FMO DATABASE

FMODB ID: N6JKQ

Calculation Name: 6VQ5-B-Xray547

Preferred Name:

Target Type:

Ligand Name: 2-(2-methoxyethoxy)ethanol

Ligand 3-letter code: PG0

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6VQ5

Chain ID: B

ChEMBL ID:

UniProt ID:

Base Structure: X-ray

Registration Date: 2025-10-06

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	114
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-973733.083011
FMO2-HF: Nuclear repulsion	925783.029862
FMO2-HF: Total energy	-47950.053149
FMO2-MP2: Total energy	-48085.573395

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(B:12:PHE)

Summations of interaction energy for fragment #1(B:12:PHE)

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.
-107.81	-100.109	3.182	-2.923	-7.959	0.003

Interaction energy analysis for fragmet #1(B:12:PHE)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.937 / q_NPA : 0.955

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	B	14	LYS	1	0.955	0.977	3.446	44.176	45.851	0.032	-0.495	-1.212	0.000
4	B	15	VAL	0	0.089	0.054	3.376	4.858	5.643	0.023	-0.202	-0.606	-0.001
5	B	16	LEU	0	0.041	0.028	2.565	3.936	5.464	0.811	-0.551	-1.789	0.004
22	B	33	LEU	0	0.002	-0.012	2.593	-0.942	-0.222	0.253	-0.180	-0.793	-0.001
43	B	55	MET	0	-0.018	-0.032	2.764	-1.998	-1.112	2.026	-0.621	-2.290	0.008
47	B	59	LEU	0	-0.100	-0.043	3.345	-6.410	-5.810	0.018	-0.178	-0.439	-0.001
68	B	80	HIS	0	-0.125	-0.066	3.654	-17.189	-15.682	0.019	-0.696	-0.830	-0.006
6	B	17	GLU	-1	-0.853	-0.933	5.951	-24.119	-24.119	0.000	0.000	0.000	0.000
7	B	18	GLU	-1	-0.900	-0.936	8.195	-29.917	-29.917	0.000	0.000	0.000	0.000
8	B	19	CYS	0	-0.055	-0.017	8.363	1.867	1.867	0.000	0.000	0.000	0.000
9	B	20	LYS	1	0.778	0.886	8.286	28.036	28.036	0.000	0.000	0.000	0.000
10	B	21	LYS	1	0.924	0.958	10.832	22.626	22.626	0.000	0.000	0.000	0.000
11	B	22	GLU	-1	-0.846	-0.914	12.846	-22.448	-22.448	0.000	0.000	0.000	0.000
12	B	23	LEU	0	-0.038	-0.022	11.416	1.246	1.246	0.000	0.000	0.000	0.000
13	B	24	ASN	0	-0.080	-0.032	14.826	0.897	0.897	0.000	0.000	0.000	0.000
14	B	25	LEU	0	-0.001	0.009	10.045	0.678	0.678	0.000	0.000	0.000	0.000
15	B	26	SER	0	0.010	-0.004	13.175	-0.050	-0.050	0.000	0.000	0.000	0.000
16	B	27	GLU	-1	-0.817	-0.910	10.010	-23.630	-23.630	0.000	0.000	0.000	0.000
17	B	28	SER	0	0.010	0.006	9.632	-1.023	-1.023	0.000	0.000	0.000	0.000
18	B	29	ILE	0	0.047	0.042	6.258	-0.483	-0.483	0.000	0.000	0.000	0.000
19	B	30	ILE	0	-0.012	-0.010	5.099	-2.519	-2.519	0.000	0.000	0.000	0.000
20	B	31	ASN	0	-0.045	-0.032	6.533	-0.483	-0.483	0.000	0.000	0.000	0.000
21	B	32	ASP	-1	-0.876	-0.932	8.487	-19.238	-19.238	0.000	0.000	0.000	0.000
23	B	34	TYR	0	-0.009	0.002	5.552	0.246	0.246	0.000	0.000	0.000	0.000
24	B	35	ASN	0	-0.019	-0.026	7.397	1.216	1.216	0.000	0.000	0.000	0.000
25	B	36	TYR	0	-0.001	-0.020	5.854	0.067	0.067	0.000	0.000	0.000	0.000
26	B	37	TRP	0	-0.013	0.004	6.579	0.419	0.419	0.000	0.000	0.000	0.000
27	B	38	LYS	1	0.837	0.927	8.656	18.069	18.069	0.000	0.000	0.000	0.000
28	B	39	GLU	-1	-0.809	-0.864	11.499	-14.995	-14.995	0.000	0.000	0.000	0.000
