FMO DATABASE

FMODB ID: YMQZ2

Calculation Name: 2OUW-A-Xray549

Preferred Name:

Target Type:

Ligand Name: acetic acid

Ligand 3-letter code: ACY

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2OUW

Chain ID: A

ChEMBL ID:

UniProt ID: Q2RXN9

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	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-998301.809523
FMO2-HF: Nuclear repulsion	946676.207462
FMO2-HF: Total energy	-51625.60206
FMO2-MP2: Total energy	-51773.091949

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:0:GLY)

Summations of interaction energy for fragment #1(A:0: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.
-18.51	-16.782	0.007	-0.888	-0.849	-0.005

Interaction energy analysis for fragmet #1(A:0:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.862 / q_NPA : 0.918

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	0.045	0.032	3.799	7.948	9.286	-0.013	-0.624	-0.702	-0.003
4	A	3	THR	0	0.000	-0.011	3.511	-13.610	-13.220	0.020	-0.264	-0.147	-0.002
5	A	4	VAL	0	0.004	0.023	6.124	1.239	1.239	0.000	0.000	0.000	0.000
6	A	5	ARG	1	0.830	0.892	4.805	23.801	23.801	0.000	0.000	0.000	0.000
7	A	6	LEU	0	-0.034	-0.018	5.808	4.261	4.261	0.000	0.000	0.000	0.000
8	A	7	LEU	0	-0.007	0.009	7.802	-0.370	-0.370	0.000	0.000	0.000	0.000
9	A	8	ASP	-1	-0.802	-0.892	10.951	-20.594	-20.594	0.000	0.000	0.000	0.000
10	A	9	ASP	-1	-0.750	-0.887	12.984	-16.527	-16.527	0.000	0.000	0.000	0.000
11	A	10	ALA	0	-0.024	0.016	16.074	1.188	1.188	0.000	0.000	0.000	0.000
12	A	11	GLU	-1	-0.754	-0.872	11.241	-25.205	-25.205	0.000	0.000	0.000	0.000
13	A	12	ILE	0	0.003	0.010	14.424	1.045	1.045	0.000	0.000	0.000	0.000
14	A	13	SER	0	-0.069	-0.052	17.593	1.072	1.072	0.000	0.000	0.000	0.000
15	A	14	THR	0	-0.083	-0.043	18.816	0.681	0.681	0.000	0.000	0.000	0.000
16	A	15	LEU	0	0.001	0.009	15.955	0.185	0.185	0.000	0.000	0.000	0.000
17	A	16	PRO	0	0.014	0.000	20.449	-0.067	-0.067	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.901	-0.950	21.968	-12.925	-12.925	0.000	0.000	0.000	0.000
19	A	18	VAL	0	0.001	-0.003	16.458	0.062	0.062	0.000	0.000	0.000	0.000
20	A	19	LYS	1	0.830	0.898	19.862	12.922	12.922	0.000	0.000	0.000	0.000
21	A	20	ALA	0	0.031	0.021	21.724	0.214	0.214	0.000	0.000	0.000	0.000
22	A	21	VAL	0	-0.009	-0.006	20.571	0.275	0.275	0.000	0.000	0.000	0.000
23	A	22	PHE	0	0.002	-0.021	14.908	-0.175	-0.175	0.000	0.000	0.000	0.000
24	A	23	ASP	-1	-0.808	-0.884	20.978	-12.518	-12.518	0.000	0.000	0.000	0.000
25	A	24	ASP	-1	-0.777	-0.859	24.510	-10.830	-10.830	0.000	0.000	0.000	0.000
26	A	25	ILE	0	-0.045	-0.018	19.676	0.187	0.187	0.000	0.000	0.000	0.000
27	A	26	ARG	1	0.791	0.878	18.868	14.927	14.927	0.000	0.000	0.000	0.000
