FMO DATABASE

FMODB ID: G8ML1

Calculation Name: 2HQ9-A-Xray547

Preferred Name:

Target Type:

Ligand Name: flavin-adenine dinucleotide | 1,2-ethanediol | chloride ion

Ligand 3-letter code: FAD | EDO | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2HQ9

Chain ID: A

ChEMBL ID:

UniProt ID: Q988L5

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	135
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1208600.341255
FMO2-HF: Nuclear repulsion	1154473.846039
FMO2-HF: Total energy	-54126.495216
FMO2-MP2: Total energy	-54284.340121

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.
-24.639	-23.803	-0.008	-0.267	-0.561	-0.001

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 : 0.826 / q_NPA : 0.897

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	LEU	0	0.071	0.045	3.817	2.469	3.305	-0.008	-0.267	-0.561	-0.001
4	A	3	VAL	0	-0.035	-0.022	6.326	4.329	4.329	0.000	0.000	0.000	0.000
5	A	4	ARG	1	0.796	0.881	8.809	20.737	20.737	0.000	0.000	0.000	0.000
6	A	5	THR	0	-0.041	-0.029	12.561	-0.316	-0.316	0.000	0.000	0.000	0.000
7	A	6	LEU	0	-0.038	0.002	15.783	0.149	0.149	0.000	0.000	0.000	0.000
8	A	7	SER	0	0.006	-0.033	18.446	0.786	0.786	0.000	0.000	0.000	0.000
9	A	8	ALA	0	0.091	0.029	22.153	-0.129	-0.129	0.000	0.000	0.000	0.000
10	A	9	LEU	0	0.025	0.023	24.789	0.111	0.111	0.000	0.000	0.000	0.000
11	A	10	GLU	-1	-0.776	-0.846	19.951	-15.943	-15.943	0.000	0.000	0.000	0.000
12	A	11	CYS	0	-0.010	0.004	21.461	-0.316	-0.316	0.000	0.000	0.000	0.000
13	A	12	THR	0	0.005	-0.005	22.850	0.251	0.251	0.000	0.000	0.000	0.000
14	A	13	LYS	1	0.945	0.984	24.026	13.395	13.395	0.000	0.000	0.000	0.000
15	A	14	VAL	0	0.031	0.028	19.654	0.255	0.255	0.000	0.000	0.000	0.000
16	A	15	LEU	0	-0.018	-0.005	22.937	0.222	0.222	0.000	0.000	0.000	0.000
17	A	16	THR	0	0.007	-0.015	25.719	0.535	0.535	0.000	0.000	0.000	0.000
18	A	17	ALA	0	-0.034	0.007	24.094	0.429	0.429	0.000	0.000	0.000	0.000
19	A	18	ASN	0	-0.062	-0.030	22.057	0.104	0.104	0.000	0.000	0.000	0.000
20	A	19	ARG	1	0.867	0.910	25.623	11.081	11.081	0.000	0.000	0.000	0.000
21	A	20	VAL	0	0.012	0.014	24.814	0.387	0.387	0.000	0.000	0.000	0.000
22	A	21	GLY	0	0.049	0.025	24.055	-0.516	-0.516	0.000	0.000	0.000	0.000
23	A	22	ARG	1	0.879	0.940	21.729	14.209	14.209	0.000	0.000	0.000	0.000
24	A	23	LEU	0	0.031	0.021	24.914	-0.174	-0.174	0.000	0.000	0.000	0.000
25	A	24	ALA	0	-0.003	-0.008	25.596	0.114	0.114	0.000	0.000	0.000	0.000
26	A	25	CYS	0	0.001	0.005	27.684	0.264	0.264	0.000	0.000	0.000	0.000
27	A	26	ALA	0	0.043	0.002	30.222	-0.255	-0.255	0.000	0.000	0.000	0.000
28	A	27	LYS	1	0.872	0.931	32.247	8.209	8.209	0.000	0.000	0.000	0.000
