FMO DATABASE

FMODB ID: 1Y6KZ

Calculation Name: 3P3V-A-Xray547

Preferred Name:

Target Type:

Ligand Name: triethylene glycol | di(hydroxyethyl)ether

Ligand 3-letter code: PGE | PEG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3P3V

Chain ID: A

ChEMBL ID:

UniProt ID: Q9A0T4

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	162
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1603792.936045
FMO2-HF: Nuclear repulsion	1541269.836289
FMO2-HF: Total energy	-62523.099755
FMO2-MP2: Total energy	-62705.958605

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:MET)

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

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.
-32.564	-30.26	2.855	-1.664	-3.495	-0.004

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.834 / q_NPA : 0.906

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	GLN	0	-0.066	-0.030	3.850	-0.678	1.202	-0.018	-0.842	-1.020	-0.003
76	A	76	PRO	0	0.002	-0.019	2.490	-0.247	0.058	2.874	-0.796	-2.384	-0.001
77	A	77	ALA	0	-0.018	0.001	4.439	-0.847	-0.728	-0.001	-0.026	-0.091	0.000
4	A	4	PRO	0	0.052	0.041	6.160	-0.407	-0.407	0.000	0.000	0.000	0.000
5	A	5	ASN	0	0.007	-0.013	7.151	0.563	0.563	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.023	-0.006	9.125	1.593	1.593	0.000	0.000	0.000	0.000
7	A	7	ILE	0	-0.023	-0.008	11.181	-0.167	-0.167	0.000	0.000	0.000	0.000
8	A	8	MET	0	0.008	0.001	14.421	1.045	1.045	0.000	0.000	0.000	0.000
9	A	9	THR	0	0.033	0.025	18.011	-0.334	-0.334	0.000	0.000	0.000	0.000
10	A	10	ARG	1	0.750	0.875	20.230	11.588	11.588	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.016	0.029	23.782	-0.024	-0.024	0.000	0.000	0.000	0.000
12	A	12	ASP	-1	-0.766	-0.892	27.058	-10.131	-10.131	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.804	-0.902	29.239	-8.786	-8.786	0.000	0.000	0.000	0.000
14	A	14	ARG	1	0.853	0.938	31.396	9.189	9.189	0.000	0.000	0.000	0.000
15	A	15	LEU	0	-0.009	-0.009	26.575	-0.045	-0.045	0.000	0.000	0.000	0.000
16	A	16	ILE	0	-0.003	-0.005	23.585	-0.139	-0.139	0.000	0.000	0.000	0.000
17	A	17	HIS	0	0.001	-0.010	27.059	-0.052	-0.052	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.028	0.015	29.510	0.353	0.353	0.000	0.000	0.000	0.000
19	A	19	GLN	0	0.015	0.002	29.023	-0.353	-0.353	0.000	0.000	0.000	0.000
20	A	20	GLY	0	0.068	0.039	25.149	-0.357	-0.357	0.000	0.000	0.000	0.000
21	A	21	GLN	0	-0.026	-0.018	24.167	-0.491	-0.491	0.000	0.000	0.000	0.000
22	A	22	LEU	0	-0.059	-0.027	25.218	-0.160	-0.160	0.000	0.000	0.000	0.000
23	A	23	TRP	0	0.041	0.014	22.230	-0.557	-0.557	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.003	0.005	19.820	-0.526	-0.526	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.890	0.941	20.062	10.996	10.996	0.000	0.000	0.000	0.000
26	A	26	PHE	0	-0.015	-0.006	21.444	-0.291	-0.291	0.000	0.000	0.000	0.000
27	A	27	LEU	0	0.008	-0.003	17.218	-0.273	-0.273	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.039	-0.009	15.263	-0.476	-0.476	0.000	0.000	0.000	0.000
29	A	29	CYS	0	-0.046	-0.004	15.341	-1.242	-1.242	0.000	0.000	0.000	0.000
30	A	30	ASN	0	0.032	0.010	11.360	0.973	0.973	0.000	0.000	0.000	0.000
31	A	31	THR	0	-0.016	-0.006	13.539	0.275	0.275	0.000	0.000	0.000	0.000
32	A	32	VAL	0	0.011	0.008	15.653	-0.142	-0.142	0.000	0.000	0.000	0.000
