FMO DATABASE

FMODB ID: 55Y5Z

Calculation Name: 2JNT-A-Other547

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2JNT

Chain ID: A

ChEMBL ID:

UniProt ID: Q8MMK7

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	106
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-890895.608504
FMO2-HF: Nuclear repulsion	846386.791222
FMO2-HF: Total energy	-44508.817282
FMO2-MP2: Total energy	-44637.003241

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:TYR)

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

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.
-169.79	-169.474	19.453	-11.357	-8.41	-0.126

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.738 / q_NPA : 0.857

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	ASP	-1	-0.752	-0.877	1.794	-130.121	-130.243	19.453	-11.281	-8.050	-0.126
4	A	4	LYS	1	0.885	0.930	4.660	41.551	41.718	-0.001	-0.025	-0.140	0.000
8	A	8	ILE	0	-0.036	-0.009	3.485	3.612	3.883	0.001	-0.051	-0.220	0.000
5	A	5	TYR	0	0.043	0.029	7.528	-2.009	-2.009	0.000	0.000	0.000	0.000
6	A	6	ASP	-1	-0.846	-0.913	6.333	-37.088	-37.088	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.859	0.888	6.413	32.729	32.729	0.000	0.000	0.000	0.000
9	A	9	ASN	0	-0.007	0.009	7.604	-1.372	-1.372	0.000	0.000	0.000	0.000
10	A	10	LEU	0	0.040	0.005	9.124	2.257	2.257	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.115	0.054	12.745	0.745	0.745	0.000	0.000	0.000	0.000
12	A	12	GLU	-1	-0.856	-0.924	8.162	-29.194	-29.194	0.000	0.000	0.000	0.000
13	A	13	ILE	0	-0.092	-0.055	10.535	-2.075	-2.075	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.004	0.007	13.010	1.209	1.209	0.000	0.000	0.000	0.000
15	A	15	GLU	-1	-0.906	-0.950	14.402	-20.544	-20.544	0.000	0.000	0.000	0.000
16	A	16	ASN	0	-0.013	-0.003	15.835	2.181	2.181	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.833	0.895	17.290	12.295	12.295	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.869	0.925	17.878	15.348	15.348	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.022	-0.008	12.190	-0.870	-0.870	0.000	0.000	0.000	0.000
20	A	20	LEU	0	0.038	0.026	14.613	-1.013	-1.013	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.793	-0.895	16.770	-15.343	-15.343	0.000	0.000	0.000	0.000
22	A	22	SER	0	-0.100	-0.038	12.619	-0.513	-0.513	0.000	0.000	0.000	0.000
23	A	23	TYR	0	0.011	-0.021	12.733	-0.917	-0.917	0.000	0.000	0.000	0.000
24	A	24	MET	0	0.015	0.029	14.294	0.082	0.082	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.830	-0.923	15.641	-16.984	-16.984	0.000	0.000	0.000	0.000
26	A	26	CYS	0	-0.123	-0.054	11.757	-1.745	-1.745	0.000	0.000	0.000	0.000
27	A	27	VAL	0	0.012	0.011	16.558	0.476	0.476	0.000	0.000	0.000	0.000
28	A	28	LEU	0	0.000	-0.002	19.782	0.724	0.724	0.000	0.000	0.000	0.000
29	A	29	GLY	0	-0.013	0.022	20.131	0.582	0.582	0.000	0.000	0.000	0.000