29	A	28	ASP	-1	-0.833	-0.903	34.993	-8.139	-8.139	0.000	0.000	0.000	0.000
30	A	29	GLY	0	0.007	0.014	32.477	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	30	GLN	0	-0.024	-0.007	29.624	-0.306	-0.306	0.000	0.000	0.000	0.000
32	A	31	PRO	0	0.027	-0.001	26.839	0.190	0.190	0.000	0.000	0.000	0.000
33	A	32	TYR	0	-0.012	-0.020	29.473	0.238	0.238	0.000	0.000	0.000	0.000
34	A	33	VAL	0	0.016	0.013	24.350	0.055	0.055	0.000	0.000	0.000	0.000
35	A	34	VAL	0	-0.008	0.001	27.710	0.113	0.113	0.000	0.000	0.000	0.000
36	A	35	PRO	0	-0.006	0.001	26.614	-0.259	-0.259	0.000	0.000	0.000	0.000
37	A	36	LEU	0	-0.021	-0.014	27.693	0.484	0.484	0.000	0.000	0.000	0.000
38	A	37	TYR	0	0.047	0.028	28.649	-0.366	-0.366	0.000	0.000	0.000	0.000
39	A	38	TYR	0	-0.070	-0.046	26.058	0.238	0.238	0.000	0.000	0.000	0.000
40	A	39	ALA	0	0.019	0.005	31.293	-0.133	-0.133	0.000	0.000	0.000	0.000
41	A	40	TYR	0	-0.053	-0.033	29.649	0.061	0.061	0.000	0.000	0.000	0.000
42	A	41	SER	0	-0.033	-0.021	31.780	0.141	0.141	0.000	0.000	0.000	0.000
43	A	42	ASP	-1	-0.845	-0.919	34.452	-8.597	-8.597	0.000	0.000	0.000	0.000
44	A	43	ALA	0	0.012	0.011	32.791	-0.353	-0.353	0.000	0.000	0.000	0.000
45	A	44	HIS	0	0.004	-0.005	33.400	-0.084	-0.084	0.000	0.000	0.000	0.000
46	A	45	LEU	0	0.005	0.008	27.799	-0.110	-0.110	0.000	0.000	0.000	0.000
47	A	46	TYR	0	-0.008	-0.001	32.257	0.321	0.321	0.000	0.000	0.000	0.000
48	A	47	ALA	0	0.033	0.008	33.419	-0.250	-0.250	0.000	0.000	0.000	0.000
49	A	48	PHE	0	-0.010	0.003	35.528	0.307	0.307	0.000	0.000	0.000	0.000
50	A	49	SER	0	-0.047	-0.050	36.523	-0.366	-0.366	0.000	0.000	0.000	0.000
51	A	50	MET	0	0.065	0.058	38.605	0.309	0.309	0.000	0.000	0.000	0.000
52	A	51	PRO	0	-0.025	-0.004	40.211	-0.163	-0.163	0.000	0.000	0.000	0.000
53	A	52	GLY	0	0.076	0.048	40.566	-0.018	-0.018	0.000	0.000	0.000	0.000
54	A	53	LYS	1	0.938	0.987	33.814	8.933	8.933	0.000	0.000	0.000	0.000
55	A	54	LYS	1	0.963	0.977	33.223	8.987	8.987	0.000	0.000	0.000	0.000
56	A	55	ILE	0	0.007	0.013	35.831	-0.082	-0.082	0.000	0.000	0.000	0.000
57	A	56	GLU	-1	-0.931	-0.971	38.695	-7.396	-7.396	0.000	0.000	0.000	0.000
58	A	57	TRP	0	-0.011	-0.033	32.999	0.001	0.001	0.000	0.000	0.000	0.000
59	A	58	MET	0	-0.032	0.010	34.247	-0.111	-0.111	0.000	0.000	0.000	0.000
60	A	59	ARG	1	0.802	0.861	36.971	7.334	7.334	0.000	0.000	0.000	0.000
61	A	60	ALA	0	-0.029	0.002	39.662	0.126	0.126	0.000	0.000	0.000	0.000
62	A	61	ASN	0	-0.027	-0.030	33.839	0.127	0.127	0.000	0.000	0.000	0.000
63	A	62	PRO	0	0.016	0.024	35.779	-0.232	-0.232	0.000	0.000	0.000	0.000
64	A	63	ARG	1	0.883	0.947	32.138	8.602	8.602	0.000	0.000	0.000	0.000