33	A	33	ILE	0	-0.018	-0.018	15.258	0.300	0.300	0.000	0.000	0.000	0.000
34	A	34	VAL	0	0.006	0.002	19.521	0.138	0.138	0.000	0.000	0.000	0.000
35	A	35	ALA	0	-0.013	-0.002	21.336	0.030	0.030	0.000	0.000	0.000	0.000
36	A	36	ASN	0	0.044	-0.012	23.312	0.535	0.535	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.792	-0.891	27.015	-10.829	-10.829	0.000	0.000	0.000	0.000
38	A	38	ALA	0	-0.019	0.007	29.019	0.156	0.156	0.000	0.000	0.000	0.000
39	A	39	VAL	0	0.009	-0.003	27.792	0.163	0.163	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.014	-0.003	26.141	-0.158	-0.158	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.928	-0.958	27.965	-9.713	-9.713	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.838	-0.915	31.614	-8.527	-8.527	0.000	0.000	0.000	0.000
43	A	43	LYS	1	0.957	0.953	30.959	8.871	8.871	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.014	0.005	32.292	-0.056	-0.056	0.000	0.000	0.000	0.000
45	A	45	GLN	0	0.031	0.018	31.007	-0.202	-0.202	0.000	0.000	0.000	0.000
46	A	46	GLN	0	-0.046	-0.033	27.627	-0.281	-0.281	0.000	0.000	0.000	0.000
47	A	47	SER	0	-0.083	-0.034	28.741	-0.328	-0.328	0.000	0.000	0.000	0.000
48	A	48	LEU	0	0.039	0.023	30.953	-0.109	-0.109	0.000	0.000	0.000	0.000
49	A	49	MET	0	-0.017	0.002	27.246	-0.240	-0.240	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.899	0.957	25.831	10.332	10.332	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.075	-0.040	27.487	-0.048	-0.048	0.000	0.000	0.000	0.000
52	A	52	VAL	0	-0.017	0.005	27.859	0.089	0.089	0.000	0.000	0.000	0.000
53	A	53	ILE	0	-0.018	-0.014	22.262	-0.263	-0.263	0.000	0.000	0.000	0.000
54	A	54	PRO	0	-0.003	0.002	23.007	0.166	0.166	0.000	0.000	0.000	0.000
55	A	55	SER	0	0.040	0.016	22.863	-0.489	-0.489	0.000	0.000	0.000	0.000
56	A	56	SER	0	-0.025	-0.007	19.660	-0.050	-0.050	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.032	-0.006	18.275	-0.851	-0.851	0.000	0.000	0.000	0.000
58	A	58	ALA	0	-0.028	-0.011	16.166	0.682	0.682	0.000	0.000	0.000	0.000
59	A	59	ILE	0	0.017	0.019	18.077	-0.490	-0.490	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.843	0.914	16.929	15.200	15.200	0.000	0.000	0.000	0.000
61	A	61	PHE	0	0.050	0.016	20.907	0.054	0.054	0.000	0.000	0.000	0.000
62	A	62	PHE	0	-0.042	-0.026	17.602	0.011	0.011	0.000	0.000	0.000	0.000
63	A	63	SER	0	0.115	0.062	23.302	-0.134	-0.134	0.000	0.000	0.000	0.000
64	A	64	ILE	0	0.026	-0.001	23.355	-0.700	-0.700	0.000	0.000	0.000	0.000
65	A	65	GLN	0	-0.008	-0.010	22.523	-0.231	-0.231	0.000	0.000	0.000	0.000
66	A	66	LYS	1	0.948	0.986	20.400	13.264	13.264	0.000	0.000	0.000	0.000
67	A	67	VAL	0	-0.025	-0.029	17.864	-0.772	-0.772	0.000	0.000	0.000	0.000
68	A	68	ILE	0	0.015	0.026	17.626	-1.126	-1.126	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.879	-0.922	17.740	-14.482	-14.482	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.129	-0.072	15.683	-0.422	-0.422	0.000	0.000	0.000	0.000
71	A	71	ILE	0	0.030	0.019	13.116	-1.311	-1.311	0.000	0.000	0.000	0.000
72	A	72	HIS	0	0.020	0.000	11.125	-3.232	-3.232	0.000	0.000	0.000	0.000
73	A	73	LYS	1	0.884	0.947	10.627	17.110	17.110	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.020	0.013	9.954	0.157	0.157	0.000	0.000	0.000	0.000
75	A	75	SER	0	0.005	-0.011	6.937	-2.754	-2.754	0.000	0.000	0.000	0.000
