FMO DATABASE

FMODB ID: N6Q1Q

Calculation Name: 1J0S-A-Other549

Preferred Name: Interleukin-18

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

PDB ID: 1J0S

Chain ID: A

ChEMBL ID: CHEMBL1741305

UniProt ID: Q14116

Base Structure: SolutionNMR

Registration Date: 2025-10-11

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	157
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1622917.628486
FMO2-HF: Nuclear repulsion	1557466.804793
FMO2-HF: Total energy	-65450.823694
FMO2-MP2: Total energy	-65636.082784

3D Structure

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.
-86.365	-76.547	6.656	-6.337	-10.137	-0.074

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 : 0.775 / q_NPA : 0.892

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	GLY	0	0.031	0.000	2.478	-10.076	-7.189	1.017	-1.744	-2.161	-0.022
4	A	4	LYS	1	0.890	0.949	5.150	25.715	25.793	-0.001	-0.006	-0.071	0.000
91	A	91	ASN	0	-0.058	-0.033	2.454	-6.390	-5.072	0.769	-0.656	-1.431	-0.005
92	A	92	ILE	0	0.007	0.010	3.313	4.600	5.207	0.007	-0.137	-0.477	0.000
93	A	93	LYS	1	0.969	0.976	2.248	15.290	18.726	3.346	-2.874	-3.908	-0.028
94	A	94	ASP	-1	-0.777	-0.896	2.526	-42.190	-40.751	1.519	-0.906	-2.051	-0.019
95	A	95	THR	0	-0.041	-0.035	4.788	-2.111	-2.058	-0.001	-0.014	-0.038	0.000
5	A	5	LEU	0	-0.075	-0.034	8.797	-1.143	-1.143	0.000	0.000	0.000	0.000
6	A	6	GLU	-1	-0.851	-0.936	11.603	-16.240	-16.240	0.000	0.000	0.000	0.000
7	A	7	SER	0	-0.062	-0.037	14.619	-0.071	-0.071	0.000	0.000	0.000	0.000
8	A	8	LYS	1	0.939	0.990	16.415	15.508	15.508	0.000	0.000	0.000	0.000
9	A	9	LEU	0	0.041	0.032	20.209	-0.427	-0.427	0.000	0.000	0.000	0.000
10	A	10	SER	0	-0.033	-0.032	22.609	-0.287	-0.287	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.022	0.026	24.341	-0.077	-0.077	0.000	0.000	0.000	0.000
12	A	12	ILE	0	-0.005	0.000	22.816	-0.115	-0.115	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.834	0.899	27.146	9.447	9.447	0.000	0.000	0.000	0.000
14	A	14	ASN	0	0.017	-0.005	30.171	-0.445	-0.445	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.044	-0.025	32.238	0.139	0.139	0.000	0.000	0.000	0.000
16	A	16	ASN	0	-0.065	-0.036	35.086	0.166	0.166	0.000	0.000	0.000	0.000
17	A	17	ASP	-1	-0.852	-0.931	35.414	-8.582	-8.582	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.063	-0.035	34.985	-0.236	-0.236	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.018	0.006	30.113	-0.316	-0.316	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.045	-0.022	25.414	0.099	0.099	0.000	0.000	0.000	0.000
21	A	21	PHE	0	0.015	0.006	29.063	-0.178	-0.178	0.000	0.000	0.000	0.000
22	A	22	ILE	0	-0.075	-0.034	26.444	-0.259	-0.259	0.000	0.000	0.000	0.000
23	A	23	ASP	-1	-0.834	-0.907	29.872	-8.523	-8.523	0.000	0.000	0.000	0.000
24	A	24	GLN	0	-0.002	-0.014	31.333	-0.141	-0.141	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.036	-0.011	32.290	-0.087	-0.087	0.000	0.000	0.000	0.000
26	A	26	ASN	0	-0.044	-0.032	26.819	-0.123	-0.123	0.000	0.000	0.000	0.000
27	A	27	ARG	1	0.934	0.976	27.609	8.732	8.732	0.000	0.000	0.000	0.000
