FMO DATABASE

FMODB ID: G46J1

Calculation Name: 3K7C-D-Xray549

Preferred Name:

Target Type:

Ligand Name: triethylene glycol | di(hydroxyethyl)ether | chloride ion

Ligand 3-letter code: PGE | PEG | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3K7C

Chain ID: D

ChEMBL ID:

UniProt ID: Q0PBT7

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	108
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-825469.262518
FMO2-HF: Nuclear repulsion	783076.531216
FMO2-HF: Total energy	-42392.731303
FMO2-MP2: Total energy	-42517.542719

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(D:6:SER)

Summations of interaction energy for fragment #1(D:6:SER)

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.
-23.932	-13.542	4.867	-7.909	-7.348	-0.091

Interaction energy analysis for fragmet #1(D:6:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.798 / q_NPA : 0.889

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	D	8	PRO	0	0.062	0.022	2.917	-11.362	-9.018	0.426	-1.265	-1.505	-0.008
5	D	10	ASP	-1	-0.860	-0.937	2.032	-95.540	-89.287	4.324	-6.020	-4.558	-0.084
6	D	11	LEU	0	-0.040	-0.005	3.181	4.316	5.507	0.108	-0.472	-0.827	0.001
7	D	12	ALA	0	0.053	0.030	4.531	6.051	6.095	-0.001	-0.015	-0.027	0.000
103	D	108	TRP	0	-0.034	-0.020	3.175	2.713	3.195	0.011	-0.137	-0.356	0.000
104	D	109	LEU	0	-0.004	-0.008	5.200	-1.077	-1.001	-0.001	0.000	-0.075	0.000
4	D	9	GLU	-1	-0.755	-0.888	5.452	-37.668	-37.668	0.000	0.000	0.000	0.000
8	D	13	LYS	1	0.973	1.000	7.166	39.789	39.789	0.000	0.000	0.000	0.000
9	D	14	ASN	0	-0.049	-0.035	5.457	6.637	6.637	0.000	0.000	0.000	0.000
10	D	15	PHE	0	0.047	0.026	8.121	3.131	3.131	0.000	0.000	0.000	0.000
11	D	16	THR	0	-0.022	-0.027	10.057	3.039	3.039	0.000	0.000	0.000	0.000
12	D	17	LYS	1	0.907	0.943	11.014	25.493	25.493	0.000	0.000	0.000	0.000
13	D	18	ASP	-1	-0.835	-0.899	11.165	-24.212	-24.212	0.000	0.000	0.000	0.000
14	D	19	LEU	0	0.024	0.021	13.924	1.687	1.687	0.000	0.000	0.000	0.000
15	D	20	TYR	0	0.001	-0.003	15.960	1.739	1.739	0.000	0.000	0.000	0.000
16	D	21	SER	0	-0.098	-0.053	16.459	0.890	0.890	0.000	0.000	0.000	0.000
17	D	22	GLY	0	0.027	-0.004	18.298	0.973	0.973	0.000	0.000	0.000	0.000
18	D	23	ASP	-1	-0.836	-0.876	15.312	-18.189	-18.189	0.000	0.000	0.000	0.000
19	D	24	THR	0	0.044	0.003	15.782	-1.115	-1.115	0.000	0.000	0.000	0.000
20	D	25	LYS	1	0.867	0.927	16.267	16.286	16.286	0.000	0.000	0.000	0.000
21	D	26	SER	0	0.003	-0.012	11.514	-0.715	-0.715	0.000	0.000	0.000	0.000
22	D	27	VAL	0	-0.006	0.003	11.553	-1.640	-1.640	0.000	0.000	0.000	0.000
23	D	28	MET	0	0.023	0.009	12.567	-0.951	-0.951	0.000	0.000	0.000	0.000
24	D	29	SER	0	-0.081	-0.033	10.151	-0.841	-0.841	0.000	0.000	0.000	0.000
25	D	30	TYR	0	-0.069	-0.059	6.546	-3.508	-3.508	0.000	0.000	0.000	0.000
26	D	31	ILE	0	0.009	0.015	9.086	-0.995	-0.995	0.000	0.000	0.000	0.000
27	D	32	ASP	-1	-0.809	-0.865	12.050	-18.739	-18.739	0.000	0.000	0.000	0.000