78	A	78	GLN	0	-0.021	0.001	7.390	1.743	1.743	0.000	0.000	0.000	0.000
79	A	79	SER	0	0.040	0.028	9.438	-1.700	-1.700	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.027	-0.021	10.582	1.878	1.878	0.000	0.000	0.000	0.000
81	A	81	PHE	0	0.030	0.015	13.701	0.121	0.121	0.000	0.000	0.000	0.000
82	A	82	ILE	0	0.001	-0.004	15.919	0.211	0.211	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.054	-0.020	19.296	0.324	0.324	0.000	0.000	0.000	0.000
84	A	84	VAL	0	0.067	0.037	23.072	0.037	0.037	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.933	0.965	25.421	9.209	9.209	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.834	-0.922	29.032	-9.801	-9.801	0.000	0.000	0.000	0.000
87	A	87	LEU	0	0.046	0.000	28.177	-0.437	-0.437	0.000	0.000	0.000	0.000
88	A	88	GLN	0	-0.016	-0.001	28.723	-0.383	-0.383	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.823	-0.927	26.376	-11.074	-11.074	0.000	0.000	0.000	0.000
90	A	90	ALA	0	-0.036	-0.026	24.126	-0.508	-0.508	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.843	0.918	23.931	10.103	10.103	0.000	0.000	0.000	0.000
92	A	92	LEU	0	0.018	0.010	25.256	-0.328	-0.328	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.041	-0.016	20.236	-0.431	-0.431	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.018	0.000	20.777	-0.646	-0.646	0.000	0.000	0.000	0.000
95	A	95	GLU	-1	-0.834	-0.914	21.751	-11.456	-11.456	0.000	0.000	0.000	0.000
96	A	96	GLY	0	-0.007	-0.002	22.044	0.073	0.073	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.006	0.002	18.975	-0.511	-0.511	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.028	-0.018	16.006	-1.500	-1.500	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.043	-0.016	12.374	0.629	0.629	0.000	0.000	0.000	0.000
100	A	100	ILE	0	-0.027	-0.017	14.973	-0.806	-0.806	0.000	0.000	0.000	0.000
101	A	101	THR	0	0.036	0.010	15.977	0.658	0.658	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.803	-0.877	18.548	-13.688	-13.688	0.000	0.000	0.000	0.000
103	A	103	ILE	0	-0.036	-0.011	20.106	-0.381	-0.381	0.000	0.000	0.000	0.000
104	A	104	ASN	0	-0.067	-0.047	22.917	0.428	0.428	0.000	0.000	0.000	0.000
105	A	105	ILE	0	0.039	0.005	24.647	0.044	0.044	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.007	-0.003	28.242	0.152	0.152	0.000	0.000	0.000	0.000
107	A	107	ASN	0	-0.117	-0.079	29.141	0.222	0.222	0.000	0.000	0.000	0.000
108	A	108	ILE	0	0.007	0.009	31.596	-0.183	-0.183	0.000	0.000	0.000	0.000
109	A	109	HIS	0	-0.004	-0.002	34.529	0.196	0.196	0.000	0.000	0.000	0.000
110	A	110	LYS	1	0.887	0.954	38.023	7.121	7.121	0.000	0.000	0.000	0.000
111	A	111	THR	0	0.028	0.008	40.834	0.045	0.045	0.000	0.000	0.000	0.000
112	A	112	ASP	-1	-0.917	-0.976	43.353	-6.633	-6.633	0.000	0.000	0.000	0.000
113	A	113	ASP	-1	-0.955	-0.967	43.708	-6.904	-6.904	0.000	0.000	0.000	0.000
114	A	114	LYS	1	0.773	0.886	36.361	8.464	8.464	0.000	0.000	0.000	0.000
115	A	115	VAL	0	0.024	0.004	41.783	0.196	0.196	0.000	0.000	0.000	0.000
116	A	116	ALA	0	-0.020	-0.014	40.583	-0.208	-0.208	0.000	0.000	0.000	0.000
117	A	117	ILE	0	-0.024	-0.001	36.478	0.094	0.094	0.000	0.000	0.000	0.000
118	A	118	THR	0	0.034	0.011	35.032	0.050	0.050	0.000	0.000	0.000	0.000
119	A	119	GLN	0	-0.049	-0.033	38.188	-0.013	-0.013	0.000	0.000	0.000	0.000
