FMO DATABASE

FMODB ID: Z98RN

Calculation Name: 1INZ-A-Other549

Preferred Name: Epsin-1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1INZ

Chain ID: A

ChEMBL ID: CHEMBL3259465

UniProt ID: Q9Y6I3

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
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	148
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1322713.97712
FMO2-HF: Nuclear repulsion	1260693.820038
FMO2-HF: Total energy	-62020.157082
FMO2-MP2: Total energy	-62196.018416

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:-3:GLY)

Summations of interaction energy for fragment #1(A:-3:GLY)

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.
41.457	44.435	4.632	-3.957	-3.652	-0.048

Interaction energy analysis for fragmet #1(A:-3:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.847 / 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

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	-1	SER	0	0.097	0.055	3.826	0.379	1.095	-0.014	-0.311	-0.391	-0.001
4	A	0	ARG	1	0.906	0.950	3.672	43.089	43.388	0.001	-0.111	-0.189	0.000
5	A	1	MET	0	0.041	0.009	2.038	-45.364	-43.637	4.646	-3.470	-2.902	-0.047
6	A	2	SER	0	0.010	0.000	3.457	5.195	5.449	0.000	-0.065	-0.190	0.000
7	A	3	THR	0	0.017	0.019	5.360	2.379	2.361	-0.001	0.000	0.020	0.000
8	A	4	SER	0	0.007	-0.005	8.943	2.066	2.066	0.000	0.000	0.000	0.000
9	A	5	SER	0	-0.004	0.004	9.990	-0.809	-0.809	0.000	0.000	0.000	0.000
10	A	6	LEU	0	0.037	0.020	11.124	-0.240	-0.240	0.000	0.000	0.000	0.000
11	A	7	ARG	1	0.913	0.952	13.762	17.762	17.762	0.000	0.000	0.000	0.000
12	A	8	ARG	1	0.990	0.994	15.840	13.242	13.242	0.000	0.000	0.000	0.000
13	A	9	GLN	0	0.039	0.030	17.808	-0.198	-0.198	0.000	0.000	0.000	0.000
14	A	10	MET	0	-0.021	-0.011	20.021	0.427	0.427	0.000	0.000	0.000	0.000
15	A	11	LYS	1	0.968	0.975	22.822	10.523	10.523	0.000	0.000	0.000	0.000
16	A	12	ASN	0	-0.005	0.000	24.425	-0.459	-0.459	0.000	0.000	0.000	0.000
17	A	13	ILE	0	0.035	0.010	25.418	0.262	0.262	0.000	0.000	0.000	0.000
18	A	14	VAL	0	-0.003	0.006	28.319	-0.066	-0.066	0.000	0.000	0.000	0.000
19	A	15	HIS	0	0.062	0.025	31.650	-0.105	-0.105	0.000	0.000	0.000	0.000
20	A	16	ASN	0	-0.049	-0.020	33.220	0.291	0.291	0.000	0.000	0.000	0.000
21	A	17	TYR	0	0.020	0.008	33.223	-0.102	-0.102	0.000	0.000	0.000	0.000
22	A	18	SER	0	-0.009	-0.011	37.524	0.287	0.287	0.000	0.000	0.000	0.000
23	A	19	GLU	-1	-0.880	-0.932	36.948	-8.507	-8.507	0.000	0.000	0.000	0.000
24	A	20	ALA	0	0.002	-0.011	39.644	0.102	0.102	0.000	0.000	0.000	0.000
25	A	21	GLU	-1	-0.872	-0.947	42.354	-7.477	-7.477	0.000	0.000	0.000	0.000
26	A	22	ILE	0	-0.006	-0.013	39.637	0.142	0.142	0.000	0.000	0.000	0.000
27	A	23	LYS	1	0.825	0.916	39.670	8.094	8.094	0.000	0.000	0.000	0.000
28	A	24	VAL	0	0.049	0.015	43.928	0.141	0.141	0.000	0.000	0.000	0.000
29	A	25	ARG	1	0.899	0.965	45.329	7.090	7.090	0.000	0.000	0.000	0.000