28	D	33	LEU	0	0.030	0.011	13.043	1.050	1.050	0.000	0.000	0.000	0.000
29	D	34	SER	0	-0.069	-0.059	15.052	1.074	1.074	0.000	0.000	0.000	0.000
30	D	35	GLU	-1	-0.844	-0.924	16.800	-13.094	-13.094	0.000	0.000	0.000	0.000
31	D	36	ALA	0	-0.007	0.017	19.443	0.636	0.636	0.000	0.000	0.000	0.000
32	D	37	LYS	1	0.815	0.890	20.268	13.345	13.345	0.000	0.000	0.000	0.000
33	D	38	SER	0	-0.024	-0.044	23.560	0.121	0.121	0.000	0.000	0.000	0.000
34	D	39	ASP	-1	-0.858	-0.944	24.606	-11.512	-11.512	0.000	0.000	0.000	0.000
35	D	40	GLU	-1	-0.890	-0.936	26.212	-10.119	-10.119	0.000	0.000	0.000	0.000
36	D	41	GLU	-1	-0.851	-0.889	23.665	-11.732	-11.732	0.000	0.000	0.000	0.000
37	D	42	LYS	1	0.848	0.926	20.578	12.079	12.079	0.000	0.000	0.000	0.000
38	D	43	THR	0	-0.039	-0.026	22.356	-0.388	-0.388	0.000	0.000	0.000	0.000
39	D	44	PHE	0	-0.002	0.001	24.641	-0.178	-0.178	0.000	0.000	0.000	0.000
40	D	45	VAL	0	0.002	-0.001	18.667	-0.211	-0.211	0.000	0.000	0.000	0.000
41	D	46	SER	0	0.006	-0.003	20.513	-0.609	-0.609	0.000	0.000	0.000	0.000
42	D	47	ASP	-1	-0.870	-0.901	21.529	-11.271	-11.271	0.000	0.000	0.000	0.000
43	D	48	LYS	1	0.965	0.988	23.024	11.894	11.894	0.000	0.000	0.000	0.000
44	D	49	ILE	0	0.002	-0.011	17.197	-0.314	-0.314	0.000	0.000	0.000	0.000
45	D	50	THR	0	0.005	-0.018	20.393	-0.348	-0.348	0.000	0.000	0.000	0.000
46	D	51	GLN	0	-0.096	-0.058	22.377	0.040	0.040	0.000	0.000	0.000	0.000
47	D	52	VAL	0	0.018	0.011	19.509	0.009	0.009	0.000	0.000	0.000	0.000
48	D	53	VAL	0	-0.009	0.000	17.446	-0.324	-0.324	0.000	0.000	0.000	0.000
49	D	54	ALA	0	0.010	0.018	20.250	0.025	0.025	0.000	0.000	0.000	0.000
50	D	55	GLU	-1	-0.907	-0.958	23.745	-11.749	-11.749	0.000	0.000	0.000	0.000
51	D	56	ASN	0	-0.038	-0.042	20.108	0.182	0.182	0.000	0.000	0.000	0.000
52	D	57	ALA	0	0.042	0.029	20.856	-0.021	-0.021	0.000	0.000	0.000	0.000
53	D	58	ALA	0	-0.045	-0.023	22.168	0.307	0.307	0.000	0.000	0.000	0.000
54	D	59	LYS	1	0.801	0.899	21.198	14.498	14.498	0.000	0.000	0.000	0.000
55	D	60	ALA	0	0.036	0.011	21.178	0.214	0.214	0.000	0.000	0.000	0.000
56	D	61	LYS	1	0.910	0.962	23.048	13.469	13.469	0.000	0.000	0.000	0.000
57	D	62	ARG	1	0.948	0.985	25.928	11.162	11.162	0.000	0.000	0.000	0.000
58	D	63	MET	0	-0.051	-0.003	24.673	0.325	0.325	0.000	0.000	0.000	0.000
59	D	64	GLY	0	0.042	0.023	26.411	-0.067	-0.067	0.000	0.000	0.000	0.000
60	D	65	GLY	0	-0.021	-0.002	22.842	-0.149	-0.149	0.000	0.000	0.000	0.000
61	D	66	VAL	0	-0.034	-0.031	16.824	0.230	0.230	0.000	0.000	0.000	0.000
62	D	67	LYS	1	0.878	0.953	20.239	13.084	13.084	0.000	0.000	0.000	0.000
63	D	68	ASP	-1	-0.842	-0.920	15.502	-19.889	-19.889	0.000	0.000	0.000	0.000
64	D	69	ILE	0	-0.075	-0.036	12.225	0.298	0.298	0.000	0.000	0.000	0.000
65	D	70	GLN	0	-0.020	-0.015	12.635	-1.480	-1.480	0.000	0.000	0.000	0.000
66	D	71	ILE	0	-0.056	-0.043	8.982	-1.157	-1.157	0.000	0.000	0.000	0.000
67	D	72	GLU	-1	-0.826	-0.894	13.577	-15.262	-15.262	0.000	0.000	0.000	0.000