65	A	64	VAL	0	-0.021	-0.018	30.039	-0.019	-0.019	0.000	0.000	0.000	0.000
66	A	65	SER	0	0.013	0.016	24.441	-0.262	-0.262	0.000	0.000	0.000	0.000
67	A	66	VAL	0	-0.027	-0.023	25.590	0.224	0.224	0.000	0.000	0.000	0.000
68	A	67	GLN	0	-0.058	-0.030	17.713	0.454	0.454	0.000	0.000	0.000	0.000
69	A	68	VAL	0	0.035	0.010	20.794	0.533	0.533	0.000	0.000	0.000	0.000
70	A	69	ASP	-1	-0.929	-0.936	16.577	-17.703	-17.703	0.000	0.000	0.000	0.000
71	A	70	GLU	-1	-0.732	-0.840	17.328	-14.756	-14.756	0.000	0.000	0.000	0.000
72	A	71	HIS	0	0.042	0.017	14.749	-0.692	-0.692	0.000	0.000	0.000	0.000
73	A	72	GLY	0	-0.002	0.002	14.337	1.010	1.010	0.000	0.000	0.000	0.000
74	A	73	GLN	0	0.012	0.002	13.890	0.219	0.219	0.000	0.000	0.000	0.000
75	A	74	GLY	0	0.027	0.025	11.491	-1.950	-1.950	0.000	0.000	0.000	0.000
76	A	75	ARG	1	0.874	0.925	7.742	28.532	28.532	0.000	0.000	0.000	0.000
77	A	76	GLY	0	0.040	0.027	9.599	-1.709	-1.709	0.000	0.000	0.000	0.000
78	A	77	TRP	0	-0.073	-0.034	8.801	3.075	3.075	0.000	0.000	0.000	0.000
79	A	78	LYS	1	0.804	0.876	12.882	17.413	17.413	0.000	0.000	0.000	0.000
80	A	79	SER	0	-0.044	-0.036	15.317	0.494	0.494	0.000	0.000	0.000	0.000
81	A	80	VAL	0	0.000	-0.005	16.864	-0.164	-0.164	0.000	0.000	0.000	0.000
82	A	81	VAL	0	0.010	0.000	18.817	0.015	0.015	0.000	0.000	0.000	0.000
83	A	82	VAL	0	-0.004	0.002	21.501	0.128	0.128	0.000	0.000	0.000	0.000
84	A	83	ASP	-1	-0.869	-0.923	25.149	-12.327	-12.327	0.000	0.000	0.000	0.000
85	A	84	GLY	0	0.032	-0.016	27.227	0.176	0.176	0.000	0.000	0.000	0.000
86	A	85	ARG	1	0.832	0.912	30.766	8.691	8.691	0.000	0.000	0.000	0.000
87	A	86	TYR	0	-0.045	-0.057	34.388	-0.001	-0.001	0.000	0.000	0.000	0.000
88	A	87	GLU	-1	-0.824	-0.892	36.222	-7.471	-7.471	0.000	0.000	0.000	0.000
89	A	88	GLU	-1	-0.753	-0.820	39.389	-7.496	-7.496	0.000	0.000	0.000	0.000
90	A	89	LEU	0	-0.058	-0.031	39.803	0.159	0.159	0.000	0.000	0.000	0.000
91	A	90	PRO	0	0.014	0.005	43.557	0.050	0.050	0.000	0.000	0.000	0.000
92	A	91	ASP	-1	-0.864	-0.922	47.193	-6.685	-6.685	0.000	0.000	0.000	0.000
93	A	92	LEU	0	0.002	0.004	48.518	0.161	0.161	0.000	0.000	0.000	0.000
94	A	93	ILE	0	0.053	0.013	48.840	-0.146	-0.146	0.000	0.000	0.000	0.000
95	A	94	GLY	0	0.008	-0.001	48.520	-0.081	-0.081	0.000	0.000	0.000	0.000
96	A	95	HIS	1	0.851	0.916	43.641	7.075	7.075	0.000	0.000	0.000	0.000
97	A	96	LYS	1	0.978	1.010	44.662	6.244	6.244	0.000	0.000	0.000	0.000
98	A	97	LEU	0	0.043	0.025	44.036	-0.091	-0.091	0.000	0.000	0.000	0.000
99	A	98	GLN	0	0.046	0.026	40.767	-0.111	-0.111	0.000	0.000	0.000	0.000
100	A	99	ARG	1	0.889	0.943	40.709	6.852	6.852	0.000	0.000	0.000	0.000
