FMO DATABASE

FMODB ID: KKY63

Calculation Name: 2AZW-A-Xray547

Preferred Name:

Target Type:

Ligand Name: pentaethylene glycol

Ligand 3-letter code: 1PE

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2AZW

Chain ID: A

ChEMBL ID:

UniProt ID: Q836H1

Base Structure: X-ray

Registration Date: 2025-10-03

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	147
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1442314.661424
FMO2-HF: Nuclear repulsion	1383795.408049
FMO2-HF: Total energy	-58519.253375
FMO2-MP2: Total energy	-58693.085582

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:2:LYS)

Summations of interaction energy for fragment #1(A:2:LYS)

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.
-220.121	-215.33	1.01	-3.08	-2.721	-0.039

Interaction energy analysis for fragmet #1(A:2:LYS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 2 / q_Mulliken : 1.759 / q_NPA : 1.868

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	4	PRO	0	-0.008	0.013	2.368	-28.703	-24.000	1.011	-3.067	-2.647	-0.039
4	A	5	THR	0	0.006	0.006	4.453	-0.156	-0.068	-0.001	-0.013	-0.074	0.000
5	A	6	PHE	0	-0.013	0.003	5.980	0.748	0.748	0.000	0.000	0.000	0.000
6	A	7	GLY	0	0.068	0.046	9.579	0.911	0.911	0.000	0.000	0.000	0.000
7	A	8	LYS	1	0.878	0.927	11.883	32.166	32.166	0.000	0.000	0.000	0.000
8	A	9	ARG	1	0.943	0.982	10.929	43.734	43.734	0.000	0.000	0.000	0.000
9	A	10	GLU	-1	-0.906	-0.962	14.377	-27.182	-27.182	0.000	0.000	0.000	0.000
10	A	11	GLU	-1	-0.935	-0.983	17.024	-31.842	-31.842	0.000	0.000	0.000	0.000
11	A	12	THR	0	-0.015	-0.004	17.835	0.927	0.927	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.011	0.010	19.348	0.946	0.946	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.035	-0.024	18.422	-1.282	-1.282	0.000	0.000	0.000	0.000
14	A	15	TYR	0	-0.032	-0.012	15.243	0.365	0.365	0.000	0.000	0.000	0.000
15	A	16	GLN	0	0.024	0.018	16.850	-0.956	-0.956	0.000	0.000	0.000	0.000
16	A	17	THR	0	0.009	-0.001	14.126	-2.013	-2.013	0.000	0.000	0.000	0.000
17	A	18	ARG	1	0.825	0.896	16.352	28.021	28.021	0.000	0.000	0.000	0.000
18	A	19	TYR	0	0.034	0.023	12.995	-0.771	-0.771	0.000	0.000	0.000	0.000
19	A	20	ALA	0	0.026	0.016	15.849	2.038	2.038	0.000	0.000	0.000	0.000
20	A	21	ALA	0	-0.022	0.003	16.391	-2.260	-2.260	0.000	0.000	0.000	0.000
21	A	22	TYR	0	-0.002	0.002	15.767	1.444	1.444	0.000	0.000	0.000	0.000
22	A	23	ILE	0	-0.011	-0.014	18.888	-1.257	-1.257	0.000	0.000	0.000	0.000
23	A	24	ILE	0	0.012	0.009	18.274	0.907	0.907	0.000	0.000	0.000	0.000
24	A	25	VAL	0	0.020	0.014	22.164	0.403	0.403	0.000	0.000	0.000	0.000
25	A	26	SER	0	0.010	0.000	25.074	0.539	0.539	0.000	0.000	0.000	0.000
26	A	27	LYS	1	0.897	0.970	26.979	19.116	19.116	0.000	0.000	0.000	0.000
27	A	28	PRO	0	0.040	0.010	28.265	0.093	0.093	0.000	0.000	0.000	0.000
28	A	29	GLU	-1	-0.899	-0.948	30.167	-18.399	-18.399	0.000	0.000	0.000	0.000
29	A	30	ASN	0	-0.043	-0.014	32.711	0.070	0.070	0.000	0.000	0.000	0.000
