FMO DATABASE

FMODB ID: Y97V2

Calculation Name: 1E3O-C-Xray547

Preferred Name: POU domain, class 2, transcription factor 1

Target Type: SINGLE PROTEIN

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1E3O

Chain ID: C

ChEMBL ID: CHEMBL3509601

UniProt ID: P14859

Base Structure: X-ray

Registration Date: 2025-09-02

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	132
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1130559.523254
FMO2-HF: Nuclear repulsion	1076224.164311
FMO2-HF: Total energy	-54335.358943
FMO2-MP2: Total energy	-54494.172276

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:GLU)

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

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.
2.163	8.082	0.501	-2.417	-4.001	-0.008

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.149 / q_NPA : -0.083

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	PRO	0	-0.044	-0.013	3.074	0.923	4.570	0.089	-1.550	-2.186	-0.003
4	A	4	SER	0	-0.003	-0.005	2.782	0.242	1.370	0.385	-0.553	-0.959	-0.007
5	A	5	ASP	-1	-0.774	-0.875	3.533	16.446	17.363	0.029	-0.292	-0.654	0.002
6	A	6	LEU	0	-0.036	-0.047	5.079	-4.804	-4.711	-0.001	-0.009	-0.082	0.000
57	A	57	PHE	0	0.110	0.059	4.506	-2.678	-2.544	-0.001	-0.013	-0.120	0.000
7	A	7	GLU	-1	-0.886	-0.934	7.878	5.306	5.306	0.000	0.000	0.000	0.000
8	A	8	GLU	-1	-0.882	-0.943	5.511	2.248	2.248	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.088	-0.037	8.398	-1.720	-1.720	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.913	-0.971	10.438	4.024	4.024	0.000	0.000	0.000	0.000
11	A	11	GLN	0	-0.004	-0.001	12.576	-0.919	-0.919	0.000	0.000	0.000	0.000
12	A	12	PHE	0	0.021	0.004	12.247	-0.505	-0.505	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.011	0.003	14.082	-0.444	-0.444	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.849	0.930	16.494	-2.206	-2.206	0.000	0.000	0.000	0.000
15	A	15	THR	0	0.043	0.014	16.888	-0.315	-0.315	0.000	0.000	0.000	0.000
16	A	16	PHE	0	0.013	0.009	17.926	-0.195	-0.195	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.918	0.959	19.711	-1.689	-1.689	0.000	0.000	0.000	0.000
18	A	18	GLN	0	-0.033	-0.026	21.787	-0.059	-0.059	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.835	0.904	22.315	-0.474	-0.474	0.000	0.000	0.000	0.000
20	A	20	ARG	1	0.857	0.923	23.801	-1.172	-1.172	0.000	0.000	0.000	0.000
21	A	21	ILE	0	-0.054	-0.021	25.677	-0.058	-0.058	0.000	0.000	0.000	0.000
22	A	22	LYS	1	0.901	0.950	27.347	-0.487	-0.487	0.000	0.000	0.000	0.000
23	A	23	LEU	0	-0.013	-0.009	26.105	-0.059	-0.059	0.000	0.000	0.000	0.000
24	A	24	GLY	0	-0.034	0.005	29.729	-0.039	-0.039	0.000	0.000	0.000	0.000
