FMO DATABASE

FMODB ID: Y1RJ2

Calculation Name: 4HWX-A-Xray547

Preferred Name:

Target Type:

Ligand Name: acetate ion | glycerol

Ligand 3-letter code: ACT | GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 4HWX

Chain ID: A

ChEMBL ID:

UniProt ID: Q9FDS0

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	112
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-793853.746241
FMO2-HF: Nuclear repulsion	750814.660691
FMO2-HF: Total energy	-43039.08555
FMO2-MP2: Total energy	-43160.435286

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:-1:GLY)

Summations of interaction energy for fragment #1(A:-1:GLY)

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.
-55.705	-54.419	-0.002	-0.525	-0.758	-0.002

Interaction energy analysis for fragmet #1(A:-1:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.873 / q_NPA : 0.923

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	2	ALA	0	0.002	0.016	3.549	8.480	9.706	-0.001	-0.507	-0.717	-0.002
4	A	3	HIS	0	0.047	0.015	4.466	-8.602	-8.542	-0.001	-0.018	-0.041	0.000
5	A	4	GLY	0	0.023	0.015	7.171	3.173	3.173	0.000	0.000	0.000	0.000
6	A	5	PRO	0	-0.014	-0.016	10.886	-0.540	-0.540	0.000	0.000	0.000	0.000
7	A	6	SER	0	0.045	0.033	10.778	-1.157	-1.157	0.000	0.000	0.000	0.000
8	A	7	ALA	0	-0.032	-0.003	13.582	0.867	0.867	0.000	0.000	0.000	0.000
9	A	8	MET	0	-0.050	0.002	16.031	-0.407	-0.407	0.000	0.000	0.000	0.000
10	A	9	VAL	0	0.000	0.003	18.810	0.585	0.585	0.000	0.000	0.000	0.000
11	A	10	PHE	0	0.010	0.007	17.034	-0.585	-0.585	0.000	0.000	0.000	0.000
12	A	11	THR	0	-0.030	-0.036	22.923	0.658	0.658	0.000	0.000	0.000	0.000
13	A	12	VAL	0	0.027	0.007	26.032	-0.280	-0.280	0.000	0.000	0.000	0.000
14	A	13	ILE	0	-0.020	-0.006	28.803	0.312	0.312	0.000	0.000	0.000	0.000
15	A	14	GLN	0	0.024	0.011	31.615	-0.085	-0.085	0.000	0.000	0.000	0.000
16	A	15	GLY	0	0.048	0.020	34.606	0.170	0.170	0.000	0.000	0.000	0.000
17	A	16	SER	0	-0.025	-0.010	32.394	-0.215	-0.215	0.000	0.000	0.000	0.000
18	A	17	GLY	0	-0.054	-0.022	30.102	-0.352	-0.352	0.000	0.000	0.000	0.000
19	A	18	GLU	-1	-0.945	-0.973	31.120	-9.058	-9.058	0.000	0.000	0.000	0.000
20	A	19	PRO	0	-0.057	-0.038	33.569	-0.074	-0.074	0.000	0.000	0.000	0.000
21	A	20	THR	0	-0.021	-0.019	34.516	0.047	0.047	0.000	0.000	0.000	0.000
22	A	21	ASP	-1	-0.800	-0.882	33.988	-8.737	-8.737	0.000	0.000	0.000	0.000
23	A	22	THR	0	-0.021	-0.011	35.128	-0.029	-0.029	0.000	0.000	0.000	0.000
24	A	23	VAL	0	0.004	-0.005	30.479	-0.141	-0.141	0.000	0.000	0.000	0.000
25	A	24	LEU	0	-0.035	-0.007	32.764	0.170	0.170	0.000	0.000	0.000	0.000
26	A	25	ARG	1	0.833	0.887	29.499	10.361	10.361	0.000	0.000	0.000	0.000
27	A	26	ALA	0	0.014	-0.003	27.253	-0.235	-0.235	0.000	0.000	0.000	0.000
28	A	27	THR	0	-0.031	0.005	24.346	0.027	0.027	0.000	0.000	0.000	0.000
29	A	28	THR	0	0.017	0.005	22.937	-0.401	-0.401	0.000	0.000	0.000	0.000
30	A	29	LEU	0	-0.018	-0.007	17.003	0.166	0.166	0.000	0.000	0.000	0.000
31	A	30	SER	0	-0.017	0.004	17.850	-0.761	-0.761	0.000	0.000	0.000	0.000
32	A	31	CYS	0	-0.036	-0.031	13.589	-0.242	-0.242	0.000	0.000	0.000	0.000