30	A	31	ASN	0	-0.007	0.000	26.890	-0.542	-0.542	0.000	0.000	0.000	0.000
31	A	32	THR	0	-0.040	-0.030	28.581	-0.170	-0.170	0.000	0.000	0.000	0.000
32	A	33	MET	0	0.011	0.000	21.672	-0.612	-0.612	0.000	0.000	0.000	0.000
33	A	34	VAL	0	-0.037	0.000	27.151	0.377	0.377	0.000	0.000	0.000	0.000
34	A	35	LEU	0	-0.028	-0.008	22.836	-1.111	-1.111	0.000	0.000	0.000	0.000
35	A	36	VAL	0	0.049	0.021	25.101	1.206	1.206	0.000	0.000	0.000	0.000
36	A	37	GLN	0	-0.082	-0.041	25.456	-0.406	-0.406	0.000	0.000	0.000	0.000
37	A	38	ALA	0	0.057	0.034	26.212	0.702	0.702	0.000	0.000	0.000	0.000
38	A	39	PRO	0	0.032	0.003	28.098	0.195	0.195	0.000	0.000	0.000	0.000
39	A	40	ASN	0	-0.069	-0.032	25.212	0.363	0.363	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.018	0.015	28.568	-0.185	-0.185	0.000	0.000	0.000	0.000
41	A	42	ALA	0	-0.081	-0.037	23.184	-0.451	-0.451	0.000	0.000	0.000	0.000
42	A	43	TYR	0	0.032	0.015	23.590	0.282	0.282	0.000	0.000	0.000	0.000
43	A	44	PHE	0	-0.037	-0.037	19.630	-1.677	-1.677	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.013	-0.005	17.592	0.876	0.876	0.000	0.000	0.000	0.000
45	A	46	PRO	0	0.029	0.018	21.410	-0.313	-0.313	0.000	0.000	0.000	0.000
46	A	47	GLY	0	-0.012	-0.011	21.581	-1.427	-1.427	0.000	0.000	0.000	0.000
47	A	48	GLY	0	0.058	0.033	21.311	0.237	0.237	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.830	-0.889	19.499	-28.473	-28.473	0.000	0.000	0.000	0.000
49	A	50	ILE	0	0.009	0.016	18.406	0.761	0.761	0.000	0.000	0.000	0.000
50	A	51	GLU	-1	-0.942	-0.965	21.881	-21.768	-21.768	0.000	0.000	0.000	0.000
51	A	52	GLY	0	-0.035	-0.028	25.198	0.048	0.048	0.000	0.000	0.000	0.000
52	A	53	THR	0	-0.077	-0.050	25.332	-0.265	-0.265	0.000	0.000	0.000	0.000
53	A	54	GLU	-1	-0.764	-0.833	24.351	-23.422	-23.422	0.000	0.000	0.000	0.000
54	A	55	THR	0	-0.046	-0.051	22.445	-1.392	-1.392	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.893	0.946	15.157	35.548	35.548	0.000	0.000	0.000	0.000
56	A	57	GLU	-1	-0.812	-0.902	19.913	-29.445	-29.445	0.000	0.000	0.000	0.000
57	A	58	GLU	-1	-0.836	-0.897	23.118	-21.802	-21.802	0.000	0.000	0.000	0.000
58	A	59	ALA	0	0.016	0.020	22.340	0.572	0.572	0.000	0.000	0.000	0.000
59	A	60	ILE	0	-0.018	-0.008	20.030	0.449	0.449	0.000	0.000	0.000	0.000
60	A	61	HIS	0	-0.029	-0.031	24.222	0.830	0.830	0.000	0.000	0.000	0.000
61	A	62	ARG	1	0.751	0.865	24.998	23.423	23.423	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.827	-0.902	23.897	-23.029	-23.029	0.000	0.000	0.000	0.000
63	A	64	VAL	0	-0.033	-0.019	26.050	0.582	0.582	0.000	0.000	0.000	0.000
64	A	65	LEU	0	-0.013	0.000	28.449	0.742	0.742	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.855	-0.943	29.725	-19.426	-19.426	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.797	-0.908	25.753	-23.133	-23.133	0.000	0.000	0.000	0.000
67	A	68	LEU	0	-0.027	-0.032	27.581	0.360	0.360	0.000	0.000	0.000	0.000
68	A	69	GLY	0	0.024	0.044	31.742	0.510	0.510	0.000	0.000	0.000	0.000