28	A	27	ALA	0	-0.026	-0.016	24.686	0.316	0.316	0.000	0.000	0.000	0.000
29	A	28	THR	0	-0.044	-0.030	26.714	0.419	0.419	0.000	0.000	0.000	0.000
30	A	29	ARG	1	0.846	0.914	19.873	14.083	14.083	0.000	0.000	0.000	0.000
31	A	30	GLY	0	0.012	0.031	26.925	0.072	0.072	0.000	0.000	0.000	0.000
32	A	31	SER	0	-0.030	-0.024	24.621	-0.034	-0.034	0.000	0.000	0.000	0.000
33	A	32	ASP	-1	-0.825	-0.903	21.416	-14.392	-14.392	0.000	0.000	0.000	0.000
34	A	33	PHE	0	-0.013	-0.009	16.477	-0.877	-0.877	0.000	0.000	0.000	0.000
35	A	34	VAL	0	0.026	0.028	16.720	0.129	0.129	0.000	0.000	0.000	0.000
36	A	35	ASN	0	-0.002	-0.006	15.527	-0.377	-0.377	0.000	0.000	0.000	0.000
37	A	36	ASN	0	0.042	-0.012	9.887	1.158	1.158	0.000	0.000	0.000	0.000
38	A	37	ILE	0	0.001	0.019	11.501	-1.328	-1.328	0.000	0.000	0.000	0.000
39	A	38	TRP	0	0.036	0.011	13.447	-0.445	-0.445	0.000	0.000	0.000	0.000
40	A	39	ARG	1	0.830	0.905	10.938	20.075	20.075	0.000	0.000	0.000	0.000
41	A	40	GLY	0	0.018	0.014	9.557	-1.632	-1.632	0.000	0.000	0.000	0.000
42	A	41	LEU	0	-0.005	-0.008	10.414	0.006	0.006	0.000	0.000	0.000	0.000
43	A	42	ALA	0	-0.017	-0.005	13.187	0.708	0.708	0.000	0.000	0.000	0.000
44	A	43	ASN	0	-0.078	-0.053	9.329	-0.288	-0.288	0.000	0.000	0.000	0.000
45	A	44	ASP	-1	-0.820	-0.911	13.282	-15.362	-15.362	0.000	0.000	0.000	0.000
46	A	45	PRO	0	0.034	0.011	16.693	0.328	0.328	0.000	0.000	0.000	0.000
47	A	46	ALA	0	0.060	0.040	19.071	0.629	0.629	0.000	0.000	0.000	0.000
48	A	47	LEU	0	-0.042	-0.021	16.387	0.627	0.627	0.000	0.000	0.000	0.000
49	A	48	LEU	0	-0.016	0.012	16.938	0.321	0.321	0.000	0.000	0.000	0.000
50	A	49	LYS	1	0.912	0.947	18.956	11.982	11.982	0.000	0.000	0.000	0.000
51	A	50	ARG	1	0.907	0.963	21.152	14.231	14.231	0.000	0.000	0.000	0.000
52	A	51	THR	0	-0.010	-0.021	19.165	0.352	0.352	0.000	0.000	0.000	0.000
53	A	52	TRP	0	-0.029	-0.040	21.490	0.044	0.044	0.000	0.000	0.000	0.000
54	A	53	GLU	-1	-0.817	-0.889	23.036	-10.530	-10.530	0.000	0.000	0.000	0.000
55	A	54	GLN	0	-0.002	0.007	25.150	0.168	0.168	0.000	0.000	0.000	0.000
56	A	55	VAL	0	-0.025	-0.014	22.355	0.247	0.247	0.000	0.000	0.000	0.000
57	A	56	LYS	1	0.796	0.884	25.622	11.236	11.236	0.000	0.000	0.000	0.000
58	A	57	THR	0	-0.015	-0.021	28.256	0.371	0.371	0.000	0.000	0.000	0.000
59	A	58	VAL	0	-0.015	0.006	28.718	0.283	0.283	0.000	0.000	0.000	0.000
60	A	59	MET	0	-0.060	-0.023	26.072	0.284	0.284	0.000	0.000	0.000	0.000
61	A	60	VAL	0	-0.055	-0.023	28.247	0.035	0.035	0.000	0.000	0.000	0.000
62	A	61	GLY	0	0.025	0.021	30.995	0.154	0.154	0.000	0.000	0.000	0.000
63	A	62	GLU	-1	-0.879	-0.938	34.715	-7.924	-7.924	0.000	0.000	0.000	0.000
64	A	63	GLY	0	-0.020	-0.016	37.442	-0.109	-0.109	0.000	0.000	0.000	0.000