28	A	28	PRO	0	0.031	0.021	26.091	0.145	0.145	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.009	-0.006	28.474	0.150	0.150	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.012	-0.016	28.757	-0.353	-0.353	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.867	-0.938	33.191	-8.584	-8.584	0.000	0.000	0.000	0.000
32	A	32	ASP	-1	-0.877	-0.919	35.443	-8.119	-8.119	0.000	0.000	0.000	0.000
33	A	33	MET	0	-0.058	-0.036	32.446	0.104	0.104	0.000	0.000	0.000	0.000
34	A	34	THR	0	0.020	0.004	37.232	-0.084	-0.084	0.000	0.000	0.000	0.000
35	A	35	ASP	-1	-0.794	-0.878	34.653	-8.981	-8.981	0.000	0.000	0.000	0.000
36	A	36	SER	0	-0.046	-0.013	37.163	-0.074	-0.074	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.907	-0.954	40.313	-7.029	-7.029	0.000	0.000	0.000	0.000
38	A	38	CYS	0	-0.035	-0.032	39.944	-0.085	-0.085	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.915	0.943	36.474	8.036	8.036	0.000	0.000	0.000	0.000
40	A	40	ASP	-1	-0.960	-0.967	36.419	-8.026	-8.026	0.000	0.000	0.000	0.000
41	A	41	ASN	0	-0.015	-0.012	35.084	-0.098	-0.098	0.000	0.000	0.000	0.000
42	A	42	ALA	0	0.036	0.034	34.331	0.107	0.107	0.000	0.000	0.000	0.000
43	A	43	PRO	0	-0.026	-0.023	34.419	-0.184	-0.184	0.000	0.000	0.000	0.000
44	A	44	ARG	1	0.881	0.955	33.386	8.182	8.182	0.000	0.000	0.000	0.000
45	A	45	THR	0	0.052	0.028	27.386	-0.013	-0.013	0.000	0.000	0.000	0.000
46	A	46	ILE	0	0.012	0.018	25.502	0.013	0.013	0.000	0.000	0.000	0.000
47	A	47	PHE	0	-0.021	-0.031	22.513	-0.215	-0.215	0.000	0.000	0.000	0.000
48	A	48	ILE	0	-0.001	-0.008	18.568	-0.018	-0.018	0.000	0.000	0.000	0.000
49	A	49	ILE	0	0.020	0.011	17.608	-0.522	-0.522	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.011	0.006	12.048	-0.071	-0.071	0.000	0.000	0.000	0.000
51	A	51	MET	0	0.008	0.003	13.834	-0.104	-0.104	0.000	0.000	0.000	0.000
52	A	52	TYR	0	-0.030	-0.042	7.355	-0.504	-0.504	0.000	0.000	0.000	0.000
53	A	53	LYS	1	0.860	0.925	8.325	29.374	29.374	0.000	0.000	0.000	0.000
54	A	54	ASP	-1	-0.860	-0.927	7.911	-29.694	-29.694	0.000	0.000	0.000	0.000
55	A	55	SER	0	-0.035	-0.027	9.522	0.289	0.289	0.000	0.000	0.000	0.000
56	A	56	GLN	0	0.042	0.029	10.100	-1.290	-1.290	0.000	0.000	0.000	0.000
57	A	57	PRO	0	-0.013	-0.010	13.349	0.788	0.788	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.956	0.958	16.932	15.513	15.513	0.000	0.000	0.000	0.000
59	A	59	GLY	0	-0.018	-0.004	16.105	0.336	0.336	0.000	0.000	0.000	0.000
60	A	60	MET	0	-0.016	0.020	15.470	-0.531	-0.531	0.000	0.000	0.000	0.000
61	A	61	ALA	0	0.022	0.021	11.678	0.690	0.690	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.027	-0.011	13.475	-0.476	-0.476	0.000	0.000	0.000	0.000
63	A	63	THR	0	0.007	-0.002	12.551	-0.220	-0.220	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.043	0.024	15.639	0.391	0.391	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.033	-0.026	17.745	-0.119	-0.119	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.044	0.035	19.801	0.310	0.310	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.920	0.946	20.027	13.251	13.251	0.000	0.000	0.000	0.000
68	A	68	CYS	0	0.040	0.011	24.310	0.351	0.351	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.942	-0.947	27.766	-9.364	-9.364	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.868	0.928	25.162	11.408	11.408	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.040	-0.019	19.295	-0.102	-0.102	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.021	-0.008	20.967	0.050	0.050	0.000	0.000	0.000	0.000
