FMO DATABASE

FMODB ID: 5Y45Z

Calculation Name: 5IT6-A-Xray547

Preferred Name:

Target Type:

Ligand Name: triethylene glycol | di(hydroxyethyl)ether | 1,2-ethanediol

Ligand 3-letter code: PGE | PEG | EDO

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 5IT6

Chain ID: A

ChEMBL ID:

UniProt ID: Q5ZHQ2

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	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1220209.883084
FMO2-HF: Nuclear repulsion	1167020.910931
FMO2-HF: Total energy	-53188.972153
FMO2-MP2: Total energy	-53342.937272

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:PRO)

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

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.
-163.265	-156.439	0.985	-3.387	-4.425	-0.026

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.866 / q_NPA : 0.915

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	5	CYS	0	0.028	0.017	3.289	0.242	2.310	0.024	-0.883	-1.209	-0.002
39	A	41	GLU	-1	-0.866	-0.925	2.690	-62.350	-59.770	0.530	-1.427	-1.684	-0.017
123	A	125	LYS	1	0.819	0.894	4.303	36.331	36.432	-0.001	-0.010	-0.090	0.000
124	A	126	ILE	0	-0.009	-0.006	4.309	4.872	4.997	-0.001	-0.017	-0.106	0.000
125	A	127	ASN	0	-0.032	-0.023	2.479	-16.114	-14.234	0.433	-1.010	-1.303	-0.007
126	A	128	GLY	0	0.044	0.023	4.127	5.639	5.711	0.000	-0.040	-0.033	0.000
4	A	6	GLY	0	0.036	0.016	5.520	1.832	1.832	0.000	0.000	0.000	0.000
5	A	7	HIS	0	0.017	0.017	9.293	2.430	2.430	0.000	0.000	0.000	0.000
6	A	8	ILE	0	-0.032	-0.017	12.278	1.392	1.392	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.983	0.981	14.832	15.036	15.036	0.000	0.000	0.000	0.000
8	A	10	GLY	0	-0.068	-0.050	17.947	0.604	0.604	0.000	0.000	0.000	0.000
9	A	11	GLY	0	0.034	0.045	17.167	0.651	0.651	0.000	0.000	0.000	0.000
10	A	12	MET	0	-0.007	0.007	16.736	0.166	0.166	0.000	0.000	0.000	0.000
11	A	13	ARG	1	0.961	0.966	19.444	12.683	12.683	0.000	0.000	0.000	0.000
12	A	14	PRO	0	0.034	0.001	23.210	-0.233	-0.233	0.000	0.000	0.000	0.000
13	A	15	GLY	0	-0.003	0.002	25.723	0.142	0.142	0.000	0.000	0.000	0.000
14	A	16	LYS	1	0.780	0.912	18.498	15.387	15.387	0.000	0.000	0.000	0.000
15	A	17	LYS	1	0.881	0.914	20.340	13.640	13.640	0.000	0.000	0.000	0.000
16	A	18	ILE	0	0.007	0.025	13.707	0.174	0.174	0.000	0.000	0.000	0.000
17	A	19	LEU	0	-0.046	-0.032	16.847	0.543	0.543	0.000	0.000	0.000	0.000
18	A	20	VAL	0	0.047	0.018	11.326	-0.776	-0.776	0.000	0.000	0.000	0.000
19	A	21	MET	0	-0.027	-0.020	14.082	1.549	1.549	0.000	0.000	0.000	0.000
20	A	22	GLY	0	0.050	0.027	12.651	-1.532	-1.532	0.000	0.000	0.000	0.000
21	A	23	ILE	0	-0.010	0.007	13.047	1.588	1.588	0.000	0.000	0.000	0.000