33	A	32	ALA	0	0.037	0.009	13.770	-1.517	-1.517	0.000	0.000	0.000	0.000
34	A	33	TYR	0	0.014	0.009	15.155	-0.370	-0.370	0.000	0.000	0.000	0.000
35	A	34	THR	0	-0.032	-0.026	17.053	0.016	0.016	0.000	0.000	0.000	0.000
36	A	35	ALA	0	-0.020	-0.009	17.515	-1.036	-1.036	0.000	0.000	0.000	0.000
37	A	36	GLU	-1	-0.887	-0.924	19.160	-13.121	-13.121	0.000	0.000	0.000	0.000
38	A	37	GLY	0	0.035	0.009	21.304	-0.599	-0.599	0.000	0.000	0.000	0.000
39	A	38	THR	0	-0.004	-0.011	23.990	0.170	0.170	0.000	0.000	0.000	0.000
40	A	39	HIS	0	-0.012	0.013	22.176	0.330	0.330	0.000	0.000	0.000	0.000
41	A	40	PRO	0	0.039	0.021	24.405	-0.034	-0.034	0.000	0.000	0.000	0.000
42	A	41	ALA	0	-0.029	-0.015	22.930	0.207	0.207	0.000	0.000	0.000	0.000
43	A	42	PRO	0	0.021	0.009	20.503	-0.801	-0.801	0.000	0.000	0.000	0.000
44	A	43	ARG	1	0.867	0.919	14.974	18.170	18.170	0.000	0.000	0.000	0.000
45	A	44	ALA	0	0.077	0.043	16.478	-1.020	-1.020	0.000	0.000	0.000	0.000
46	A	45	ALA	0	0.030	0.024	17.090	-0.599	-0.599	0.000	0.000	0.000	0.000
47	A	47	ASP	-1	-0.899	-0.956	12.408	-22.471	-22.471	0.000	0.000	0.000	0.000
48	A	48	ALA	0	-0.011	-0.006	12.361	-1.526	-1.526	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.013	0.007	12.483	-0.537	-0.537	0.000	0.000	0.000	0.000
50	A	50	ASN	0	0.002	0.012	8.443	-3.195	-3.195	0.000	0.000	0.000	0.000
51	A	51	ALA	0	-0.016	-0.001	8.288	-2.890	-2.890	0.000	0.000	0.000	0.000
52	A	52	THR	0	-0.038	-0.023	10.760	0.244	0.244	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.941	-0.970	5.237	-43.852	-43.852	0.000	0.000	0.000	0.000
54	A	54	GLY	0	-0.007	-0.006	7.733	-0.828	-0.828	0.000	0.000	0.000	0.000
55	A	55	GLU	-1	-0.931	-0.951	10.152	-17.326	-17.326	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.059	0.003	12.938	0.333	0.333	0.000	0.000	0.000	0.000
57	A	57	ASN	0	0.026	0.022	15.541	1.432	1.432	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.836	0.912	9.826	25.119	25.119	0.000	0.000	0.000	0.000
59	A	59	LEU	0	-0.029	-0.010	15.707	-0.198	-0.198	0.000	0.000	0.000	0.000
60	A	60	LEU	0	-0.023	-0.002	17.963	0.680	0.680	0.000	0.000	0.000	0.000
61	A	61	ALA	0	-0.047	-0.021	19.968	-0.665	-0.665	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.010	-0.009	22.229	0.481	0.481	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.003	-0.003	25.395	-0.117	-0.117	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.819	-0.876	28.146	-9.755	-9.755	0.000	0.000	0.000	0.000
65	A	65	PRO	0	-0.034	-0.027	30.173	0.213	0.213	0.000	0.000	0.000	0.000
66	A	66	SER	0	-0.090	-0.059	32.941	0.372	0.372	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.029	-0.008	30.811	0.250	0.250	0.000	0.000	0.000	0.000
68	A	68	VAL	0	-0.005	-0.003	34.877	0.040	0.040	0.000	0.000	0.000	0.000
69	A	69	CYS	0	-0.018	0.008	32.270	-0.344	-0.344	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.002	0.013	37.484	0.140	0.140	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.006	-0.018	36.150	-0.218	-0.218	0.000	0.000	0.000	0.000
72	A	72	TYR	0	-0.003	0.008	39.291	0.105	0.105	0.000	0.000	0.000	0.000