65	A	64	ALA	0	-0.008	0.004	37.910	0.129	0.129	0.000	0.000	0.000	0.000
66	A	65	LEU	0	0.014	0.004	34.917	-0.259	-0.259	0.000	0.000	0.000	0.000
67	A	66	ASP	-1	-0.756	-0.843	35.994	-8.720	-8.720	0.000	0.000	0.000	0.000
68	A	67	PRO	0	0.057	-0.004	31.826	-0.221	-0.221	0.000	0.000	0.000	0.000
69	A	68	LEU	0	-0.012	0.006	31.061	-0.432	-0.432	0.000	0.000	0.000	0.000
70	A	69	THR	0	-0.008	-0.028	31.729	-0.247	-0.247	0.000	0.000	0.000	0.000
71	A	70	ARG	1	0.784	0.885	30.733	8.987	8.987	0.000	0.000	0.000	0.000
72	A	71	GLU	-1	-0.804	-0.868	25.125	-12.561	-12.561	0.000	0.000	0.000	0.000
73	A	72	MET	0	0.000	-0.011	27.690	-0.382	-0.382	0.000	0.000	0.000	0.000
74	A	73	ILE	0	0.031	0.028	29.631	-0.168	-0.168	0.000	0.000	0.000	0.000
75	A	74	TYR	0	0.008	-0.003	22.134	-0.547	-0.547	0.000	0.000	0.000	0.000
76	A	75	LEU	0	-0.023	0.003	24.334	-0.598	-0.598	0.000	0.000	0.000	0.000
77	A	76	ALA	0	0.050	0.032	25.751	-0.326	-0.326	0.000	0.000	0.000	0.000
78	A	77	VAL	0	0.013	0.008	25.004	-0.189	-0.189	0.000	0.000	0.000	0.000
79	A	78	SER	0	-0.078	-0.067	21.736	-0.645	-0.645	0.000	0.000	0.000	0.000
80	A	79	THR	0	-0.063	-0.039	22.259	-0.705	-0.705	0.000	0.000	0.000	0.000
81	A	80	ALA	0	0.011	0.013	24.563	-0.158	-0.158	0.000	0.000	0.000	0.000
82	A	81	ASN	0	-0.029	-0.013	21.984	0.244	0.244	0.000	0.000	0.000	0.000
83	A	82	SER	0	0.002	0.005	20.628	-0.584	-0.584	0.000	0.000	0.000	0.000
84	A	83	CYS	0	-0.023	0.020	15.709	-0.993	-0.993	0.000	0.000	0.000	0.000
85	A	84	SER	0	0.041	0.014	15.853	0.352	0.352	0.000	0.000	0.000	0.000
86	A	85	TYR	0	0.061	0.024	13.246	0.550	0.550	0.000	0.000	0.000	0.000
87	A	87	ALA	0	0.079	0.041	18.775	0.696	0.696	0.000	0.000	0.000	0.000
88	A	88	HIS	0	0.005	0.012	17.517	0.942	0.942	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.049	-0.048	17.570	0.776	0.776	0.000	0.000	0.000	0.000
90	A	90	HIS	1	0.870	0.918	19.604	14.398	14.398	0.000	0.000	0.000	0.000
91	A	91	THR	0	0.016	0.009	22.884	0.802	0.802	0.000	0.000	0.000	0.000
92	A	92	ALA	0	-0.048	-0.026	21.637	0.481	0.481	0.000	0.000	0.000	0.000
93	A	93	ALA	0	-0.004	0.000	23.279	0.444	0.444	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.052	0.018	24.902	0.456	0.456	0.000	0.000	0.000	0.000
95	A	95	ARG	1	0.880	0.938	25.725	11.970	11.970	0.000	0.000	0.000	0.000
96	A	96	ALA	0	-0.022	-0.005	26.342	0.334	0.334	0.000	0.000	0.000	0.000
97	A	97	LYS	1	0.814	0.903	27.518	11.285	11.285	0.000	0.000	0.000	0.000
98	A	98	GLY	0	0.042	0.024	30.941	0.311	0.311	0.000	0.000	0.000	0.000
99	A	99	MET	0	-0.086	-0.026	28.177	0.239	0.239	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.009	-0.019	32.126	-0.146	-0.146	0.000	0.000	0.000	0.000
