FMO DATABASE

FMODB ID: NLL1Q

Calculation Name: 2O4T-A-Xray547

Preferred Name:

Target Type:

Ligand Name: di(hydroxyethyl)ether

Ligand 3-letter code: PEG

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2O4T

Chain ID: A

ChEMBL ID:

UniProt ID: Q9K5W1

Base Structure: X-ray

Registration Date: 2025-10-05

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	90
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-565473.725056
FMO2-HF: Nuclear repulsion	531274.809979
FMO2-HF: Total energy	-34198.915077
FMO2-MP2: Total energy	-34300.408315

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:16:HIS)

Summations of interaction energy for fragment #1(A:16:HIS)

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.
-66.308	-64.61	-0.019	-0.749	-0.93	-0.001

Interaction energy analysis for fragmet #1(A:16:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.848 / 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	18	SER	0	0.065	0.040	3.865	2.229	3.839	-0.018	-0.745	-0.847	-0.001
7	A	22	LYS	1	0.870	0.940	4.385	38.742	38.830	-0.001	-0.004	-0.083	0.000
4	A	19	ARG	1	0.905	0.934	6.598	24.743	24.743	0.000	0.000	0.000	0.000
5	A	20	VAL	0	0.083	0.047	8.721	1.241	1.241	0.000	0.000	0.000	0.000
6	A	21	GLU	-1	-0.926	-0.979	7.954	-34.053	-34.053	0.000	0.000	0.000	0.000
8	A	23	LEU	0	0.022	0.047	10.260	1.151	1.151	0.000	0.000	0.000	0.000
9	A	24	PRO	0	0.037	0.035	13.878	-0.469	-0.469	0.000	0.000	0.000	0.000
10	A	25	LYS	1	0.873	0.910	14.308	19.746	19.746	0.000	0.000	0.000	0.000
11	A	26	ASP	-1	-0.793	-0.908	18.056	-13.945	-13.945	0.000	0.000	0.000	0.000
12	A	27	TYR	0	0.044	-0.004	17.781	0.108	0.108	0.000	0.000	0.000	0.000
13	A	28	GLN	0	-0.063	-0.031	12.869	-0.009	-0.009	0.000	0.000	0.000	0.000
14	A	29	ILE	0	-0.057	-0.018	17.443	-0.029	-0.029	0.000	0.000	0.000	0.000
15	A	30	VAL	0	0.084	0.044	20.956	0.086	0.086	0.000	0.000	0.000	0.000
16	A	31	TYR	0	-0.040	-0.033	14.917	-0.304	-0.304	0.000	0.000	0.000	0.000
17	A	32	LYS	1	0.836	0.917	16.188	17.308	17.308	0.000	0.000	0.000	0.000
18	A	33	GLU	-1	-0.915	-0.965	20.220	-11.393	-11.393	0.000	0.000	0.000	0.000
19	A	34	ILE	0	0.049	0.021	21.380	0.334	0.334	0.000	0.000	0.000	0.000
20	A	35	GLN	0	0.019	0.021	15.363	0.223	0.223	0.000	0.000	0.000	0.000
21	A	36	LYS	1	0.896	0.951	21.084	12.507	12.507	0.000	0.000	0.000	0.000
22	A	37	TYR	0	-0.100	-0.077	24.357	0.427	0.427	0.000	0.000	0.000	0.000
23	A	38	LEU	0	0.096	0.030	21.694	0.327	0.327	0.000	0.000	0.000	0.000
