FMO DATABASE

FMODB ID: NZRVQ

Calculation Name: 2HQ7-A-Xray547

Preferred Name:

Target Type:

Ligand Name: 1,2-ethanediol | chloride ion

Ligand 3-letter code: EDO | CL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2HQ7

Chain ID: A

ChEMBL ID:

UniProt ID: Q97DI6

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	141
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1344463.586925
FMO2-HF: Nuclear repulsion	1285864.713566
FMO2-HF: Total energy	-58598.873359
FMO2-MP2: Total energy	-58765.699554

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:ILE)

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

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.
-120.55	-115.853	10.593	-4.023	-11.268	-0.031

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.821 / q_NPA : 0.904

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	GLU	-1	-0.796	-0.903	2.944	-52.959	-50.270	0.256	-1.295	-1.651	-0.007
4	A	5	LYS	1	0.853	0.939	5.247	27.688	27.763	-0.001	-0.002	-0.072	0.000
5	A	6	PHE	0	-0.012	-0.036	2.164	2.565	1.059	5.899	-0.907	-3.487	-0.006
6	A	7	LEU	0	0.064	0.051	2.216	2.199	2.465	1.683	-0.435	-1.515	-0.004
134	A	135	ILE	0	-0.044	0.001	2.974	-0.460	0.055	0.163	-0.117	-0.560	0.000
136	A	137	PHE	0	0.012	-0.004	2.593	-6.506	-4.774	0.604	-0.544	-1.792	-0.003
137	A	138	LYS	1	0.978	1.000	4.024	31.702	31.822	0.000	-0.024	-0.095	0.000
141	A	142	ILE	-1	-0.968	-0.964	2.349	-50.266	-49.460	1.989	-0.699	-2.096	-0.011
7	A	8	ILE	0	0.007	0.013	5.693	3.310	3.310	0.000	0.000	0.000	0.000
8	A	9	GLU	-1	-0.785	-0.862	9.095	-19.835	-19.835	0.000	0.000	0.000	0.000
9	A	10	SER	0	-0.043	-0.035	7.519	1.534	1.534	0.000	0.000	0.000	0.000
10	A	11	ASN	0	-0.015	-0.019	8.529	2.277	2.277	0.000	0.000	0.000	0.000
11	A	12	GLU	-1	-0.879	-0.941	11.537	-17.941	-17.941	0.000	0.000	0.000	0.000
12	A	13	LEU	0	-0.047	-0.005	13.108	1.210	1.210	0.000	0.000	0.000	0.000
13	A	14	VAL	0	-0.014	-0.003	12.589	0.904	0.904	0.000	0.000	0.000	0.000
14	A	15	GLU	-1	-0.957	-0.981	14.797	-16.944	-16.944	0.000	0.000	0.000	0.000
15	A	16	SER	0	-0.062	-0.046	17.516	0.946	0.946	0.000	0.000	0.000	0.000
16	A	17	SER	0	-0.057	-0.018	18.060	0.777	0.777	0.000	0.000	0.000	0.000
17	A	18	LYS	0	0.044	0.018	20.069	-0.221	-0.221	0.000	0.000	0.000	0.000
18	A	19	ILE	0	-0.007	-0.001	23.241	0.048	0.048	0.000	0.000	0.000	0.000
19	A	20	VAL	0	-0.008	0.000	18.035	-0.511	-0.511	0.000	0.000	0.000	0.000
20	A	21	MET	0	-0.021	-0.007	20.069	0.786	0.786	0.000	0.000	0.000	0.000
21	A	22	VAL	0	0.029	0.004	19.859	-0.715	-0.715	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.003	0.002	20.548	0.628	0.628	0.000	0.000	0.000	0.000
23	A	24	THR	0	-0.026	-0.032	21.717	-0.105	-0.105	0.000	0.000	0.000	0.000
24	A	25	ASN	0	0.007	-0.015	22.483	0.270	0.270	0.000	0.000	0.000	0.000