25	A	25	PHE	0	0.014	0.014	28.114	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.025	-0.049	29.216	0.102	0.102	0.000	0.000	0.000	0.000
27	A	27	GLN	0	-0.029	-0.047	24.952	-0.052	-0.052	0.000	0.000	0.000	0.000
28	A	28	GLY	0	-0.004	-0.005	27.082	0.035	0.035	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.793	-0.863	29.555	0.564	0.564	0.000	0.000	0.000	0.000
30	A	30	VAL	0	0.015	0.016	23.316	-0.033	-0.033	0.000	0.000	0.000	0.000
31	A	31	GLY	0	0.008	0.006	25.520	-0.012	-0.012	0.000	0.000	0.000	0.000
32	A	32	LEU	0	0.008	-0.005	26.528	-0.037	-0.037	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.001	0.000	27.147	-0.056	-0.056	0.000	0.000	0.000	0.000
34	A	34	MET	0	-0.028	-0.003	20.842	-0.053	-0.053	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.031	0.020	25.154	-0.053	-0.053	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.858	0.912	27.826	-0.343	-0.343	0.000	0.000	0.000	0.000
37	A	37	LEU	0	0.007	0.023	26.521	-0.043	-0.043	0.000	0.000	0.000	0.000
38	A	38	TYR	0	-0.065	-0.049	23.171	-0.031	-0.031	0.000	0.000	0.000	0.000
39	A	39	GLY	0	0.003	0.021	24.769	-0.016	-0.016	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.080	-0.054	21.931	-0.021	-0.021	0.000	0.000	0.000	0.000
41	A	41	ASP	-1	-0.900	-0.933	24.567	0.690	0.690	0.000	0.000	0.000	0.000
42	A	42	PHE	0	-0.028	-0.021	20.399	0.152	0.152	0.000	0.000	0.000	0.000
43	A	43	SER	0	0.036	0.026	25.356	-0.013	-0.013	0.000	0.000	0.000	0.000
44	A	44	GLN	0	0.072	0.020	25.686	0.078	0.078	0.000	0.000	0.000	0.000
45	A	45	THR	0	-0.040	-0.026	25.369	0.068	0.068	0.000	0.000	0.000	0.000
46	A	46	THR	0	-0.050	-0.028	20.903	0.168	0.168	0.000	0.000	0.000	0.000
47	A	47	ILE	0	0.045	0.031	21.174	0.207	0.207	0.000	0.000	0.000	0.000
48	A	48	SER	0	-0.035	-0.012	21.834	0.164	0.164	0.000	0.000	0.000	0.000
49	A	49	ARG	1	0.929	0.954	20.171	-1.638	-1.638	0.000	0.000	0.000	0.000
50	A	50	PHE	0	0.040	0.017	14.136	0.287	0.287	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.760	-0.886	17.595	1.603	1.603	0.000	0.000	0.000	0.000
52	A	52	ALA	0	-0.060	-0.015	20.118	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	53	LEU	0	0.073	0.048	13.062	0.144	0.144	0.000	0.000	0.000	0.000
54	A	54	ASN	0	-0.091	-0.036	16.493	0.028	0.028	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.103	-0.082	15.686	-0.377	-0.377	0.000	0.000	0.000	0.000
56	A	56	SER	0	0.039	0.030	13.250	0.352	0.352	0.000	0.000	0.000	0.000
58	A	58	LYS	1	0.970	0.992	9.627	-3.861	-3.861	0.000	0.000	0.000	0.000
59	A	59	ASN	0	-0.035	-0.032	10.685	-0.748	-0.748	0.000	0.000	0.000	0.000
60	A	60	MET	0	0.025	0.039	11.291	-0.711	-0.711	0.000	0.000	0.000	0.000