73	A	73	PHE	0	-0.014	-0.016	34.998	-0.229	-0.229	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.927	-0.965	37.797	-7.753	-7.753	0.000	0.000	0.000	0.000
75	A	75	PRO	0	-0.045	-0.003	33.994	-0.153	-0.153	0.000	0.000	0.000	0.000
76	A	76	VAL	0	0.023	0.012	30.555	0.070	0.070	0.000	0.000	0.000	0.000
77	A	77	THR	0	-0.015	-0.016	27.806	-0.270	-0.270	0.000	0.000	0.000	0.000
78	A	78	VAL	0	-0.006	0.006	23.693	0.146	0.146	0.000	0.000	0.000	0.000
79	A	79	THR	0	-0.005	0.002	23.463	0.051	0.051	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.020	0.025	18.451	-0.077	-0.077	0.000	0.000	0.000	0.000
81	A	81	ASP	-1	-0.856	-0.929	19.661	-13.847	-13.847	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.003	-0.023	18.302	0.291	0.291	0.000	0.000	0.000	0.000
83	A	83	VAL	0	-0.055	-0.020	13.288	0.070	0.070	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.064	0.031	9.695	0.553	0.553	0.000	0.000	0.000	0.000
85	A	85	ASN	0	-0.011	-0.028	6.667	0.042	0.042	0.000	0.000	0.000	0.000
86	A	86	GLY	0	-0.018	-0.006	8.322	-2.794	-2.794	0.000	0.000	0.000	0.000
87	A	87	ARG	1	0.851	0.934	6.720	34.316	34.316	0.000	0.000	0.000	0.000
88	A	88	ARG	1	0.881	0.926	11.743	16.237	16.237	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.002	-0.003	13.726	-0.528	-0.528	0.000	0.000	0.000	0.000
90	A	90	ALA	0	0.016	0.005	16.282	0.729	0.729	0.000	0.000	0.000	0.000
91	A	91	TRP	0	-0.027	-0.010	18.331	-0.093	-0.093	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.973	0.979	20.411	11.345	11.345	0.000	0.000	0.000	0.000
93	A	93	HIS	0	-0.001	0.014	23.096	-0.307	-0.307	0.000	0.000	0.000	0.000
94	A	94	THR	0	0.003	-0.002	25.036	0.118	0.118	0.000	0.000	0.000	0.000
95	A	95	PHE	0	-0.010	-0.009	24.729	-0.092	-0.092	0.000	0.000	0.000	0.000
96	A	96	SER	0	0.037	0.004	30.584	0.118	0.118	0.000	0.000	0.000	0.000
97	A	97	ASN	0	0.040	0.016	33.613	0.124	0.124	0.000	0.000	0.000	0.000
98	A	98	THR	0	0.060	0.011	32.588	-0.260	-0.260	0.000	0.000	0.000	0.000
99	A	100	VAL	0	0.011	0.001	30.752	-0.265	-0.265	0.000	0.000	0.000	0.000
100	A	101	MET	0	-0.004	0.008	26.805	-0.219	-0.219	0.000	0.000	0.000	0.000
101	A	102	SER	0	-0.029	-0.013	27.583	-0.521	-0.521	0.000	0.000	0.000	0.000
102	A	103	ALA	0	0.037	0.013	27.857	-0.314	-0.314	0.000	0.000	0.000	0.000
103	A	104	ASN	0	-0.054	-0.039	25.666	-0.403	-0.403	0.000	0.000	0.000	0.000
104	A	105	LEU	0	-0.002	0.010	22.306	-0.671	-0.671	0.000	0.000	0.000	0.000
105	A	106	ASN	0	-0.015	-0.004	22.722	-0.582	-0.582	0.000	0.000	0.000	0.000
106	A	107	SER	0	0.004	-0.007	23.768	0.695	0.695	0.000	0.000	0.000	0.000
107	A	108	ASN	0	-0.019	-0.003	17.773	-0.471	-0.471	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.039	0.009	19.252	0.318	0.318	0.000	0.000	0.000	0.000
109	A	110	VAL	0	-0.005	0.003	16.904	0.368	0.368	0.000	0.000	0.000	0.000
110	A	111	TYR	0	-0.028	-0.051	20.072	0.107	0.107	0.000	0.000	0.000	0.000
111	A	112	ALA	0	-0.018	0.013	23.546	0.534	0.534	0.000	0.000	0.000	0.000
112	A	113	PHE	-1	-0.855	-0.898	23.620	-10.486	-10.486	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-1:GLY)