22	A	24	VAL	0	-0.019	0.001	12.819	-1.883	-1.883	0.000	0.000	0.000	0.000
23	A	25	ASP	-1	-0.832	-0.924	11.130	-23.822	-23.822	0.000	0.000	0.000	0.000
24	A	26	LEU	0	0.000	-0.017	14.287	0.792	0.792	0.000	0.000	0.000	0.000
25	A	27	ASN	0	-0.083	-0.046	16.319	1.477	1.477	0.000	0.000	0.000	0.000
26	A	28	PRO	0	-0.026	0.009	13.990	-0.740	-0.740	0.000	0.000	0.000	0.000
27	A	29	GLU	-1	-0.915	-0.959	13.151	-20.094	-20.094	0.000	0.000	0.000	0.000
28	A	30	SER	0	-0.072	-0.054	11.444	0.619	0.619	0.000	0.000	0.000	0.000
29	A	31	PHE	0	-0.005	0.008	8.730	-1.878	-1.878	0.000	0.000	0.000	0.000
30	A	32	GLY	0	0.000	0.008	7.726	2.801	2.801	0.000	0.000	0.000	0.000
31	A	33	ILE	0	-0.020	-0.015	7.452	-2.966	-2.966	0.000	0.000	0.000	0.000
32	A	34	SER	0	0.023	0.006	8.087	2.941	2.941	0.000	0.000	0.000	0.000
33	A	35	LEU	0	-0.032	-0.012	9.107	-1.315	-1.315	0.000	0.000	0.000	0.000
34	A	36	THR	0	0.002	-0.022	8.739	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	37	CYS	0	-0.074	-0.026	11.384	1.058	1.058	0.000	0.000	0.000	0.000
36	A	38	GLY	0	0.048	0.027	12.180	0.259	0.259	0.000	0.000	0.000	0.000
37	A	39	GLU	-1	-0.908	-0.982	7.809	-30.034	-30.034	0.000	0.000	0.000	0.000
38	A	40	SER	0	-0.053	-0.030	7.170	-4.197	-4.197	0.000	0.000	0.000	0.000
40	A	42	ASP	-1	-0.928	-0.953	6.624	-22.411	-22.411	0.000	0.000	0.000	0.000
41	A	43	PRO	0	0.018	0.004	9.720	0.868	0.868	0.000	0.000	0.000	0.000
42	A	44	PRO	0	-0.023	-0.008	9.082	-0.767	-0.767	0.000	0.000	0.000	0.000
43	A	45	ALA	0	-0.036	-0.002	9.615	2.063	2.063	0.000	0.000	0.000	0.000
44	A	46	ASP	-1	-0.839	-0.906	11.276	-18.185	-18.185	0.000	0.000	0.000	0.000
45	A	47	VAL	0	-0.037	-0.022	10.484	-0.725	-0.725	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.014	-0.004	13.025	1.327	1.327	0.000	0.000	0.000	0.000
47	A	49	ILE	0	-0.055	-0.037	13.992	1.289	1.289	0.000	0.000	0.000	0.000
48	A	50	GLU	-1	-0.877	-0.935	9.737	-27.107	-27.107	0.000	0.000	0.000	0.000
49	A	51	LEU	0	-0.063	-0.035	11.827	2.043	2.043	0.000	0.000	0.000	0.000
50	A	52	LYS	1	0.997	0.993	11.015	21.674	21.674	0.000	0.000	0.000	0.000
51	A	53	ALA	0	-0.039	-0.003	12.527	1.778	1.778	0.000	0.000	0.000	0.000
52	A	54	VAL	0	0.020	-0.006	13.411	-1.542	-1.542	0.000	0.000	0.000	0.000
53	A	55	PHE	0	0.003	-0.020	13.762	1.222	1.222	0.000	0.000	0.000	0.000
54	A	56	THR	0	-0.045	-0.013	18.095	0.990	0.990	0.000	0.000	0.000	0.000
55	A	57	ASP	-1	-0.851	-0.929	20.071	-14.134	-14.134	0.000	0.000	0.000	0.000
56	A	58	ARG	1	0.874	0.951	20.384	13.652	13.652	0.000	0.000	0.000	0.000
57	A	59	GLN	0	0.014	0.017	18.735	0.626	0.626	0.000	0.000	0.000	0.000
58	A	60	PHE	0	0.002	-0.027	14.420	-0.735	-0.735	0.000	0.000	0.000	0.000