25	A	26	GLY	0	0.026	0.019	26.034	0.237	0.237	0.000	0.000	0.000	0.000
26	A	27	GLU	-1	-0.796	-0.897	29.561	-9.030	-9.030	0.000	0.000	0.000	0.000
27	A	28	ASN	0	-0.060	-0.044	32.648	-0.012	-0.012	0.000	0.000	0.000	0.000
28	A	29	GLY	0	0.015	0.022	29.566	0.055	0.055	0.000	0.000	0.000	0.000
29	A	30	TYR	0	-0.007	0.009	28.454	-0.255	-0.255	0.000	0.000	0.000	0.000
30	A	31	PRO	0	0.015	0.006	24.132	-0.019	-0.019	0.000	0.000	0.000	0.000
31	A	32	ASN	0	-0.039	-0.019	26.066	0.605	0.605	0.000	0.000	0.000	0.000
32	A	33	ILE	0	0.025	0.015	22.821	-0.338	-0.338	0.000	0.000	0.000	0.000
33	A	34	LYS	1	0.844	0.910	25.071	10.064	10.064	0.000	0.000	0.000	0.000
34	A	35	ALA	0	0.045	0.032	24.753	-0.447	-0.447	0.000	0.000	0.000	0.000
35	A	36	MET	0	-0.085	-0.039	23.653	0.370	0.370	0.000	0.000	0.000	0.000
36	A	37	MET	0	0.065	0.053	24.017	-0.323	-0.323	0.000	0.000	0.000	0.000
37	A	38	ARG	1	0.831	0.898	18.610	14.166	14.166	0.000	0.000	0.000	0.000
38	A	39	LEU	0	-0.011	0.012	22.668	0.106	0.106	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.967	0.969	21.602	12.523	12.523	0.000	0.000	0.000	0.000
40	A	41	HIS	0	-0.002	0.002	15.236	0.687	0.687	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.942	-0.959	15.986	-17.280	-17.280	0.000	0.000	0.000	0.000
42	A	43	GLY	0	0.061	0.029	12.418	-0.858	-0.858	0.000	0.000	0.000	0.000
43	A	44	LEU	0	0.031	0.002	6.907	0.629	0.629	0.000	0.000	0.000	0.000
44	A	45	LYS	1	0.807	0.892	10.941	21.699	21.699	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.885	0.931	12.908	15.964	15.964	0.000	0.000	0.000	0.000
46	A	47	PHE	0	0.033	0.014	13.354	-0.006	-0.006	0.000	0.000	0.000	0.000
47	A	48	TRP	0	-0.010	-0.005	18.516	0.208	0.208	0.000	0.000	0.000	0.000
48	A	49	LEU	0	0.000	0.000	20.267	-0.065	-0.065	0.000	0.000	0.000	0.000
49	A	50	SER	0	0.050	0.033	24.068	0.432	0.432	0.000	0.000	0.000	0.000
50	A	51	THR	0	-0.013	-0.009	27.226	-0.102	-0.102	0.000	0.000	0.000	0.000
51	A	52	ASN	0	0.086	0.069	29.546	-0.088	-0.088	0.000	0.000	0.000	0.000
52	A	53	THR	0	-0.020	-0.023	32.831	-0.262	-0.262	0.000	0.000	0.000	0.000
53	A	54	SER	0	0.009	-0.002	33.496	0.199	0.199	0.000	0.000	0.000	0.000
54	A	55	THR	0	0.050	0.023	34.293	-0.245	-0.245	0.000	0.000	0.000	0.000
55	A	56	ARG	1	0.870	0.930	34.347	8.357	8.357	0.000	0.000	0.000	0.000
56	A	57	MET	0	0.042	0.027	28.352	-0.204	-0.204	0.000	0.000	0.000	0.000
57	A	58	VAL	0	0.033	0.014	30.790	-0.272	-0.272	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.869	-0.937	32.091	-8.473	-8.473	0.000	0.000	0.000	0.000
59	A	60	ARG	1	0.787	0.902	28.651	9.746	9.746	0.000	0.000	0.000	0.000
60	A	61	LEU	0	0.023	0.005	25.446	-0.189	-0.189	0.000	0.000	0.000	0.000
61	A	62	LYS	1	0.853	0.913	27.811	8.190	8.190	0.000	0.000	0.000	0.000
62	A	63	LYS	1	0.912	0.959	30.409	9.145	9.145	0.000	0.000	0.000	0.000