30	A	26	GLU	-1	-0.869	-0.942	43.312	-7.162	-7.162	0.000	0.000	0.000	0.000
31	A	27	ALA	0	-0.026	-0.008	46.478	0.088	0.088	0.000	0.000	0.000	0.000
32	A	28	THR	0	-0.102	-0.056	48.813	0.181	0.181	0.000	0.000	0.000	0.000
33	A	29	SER	0	-0.082	-0.078	49.902	0.208	0.208	0.000	0.000	0.000	0.000
34	A	30	ASN	0	-0.026	-0.001	46.250	-0.143	-0.143	0.000	0.000	0.000	0.000
35	A	31	ASP	-1	-0.906	-0.932	48.972	-6.158	-6.158	0.000	0.000	0.000	0.000
36	A	32	PRO	0	-0.011	0.004	44.166	0.004	0.004	0.000	0.000	0.000	0.000
37	A	33	TRP	0	0.027	0.004	42.794	-0.001	-0.001	0.000	0.000	0.000	0.000
38	A	34	GLY	0	0.016	-0.001	40.638	-0.102	-0.102	0.000	0.000	0.000	0.000
39	A	35	PRO	0	-0.036	-0.009	38.605	0.059	0.059	0.000	0.000	0.000	0.000
40	A	36	SER	0	0.006	0.004	40.669	0.134	0.134	0.000	0.000	0.000	0.000
41	A	37	SER	0	0.017	0.006	40.747	0.065	0.065	0.000	0.000	0.000	0.000
42	A	38	SER	0	0.021	-0.009	43.456	0.203	0.203	0.000	0.000	0.000	0.000
43	A	39	LEU	0	0.017	0.016	42.689	-0.041	-0.041	0.000	0.000	0.000	0.000
44	A	40	MET	0	0.015	-0.003	45.167	-0.029	-0.029	0.000	0.000	0.000	0.000
45	A	41	SER	0	0.007	0.017	45.088	0.053	0.053	0.000	0.000	0.000	0.000
46	A	42	GLU	-1	-0.774	-0.884	39.762	-8.116	-8.116	0.000	0.000	0.000	0.000
47	A	43	ILE	0	-0.035	-0.005	43.739	-0.010	-0.010	0.000	0.000	0.000	0.000
48	A	44	ALA	0	0.009	-0.009	46.248	0.069	0.069	0.000	0.000	0.000	0.000
49	A	45	ASP	-1	-0.884	-0.933	41.359	-7.567	-7.567	0.000	0.000	0.000	0.000
50	A	46	LEU	0	0.000	-0.007	40.783	0.022	0.022	0.000	0.000	0.000	0.000
51	A	47	THR	0	-0.113	-0.072	44.451	0.102	0.102	0.000	0.000	0.000	0.000
52	A	48	TYR	0	0.007	0.015	45.814	0.115	0.115	0.000	0.000	0.000	0.000
53	A	49	ASN	0	-0.010	0.005	41.386	0.101	0.101	0.000	0.000	0.000	0.000
54	A	50	VAL	0	-0.034	-0.032	45.028	0.176	0.176	0.000	0.000	0.000	0.000
55	A	51	VAL	0	0.026	0.009	43.095	0.128	0.128	0.000	0.000	0.000	0.000
56	A	52	ALA	0	0.046	0.018	43.149	0.129	0.129	0.000	0.000	0.000	0.000
57	A	53	PHE	0	0.048	0.021	45.192	0.092	0.092	0.000	0.000	0.000	0.000
58	A	54	SER	0	0.030	0.018	48.700	0.176	0.176	0.000	0.000	0.000	0.000
59	A	55	GLU	-1	-0.907	-0.943	44.800	-6.916	-6.916	0.000	0.000	0.000	0.000
60	A	56	ILE	0	-0.042	-0.027	46.088	0.072	0.072	0.000	0.000	0.000	0.000
61	A	57	MET	0	0.011	0.017	49.410	0.065	0.065	0.000	0.000	0.000	0.000
62	A	58	SER	0	-0.021	-0.011	51.106	0.151	0.151	0.000	0.000	0.000	0.000
63	A	59	MET	0	-0.094	-0.046	46.409	0.075	0.075	0.000	0.000	0.000	0.000
64	A	60	ILE	0	0.020	0.013	51.690	0.061	0.061	0.000	0.000	0.000	0.000
65	A	61	TRP	0	0.046	-0.004	54.107	0.118	0.118	0.000	0.000	0.000	0.000
66	A	62	LYS	1	0.893	0.949	51.948	6.205	6.205	0.000	0.000	0.000	0.000
67	A	63	ARG	1	0.905	0.958	49.581	6.334	6.334	0.000	0.000	0.000	0.000
68	A	64	LEU	0	0.020	0.010	55.883	0.051	0.051	0.000	0.000	0.000	0.000
69	A	65	ASN	0	-0.005	-0.001	59.145	0.127	0.127	0.000	0.000	0.000	0.000
70	A	66	ASP	-1	-0.881	-0.940	57.215	-5.641	-5.641	0.000	0.000	0.000	0.000