69	A	70	ILE	0	-0.053	-0.033	29.145	0.521	0.521	0.000	0.000	0.000	0.000
70	A	71	SER	0	0.007	0.009	31.608	-0.067	-0.067	0.000	0.000	0.000	0.000
71	A	72	VAL	0	0.016	-0.015	26.310	0.142	0.142	0.000	0.000	0.000	0.000
72	A	73	GLU	-1	-0.892	-0.932	26.963	-21.568	-21.568	0.000	0.000	0.000	0.000
73	A	74	ILE	0	-0.030	-0.015	21.735	-0.599	-0.599	0.000	0.000	0.000	0.000
74	A	75	GLY	0	0.029	0.023	22.718	0.358	0.358	0.000	0.000	0.000	0.000
75	A	76	CYS	0	-0.041	-0.021	17.627	-1.548	-1.548	0.000	0.000	0.000	0.000
76	A	77	TYR	0	0.035	0.020	11.573	-0.705	-0.705	0.000	0.000	0.000	0.000
77	A	78	LEU	0	0.010	0.003	13.775	-1.625	-1.625	0.000	0.000	0.000	0.000
78	A	79	GLY	0	-0.032	-0.014	10.280	-4.315	-4.315	0.000	0.000	0.000	0.000
79	A	80	GLU	-1	-0.908	-0.954	8.389	-57.209	-57.209	0.000	0.000	0.000	0.000
80	A	81	ALA	0	-0.038	-0.029	7.707	-6.490	-6.490	0.000	0.000	0.000	0.000
81	A	82	ASP	-1	-0.796	-0.879	6.918	-60.576	-60.576	0.000	0.000	0.000	0.000
82	A	83	GLU	-1	-0.802	-0.901	8.987	-41.727	-41.727	0.000	0.000	0.000	0.000
83	A	84	TYR	0	-0.034	-0.015	8.466	0.474	0.474	0.000	0.000	0.000	0.000
84	A	85	PHE	0	-0.024	-0.018	13.083	1.069	1.069	0.000	0.000	0.000	0.000
85	A	86	TYR	0	0.027	0.006	16.810	-0.184	-0.184	0.000	0.000	0.000	0.000
86	A	87	SER	0	-0.042	0.002	20.356	0.469	0.469	0.000	0.000	0.000	0.000
87	A	88	ASN	0	0.058	-0.001	23.052	0.075	0.075	0.000	0.000	0.000	0.000
88	A	89	HIS	0	0.023	0.011	25.773	0.314	0.314	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.818	0.868	21.711	25.485	25.485	0.000	0.000	0.000	0.000
90	A	91	GLN	0	-0.007	0.026	26.506	-0.511	-0.511	0.000	0.000	0.000	0.000
91	A	92	THR	0	-0.010	0.001	21.481	-0.038	-0.038	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.002	0.009	18.535	-0.383	-0.383	0.000	0.000	0.000	0.000
93	A	94	TYR	0	0.027	-0.001	17.457	0.476	0.476	0.000	0.000	0.000	0.000
94	A	95	TYR	0	-0.093	-0.071	7.655	1.088	1.088	0.000	0.000	0.000	0.000
95	A	96	ASN	0	-0.005	-0.017	12.890	1.579	1.579	0.000	0.000	0.000	0.000
96	A	97	PRO	0	0.039	0.027	10.406	-0.616	-0.616	0.000	0.000	0.000	0.000
97	A	98	GLY	0	0.006	0.018	11.520	3.691	3.691	0.000	0.000	0.000	0.000
98	A	99	TYR	0	-0.038	-0.030	11.935	-3.815	-3.815	0.000	0.000	0.000	0.000
99	A	100	PHE	0	0.020	0.003	12.147	2.901	2.901	0.000	0.000	0.000	0.000
100	A	101	TYR	0	-0.039	-0.049	15.530	-2.046	-2.046	0.000	0.000	0.000	0.000
101	A	102	VAL	0	0.014	0.012	18.325	0.080	0.080	0.000	0.000	0.000	0.000
102	A	103	ALA	0	0.010	0.009	21.138	0.351	0.351	0.000	0.000	0.000	0.000
103	A	104	ASN	0	-0.041	-0.027	24.308	-0.745	-0.745	0.000	0.000	0.000	0.000
104	A	105	THR	0	-0.008	-0.010	26.313	0.757	0.757	0.000	0.000	0.000	0.000
105	A	106	TRP	0	-0.035	-0.023	29.139	-0.257	-0.257	0.000	0.000	0.000	0.000
106	A	107	ARG	1	0.926	0.970	31.384	17.756	17.756	0.000	0.000	0.000	0.000
107	A	108	GLN	0	-0.019	-0.014	34.824	-0.477	-0.477	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.077	-0.041	35.652	0.424	0.424	0.000	0.000	0.000	0.000