24	A	39	PHE	0	-0.068	-0.025	23.479	0.266	0.266	0.000	0.000	0.000	0.000
25	A	40	LYS	1	0.843	0.920	25.215	10.747	10.747	0.000	0.000	0.000	0.000
26	A	41	VAL	0	-0.011	-0.002	28.403	0.360	0.360	0.000	0.000	0.000	0.000
27	A	42	GLY	0	0.037	0.033	26.453	0.163	0.163	0.000	0.000	0.000	0.000
28	A	43	PRO	0	-0.012	-0.009	25.256	0.220	0.220	0.000	0.000	0.000	0.000
29	A	44	VAL	0	-0.004	0.006	25.697	-0.330	-0.330	0.000	0.000	0.000	0.000
30	A	45	GLU	-1	-0.893	-0.944	25.727	-10.734	-10.734	0.000	0.000	0.000	0.000
31	A	46	LEU	0	-0.020	-0.016	19.237	-0.366	-0.366	0.000	0.000	0.000	0.000
32	A	47	ASN	0	0.006	-0.015	19.906	-0.977	-0.977	0.000	0.000	0.000	0.000
33	A	48	GLU	-1	-0.878	-0.925	20.594	-11.295	-11.295	0.000	0.000	0.000	0.000
34	A	49	GLY	0	0.040	0.024	21.936	-0.087	-0.087	0.000	0.000	0.000	0.000
35	A	50	ILE	0	-0.043	-0.034	15.461	-0.518	-0.518	0.000	0.000	0.000	0.000
36	A	51	GLY	0	0.017	0.023	17.395	-0.691	-0.691	0.000	0.000	0.000	0.000
37	A	52	LEU	0	0.064	0.034	19.238	-0.379	-0.379	0.000	0.000	0.000	0.000
38	A	53	LEU	0	-0.010	-0.013	16.906	-0.230	-0.230	0.000	0.000	0.000	0.000
39	A	54	SER	0	-0.055	-0.027	15.256	-1.200	-1.200	0.000	0.000	0.000	0.000
40	A	55	GLU	-1	-0.905	-0.943	16.208	-12.727	-12.727	0.000	0.000	0.000	0.000
41	A	56	ILE	0	0.007	-0.002	19.347	-0.063	-0.063	0.000	0.000	0.000	0.000
42	A	57	LEU	0	-0.069	-0.027	11.406	-0.379	-0.379	0.000	0.000	0.000	0.000
43	A	58	GLY	0	0.040	0.023	16.108	-0.370	-0.370	0.000	0.000	0.000	0.000
44	A	59	PHE	0	0.017	-0.002	17.194	0.159	0.159	0.000	0.000	0.000	0.000
45	A	60	PHE	0	-0.048	-0.029	17.280	0.202	0.202	0.000	0.000	0.000	0.000
46	A	61	GLU	-1	-0.889	-0.960	11.808	-22.317	-22.317	0.000	0.000	0.000	0.000
47	A	62	GLU	-1	-0.895	-0.942	16.123	-13.869	-13.869	0.000	0.000	0.000	0.000
48	A	63	GLY	0	-0.001	0.001	19.363	0.480	0.480	0.000	0.000	0.000	0.000
49	A	64	ALA	0	-0.035	-0.028	16.831	0.327	0.327	0.000	0.000	0.000	0.000
50	A	65	ALA	0	-0.039	-0.011	17.618	0.183	0.183	0.000	0.000	0.000	0.000
51	A	66	ALA	0	-0.022	-0.009	19.141	0.449	0.449	0.000	0.000	0.000	0.000
52	A	67	GLY	0	-0.057	-0.022	21.664	0.579	0.579	0.000	0.000	0.000	0.000
53	A	68	LYS	1	0.907	0.967	22.967	11.266	11.266	0.000	0.000	0.000	0.000
54	A	69	GLY	0	0.047	0.041	22.791	-0.622	-0.622	0.000	0.000	0.000	0.000
55	A	70	VAL	0	0.013	-0.007	21.976	0.233	0.233	0.000	0.000	0.000	0.000
56	A	71	LEU	0	-0.021	-0.015	23.692	0.203	0.203	0.000	0.000	0.000	0.000
57	A	72	ASP	-1	-0.939	-0.959	26.830	-10.252	-10.252	0.000	0.000	0.000	0.000
