-0.031	-0.004	15.756	-1.292	-1.292	0.000	0.000	0.000	0.000
44	A	45	ILE	0	0.016	0.005	14.022	0.885	0.885	0.000	0.000	0.000	0.000
45	A	46	HIS	0	-0.014	0.017	16.519	-0.218	-0.218	0.000	0.000	0.000	0.000
46	A	47	GLY	0	0.029	0.027	18.272	0.072	0.072	0.000	0.000	0.000	0.000
47	A	48	THR	0	-0.066	-0.032	15.225	-1.072	-1.072	0.000	0.000	0.000	0.000
48	A	49	LYS	1	1.057	1.027	8.398	33.641	33.641	0.000	0.000	0.000	0.000
49	A	50	LYS	1	0.951	0.979	11.472	19.706	19.706	0.000	0.000	0.000	0.000
50	A	51	ASN	0	-0.007	-0.007	12.820	0.105	0.105	0.000	0.000	0.000	0.000
51	A	52	ILE	0	0.073	0.050	11.466	0.478	0.478	0.000	0.000	0.000	0.000
53	A	54	ALA	0	-0.047	-0.027	9.908	0.454	0.454	0.000	0.000	0.000	0.000
54	A	55	ILE	0	0.007	0.023	12.942	1.130	1.130	0.000	0.000	0.000	0.000
55	A	56	CYS	0	-0.056	-0.032	7.624	-1.064	-1.064	0.000	0.000	0.000	0.000
56	A	57	GLY	0	-0.017	0.009	11.384	0.428	0.428	0.000	0.000	0.000	0.000
57	A	58	LYS	1	0.959	0.951	13.240	16.596	16.596	0.000	0.000	0.000	0.000
58	A	59	LYS	1	0.908	0.964	16.052	17.027	17.027	0.000	0.000	0.000	0.000
59	A	60	GLY	0	0.051	0.028	16.443	-0.082	-0.082	0.000	0.000	0.000	0.000
60	A	61	SER	0	-0.031	0.000	17.380	0.380	0.380	0.000	0.000	0.000	0.000
61	A	62	PRO	0	-0.011	-0.012	17.610	-0.702	-0.702	0.000	0.000	0.000	0.000
62	A	63	TYR	0	0.015	0.000	18.077	0.702	0.702	0.000	0.000	0.000	0.000
63	A	64	GLY	0	0.062	0.031	19.330	-0.075	-0.075	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.938	-0.971	18.311	-12.998	-12.998	0.000	0.000	0.000	0.000
65	A	66	ASN	0	-0.043	-0.023	14.235	-0.139	-0.139	0.000	0.000	0.000	0.000
66	A	67	PHE	0	0.002	-0.003	13.275	-1.429	-1.429	0.000	0.000	0.000	0.000
67	A	68	ARG	1	0.806	0.906	12.600	18.040	18.040	0.000	0.000	0.000	0.000
68	A	69	ILE	0	0.056	0.037	15.451	-0.399	-0.399	0.000	0.000	0.000	0.000
69	A	70	SER	0	-0.038	-0.032	17.556	-0.191	-0.191	0.000	0.000	0.000	0.000
70	A	71	ASN	0	0.031	0.009	18.538	0.644	0.644	0.000	0.000	0.000	0.000
71	A	72	SER	0	-0.017	-0.006	20.532	0.435	0.435	0.000	0.000	0.000	0.000
72	A	73	PRO	0	0.021	0.020	21.061	-0.676	-0.676	0.000	0.000	0.000	0.000
73	A	74	PHE	0	-0.041	-0.028	16.431	-0.692	-0.692	0.000	0.000	0.000	0.000
74	A	75	GLN	0	0.020	0.033	21.123	0.682	0.682	0.000	0.000	0.000	0.000
75	A	76	ILE	0	0.019	-0.002	19.440	-0.988	-0.988	0.000	0.000	0.000	0.000
76	A	77	THR	0	0.007	-0.022	21.145	1.090	1.090	0.000	0.000	0.000	0.000
77	A	78	THR	0	0.008	0.001	21.587	-0.677	-0.677	0.000	0.000	0.000	0.000
78	A	80	THR	0	0.033	0.010	23.993	-0.374	-0.374	0.000	0.000	0.000	0.000