120	A	120	PHE	0	-0.053	-0.024	34.141	0.075	0.075	0.000	0.000	0.000	0.000
121	A	121	ILE	0	0.055	0.030	31.781	-0.183	-0.183	0.000	0.000	0.000	0.000
122	A	122	SER	0	0.014	0.011	35.772	0.313	0.313	0.000	0.000	0.000	0.000
123	A	123	LEU	0	-0.006	0.000	34.224	-0.223	-0.223	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.071	0.030	37.966	0.284	0.284	0.000	0.000	0.000	0.000
125	A	125	GLU	-1	-0.819	-0.910	38.289	-7.962	-7.962	0.000	0.000	0.000	0.000
126	A	126	THR	0	-0.017	0.004	35.927	-0.136	-0.136	0.000	0.000	0.000	0.000
127	A	127	ASP	-1	-0.759	-0.855	33.758	-9.215	-9.215	0.000	0.000	0.000	0.000
128	A	128	LYS	1	0.905	0.936	33.571	7.590	7.590	0.000	0.000	0.000	0.000
129	A	129	SER	0	-0.034	-0.033	34.711	-0.122	-0.122	0.000	0.000	0.000	0.000
130	A	130	ALA	0	-0.031	-0.008	30.333	-0.195	-0.195	0.000	0.000	0.000	0.000
131	A	131	ILE	0	0.008	0.003	29.992	-0.389	-0.389	0.000	0.000	0.000	0.000
132	A	132	ARG	1	0.839	0.910	30.318	8.248	8.248	0.000	0.000	0.000	0.000
133	A	133	CYS	0	-0.063	-0.018	30.112	-0.277	-0.277	0.000	0.000	0.000	0.000
134	A	134	LEU	0	0.001	-0.013	24.634	-0.377	-0.377	0.000	0.000	0.000	0.000
135	A	135	ALA	0	0.043	0.038	26.091	-0.501	-0.501	0.000	0.000	0.000	0.000
136	A	136	HIS	0	-0.003	-0.019	27.842	-0.449	-0.449	0.000	0.000	0.000	0.000
137	A	137	ASP	-1	-0.875	-0.925	28.775	-10.431	-10.431	0.000	0.000	0.000	0.000
138	A	138	HIS	0	-0.053	-0.037	23.662	-0.733	-0.733	0.000	0.000	0.000	0.000
139	A	139	HIS	1	0.775	0.903	23.181	11.663	11.663	0.000	0.000	0.000	0.000
140	A	140	VAL	0	0.011	0.013	21.450	-0.539	-0.539	0.000	0.000	0.000	0.000
141	A	141	VAL	0	-0.003	0.003	21.585	0.686	0.686	0.000	0.000	0.000	0.000
142	A	142	PHE	0	0.034	-0.004	23.657	-0.318	-0.318	0.000	0.000	0.000	0.000
143	A	143	ASN	0	-0.006	-0.011	23.328	0.440	0.440	0.000	0.000	0.000	0.000
144	A	144	THR	0	0.030	-0.001	26.937	-0.137	-0.137	0.000	0.000	0.000	0.000
145	A	145	LYS	1	0.882	0.957	22.850	13.413	13.413	0.000	0.000	0.000	0.000
146	A	146	THR	0	0.048	0.030	27.542	-0.274	-0.274	0.000	0.000	0.000	0.000
147	A	147	THR	0	-0.044	-0.045	28.365	-0.238	-0.238	0.000	0.000	0.000	0.000
148	A	148	PRO	0	0.020	0.011	24.872	0.145	0.145	0.000	0.000	0.000	0.000
149	A	149	ALA	0	-0.035	-0.012	26.912	-0.016	-0.016	0.000	0.000	0.000	0.000
150	A	150	GLY	0	0.023	0.025	29.903	0.196	0.196	0.000	0.000	0.000	0.000
151	A	151	ASN	0	-0.007	-0.005	31.002	0.333	0.333	0.000	0.000	0.000	0.000
152	A	152	SER	0	0.061	0.028	33.600	-0.077	-0.077	0.000	0.000	0.000	0.000
153	A	153	ALA	0	0.019	0.014	34.599	-0.017	-0.017	0.000	0.000	0.000	0.000
154	A	154	SER	0	-0.093	-0.049	33.652	0.062	0.062	0.000	0.000	0.000	0.000
155	A	155	ASP	-1	-0.878	-0.927	29.446	-10.726	-10.726	0.000	0.000	0.000	0.000
156	A	156	VAL	0	-0.023	-0.019	32.132	0.227	0.227	0.000	0.000	0.000	0.000
157	A	157	ASP	-1	-0.824	-0.905	31.401	-10.466	-10.466	0.000	0.000	0.000	0.000
158	A	158	ILE	0	-0.033	-0.033	30.203	0.282	0.282	0.000	0.000	0.000	0.000
159	A	159	LEU	0	-0.033	-0.038	29.741	0.164	0.164	0.000	0.000	0.000	0.000
160	A	160	ASP	-1	-0.903	-0.934	33.770	-8.536	-8.536	0.000	0.000	0.000	0.000
161	A	161	TYR	0	-0.091	-0.047	35.943	0.401	0.401	0.000	0.000	0.000	0.000
162	A	162	ILE	-1	-0.890	-0.926	33.616	-8.266	-8.266	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

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