29	B	40	ASP	-1	-0.912	-0.915	12.951	-14.131	-14.131	0.000	0.000	0.000	0.000
30	B	41	TYR	0	0.022	-0.050	11.748	-1.330	-1.330	0.000	0.000	0.000	0.000
31	B	42	SER	0	-0.106	-0.067	14.501	0.273	0.273	0.000	0.000	0.000	0.000
32	B	43	LEU	0	-0.020	-0.016	15.110	0.516	0.516	0.000	0.000	0.000	0.000
33	B	44	LEU	0	-0.032	0.009	10.061	-0.365	-0.365	0.000	0.000	0.000	0.000
34	B	45	ASN	0	0.030	0.012	13.339	-0.134	-0.134	0.000	0.000	0.000	0.000
35	B	46	ARG	1	0.903	0.896	13.571	14.194	14.194	0.000	0.000	0.000	0.000
36	B	47	ASP	-1	-0.883	-0.938	13.305	-16.965	-16.965	0.000	0.000	0.000	0.000
37	B	48	VAL	0	0.011	0.006	8.086	-1.618	-1.618	0.000	0.000	0.000	0.000
38	B	49	GLY	0	0.037	0.028	9.369	-1.844	-1.844	0.000	0.000	0.000	0.000
39	B	50	CYS	0	-0.113	-0.053	11.241	-1.299	-1.299	0.000	0.000	0.000	0.000
40	B	51	ALA	0	0.039	0.017	7.663	-0.789	-0.789	0.000	0.000	0.000	0.000
41	B	52	ILE	0	0.033	0.023	6.252	-2.733	-2.733	0.000	0.000	0.000	0.000
42	B	53	VAL	0	0.006	0.014	7.858	-1.177	-1.177	0.000	0.000	0.000	0.000
44	B	56	SER	0	0.004	-0.011	6.865	-3.387	-3.387	0.000	0.000	0.000	0.000
45	B	57	LYS	1	0.935	0.973	8.861	20.367	20.367	0.000	0.000	0.000	0.000
46	B	58	LYS	1	0.762	0.849	7.356	28.718	28.718	0.000	0.000	0.000	0.000
48	B	60	GLU	-1	-0.937	-0.959	7.474	-22.280	-22.280	0.000	0.000	0.000	0.000
49	B	61	LEU	0	0.009	0.023	8.204	1.465	1.465	0.000	0.000	0.000	0.000
50	B	62	ILE	0	-0.062	-0.023	11.361	1.599	1.599	0.000	0.000	0.000	0.000
51	B	63	ASP	-1	-0.839	-0.916	14.197	-16.875	-16.875	0.000	0.000	0.000	0.000
52	B	64	THR	0	-0.043	-0.044	17.391	-0.194	-0.194	0.000	0.000	0.000	0.000
53	B	65	SER	0	-0.049	-0.026	19.437	0.538	0.538	0.000	0.000	0.000	0.000
54	B	66	GLY	0	-0.024	-0.014	17.592	0.529	0.529	0.000	0.000	0.000	0.000
55	B	67	LYS	1	0.809	0.920	17.595	14.042	14.042	0.000	0.000	0.000	0.000
56	B	68	ILE	0	0.018	0.002	13.015	-0.919	-0.919	0.000	0.000	0.000	0.000
57	B	69	HIS	0	0.010	0.026	14.828	0.341	0.341	0.000	0.000	0.000	0.000
58	B	70	HIS	0	0.011	-0.006	14.795	-1.199	-1.199	0.000	0.000	0.000	0.000
59	B	71	GLY	0	0.016	0.004	15.828	-0.469	-0.469	0.000	0.000	0.000	0.000
60	B	72	ASN	0	0.025	-0.011	11.737	0.028	0.028	0.000	0.000	0.000	0.000
61	B	73	ALA	0	0.009	0.005	11.124	-2.635	-2.635	0.000	0.000	0.000	0.000
62	B	74	GLU	-1	-0.911	-0.958	11.636	-18.018	-18.018	0.000	0.000	0.000	0.000
63	B	75	ASP	-1	-0.917	-0.955	11.725	-21.608	-21.608	0.000	0.000	0.000	0.000
64	B	76	LEU	0	-0.086	-0.055	5.906	-3.300	-3.300	0.000	0.000	0.000	0.000
65	B	77	ALA	0	0.044	0.033	8.255	-2.797	-2.797	0.000	0.000	0.000	0.000
66	B	78	LYS	1	0.946	0.978	10.604	18.605	18.605	0.000	0.000	0.000	0.000
67	B	79	LYS	1	0.868	0.942	5.623	39.937	39.937	0.000	0.000	0.000	0.000
69	B	81	GLY	0	0.021	0.014	8.031	1.377	1.377	0.000	0.000	0.000	0.000
70	B	82	ALA	0	0.022	0.028	11.681	1.810	1.810	0.000	0.000	0.000	0.000
71	B	83	ASP	-1	-0.828	-0.914	13.680	-15.879	-15.879	0.000	0.000	0.000	0.000
72	B	84	SER	0	-0.025	-0.043	16.836	-0.729	-0.729	0.000	0.000	0.000	0.000
73	B	85	GLU	-1	-0.875	-0.912	19.041	-12.773	-12.773	0.000	0.000	0.000	0.000