59	A	61	ILE	0	0.019	0.027	15.089	0.772	0.772	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.833	0.908	15.656	13.269	13.269	0.000	0.000	0.000	0.000
61	A	63	ASN	0	0.045	0.013	15.496	1.203	1.203	0.000	0.000	0.000	0.000
62	A	64	SER	0	-0.012	-0.005	15.385	-0.314	-0.314	0.000	0.000	0.000	0.000
63	A	65	CYS	0	-0.051	-0.005	13.882	0.473	0.473	0.000	0.000	0.000	0.000
64	A	66	VAL	0	0.038	0.010	15.895	-0.358	-0.358	0.000	0.000	0.000	0.000
65	A	67	ALA	0	0.002	-0.003	17.570	0.567	0.567	0.000	0.000	0.000	0.000
66	A	68	GLY	0	-0.003	-0.004	15.234	0.328	0.328	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.964	-0.973	16.300	-12.984	-12.984	0.000	0.000	0.000	0.000
68	A	70	TRP	0	-0.028	-0.025	11.477	-0.365	-0.365	0.000	0.000	0.000	0.000
69	A	71	GLY	0	0.011	0.012	18.244	0.770	0.770	0.000	0.000	0.000	0.000
70	A	72	GLU	-1	-0.915	-0.955	20.464	-11.685	-11.685	0.000	0.000	0.000	0.000
71	A	73	GLU	-1	-0.913	-0.952	17.842	-16.149	-16.149	0.000	0.000	0.000	0.000
72	A	74	GLN	0	-0.055	-0.030	19.903	0.518	0.518	0.000	0.000	0.000	0.000
73	A	75	SER	0	0.060	0.015	20.114	-0.472	-0.472	0.000	0.000	0.000	0.000
74	A	76	SER	0	-0.008	0.008	21.829	-0.112	-0.112	0.000	0.000	0.000	0.000
75	A	77	ILE	0	0.016	0.009	21.594	-0.419	-0.419	0.000	0.000	0.000	0.000
76	A	78	PRO	0	-0.027	0.007	24.827	0.356	0.356	0.000	0.000	0.000	0.000
77	A	79	TYR	0	0.022	-0.010	24.258	0.476	0.476	0.000	0.000	0.000	0.000
78	A	80	PHE	0	0.000	0.012	17.308	-0.170	-0.170	0.000	0.000	0.000	0.000
79	A	81	PRO	0	-0.048	-0.027	19.058	0.398	0.398	0.000	0.000	0.000	0.000
80	A	82	PHE	0	-0.008	0.018	16.143	-0.083	-0.083	0.000	0.000	0.000	0.000
81	A	83	ILE	0	-0.009	-0.022	19.045	0.565	0.565	0.000	0.000	0.000	0.000
82	A	84	PRO	0	0.028	0.003	17.646	-0.491	-0.491	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.911	-0.966	17.422	-14.281	-14.281	0.000	0.000	0.000	0.000
84	A	86	GLN	0	-0.049	0.002	18.683	0.682	0.682	0.000	0.000	0.000	0.000
85	A	87	PRO	0	-0.020	-0.012	17.383	-1.045	-1.045	0.000	0.000	0.000	0.000
86	A	88	PHE	0	-0.002	0.003	11.953	0.701	0.701	0.000	0.000	0.000	0.000
87	A	89	ARG	1	0.857	0.912	16.748	12.658	12.658	0.000	0.000	0.000	0.000
88	A	90	VAL	0	0.018	0.014	14.718	0.702	0.702	0.000	0.000	0.000	0.000
89	A	91	GLU	-1	-0.835	-0.905	16.650	-14.132	-14.132	0.000	0.000	0.000	0.000
90	A	92	ILE	0	0.029	0.021	14.008	0.581	0.581	0.000	0.000	0.000	0.000
91	A	93	LEU	0	-0.014	-0.003	18.328	-0.036	-0.036	0.000	0.000	0.000	0.000
92	A	94	CYS	0	-0.014	0.010	20.340	-0.190	-0.190	0.000	0.000	0.000	0.000
93	A	95	GLU	-1	-0.816	-0.897	22.185	-10.327	-10.327	0.000	0.000	0.000	0.000
94	A	96	HIS	0	0.027	0.010	24.773	-0.498	-0.498	0.000	0.000	0.000	0.000
95	A	97	PRO	0	0.033	0.009	26.137	-0.232	-0.232	0.000	0.000	0.000	0.000