58	A	73	VAL	0	-0.093	-0.039	22.752	0.122	0.122	0.000	0.000	0.000	0.000
59	A	74	THR	0	-0.017	-0.031	24.534	-0.017	-0.017	0.000	0.000	0.000	0.000
60	A	75	GLY	0	0.028	0.034	27.164	0.370	0.370	0.000	0.000	0.000	0.000
61	A	76	THR	0	-0.033	-0.036	29.436	-0.275	-0.275	0.000	0.000	0.000	0.000
62	A	77	ASP	-1	-0.883	-0.930	31.404	-9.242	-9.242	0.000	0.000	0.000	0.000
63	A	78	VAL	0	0.051	0.011	25.837	-0.098	-0.098	0.000	0.000	0.000	0.000
64	A	79	ALA	0	0.002	0.019	28.071	-0.274	-0.274	0.000	0.000	0.000	0.000
65	A	80	ALA	0	0.041	0.017	30.361	-0.080	-0.080	0.000	0.000	0.000	0.000
66	A	81	PHE	0	-0.029	-0.015	23.470	-0.073	-0.073	0.000	0.000	0.000	0.000
67	A	82	CYS	0	-0.060	-0.030	25.928	-0.389	-0.389	0.000	0.000	0.000	0.000
68	A	83	ASP	-1	-0.808	-0.893	27.506	-9.532	-9.532	0.000	0.000	0.000	0.000
69	A	84	ALA	0	-0.064	-0.034	30.133	0.147	0.147	0.000	0.000	0.000	0.000
70	A	85	LEU	0	-0.049	-0.019	24.246	-0.016	-0.016	0.000	0.000	0.000	0.000
71	A	86	ILE	0	-0.026	-0.015	27.211	-0.301	-0.301	0.000	0.000	0.000	0.000
72	A	87	GLY	0	-0.034	-0.003	29.349	0.161	0.161	0.000	0.000	0.000	0.000
73	A	88	ASP	-1	-0.887	-0.932	31.140	-8.912	-8.912	0.000	0.000	0.000	0.000
74	A	89	SER	0	0.066	0.043	28.218	-0.150	-0.150	0.000	0.000	0.000	0.000
75	A	90	LYS	1	0.833	0.891	28.693	8.564	8.564	0.000	0.000	0.000	0.000
76	A	91	THR	0	0.045	0.024	24.587	0.125	0.125	0.000	0.000	0.000	0.000
77	A	92	TYR	0	0.014	0.011	21.712	-0.574	-0.574	0.000	0.000	0.000	0.000
78	A	93	ALA	0	-0.006	-0.014	25.342	-0.154	-0.154	0.000	0.000	0.000	0.000
79	A	94	ASP	-1	-0.923	-0.958	27.776	-10.419	-10.419	0.000	0.000	0.000	0.000
80	A	95	LEU	0	0.013	0.009	21.532	-0.159	-0.159	0.000	0.000	0.000	0.000
81	A	96	TYR	0	-0.056	-0.022	23.871	-0.363	-0.363	0.000	0.000	0.000	0.000
82	A	97	GLN	0	-0.021	-0.016	25.196	0.025	0.025	0.000	0.000	0.000	0.000
83	A	98	GLU	-1	-0.830	-0.912	25.697	-10.477	-10.477	0.000	0.000	0.000	0.000
84	A	99	SER	0	-0.021	-0.004	21.761	-0.116	-0.116	0.000	0.000	0.000	0.000
85	A	100	ILE	0	-0.042	-0.020	24.397	-0.011	-0.011	0.000	0.000	0.000	0.000
86	A	101	GLN	0	-0.064	-0.031	27.279	0.404	0.404	0.000	0.000	0.000	0.000
87	A	102	GLN	0	-0.017	-0.019	23.705	-0.308	-0.308	0.000	0.000	0.000	0.000
88	A	103	HIS	0	-0.117	-0.061	21.239	-0.552	-0.552	0.000	0.000	0.000	0.000
89	A	104	VAL	0	-0.121	-0.050	26.104	0.171	0.171	0.000	0.000	0.000	0.000
90	A	105	ASP	-2	-1.932	-1.955	25.755	-21.306	-21.306	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:16:HIS)