79	A	81	HIS	0	-0.009	-0.013	26.338	0.386	0.386	0.000	0.000	0.000	0.000
80	A	82	SER	0	-0.045	-0.027	27.934	0.343	0.343	0.000	0.000	0.000	0.000
81	A	83	ARG	1	0.790	0.848	27.395	10.875	10.875	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.054	0.031	31.754	0.345	0.345	0.000	0.000	0.000	0.000
83	A	85	SER	0	-0.028	-0.003	33.265	-0.001	-0.001	0.000	0.000	0.000	0.000
84	A	86	PRO	0	-0.003	0.008	28.694	-0.169	-0.169	0.000	0.000	0.000	0.000
85	A	87	TRP	0	0.008	-0.013	29.163	-0.293	-0.293	0.000	0.000	0.000	0.000
86	A	88	PRO	0	0.035	0.000	28.167	-0.205	-0.205	0.000	0.000	0.000	0.000
87	A	89	PRO	0	-0.049	-0.016	28.158	-0.339	-0.339	0.000	0.000	0.000	0.000
88	A	91	GLY	0	0.063	0.047	27.762	-0.222	-0.222	0.000	0.000	0.000	0.000
89	A	92	TYR	0	-0.096	-0.085	23.812	-0.260	-0.260	0.000	0.000	0.000	0.000
90	A	93	ARG	1	0.957	0.987	28.405	9.479	9.479	0.000	0.000	0.000	0.000
91	A	94	ALA	0	-0.023	-0.019	26.904	-0.461	-0.461	0.000	0.000	0.000	0.000
92	A	95	PHE	0	0.005	0.016	26.801	0.463	0.463	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.838	0.918	26.077	10.251	10.251	0.000	0.000	0.000	0.000
94	A	97	ASP	-1	-0.735	-0.853	25.610	-11.005	-11.005	0.000	0.000	0.000	0.000
95	A	98	PHE	0	-0.084	-0.067	24.159	-0.628	-0.628	0.000	0.000	0.000	0.000
96	A	99	ARG	1	0.871	0.923	23.262	11.695	11.695	0.000	0.000	0.000	0.000
97	A	100	TYR	0	-0.025	-0.003	21.753	-0.628	-0.628	0.000	0.000	0.000	0.000
98	A	101	ILE	0	0.002	0.001	16.002	0.024	0.024	0.000	0.000	0.000	0.000
99	A	102	VAL	0	0.050	0.029	16.929	-0.296	-0.296	0.000	0.000	0.000	0.000
100	A	103	ILE	0	-0.021	-0.014	10.705	-0.597	-0.597	0.000	0.000	0.000	0.000
101	A	104	ALA	0	0.045	0.035	10.840	0.840	0.840	0.000	0.000	0.000	0.000
104	A	108	GLY	0	-0.034	-0.026	5.766	-2.241	-2.241	0.000	0.000	0.000	0.000
108	A	112	HIS	0	0.003	0.005	7.232	-0.003	-0.003	0.000	0.000	0.000	0.000
109	A	113	PHE	0	-0.007	-0.021	11.068	-0.653	-0.653	0.000	0.000	0.000	0.000
110	A	114	ASP	-1	-0.838	-0.891	14.294	-13.767	-13.767	0.000	0.000	0.000	0.000
111	A	115	GLU	-1	-0.772	-0.884	17.592	-15.681	-15.681	0.000	0.000	0.000	0.000
112	A	116	SER	0	-0.056	-0.039	20.394	0.739	0.739	0.000	0.000	0.000	0.000
113	A	117	PHE	0	0.008	0.011	21.000	0.530	0.530	0.000	0.000	0.000	0.000
114	A	118	ILE	0	-0.081	-0.049	21.312	0.206	0.206	0.000	0.000	0.000	0.000
115	A	119	SER	0	-0.044	-0.028	24.168	0.263	0.263	0.000	0.000	0.000	0.000
116	A	120	PRO	-1	-0.864	-0.893	26.623	-10.317	-10.317	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ASN)