61	A	61	SER	0	0.057	0.015	7.948	-0.054	-0.054	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.882	0.949	10.144	-2.518	-2.518	0.000	0.000	0.000	0.000
63	A	63	LEU	0	-0.006	-0.013	13.104	-0.519	-0.519	0.000	0.000	0.000	0.000
64	A	64	LYS	1	0.904	0.966	9.586	-1.780	-1.780	0.000	0.000	0.000	0.000
65	A	65	PRO	0	0.026	0.007	11.299	-0.368	-0.368	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.061	-0.019	13.922	-0.284	-0.284	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.011	-0.010	16.815	-0.185	-0.185	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.848	-0.920	12.761	0.448	0.448	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.919	0.970	16.800	-0.099	-0.099	0.000	0.000	0.000	0.000
70	A	70	TRP	0	0.061	0.017	19.692	-0.018	-0.018	0.000	0.000	0.000	0.000
71	A	71	LEU	0	-0.065	-0.039	17.342	0.004	0.004	0.000	0.000	0.000	0.000
72	A	72	ASN	0	-0.017	-0.012	17.161	-0.055	-0.055	0.000	0.000	0.000	0.000
73	A	73	ASP	-1	-0.918	-0.945	21.240	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.071	-0.037	24.435	-0.018	-0.018	0.000	0.000	0.000	0.000
75	A	75	GLU	-2	-1.744	-1.830	22.902	0.439	0.439	0.000	0.000	0.000	0.000
76	A	104	LYS	1	0.980	0.973	41.564	-0.536	-0.536	0.000	0.000	0.000	0.000
77	A	105	ARG	1	0.958	0.986	36.191	-0.686	-0.686	0.000	0.000	0.000	0.000
78	A	106	THR	0	0.044	0.023	38.349	-0.018	-0.018	0.000	0.000	0.000	0.000
79	A	107	SER	0	-0.018	-0.007	37.630	0.060	0.060	0.000	0.000	0.000	0.000
80	A	108	ILE	0	0.037	0.022	34.072	-0.028	-0.028	0.000	0.000	0.000	0.000
81	A	109	GLU	-1	-0.757	-0.854	37.968	0.739	0.739	0.000	0.000	0.000	0.000
82	A	110	THR	0	-0.019	-0.034	38.414	0.055	0.055	0.000	0.000	0.000	0.000
83	A	111	ASN	0	0.021	-0.010	38.292	0.035	0.035	0.000	0.000	0.000	0.000
84	A	112	ILE	0	0.036	0.016	37.734	0.014	0.014	0.000	0.000	0.000	0.000
85	A	113	ARG	1	0.836	0.913	34.112	-0.912	-0.912	0.000	0.000	0.000	0.000
86	A	114	VAL	0	0.020	0.014	34.026	0.058	0.058	0.000	0.000	0.000	0.000
87	A	115	ALA	0	0.037	0.030	35.075	0.033	0.033	0.000	0.000	0.000	0.000
88	A	116	LEU	0	0.005	0.008	32.872	0.021	0.021	0.000	0.000	0.000	0.000
89	A	117	GLU	-1	-0.851	-0.923	28.649	1.598	1.598	0.000	0.000	0.000	0.000
90	A	118	LYS	1	0.825	0.905	30.745	-1.028	-1.028	0.000	0.000	0.000	0.000
91	A	119	SER	0	0.009	0.012	32.656	0.028	0.028	0.000	0.000	0.000	0.000
92	A	120	PHE	0	-0.026	-0.030	23.442	0.019	0.019	0.000	0.000	0.000	0.000
93	A	121	MET	0	-0.041	-0.021	28.017	0.057	0.057	0.000	0.000	0.000	0.000
94	A	122	GLU	-1	-0.886	-0.919	29.250	0.972	0.972	0.000	0.000	0.000	0.000
95	A	123	ASN	0	0.020	0.004	28.828	0.099	0.099	0.000	0.000	0.000	0.000
96	A	124	GLN	0	0.061	0.034	21.986	0.050	0.050	0.000	0.000	0.000	0.000
97	A	125	LYS	1	0.870	0.924	25.004	-1.280	-1.280	0.000	0.000	0.000	0.000