101	A	100	ASP	-1	-0.841	-0.944	42.156	-6.964	-6.964	0.000	0.000	0.000	0.000
102	A	101	HIS	0	-0.006	0.007	36.331	0.065	0.065	0.000	0.000	0.000	0.000
103	A	102	ALA	0	0.032	0.018	37.549	-0.173	-0.173	0.000	0.000	0.000	0.000
104	A	103	TRP	0	0.023	0.005	37.936	-0.222	-0.222	0.000	0.000	0.000	0.000
105	A	104	SER	0	-0.059	-0.039	39.997	-0.070	-0.070	0.000	0.000	0.000	0.000
106	A	105	VAL	0	-0.027	-0.010	33.884	-0.141	-0.141	0.000	0.000	0.000	0.000
107	A	106	LEU	0	-0.020	-0.029	32.950	-0.208	-0.208	0.000	0.000	0.000	0.000
108	A	107	SER	0	-0.013	0.014	36.456	-0.070	-0.070	0.000	0.000	0.000	0.000
109	A	108	LYS	1	0.904	0.941	34.159	9.228	9.228	0.000	0.000	0.000	0.000
110	A	109	HIS	0	0.005	0.008	31.135	-0.036	-0.036	0.000	0.000	0.000	0.000
111	A	110	THR	0	-0.036	-0.029	35.140	-0.127	-0.127	0.000	0.000	0.000	0.000
112	A	111	ASP	-1	-0.906	-0.952	37.651	-7.977	-7.977	0.000	0.000	0.000	0.000
113	A	112	TRP	0	-0.075	-0.036	31.869	-0.255	-0.255	0.000	0.000	0.000	0.000
114	A	113	TRP	0	-0.134	-0.064	34.134	-0.225	-0.225	0.000	0.000	0.000	0.000
115	A	114	GLU	-2	-1.853	-1.908	36.163	-15.376	-15.376	0.000	0.000	0.000	0.000
116	A	129	ALA	1	0.863	0.925	46.846	6.716	6.716	0.000	0.000	0.000	0.000
117	A	130	PRO	0	0.084	0.043	46.863	-0.011	-0.011	0.000	0.000	0.000	0.000
118	A	131	HIS	0	0.082	0.039	41.740	0.006	0.006	0.000	0.000	0.000	0.000
119	A	132	VAL	0	-0.049	-0.024	40.858	0.142	0.142	0.000	0.000	0.000	0.000
120	A	133	PHE	0	0.006	0.003	38.963	-0.170	-0.170	0.000	0.000	0.000	0.000
121	A	134	PHE	0	-0.006	-0.013	33.839	0.107	0.107	0.000	0.000	0.000	0.000
122	A	135	ARG	1	0.840	0.902	35.780	7.939	7.939	0.000	0.000	0.000	0.000
123	A	136	ILE	0	-0.048	-0.010	30.562	0.121	0.121	0.000	0.000	0.000	0.000
124	A	137	LEU	0	0.029	0.024	32.965	-0.111	-0.111	0.000	0.000	0.000	0.000
125	A	138	ILE	0	-0.018	-0.018	28.319	-0.232	-0.232	0.000	0.000	0.000	0.000
126	A	139	GLU	-1	-0.874	-0.921	30.561	-8.914	-8.914	0.000	0.000	0.000	0.000
127	A	140	GLN	0	-0.045	-0.030	26.242	-0.253	-0.253	0.000	0.000	0.000	0.000
128	A	141	VAL	0	-0.013	-0.012	23.646	-0.048	-0.048	0.000	0.000	0.000	0.000
129	A	142	SER	0	-0.022	0.008	20.088	-0.313	-0.313	0.000	0.000	0.000	0.000
130	A	143	GLY	0	0.111	0.027	18.132	0.252	0.252	0.000	0.000	0.000	0.000
131	A	144	ARG	1	0.846	0.926	12.444	21.033	21.033	0.000	0.000	0.000	0.000
132	A	145	GLU	-1	-0.798	-0.896	12.622	-20.001	-20.001	0.000	0.000	0.000	0.000
133	A	146	ALA	0	-0.043	-0.010	7.774	-1.718	-1.718	0.000	0.000	0.000	0.000
134	A	147	SER	0	0.006	0.002	8.621	4.077	4.077	0.000	0.000	0.000	0.000
135	A	148	GLU	-2	-1.765	-1.882	5.634	-90.531	-90.531	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)