30	A	30	LYS	1	0.752	0.840	19.712	14.666	14.666	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.010	0.005	17.406	0.400	0.400	0.000	0.000	0.000	0.000
32	A	32	LYS	1	0.886	0.950	10.548	26.085	26.085	0.000	0.000	0.000	0.000
33	A	34	THR	0	-0.021	-0.007	8.220	2.193	2.193	0.000	0.000	0.000	0.000
34	A	35	PRO	0	-0.020	-0.014	11.174	0.091	0.091	0.000	0.000	0.000	0.000
35	A	36	GLU	-1	-0.744	-0.858	10.269	-25.602	-25.602	0.000	0.000	0.000	0.000
36	A	37	GLY	0	-0.008	-0.017	10.972	-0.196	-0.196	0.000	0.000	0.000	0.000
37	A	38	LYS	1	0.927	0.958	11.678	17.381	17.381	0.000	0.000	0.000	0.000
38	A	39	GLU	-1	-0.910	-0.943	15.263	-16.439	-16.439	0.000	0.000	0.000	0.000
39	A	40	LEU	0	-0.061	-0.015	10.696	0.544	0.544	0.000	0.000	0.000	0.000
40	A	41	LYS	1	0.810	0.913	10.234	28.498	28.498	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.918	-0.949	16.244	-13.813	-13.813	0.000	0.000	0.000	0.000
42	A	43	HIS	0	0.042	0.004	19.300	1.013	1.013	0.000	0.000	0.000	0.000
43	A	44	LEU	0	-0.059	0.001	15.903	0.478	0.478	0.000	0.000	0.000	0.000
44	A	45	GLN	0	-0.010	-0.028	16.728	0.742	0.742	0.000	0.000	0.000	0.000
45	A	46	GLU	-1	-0.911	-0.937	20.718	-11.888	-11.888	0.000	0.000	0.000	0.000
46	A	47	ALA	0	-0.061	-0.030	22.490	0.524	0.524	0.000	0.000	0.000	0.000
47	A	48	LEU	0	-0.030	-0.002	20.851	0.336	0.336	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.725	-0.847	23.916	-10.407	-10.407	0.000	0.000	0.000	0.000
49	A	50	THR	0	-0.078	-0.049	27.256	0.203	0.203	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.064	0.040	27.353	0.282	0.282	0.000	0.000	0.000	0.000
51	A	52	CYS	0	-0.111	-0.062	25.610	1.075	1.075	0.000	0.000	0.000	0.000
52	A	53	GLU	-1	-0.793	-0.895	25.793	-10.862	-10.862	0.000	0.000	0.000	0.000
53	A	54	LYS	1	0.891	0.948	26.247	10.190	10.190	0.000	0.000	0.000	0.000
54	A	56	THR	0	0.013	0.005	21.886	0.019	0.019	0.000	0.000	0.000	0.000
55	A	57	GLU	-1	-0.849	-0.928	20.423	-14.473	-14.473	0.000	0.000	0.000	0.000
56	A	58	ALA	0	-0.019	-0.021	17.420	-0.396	-0.396	0.000	0.000	0.000	0.000
57	A	59	GLN	0	0.014	0.004	18.736	-0.395	-0.395	0.000	0.000	0.000	0.000
58	A	60	GLU	-1	-0.839	-0.895	21.193	-13.480	-13.480	0.000	0.000	0.000	0.000
59	A	61	LYS	1	0.822	0.892	18.622	14.046	14.046	0.000	0.000	0.000	0.000
60	A	62	GLY	0	0.041	0.017	17.550	-0.515	-0.515	0.000	0.000	0.000	0.000
61	A	63	ALA	0	0.033	0.027	18.431	-0.255	-0.255	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.843	-0.914	21.547	-13.154	-13.154	0.000	0.000	0.000	0.000
63	A	65	THR	0	-0.066	-0.038	15.611	-0.101	-0.101	0.000	0.000	0.000	0.000
64	A	66	SER	0	-0.001	-0.032	18.150	-0.536	-0.536	0.000	0.000	0.000	0.000
65	A	67	ILE	0	-0.014	-0.013	19.731	0.319	0.319	0.000	0.000	0.000	0.000
66	A	68	ASP	-1	-0.807	-0.884	21.067	-13.845	-13.845	0.000	0.000	0.000	0.000
67	A	69	TYR	0	0.013	0.002	18.971	0.307	0.307	0.000	0.000	0.000	0.000
68	A	70	LEU	0	-0.036	-0.011	21.086	0.265	0.265	0.000	0.000	0.000	0.000