68	D	73	GLU	-1	-0.889	-0.947	15.968	-15.710	-15.710	0.000	0.000	0.000	0.000
69	D	74	LYS	1	0.832	0.895	10.068	26.867	26.867	0.000	0.000	0.000	0.000
70	D	75	THR	0	0.004	0.017	14.322	1.050	1.050	0.000	0.000	0.000	0.000
71	D	76	ILE	0	-0.009	-0.011	9.385	-1.268	-1.268	0.000	0.000	0.000	0.000
72	D	77	ASN	0	0.019	0.014	12.851	1.300	1.300	0.000	0.000	0.000	0.000
73	D	78	LYS	1	0.944	0.969	11.593	15.596	15.596	0.000	0.000	0.000	0.000
74	D	79	ASP	-1	-0.867	-0.944	10.551	-21.651	-21.651	0.000	0.000	0.000	0.000
75	D	80	SER	0	0.027	0.028	11.646	0.171	0.171	0.000	0.000	0.000	0.000
76	D	81	ALA	0	-0.005	-0.010	10.058	-0.750	-0.750	0.000	0.000	0.000	0.000
77	D	82	LYS	1	0.933	0.985	12.158	17.599	17.599	0.000	0.000	0.000	0.000
78	D	83	ILE	0	0.003	-0.005	8.724	0.005	0.005	0.000	0.000	0.000	0.000
79	D	84	ARG	1	0.850	0.945	12.947	15.665	15.665	0.000	0.000	0.000	0.000
80	D	85	VAL	0	-0.002	-0.001	11.393	-0.590	-0.590	0.000	0.000	0.000	0.000
81	D	86	LEU	0	-0.008	-0.011	14.204	1.404	1.404	0.000	0.000	0.000	0.000
82	D	87	VAL	0	-0.039	-0.019	15.797	-1.180	-1.180	0.000	0.000	0.000	0.000
83	D	88	LEU	0	0.036	0.028	17.877	1.004	1.004	0.000	0.000	0.000	0.000
84	D	89	PHE	0	-0.002	-0.014	20.172	-0.668	-0.668	0.000	0.000	0.000	0.000
85	D	90	ASN	0	-0.021	-0.029	22.724	0.100	0.100	0.000	0.000	0.000	0.000
86	D	91	ASN	0	-0.035	-0.019	25.226	0.006	0.006	0.000	0.000	0.000	0.000
87	D	92	ASP	-1	-0.872	-0.936	26.087	-11.388	-11.388	0.000	0.000	0.000	0.000
88	D	93	ASN	0	-0.043	-0.003	26.237	0.229	0.229	0.000	0.000	0.000	0.000
89	D	94	ASN	0	0.059	0.016	22.485	-0.608	-0.608	0.000	0.000	0.000	0.000
90	D	95	GLN	0	0.002	0.003	21.364	0.210	0.210	0.000	0.000	0.000	0.000
91	D	96	SER	0	0.021	0.013	18.481	-0.626	-0.626	0.000	0.000	0.000	0.000
92	D	97	SER	0	-0.016	-0.006	16.757	1.056	1.056	0.000	0.000	0.000	0.000
93	D	98	ASN	0	-0.062	-0.033	15.792	-1.350	-1.350	0.000	0.000	0.000	0.000
94	D	99	VAL	0	0.043	0.034	10.339	0.516	0.516	0.000	0.000	0.000	0.000
95	D	100	PHE	0	0.046	0.008	12.852	-0.530	-0.530	0.000	0.000	0.000	0.000
96	D	101	LEU	0	-0.020	-0.005	6.952	-1.447	-1.447	0.000	0.000	0.000	0.000
97	D	102	ALA	0	0.031	0.008	9.870	1.424	1.424	0.000	0.000	0.000	0.000
98	D	103	LYS	1	0.811	0.909	6.409	29.468	29.468	0.000	0.000	0.000	0.000
99	D	104	LYS	1	0.895	0.943	8.925	20.759	20.759	0.000	0.000	0.000	0.000
100	D	105	ASP	-1	-0.833	-0.910	9.735	-21.170	-21.170	0.000	0.000	0.000	0.000
101	D	106	ARG	1	0.942	0.952	7.782	26.843	26.843	0.000	0.000	0.000	0.000
102	D	107	LYS	1	0.886	0.962	4.895	26.921	26.921	0.000	0.000	0.000	0.000
105	D	110	VAL	0	-0.001	-0.008	8.002	-0.260	-0.260	0.000	0.000	0.000	0.000
106	D	111	LEU	0	-0.038	-0.026	10.538	1.200	1.200	0.000	0.000	0.000	0.000
107	D	112	LEU	0	-0.034	-0.020	14.005	-0.272	-0.272	0.000	0.000	0.000	0.000
108	D	113	LYS	-1	-0.896	-0.937	17.231	-14.217	-14.217	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(D:6:SER)