101	A	101	PRO	0	0.008	-0.021	33.296	-0.123	-0.123	0.000	0.000	0.000	0.000
102	A	102	ALA	0	0.028	0.024	34.353	-0.072	-0.072	0.000	0.000	0.000	0.000
103	A	103	GLN	0	0.092	0.065	34.646	-0.083	-0.083	0.000	0.000	0.000	0.000
104	A	104	HIS	0	0.026	0.010	27.303	0.011	0.011	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.006	-0.004	32.056	-0.191	-0.191	0.000	0.000	0.000	0.000
106	A	106	GLU	-1	-0.866	-0.932	34.315	-8.262	-8.262	0.000	0.000	0.000	0.000
107	A	107	VAL	0	-0.002	-0.009	30.195	-0.053	-0.053	0.000	0.000	0.000	0.000
108	A	108	LEU	0	-0.044	-0.027	28.046	-0.188	-0.188	0.000	0.000	0.000	0.000
109	A	109	ALA	0	0.015	0.018	31.854	-0.055	-0.055	0.000	0.000	0.000	0.000
110	A	110	ILE	0	0.003	0.003	34.665	0.042	0.042	0.000	0.000	0.000	0.000
111	A	111	ILE	0	-0.033	-0.016	28.337	-0.038	-0.038	0.000	0.000	0.000	0.000
112	A	112	GLY	0	0.000	0.003	32.196	-0.077	-0.077	0.000	0.000	0.000	0.000
113	A	113	LEU	0	0.024	0.011	33.592	0.068	0.068	0.000	0.000	0.000	0.000
114	A	114	ALA	0	0.023	0.025	33.748	0.152	0.152	0.000	0.000	0.000	0.000
115	A	115	ALA	0	-0.028	-0.012	31.402	0.014	0.014	0.000	0.000	0.000	0.000
116	A	116	GLN	0	-0.020	-0.012	33.277	0.212	0.212	0.000	0.000	0.000	0.000
117	A	117	THR	0	-0.009	-0.028	36.436	0.122	0.122	0.000	0.000	0.000	0.000
118	A	118	ASN	0	0.045	0.024	33.589	0.337	0.337	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.011	0.014	34.488	0.045	0.045	0.000	0.000	0.000	0.000
120	A	120	LEU	0	-0.007	-0.006	36.202	0.122	0.122	0.000	0.000	0.000	0.000
121	A	121	VAL	0	0.020	0.008	39.532	0.159	0.159	0.000	0.000	0.000	0.000
122	A	122	THR	0	-0.035	-0.028	35.431	0.061	0.061	0.000	0.000	0.000	0.000
123	A	123	ALA	0	-0.048	-0.025	38.599	0.072	0.072	0.000	0.000	0.000	0.000
124	A	124	MET	0	-0.060	-0.034	40.172	0.200	0.200	0.000	0.000	0.000	0.000
125	A	125	GLN	0	-0.086	-0.039	39.240	0.220	0.220	0.000	0.000	0.000	0.000
126	A	126	ILE	0	-0.006	0.005	43.076	0.155	0.155	0.000	0.000	0.000	0.000
127	A	127	PRO	0	-0.020	0.000	44.170	-0.131	-0.131	0.000	0.000	0.000	0.000
128	A	128	VAL	0	-0.010	-0.016	43.822	0.015	0.015	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.879	-0.940	46.469	-6.490	-6.490	0.000	0.000	0.000	0.000
130	A	130	GLU	-1	-0.889	-0.957	49.622	-6.116	-6.116	0.000	0.000	0.000	0.000
131	A	131	ALA	0	-0.046	-0.025	51.715	0.024	0.024	0.000	0.000	0.000	0.000
132	A	132	PHE	0	-0.101	-0.053	46.627	-0.013	-0.013	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.072	-0.034	46.816	-0.169	-0.169	0.000	0.000	0.000	0.000
134	A	134	VAL	-1	-0.976	-0.959	49.807	-6.141	-6.141	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Data Search

Manual

Support

Interactive mode: IFIE and PIEDA for fragment #1(A:0:GLY)