69	A	71	ILE	0	-0.033	-0.009	22.664	0.516	0.516	0.000	0.000	0.000	0.000
70	A	72	LYS	1	0.759	0.864	22.720	14.083	14.083	0.000	0.000	0.000	0.000
71	A	73	ASN	0	-0.065	-0.020	20.647	0.583	0.583	0.000	0.000	0.000	0.000
72	A	74	GLU	-1	-0.763	-0.847	20.568	-13.986	-13.986	0.000	0.000	0.000	0.000
73	A	75	LEU	0	0.065	0.020	23.882	0.052	0.052	0.000	0.000	0.000	0.000
74	A	76	GLU	-1	-0.889	-0.960	25.705	-11.984	-11.984	0.000	0.000	0.000	0.000
75	A	77	ILE	0	0.045	0.020	22.060	0.116	0.116	0.000	0.000	0.000	0.000
76	A	78	TRP	0	-0.020	-0.010	25.351	0.209	0.209	0.000	0.000	0.000	0.000
77	A	79	LYS	1	0.928	0.973	26.878	10.047	10.047	0.000	0.000	0.000	0.000
78	A	80	GLU	-1	-0.929	-0.954	25.699	-12.144	-12.144	0.000	0.000	0.000	0.000
79	A	81	LEU	0	0.008	-0.005	23.024	0.161	0.161	0.000	0.000	0.000	0.000
80	A	82	THR	0	-0.040	-0.032	27.200	0.300	0.300	0.000	0.000	0.000	0.000
81	A	83	ALA	0	-0.037	-0.034	30.696	0.282	0.282	0.000	0.000	0.000	0.000
82	A	84	HIS	0	-0.051	-0.010	27.244	0.178	0.178	0.000	0.000	0.000	0.000
83	A	85	PHE	0	-0.021	-0.004	25.522	0.039	0.039	0.000	0.000	0.000	0.000
84	A	86	ASP	-1	-0.812	-0.924	31.534	-8.490	-8.490	0.000	0.000	0.000	0.000
85	A	87	PRO	0	0.019	0.013	34.676	0.016	0.016	0.000	0.000	0.000	0.000
86	A	88	ASP	-1	-0.971	-0.980	36.008	-7.968	-7.968	0.000	0.000	0.000	0.000
87	A	89	GLY	0	0.000	0.012	36.376	0.163	0.163	0.000	0.000	0.000	0.000
88	A	90	LYS	1	0.852	0.917	37.445	7.993	7.993	0.000	0.000	0.000	0.000
89	A	91	TRP	0	0.003	-0.011	34.511	0.171	0.171	0.000	0.000	0.000	0.000
90	A	92	ARG	1	0.969	0.999	34.671	7.758	7.758	0.000	0.000	0.000	0.000
91	A	93	LYS	1	0.840	0.893	35.340	7.930	7.930	0.000	0.000	0.000	0.000
92	A	94	LYS	1	0.782	0.861	31.851	10.004	10.004	0.000	0.000	0.000	0.000
93	A	95	TYR	0	0.022	0.017	29.200	-0.073	-0.073	0.000	0.000	0.000	0.000
94	A	96	GLU	-1	-0.822	-0.894	31.497	-8.525	-8.525	0.000	0.000	0.000	0.000
95	A	97	ASP	-1	-0.892	-0.931	33.256	-9.679	-9.679	0.000	0.000	0.000	0.000
96	A	98	ARG	1	0.804	0.891	27.550	11.109	11.109	0.000	0.000	0.000	0.000
97	A	99	ALA	0	0.022	0.012	28.637	-0.405	-0.405	0.000	0.000	0.000	0.000
98	A	100	LYS	1	0.810	0.888	29.751	8.872	8.872	0.000	0.000	0.000	0.000
99	A	101	ALA	0	-0.009	-0.004	32.645	0.097	0.097	0.000	0.000	0.000	0.000
100	A	102	LYS	1	0.820	0.901	26.196	11.803	11.803	0.000	0.000	0.000	0.000
101	A	103	GLY	0	-0.020	0.002	28.304	-0.301	-0.301	0.000	0.000	0.000	0.000
102	A	104	ILE	0	-0.035	-0.008	25.009	-0.109	-0.109	0.000	0.000	0.000	0.000
103	A	105	VAL	0	-0.034	-0.019	28.530	0.395	0.395	0.000	0.000	0.000	0.000
104	A	106	ILE	0	0.018	0.017	30.635	-0.091	-0.091	0.000	0.000	0.000	0.000
105	A	107	PRO	0	-0.066	-0.039	32.884	0.155	0.155	0.000	0.000	0.000	0.000
106	A	108	GLU	-2	-1.810	-1.878	36.619	-16.370	-16.370	0.000	0.000	0.000	0.000

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