74	B	86	VAL	0	-0.004	-0.012	14.908	-0.042	-0.042	0.000	0.000	0.000	0.000
75	B	87	ALA	0	0.005	-0.003	14.516	-0.523	-0.523	0.000	0.000	0.000	0.000
76	B	88	ALA	0	0.037	0.025	15.522	-0.224	-0.224	0.000	0.000	0.000	0.000
77	B	89	LYS	1	0.810	0.889	17.963	13.973	13.973	0.000	0.000	0.000	0.000
78	B	90	LEU	0	0.022	0.013	11.606	0.158	0.158	0.000	0.000	0.000	0.000
79	B	91	VAL	0	-0.011	0.001	14.785	-0.222	-0.222	0.000	0.000	0.000	0.000
80	B	92	ALA	0	-0.006	0.004	15.632	0.435	0.435	0.000	0.000	0.000	0.000
81	B	93	ILE	0	0.021	0.015	15.042	0.437	0.437	0.000	0.000	0.000	0.000
82	B	94	LEU	0	-0.013	-0.002	11.475	0.126	0.126	0.000	0.000	0.000	0.000
83	B	95	HIS	0	-0.029	-0.015	14.877	0.923	0.923	0.000	0.000	0.000	0.000
84	B	96	GLU	-1	-0.864	-0.941	18.143	-11.945	-11.945	0.000	0.000	0.000	0.000
85	B	97	CYS	0	-0.051	0.014	12.810	1.069	1.069	0.000	0.000	0.000	0.000
86	B	98	GLU	-1	-0.833	-0.916	16.592	-15.918	-15.918	0.000	0.000	0.000	0.000
87	B	99	LYS	1	0.922	0.955	17.810	12.704	12.704	0.000	0.000	0.000	0.000
88	B	100	THR	0	-0.044	-0.028	20.041	0.646	0.646	0.000	0.000	0.000	0.000
89	B	101	HIS	0	-0.053	-0.039	17.872	0.651	0.651	0.000	0.000	0.000	0.000
90	B	102	ASP	-1	-0.818	-0.918	20.192	-13.883	-13.883	0.000	0.000	0.000	0.000
91	B	103	ALA	0	-0.035	-0.016	21.619	0.014	0.014	0.000	0.000	0.000	0.000
92	B	104	ILE	0	-0.043	-0.012	18.807	0.346	0.346	0.000	0.000	0.000	0.000
93	B	105	GLU	-1	-0.920	-0.960	21.046	-11.539	-11.539	0.000	0.000	0.000	0.000
94	B	106	ASP	-1	-0.804	-0.871	18.784	-15.024	-15.024	0.000	0.000	0.000	0.000
95	B	107	GLN	0	0.053	0.006	16.789	-1.079	-1.079	0.000	0.000	0.000	0.000
96	B	109	MET	0	0.030	0.017	14.083	-0.891	-0.891	0.000	0.000	0.000	0.000
97	B	110	LYS	1	0.852	0.945	15.873	14.641	14.641	0.000	0.000	0.000	0.000
98	B	111	ALA	0	0.004	-0.001	11.131	-0.224	-0.224	0.000	0.000	0.000	0.000
99	B	112	LEU	0	0.005	0.000	11.032	-1.092	-1.092	0.000	0.000	0.000	0.000
100	B	113	GLU	-1	-0.825	-0.905	12.522	-15.434	-15.434	0.000	0.000	0.000	0.000
101	B	114	ILE	0	-0.020	0.005	12.531	0.061	0.061	0.000	0.000	0.000	0.000
102	B	115	ALA	0	0.026	0.017	8.672	-0.279	-0.279	0.000	0.000	0.000	0.000
103	B	116	LYS	1	0.819	0.915	10.573	15.333	15.333	0.000	0.000	0.000	0.000
104	B	118	PHE	0	0.011	0.002	8.443	0.298	0.298	0.000	0.000	0.000	0.000
105	B	119	ARG	1	0.815	0.890	9.535	20.257	20.257	0.000	0.000	0.000	0.000
106	B	120	THR	0	-0.024	-0.021	11.606	0.235	0.235	0.000	0.000	0.000	0.000
107	B	121	ASN	0	-0.105	-0.065	15.360	1.186	1.186	0.000	0.000	0.000	0.000
108	B	122	ILE	0	-0.013	0.000	10.868	0.183	0.183	0.000	0.000	0.000	0.000
109	B	123	HIS	0	-0.005	0.014	15.438	-0.151	-0.151	0.000	0.000	0.000	0.000
110	B	124	GLU	-1	-0.927	-0.969	17.387	-13.699	-13.699	0.000	0.000	0.000	0.000
111	B	125	LEU	0	-0.075	-0.035	15.922	0.324	0.324	0.000	0.000	0.000	0.000
112	B	126	ASN	0	-0.059	-0.031	15.940	-1.246	-1.246	0.000	0.000	0.000	0.000
113	B	127	TRP	0	-0.024	-0.037	7.242	-0.147	-0.147	0.000	0.000	0.000	0.000
114	B	128	ALA	-1	-0.888	-0.929	8.246	-30.033	-30.033	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(B:12:PHE)