63	A	64	ASN	0	-0.064	-0.045	24.543	-0.387	-0.387	0.000	0.000	0.000	0.000
64	A	65	ASN	0	0.031	0.030	23.234	-0.076	-0.076	0.000	0.000	0.000	0.000
65	A	66	LYS	1	0.962	0.987	20.014	13.131	13.131	0.000	0.000	0.000	0.000
66	A	67	ILE	0	-0.043	-0.020	19.210	0.616	0.616	0.000	0.000	0.000	0.000
67	A	68	CYS	0	-0.044	-0.021	16.292	-0.562	-0.562	0.000	0.000	0.000	0.000
68	A	69	LEU	0	0.037	0.035	15.790	0.953	0.953	0.000	0.000	0.000	0.000
69	A	70	TYR	0	-0.023	-0.022	15.196	-0.996	-0.996	0.000	0.000	0.000	0.000
70	A	71	PHE	0	0.037	0.011	13.942	0.816	0.816	0.000	0.000	0.000	0.000
71	A	72	VAL	0	0.039	0.004	15.805	-0.775	-0.775	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.781	-0.875	16.194	-16.022	-16.022	0.000	0.000	0.000	0.000
73	A	74	ASP	-1	-0.895	-0.943	18.205	-12.152	-12.152	0.000	0.000	0.000	0.000
74	A	75	ASN	0	-0.083	-0.035	20.034	0.966	0.966	0.000	0.000	0.000	0.000
75	A	76	LYS	1	0.782	0.870	14.468	17.622	17.622	0.000	0.000	0.000	0.000
76	A	77	PHE	0	-0.009	0.001	18.088	-0.254	-0.254	0.000	0.000	0.000	0.000
77	A	78	ALA	0	-0.042	-0.037	13.721	-0.696	-0.696	0.000	0.000	0.000	0.000
78	A	79	GLY	0	0.067	0.039	13.568	1.076	1.076	0.000	0.000	0.000	0.000
79	A	80	LEU	0	-0.046	-0.002	8.674	-1.520	-1.520	0.000	0.000	0.000	0.000
80	A	81	MET	0	-0.037	-0.009	11.293	1.576	1.576	0.000	0.000	0.000	0.000
81	A	82	LEU	0	0.018	0.015	9.723	-2.084	-2.084	0.000	0.000	0.000	0.000
82	A	83	VAL	0	0.000	-0.017	12.304	1.642	1.642	0.000	0.000	0.000	0.000
83	A	84	GLY	0	0.035	0.025	13.346	-1.309	-1.309	0.000	0.000	0.000	0.000
84	A	85	THR	0	-0.030	-0.009	16.014	0.973	0.973	0.000	0.000	0.000	0.000
85	A	86	ILE	0	-0.042	-0.012	19.606	-0.331	-0.331	0.000	0.000	0.000	0.000
86	A	87	GLU	-1	-0.933	-0.957	22.355	-11.834	-11.834	0.000	0.000	0.000	0.000
87	A	88	ILE	0	-0.018	-0.025	25.522	-0.100	-0.100	0.000	0.000	0.000	0.000
88	A	89	LEU	0	-0.018	-0.002	25.749	0.149	0.149	0.000	0.000	0.000	0.000
89	A	90	HIS	0	0.022	-0.008	29.785	0.298	0.298	0.000	0.000	0.000	0.000
90	A	91	ASP	-1	-0.870	-0.899	31.862	-9.280	-9.280	0.000	0.000	0.000	0.000
91	A	92	ARG	1	0.794	0.840	33.694	7.706	7.706	0.000	0.000	0.000	0.000
92	A	93	ALA	0	0.039	0.025	33.977	-0.052	-0.052	0.000	0.000	0.000	0.000
93	A	94	SER	0	-0.012	-0.036	29.079	-0.278	-0.278	0.000	0.000	0.000	0.000
94	A	95	LYS	1	0.860	0.946	30.072	8.392	8.392	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.867	-0.915	32.151	-8.237	-8.237	0.000	0.000	0.000	0.000
96	A	97	MET	0	-0.064	-0.041	29.152	-0.127	-0.127	0.000	0.000	0.000	0.000
97	A	98	LEU	0	-0.068	-0.030	25.197	-0.400	-0.400	0.000	0.000	0.000	0.000
98	A	99	TRP	0	0.021	0.027	28.501	-0.120	-0.120	0.000	0.000	0.000	0.000
99	A	100	THR	0	-0.030	-0.017	26.720	-0.154	-0.154	0.000	0.000	0.000	0.000
100	A	101	ASP	-1	-0.899	-0.952	30.170	-8.688	-8.688	0.000	0.000	0.000	0.000