73	A	73	THR	0	-0.034	-0.024	15.290	-0.061	-0.061	0.000	0.000	0.000	0.000
74	A	74	LEU	0	-0.025	0.002	18.672	0.323	0.323	0.000	0.000	0.000	0.000
75	A	75	SER	0	-0.013	-0.026	17.109	-0.943	-0.943	0.000	0.000	0.000	0.000
76	A	76	CYS	0	0.015	-0.001	17.158	0.877	0.877	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.811	-0.901	17.804	-13.193	-13.193	0.000	0.000	0.000	0.000
78	A	78	ASN	0	-0.120	-0.076	18.703	-0.137	-0.137	0.000	0.000	0.000	0.000
79	A	79	LYS	1	0.951	0.968	21.153	11.315	11.315	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.016	0.018	23.667	0.370	0.370	0.000	0.000	0.000	0.000
81	A	81	ILE	0	-0.003	0.007	21.729	-0.639	-0.639	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.029	-0.015	21.270	0.459	0.459	0.000	0.000	0.000	0.000
83	A	83	PHE	0	0.048	0.013	21.322	-0.616	-0.616	0.000	0.000	0.000	0.000
84	A	84	LYS	1	0.930	0.976	17.816	15.248	15.248	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.836	-0.923	19.767	-12.162	-12.162	0.000	0.000	0.000	0.000
86	A	86	MET	0	-0.029	-0.009	12.765	-0.320	-0.320	0.000	0.000	0.000	0.000
87	A	87	ASN	0	-0.027	0.003	13.201	0.978	0.978	0.000	0.000	0.000	0.000
88	A	88	PRO	0	0.065	0.023	13.219	-0.762	-0.762	0.000	0.000	0.000	0.000
89	A	89	PRO	0	-0.016	0.004	8.311	-0.010	-0.010	0.000	0.000	0.000	0.000
90	A	90	ASP	-1	-0.798	-0.874	7.615	-24.337	-24.337	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.871	0.943	6.434	27.306	27.306	0.000	0.000	0.000	0.000
97	A	97	SER	0	-0.029	-0.022	9.059	0.414	0.414	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.819	-0.900	10.382	-19.388	-19.388	0.000	0.000	0.000	0.000
99	A	99	ILE	0	-0.013	-0.021	11.185	0.885	0.885	0.000	0.000	0.000	0.000
100	A	100	ILE	0	-0.097	-0.027	9.764	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	101	PHE	0	0.031	0.016	13.254	0.858	0.858	0.000	0.000	0.000	0.000
102	A	102	PHE	0	0.012	-0.002	11.404	-1.135	-1.135	0.000	0.000	0.000	0.000
103	A	103	GLN	0	-0.013	0.007	16.673	0.976	0.976	0.000	0.000	0.000	0.000
104	A	104	ARG	1	0.910	0.950	18.706	14.638	14.638	0.000	0.000	0.000	0.000
105	A	105	SER	0	0.053	0.017	21.709	0.307	0.307	0.000	0.000	0.000	0.000
106	A	106	VAL	0	-0.017	-0.019	25.005	-0.112	-0.112	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.031	-0.008	27.699	0.179	0.179	0.000	0.000	0.000	0.000
108	A	108	GLY	0	0.006	-0.009	30.298	0.178	0.178	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.038	-0.028	31.764	0.351	0.351	0.000	0.000	0.000	0.000
110	A	110	ASP	-1	-0.918	-0.944	32.980	-9.362	-9.362	0.000	0.000	0.000	0.000
111	A	111	ASN	0	0.014	-0.005	28.098	-0.547	-0.547	0.000	0.000	0.000	0.000
112	A	112	LYS	1	0.822	0.921	29.028	9.961	9.961	0.000	0.000	0.000	0.000
113	A	113	MET	0	-0.034	-0.002	24.108	-0.501	-0.501	0.000	0.000	0.000	0.000
114	A	114	GLN	0	0.017	0.002	24.176	0.179	0.179	0.000	0.000	0.000	0.000
115	A	115	PHE	0	-0.018	-0.017	19.747	-0.649	-0.649	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.849	-0.930	19.002	-14.635	-14.635	0.000	0.000	0.000	0.000