96	A	98	ARG	1	0.788	0.872	23.705	10.605	10.605	0.000	0.000	0.000	0.000
97	A	99	PHE	0	0.037	0.013	17.711	0.029	0.029	0.000	0.000	0.000	0.000
98	A	100	ARG	1	0.827	0.890	21.476	11.418	11.418	0.000	0.000	0.000	0.000
99	A	101	ILE	0	-0.002	0.010	18.143	-0.382	-0.382	0.000	0.000	0.000	0.000
100	A	102	PHE	0	-0.037	-0.030	20.717	0.788	0.788	0.000	0.000	0.000	0.000
101	A	103	VAL	0	0.020	0.007	18.537	-0.886	-0.886	0.000	0.000	0.000	0.000
102	A	104	ASP	-1	-0.827	-0.916	20.515	-13.746	-13.746	0.000	0.000	0.000	0.000
103	A	105	GLY	0	-0.066	-0.042	22.483	0.587	0.587	0.000	0.000	0.000	0.000
104	A	106	HIS	0	0.000	0.011	24.555	0.582	0.582	0.000	0.000	0.000	0.000
105	A	107	GLN	0	-0.051	-0.025	24.132	-0.469	-0.469	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.008	0.002	20.725	0.311	0.311	0.000	0.000	0.000	0.000
107	A	109	PHE	0	0.011	-0.007	18.220	0.307	0.307	0.000	0.000	0.000	0.000
108	A	110	ASP	-1	-0.784	-0.854	23.043	-11.669	-11.669	0.000	0.000	0.000	0.000
109	A	111	PHE	0	0.007	-0.004	18.430	-0.079	-0.079	0.000	0.000	0.000	0.000
110	A	112	TYR	0	0.025	-0.002	21.976	-0.095	-0.095	0.000	0.000	0.000	0.000
111	A	113	HIS	1	0.792	0.903	20.406	12.994	12.994	0.000	0.000	0.000	0.000
112	A	114	ARG	1	0.894	0.945	19.717	14.513	14.513	0.000	0.000	0.000	0.000
113	A	115	ILE	0	0.034	0.029	16.508	0.349	0.349	0.000	0.000	0.000	0.000
114	A	116	GLU	-1	-0.907	-0.967	20.558	-11.278	-11.278	0.000	0.000	0.000	0.000
115	A	117	THR	0	-0.023	-0.007	21.198	0.273	0.273	0.000	0.000	0.000	0.000
116	A	118	LEU	0	0.000	-0.013	20.197	-0.620	-0.620	0.000	0.000	0.000	0.000
117	A	119	SER	0	-0.005	-0.002	19.279	-0.751	-0.751	0.000	0.000	0.000	0.000
118	A	120	ALA	0	0.011	0.004	18.567	-0.159	-0.159	0.000	0.000	0.000	0.000
119	A	121	ILE	0	-0.012	0.005	14.513	-0.846	-0.846	0.000	0.000	0.000	0.000
120	A	122	ASP	-1	-0.846	-0.926	13.429	-20.424	-20.424	0.000	0.000	0.000	0.000
121	A	123	THR	0	-0.025	0.002	8.255	-1.003	-1.003	0.000	0.000	0.000	0.000
122	A	124	ILE	0	-0.029	-0.008	8.876	1.118	1.118	0.000	0.000	0.000	0.000
127	A	129	ASP	-1	-0.782	-0.878	6.910	-27.717	-27.717	0.000	0.000	0.000	0.000
128	A	130	LEU	0	-0.041	-0.026	6.740	2.915	2.915	0.000	0.000	0.000	0.000
129	A	131	GLN	0	0.003	0.020	8.296	-2.917	-2.917	0.000	0.000	0.000	0.000
130	A	132	LEU	0	-0.030	-0.011	8.018	1.904	1.904	0.000	0.000	0.000	0.000
131	A	133	THR	0	-0.050	-0.035	10.130	0.935	0.935	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.857	0.912	13.730	17.510	17.510	0.000	0.000	0.000	0.000
133	A	135	LEU	0	0.034	0.029	10.841	-0.778	-0.778	0.000	0.000	0.000	0.000
134	A	136	GLY	-1	-0.872	-0.922	14.255	-16.086	-16.086	0.000	0.000	0.000	0.000

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