101	A	102	GLY	0	-0.004	-0.012	31.055	-0.325	-0.325	0.000	0.000	0.000	0.000
102	A	103	CYS	0	-0.066	-0.027	30.501	-0.049	-0.049	0.000	0.000	0.000	0.000
103	A	104	GLU	-1	-0.840	-0.922	32.841	-8.439	-8.439	0.000	0.000	0.000	0.000
104	A	105	ILE	0	-0.090	-0.034	34.306	0.267	0.267	0.000	0.000	0.000	0.000
105	A	106	TYR	-1	-0.925	-0.962	30.408	-9.463	-9.463	0.000	0.000	0.000	0.000
106	A	107	TYR	0	-0.055	-0.036	30.336	0.143	0.143	0.000	0.000	0.000	0.000
107	A	108	PRO	0	0.043	0.022	36.813	0.029	0.029	0.000	0.000	0.000	0.000
108	A	109	LEU	0	-0.065	-0.042	40.209	0.178	0.178	0.000	0.000	0.000	0.000
109	A	110	GLY	0	-0.002	0.009	37.767	0.058	0.058	0.000	0.000	0.000	0.000
110	A	111	ILE	0	0.000	-0.016	35.034	-0.107	-0.107	0.000	0.000	0.000	0.000
111	A	112	ASP	-1	-0.847	-0.900	36.877	-7.705	-7.705	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.813	-0.892	37.455	-7.620	-7.620	0.000	0.000	0.000	0.000
113	A	114	PRO	0	-0.025	-0.017	37.855	-0.178	-0.178	0.000	0.000	0.000	0.000
114	A	115	ASP	-1	-0.913	-0.940	36.645	-7.905	-7.905	0.000	0.000	0.000	0.000
115	A	116	TYR	0	-0.025	-0.021	30.259	-0.417	-0.417	0.000	0.000	0.000	0.000
116	A	117	THR	0	-0.040	-0.028	29.955	0.051	0.051	0.000	0.000	0.000	0.000
117	A	118	ALA	0	0.053	0.024	28.286	-0.218	-0.218	0.000	0.000	0.000	0.000
118	A	119	LEU	0	-0.051	-0.033	24.835	0.145	0.145	0.000	0.000	0.000	0.000
119	A	120	CYS	0	-0.004	0.006	21.430	-0.388	-0.388	0.000	0.000	0.000	0.000
120	A	121	PHE	0	0.019	0.010	14.596	0.147	0.147	0.000	0.000	0.000	0.000
121	A	122	THR	0	0.017	0.004	16.071	-0.306	-0.306	0.000	0.000	0.000	0.000
122	A	123	ALA	0	0.024	0.031	12.045	0.280	0.280	0.000	0.000	0.000	0.000
123	A	124	GLU	-1	-0.936	-0.984	12.065	-17.705	-17.705	0.000	0.000	0.000	0.000
124	A	125	TRP	0	-0.014	-0.026	7.443	-2.613	-2.613	0.000	0.000	0.000	0.000
125	A	126	GLY	0	0.054	0.032	7.580	2.184	2.184	0.000	0.000	0.000	0.000
126	A	127	ASN	0	-0.052	-0.029	7.411	-1.855	-1.855	0.000	0.000	0.000	0.000
127	A	128	TYR	0	0.032	0.008	7.254	2.144	2.144	0.000	0.000	0.000	0.000
128	A	129	TYR	0	0.034	0.008	8.773	-0.652	-0.652	0.000	0.000	0.000	0.000
129	A	130	ARG	1	0.899	0.933	11.572	19.881	19.881	0.000	0.000	0.000	0.000
130	A	131	HIS	0	-0.024	-0.008	12.645	0.238	0.238	0.000	0.000	0.000	0.000
131	A	132	LEU	0	-0.008	-0.007	15.263	0.082	0.082	0.000	0.000	0.000	0.000
132	A	133	LYS	1	0.926	0.973	10.923	19.320	19.320	0.000	0.000	0.000	0.000
133	A	134	ASN	0	0.025	-0.001	9.167	1.493	1.493	0.000	0.000	0.000	0.000
135	A	136	THR	0	-0.029	-0.013	5.545	1.411	1.411	0.000	0.000	0.000	0.000
138	A	139	ILE	0	-0.002	-0.010	5.369	-3.995	-3.995	0.000	0.000	0.000	0.000
139	A	140	ASP	-1	-0.862	-0.914	7.859	-24.100	-24.100	0.000	0.000	0.000	0.000
140	A	141	GLU	-1	-1.022	-1.022	4.995	-39.338	-39.338	0.000	0.000	0.000	0.000

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