109	A	110	SER	0	-0.046	-0.034	37.297	0.436	0.436	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.783	-0.861	37.977	-15.821	-15.821	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.029	0.001	33.831	-0.129	-0.129	0.000	0.000	0.000	0.000
112	A	113	LEU	0	-0.012	0.004	34.274	0.582	0.582	0.000	0.000	0.000	0.000
113	A	114	GLU	-1	-0.809	-0.866	30.652	-19.204	-19.204	0.000	0.000	0.000	0.000
114	A	115	ARG	1	0.788	0.853	32.998	15.794	15.794	0.000	0.000	0.000	0.000
115	A	116	THR	0	-0.064	-0.055	32.502	0.536	0.536	0.000	0.000	0.000	0.000
116	A	117	ASN	0	-0.065	-0.042	29.079	-0.657	-0.657	0.000	0.000	0.000	0.000
117	A	118	THR	0	-0.012	-0.002	31.004	0.489	0.489	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.011	0.000	29.810	-0.711	-0.711	0.000	0.000	0.000	0.000
119	A	120	HIS	0	-0.007	-0.006	28.921	0.586	0.586	0.000	0.000	0.000	0.000
120	A	121	TRP	0	0.019	0.006	29.039	-0.699	-0.699	0.000	0.000	0.000	0.000
121	A	122	VAL	0	0.009	0.005	26.578	0.615	0.615	0.000	0.000	0.000	0.000
122	A	123	ALA	0	0.063	0.034	27.931	-0.349	-0.349	0.000	0.000	0.000	0.000
123	A	124	PRO	0	0.025	0.017	22.600	-0.489	-0.489	0.000	0.000	0.000	0.000
124	A	125	GLU	-1	-0.844	-0.945	22.738	-25.451	-25.451	0.000	0.000	0.000	0.000
125	A	126	GLU	-1	-0.881	-0.923	23.958	-22.191	-22.191	0.000	0.000	0.000	0.000
126	A	127	ALA	0	0.006	0.000	22.647	-0.225	-0.225	0.000	0.000	0.000	0.000
127	A	128	VAL	0	-0.031	-0.018	18.604	-0.597	-0.597	0.000	0.000	0.000	0.000
128	A	129	ARG	1	0.797	0.883	20.281	22.852	22.852	0.000	0.000	0.000	0.000
129	A	130	LEU	0	-0.008	0.008	23.008	0.061	0.061	0.000	0.000	0.000	0.000
130	A	131	LEU	0	-0.027	0.006	18.675	-0.003	-0.003	0.000	0.000	0.000	0.000
131	A	132	LYS	1	0.923	0.971	19.338	24.785	24.785	0.000	0.000	0.000	0.000
132	A	133	ARG	1	0.871	0.932	15.056	32.607	32.607	0.000	0.000	0.000	0.000
133	A	134	GLY	0	-0.012	-0.004	12.424	0.449	0.449	0.000	0.000	0.000	0.000
134	A	135	SER	0	-0.046	-0.055	10.928	0.003	0.003	0.000	0.000	0.000	0.000
135	A	136	HIS	0	0.013	0.007	11.916	0.606	0.606	0.000	0.000	0.000	0.000
136	A	137	ARG	1	0.897	0.956	15.038	34.837	34.837	0.000	0.000	0.000	0.000
137	A	138	TRP	0	0.025	0.012	8.279	-0.641	-0.641	0.000	0.000	0.000	0.000
138	A	139	ALA	0	-0.006	0.007	13.003	-0.151	-0.151	0.000	0.000	0.000	0.000
139	A	140	VAL	0	0.030	0.008	14.741	1.059	1.059	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-0.938	-0.976	14.374	-38.011	-38.011	0.000	0.000	0.000	0.000
141	A	142	LYS	1	0.836	0.906	9.186	52.453	52.453	0.000	0.000	0.000	0.000
142	A	143	TRP	0	0.011	-0.010	13.865	0.831	0.831	0.000	0.000	0.000	0.000
143	A	144	LEU	0	-0.006	-0.004	17.307	1.094	1.094	0.000	0.000	0.000	0.000
144	A	145	ALA	0	-0.051	-0.015	14.772	0.948	0.948	0.000	0.000	0.000	0.000
145	A	146	ALA	0	-0.086	-0.035	16.274	-0.386	-0.386	0.000	0.000	0.000	0.000
146	A	147	ALA	0	-0.030	-0.011	17.691	1.381	1.381	0.000	0.000	0.000	0.000
147	A	148	SER	-1	-0.957	-0.969	20.296	-26.540	-26.540	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:LYS)