71	A	67	HIS	0	0.040	0.023	59.428	0.163	0.163	0.000	0.000	0.000	0.000
72	A	68	GLY	0	0.071	0.030	62.653	-0.011	-0.011	0.000	0.000	0.000	0.000
73	A	69	LYS	1	0.745	0.849	62.550	5.009	5.009	0.000	0.000	0.000	0.000
74	A	70	ASN	0	-0.073	-0.061	58.695	-0.110	-0.110	0.000	0.000	0.000	0.000
75	A	71	TRP	0	0.094	0.050	59.715	-0.134	-0.134	0.000	0.000	0.000	0.000
76	A	72	ARG	1	0.945	0.986	55.333	5.645	5.645	0.000	0.000	0.000	0.000
77	A	73	HIS	1	0.888	0.944	54.243	5.799	5.799	0.000	0.000	0.000	0.000
78	A	74	VAL	0	0.079	0.068	56.330	-0.080	-0.080	0.000	0.000	0.000	0.000
79	A	75	TYR	0	0.008	-0.007	58.768	-0.016	-0.016	0.000	0.000	0.000	0.000
80	A	76	LYS	1	0.934	0.989	53.189	5.938	5.938	0.000	0.000	0.000	0.000
81	A	77	ALA	0	0.033	0.006	54.587	-0.082	-0.082	0.000	0.000	0.000	0.000
82	A	78	MET	0	-0.048	0.013	55.615	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	79	THR	0	-0.043	-0.025	54.416	0.016	0.016	0.000	0.000	0.000	0.000
84	A	80	LEU	0	-0.012	-0.001	49.771	-0.041	-0.041	0.000	0.000	0.000	0.000
85	A	81	MET	0	0.003	0.008	53.515	-0.046	-0.046	0.000	0.000	0.000	0.000
86	A	82	GLU	-1	-0.842	-0.915	55.884	-5.378	-5.378	0.000	0.000	0.000	0.000
87	A	83	TYR	0	-0.036	-0.016	49.358	-0.011	-0.011	0.000	0.000	0.000	0.000
88	A	84	LEU	0	-0.012	-0.007	49.504	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	85	ILE	0	0.011	0.007	52.983	-0.034	-0.034	0.000	0.000	0.000	0.000
90	A	86	LYS	1	0.936	0.981	55.866	5.631	5.631	0.000	0.000	0.000	0.000
91	A	87	THR	0	0.023	0.007	50.296	-0.011	-0.011	0.000	0.000	0.000	0.000
92	A	88	GLY	0	-0.015	0.007	49.804	-0.150	-0.150	0.000	0.000	0.000	0.000
93	A	89	SER	0	0.034	-0.007	50.123	-0.109	-0.109	0.000	0.000	0.000	0.000
94	A	90	GLU	-1	-0.843	-0.915	52.631	-5.690	-5.690	0.000	0.000	0.000	0.000
95	A	91	ARG	1	0.839	0.938	49.082	6.547	6.547	0.000	0.000	0.000	0.000
96	A	92	VAL	0	0.004	-0.004	52.455	0.052	0.052	0.000	0.000	0.000	0.000
97	A	93	SER	0	0.030	0.013	55.346	0.115	0.115	0.000	0.000	0.000	0.000
98	A	94	GLN	0	0.013	0.009	58.149	0.161	0.161	0.000	0.000	0.000	0.000
99	A	95	GLN	0	0.028	0.008	55.947	0.024	0.024	0.000	0.000	0.000	0.000
100	A	96	CYS	0	-0.044	-0.013	58.922	0.082	0.082	0.000	0.000	0.000	0.000
101	A	97	LYS	1	0.888	0.944	60.739	5.133	5.133	0.000	0.000	0.000	0.000
102	A	98	GLU	-1	-0.928	-0.967	61.217	-4.999	-4.999	0.000	0.000	0.000	0.000
103	A	99	ASN	0	-0.031	-0.019	59.670	0.136	0.136	0.000	0.000	0.000	0.000
104	A	100	MET	0	0.024	0.029	62.992	0.015	0.015	0.000	0.000	0.000	0.000
105	A	101	TYR	0	0.045	0.003	65.363	0.036	0.036	0.000	0.000	0.000	0.000
106	A	102	ALA	0	0.003	0.011	62.105	0.030	0.030	0.000	0.000	0.000	0.000
107	A	103	VAL	0	-0.021	-0.014	61.891	-0.061	-0.061	0.000	0.000	0.000	0.000
108	A	104	GLN	0	-0.009	-0.021	64.248	0.014	0.014	0.000	0.000	0.000	0.000
109	A	105	THR	0	-0.025	0.005	65.218	0.051	0.051	0.000	0.000	0.000	0.000