117	A	117	SER	0	0.027	0.004	17.424	-1.077	-1.077	0.000	0.000	0.000	0.000
118	A	118	SER	0	-0.013	-0.005	12.174	-0.252	-0.252	0.000	0.000	0.000	0.000
119	A	119	SER	0	-0.048	-0.029	13.139	-1.436	-1.436	0.000	0.000	0.000	0.000
120	A	120	TYR	0	-0.040	-0.036	14.269	-0.820	-0.820	0.000	0.000	0.000	0.000
121	A	121	GLU	-1	-0.895	-0.931	17.014	-13.074	-13.074	0.000	0.000	0.000	0.000
122	A	122	GLY	0	-0.027	-0.003	20.715	-0.102	-0.102	0.000	0.000	0.000	0.000
123	A	123	TYR	0	-0.065	-0.044	21.037	0.726	0.726	0.000	0.000	0.000	0.000
124	A	124	PHE	0	0.047	0.013	21.765	-0.695	-0.695	0.000	0.000	0.000	0.000
125	A	125	LEU	0	-0.037	-0.016	21.561	0.328	0.328	0.000	0.000	0.000	0.000
126	A	126	ALA	0	0.033	0.018	24.869	0.190	0.190	0.000	0.000	0.000	0.000
127	A	127	CYS	0	-0.059	-0.016	28.666	-0.043	-0.043	0.000	0.000	0.000	0.000
128	A	128	GLU	-1	-0.753	-0.870	31.370	-9.212	-9.212	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.832	0.923	33.822	8.008	8.008	0.000	0.000	0.000	0.000
130	A	130	GLU	-1	-0.864	-0.911	35.246	-8.441	-8.441	0.000	0.000	0.000	0.000
131	A	131	ARG	1	0.962	0.971	37.796	7.396	7.396	0.000	0.000	0.000	0.000
132	A	132	ASP	-1	-0.838	-0.923	40.923	-7.248	-7.248	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.021	-0.006	36.104	-0.046	-0.046	0.000	0.000	0.000	0.000
134	A	134	PHE	0	-0.027	-0.021	34.083	0.045	0.045	0.000	0.000	0.000	0.000
135	A	135	LYS	1	0.815	0.895	31.404	8.520	8.520	0.000	0.000	0.000	0.000
136	A	136	LEU	0	-0.012	0.012	24.265	0.017	0.017	0.000	0.000	0.000	0.000
137	A	137	ILE	0	-0.046	-0.024	26.554	-0.183	-0.183	0.000	0.000	0.000	0.000
138	A	138	LEU	0	0.001	-0.001	21.323	-0.237	-0.237	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.840	0.906	25.161	9.820	9.820	0.000	0.000	0.000	0.000
140	A	140	LYS	1	0.868	0.939	26.434	10.289	10.289	0.000	0.000	0.000	0.000
141	A	141	GLU	-1	-0.843	-0.916	28.642	-9.120	-9.120	0.000	0.000	0.000	0.000
142	A	142	ASP	-1	-0.943	-0.977	31.211	-9.056	-9.056	0.000	0.000	0.000	0.000
143	A	143	GLU	-1	-0.917	-0.955	32.797	-8.912	-8.912	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.016	-0.026	26.587	-0.137	-0.137	0.000	0.000	0.000	0.000
145	A	145	GLY	0	-0.003	0.004	29.653	-0.277	-0.277	0.000	0.000	0.000	0.000
146	A	146	ASP	-1	-0.805	-0.888	32.298	-8.637	-8.637	0.000	0.000	0.000	0.000
147	A	147	ARG	1	0.956	0.964	32.225	8.006	8.006	0.000	0.000	0.000	0.000
148	A	148	SER	0	-0.022	-0.031	32.506	-0.164	-0.164	0.000	0.000	0.000	0.000
149	A	149	ILE	0	-0.014	-0.002	27.877	-0.114	-0.114	0.000	0.000	0.000	0.000
150	A	150	MET	0	-0.084	-0.002	27.612	-0.492	-0.492	0.000	0.000	0.000	0.000
151	A	151	PHE	0	0.021	0.005	25.889	0.306	0.306	0.000	0.000	0.000	0.000
152	A	152	THR	0	0.011	-0.006	28.296	0.114	0.114	0.000	0.000	0.000	0.000
153	A	153	VAL	0	-0.031	-0.005	22.745	-0.002	-0.002	0.000	0.000	0.000	0.000
154	A	154	GLN	0	0.026	0.019	26.138	-0.102	-0.102	0.000	0.000	0.000	0.000
155	A	155	ASN	0	-0.022	-0.028	23.835	-0.732	-0.732	0.000	0.000	0.000	0.000
156	A	156	GLU	-1	-0.951	-0.991	25.625	-10.245	-10.245	0.000	0.000	0.000	0.000
157	A	157	ASP	-2	-1.903	-1.923	26.297	-21.868	-21.868	0.000	0.000	0.000	0.000

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