98	A	126	PRO	0	0.020	0.036	27.701	-0.041	-0.041	0.000	0.000	0.000	0.000
99	A	127	THR	0	-0.059	-0.065	31.078	0.014	0.014	0.000	0.000	0.000	0.000
100	A	128	SER	0	-0.019	-0.029	33.308	0.018	0.018	0.000	0.000	0.000	0.000
101	A	129	GLU	-1	-0.809	-0.881	35.722	0.654	0.654	0.000	0.000	0.000	0.000
102	A	130	ASP	-1	-0.803	-0.865	34.545	0.852	0.852	0.000	0.000	0.000	0.000
103	A	131	ILE	0	-0.048	-0.036	31.735	0.010	0.010	0.000	0.000	0.000	0.000
104	A	132	THR	0	0.004	-0.007	36.140	-0.018	-0.018	0.000	0.000	0.000	0.000
105	A	133	LEU	0	0.046	0.040	39.845	-0.013	-0.013	0.000	0.000	0.000	0.000
106	A	134	ILE	0	-0.038	-0.028	34.763	-0.003	-0.003	0.000	0.000	0.000	0.000
107	A	135	ALA	0	-0.038	-0.025	38.793	0.001	0.001	0.000	0.000	0.000	0.000
108	A	136	GLU	-1	-0.901	-0.954	40.142	0.534	0.534	0.000	0.000	0.000	0.000
109	A	137	GLN	0	-0.064	-0.030	41.161	-0.014	-0.014	0.000	0.000	0.000	0.000
110	A	138	LEU	0	-0.041	-0.018	37.880	0.001	0.001	0.000	0.000	0.000	0.000
111	A	139	ASN	0	-0.056	-0.013	42.385	-0.022	-0.022	0.000	0.000	0.000	0.000
112	A	140	MET	0	-0.078	-0.037	38.510	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	141	GLU	-1	-0.843	-0.927	40.112	0.658	0.658	0.000	0.000	0.000	0.000
114	A	142	LYS	0	0.054	0.007	37.727	0.056	0.056	0.000	0.000	0.000	0.000
115	A	143	GLU	-1	-0.775	-0.844	34.101	0.899	0.899	0.000	0.000	0.000	0.000
116	A	144	VAL	0	-0.050	-0.029	34.490	0.070	0.070	0.000	0.000	0.000	0.000
117	A	145	ILE	0	0.039	0.026	34.082	0.081	0.081	0.000	0.000	0.000	0.000
118	A	146	ARG	1	0.826	0.872	29.921	-0.843	-0.843	0.000	0.000	0.000	0.000
119	A	147	VAL	0	-0.024	-0.019	30.094	0.110	0.110	0.000	0.000	0.000	0.000
120	A	148	TRP	0	-0.026	0.000	29.185	0.117	0.117	0.000	0.000	0.000	0.000
121	A	149	PHE	0	0.083	0.020	28.548	0.131	0.131	0.000	0.000	0.000	0.000
122	A	150	SER	0	-0.104	-0.046	25.311	0.122	0.122	0.000	0.000	0.000	0.000
123	A	151	ASN	0	-0.041	-0.036	24.497	0.234	0.234	0.000	0.000	0.000	0.000
124	A	152	ARG	1	0.716	0.841	23.277	-1.750	-1.750	0.000	0.000	0.000	0.000
125	A	153	ARG	1	0.944	0.964	22.080	-1.392	-1.392	0.000	0.000	0.000	0.000
126	A	154	GLN	0	-0.074	-0.032	20.185	0.159	0.159	0.000	0.000	0.000	0.000
127	A	155	LYS	1	0.924	0.960	19.571	-1.550	-1.550	0.000	0.000	0.000	0.000
128	A	156	GLU	-1	-0.797	-0.879	19.686	2.603	2.603	0.000	0.000	0.000	0.000
129	A	157	LYS	1	0.904	0.959	15.656	-2.747	-2.747	0.000	0.000	0.000	0.000
130	A	158	ARG	1	0.833	0.928	14.830	-1.995	-1.995	0.000	0.000	0.000	0.000
131	A	159	ILE	0	0.030	0.023	10.846	0.305	0.305	0.000	0.000	0.000	0.000
132	A	160	ASN	-1	-0.851	-0.918	14.670	2.718	2.718	0.000	0.000	0.000	0.000

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