110	A	106	LEU	0	0.009	-0.007	62.026	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	107	LYS	1	0.924	0.965	66.666	4.450	4.450	0.000	0.000	0.000	0.000
112	A	108	ASP	-1	-0.937	-0.973	69.820	-4.554	-4.554	0.000	0.000	0.000	0.000
113	A	109	PHE	0	0.023	0.020	63.888	0.029	0.029	0.000	0.000	0.000	0.000
114	A	110	GLN	0	-0.058	-0.022	68.628	0.011	0.011	0.000	0.000	0.000	0.000
115	A	111	TYR	0	-0.005	-0.021	68.140	0.028	0.028	0.000	0.000	0.000	0.000
116	A	112	VAL	0	-0.036	-0.001	68.822	-0.065	-0.065	0.000	0.000	0.000	0.000
117	A	113	ASP	-1	-0.809	-0.891	67.499	-4.812	-4.812	0.000	0.000	0.000	0.000
118	A	114	ARG	1	0.946	0.962	70.446	4.428	4.428	0.000	0.000	0.000	0.000
119	A	115	ASP	-1	-0.900	-0.951	73.286	-4.178	-4.178	0.000	0.000	0.000	0.000
120	A	116	GLY	0	0.002	0.018	71.826	-0.066	-0.066	0.000	0.000	0.000	0.000
121	A	117	LYS	1	0.882	0.926	70.903	4.438	4.438	0.000	0.000	0.000	0.000
122	A	118	ASP	-1	-0.864	-0.924	70.571	-4.542	-4.542	0.000	0.000	0.000	0.000
123	A	119	GLN	0	-0.005	-0.009	64.885	-0.060	-0.060	0.000	0.000	0.000	0.000
124	A	120	GLY	0	0.008	0.007	67.057	-0.075	-0.075	0.000	0.000	0.000	0.000
125	A	121	VAL	0	0.046	0.012	68.027	-0.022	-0.022	0.000	0.000	0.000	0.000
126	A	122	ASN	0	0.013	0.008	63.228	0.048	0.048	0.000	0.000	0.000	0.000
127	A	123	VAL	0	-0.024	-0.027	62.551	-0.055	-0.055	0.000	0.000	0.000	0.000
128	A	124	ARG	1	0.974	1.008	64.506	4.428	4.428	0.000	0.000	0.000	0.000
129	A	125	GLU	-1	-0.912	-0.963	67.869	-4.556	-4.556	0.000	0.000	0.000	0.000
130	A	126	LYS	1	0.809	0.900	60.231	5.301	5.301	0.000	0.000	0.000	0.000
131	A	127	ALA	0	0.069	0.019	63.774	-0.057	-0.057	0.000	0.000	0.000	0.000
132	A	128	LYS	1	0.948	0.977	65.006	4.582	4.582	0.000	0.000	0.000	0.000
133	A	129	GLN	0	-0.035	-0.021	64.267	0.053	0.053	0.000	0.000	0.000	0.000
134	A	130	LEU	0	0.003	0.003	59.288	-0.004	-0.004	0.000	0.000	0.000	0.000
135	A	131	VAL	0	-0.006	-0.018	63.433	-0.015	-0.015	0.000	0.000	0.000	0.000
136	A	132	ALA	0	-0.036	-0.019	66.060	0.029	0.029	0.000	0.000	0.000	0.000
137	A	133	LEU	0	0.003	0.002	62.258	0.013	0.013	0.000	0.000	0.000	0.000
138	A	134	LEU	0	-0.058	-0.017	60.778	-0.028	-0.028	0.000	0.000	0.000	0.000
139	A	135	ARG	1	0.770	0.870	64.665	4.675	4.675	0.000	0.000	0.000	0.000
140	A	136	ASP	-1	-0.917	-0.935	68.505	-4.526	-4.526	0.000	0.000	0.000	0.000
141	A	137	GLU	-1	-0.937	-0.965	70.692	-4.200	-4.200	0.000	0.000	0.000	0.000
142	A	138	ASP	-1	-0.854	-0.913	72.185	-4.568	-4.568	0.000	0.000	0.000	0.000
143	A	139	ARG	1	0.915	0.945	74.309	4.213	4.213	0.000	0.000	0.000	0.000
144	A	140	LEU	0	-0.030	-0.015	76.223	0.039	0.039	0.000	0.000	0.000	0.000
145	A	141	ARG	1	0.819	0.907	72.068	4.369	4.369	0.000	0.000	0.000	0.000
146	A	142	GLU	-1	-0.939	-0.976	76.637	-4.074	-4.074	0.000	0.000	0.000	0.000
147	A	143	GLU	-1	-0.890	-0.938	74.904	-4.404	-4.404	0.000	0.000	0.000	0.000
148	A	144	ARG	0	0.022	0.026	78.055	-0.041	-0.041	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-3:GLY)