FMO DATABASE

FMODB ID: J4869

Calculation Name: 2HQ6-A-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol | iodide ion

Ligand 3-letter code: GOL | IOD

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2HQ6

Chain ID: A

ChEMBL ID:

UniProt ID: Q6UX04

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	169
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1788765.091332
FMO2-HF: Nuclear repulsion	1722393.043496
FMO2-HF: Total energy	-66372.047837
FMO2-MP2: Total energy	-66566.172486

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:3:VAL)

Summations of interaction energy for fragment #1(A:3:VAL)

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.
10.978	14.377	1.481	-1.861	-3.018	-0.016

Interaction energy analysis for fragmet #1(A:3:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.871 / q_NPA : 0.926

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	5	ARG	1	0.999	0.990	2.699	27.564	29.901	0.538	-1.218	-1.656	-0.012
4	A	6	GLY	0	0.020	0.005	5.321	2.003	2.075	-0.001	-0.004	-0.067	0.000
5	A	7	SER	0	-0.048	-0.014	2.588	-1.052	-0.209	0.946	-0.619	-1.169	-0.004
6	A	8	GLU	-1	-0.759	-0.857	4.488	-23.145	-23.081	-0.001	-0.013	-0.051	0.000
88	A	90	ARG	1	0.846	0.906	4.068	33.520	33.603	-0.001	-0.007	-0.075	0.000
7	A	9	PRO	0	-0.004	-0.001	6.502	-2.968	-2.968	0.000	0.000	0.000	0.000
8	A	10	PRO	0	-0.026	0.001	8.545	0.012	0.012	0.000	0.000	0.000	0.000
9	A	11	THR	0	-0.002	0.000	10.390	0.506	0.506	0.000	0.000	0.000	0.000
10	A	12	ASN	0	-0.009	-0.013	13.767	0.095	0.095	0.000	0.000	0.000	0.000
11	A	13	GLY	0	0.056	0.055	17.073	0.439	0.439	0.000	0.000	0.000	0.000
12	A	14	LYS	1	0.729	0.843	18.403	14.189	14.189	0.000	0.000	0.000	0.000
13	A	15	VAL	0	0.007	-0.006	21.405	0.570	0.570	0.000	0.000	0.000	0.000
14	A	16	LEU	0	-0.020	0.007	23.717	-0.379	-0.379	0.000	0.000	0.000	0.000
15	A	17	LEU	0	0.020	0.002	26.152	0.428	0.428	0.000	0.000	0.000	0.000
16	A	18	LYS	1	0.863	0.926	28.294	9.467	9.467	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.016	-0.030	29.341	0.308	0.308	0.000	0.000	0.000	0.000
18	A	20	THR	0	-0.014	-0.024	32.144	0.049	0.049	0.000	0.000	0.000	0.000
19	A	21	ALA	0	0.009	0.017	30.292	0.136	0.136	0.000	0.000	0.000	0.000
20	A	22	GLY	0	0.000	0.004	30.404	-0.216	-0.216	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.879	-0.932	27.429	-10.240	-10.240	0.000	0.000	0.000	0.000
22	A	24	ILE	0	-0.002	-0.003	23.628	-0.393	-0.393	0.000	0.000	0.000	0.000
23	A	25	ASP	-1	-0.794	-0.886	21.214	-13.694	-13.694	0.000	0.000	0.000	0.000
24	A	26	ILE	0	0.003	0.001	20.066	-0.694	-0.694	0.000	0.000	0.000	0.000
25	A	27	GLU	-1	-0.853	-0.932	14.789	-18.078	-18.078	0.000	0.000	0.000	0.000
26	A	28	LEU	0	0.025	0.006	17.327	-0.296	-0.296	0.000	0.000	0.000	0.000
27	A	29	TRP	0	-0.046	-0.044	11.239	-0.461	-0.461	0.000	0.000	0.000	0.000
28	A	30	SER	0	-0.002	-0.035	16.341	0.275	0.275	0.000	0.000	0.000	0.000
29	A	31	LYS	1	0.927	0.972	13.136	19.032	19.032	0.000	0.000	0.000	0.000
30	A	32	GLU	-1	-0.939	-0.990	13.399	-18.382	-18.382	0.000	0.000	0.000	0.000
31	A	33	ALA	0	0.002	0.005	16.861	0.388	0.388	0.000	0.000	0.000	0.000
32	A	34	PRO	0	0.014	0.023	20.023	0.315	0.315	0.000	0.000	0.000	0.000
33	A	35	LYS	1	0.944	0.968	22.389	10.654	10.654	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.053	0.026	22.717	0.382	0.382	0.000	0.000	0.000	0.000
35	A	37	CYS	0	-0.052	0.002	20.511	0.029	0.029	0.000	0.000	0.000	0.000
36	A	38	ARG	1	0.966	0.987	23.236	10.602	10.602	0.000	0.000	0.000	0.000
37	A	39	ASN	0	0.015	0.006	26.493	0.570	0.570	0.000	0.000	0.000	0.000
38	A	40	PHE	0	0.014	0.006	24.398	0.179	0.179	0.000	0.000	0.000	0.000
39	A	41	ILE	0	0.025	-0.002	23.605	0.176	0.176	0.000	0.000	0.000	0.000
40	A	42	GLN	0	-0.051	-0.030	27.506	0.022	0.022	0.000	0.000	0.000	0.000
41	A	43	LEU	0	0.022	0.009	30.497	0.260	0.260	0.000	0.000	0.000	0.000
42	A	44	CYS	0	-0.145	-0.041	28.915	-0.245	-0.245	0.000	0.000	0.000	0.000
43	A	45	LEU	0	-0.017	-0.016	30.299	0.195	0.195	0.000	0.000	0.000	0.000
44	A	46	GLU	-1	-0.925	-0.952	33.009	-8.171	-8.171	0.000	0.000	0.000	0.000
45	A	47	ALA	0	-0.009	0.000	34.861	0.227	0.227	0.000	0.000	0.000	0.000
46	A	48	TYR	0	0.040	0.027	34.290	0.075	0.075	0.000	0.000	0.000	0.000
47	A	49	TYR	0	-0.039	-0.045	28.998	-0.039	-0.039	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.811	-0.894	33.775	-8.774	-8.774	0.000	0.000	0.000	0.000
49	A	51	ASN	0	-0.044	-0.015	36.038	0.189	0.189	0.000	0.000	0.000	0.000
50	A	52	THR	0	-0.040	-0.009	34.457	0.088	0.088	0.000	0.000	0.000	0.000
51	A	53	ILE	0	-0.027	-0.020	35.588	-0.078	-0.078	0.000	0.000	0.000	0.000
52	A	54	PHE	0	0.004	-0.018	28.409	-0.174	-0.174	0.000	0.000	0.000	0.000
53	A	55	HIS	0	-0.010	0.011	33.275	0.144	0.144	0.000	0.000	0.000	0.000
54	A	56	ARG	1	0.831	0.889	30.688	9.607	9.607	0.000	0.000	0.000	0.000
55	A	57	VAL	0	-0.016	-0.010	30.869	-0.419	-0.419	0.000	0.000	0.000	0.000
56	A	58	VAL	0	0.058	0.044	29.382	0.185	0.185	0.000	0.000	0.000	0.000
57	A	59	PRO	0	0.064	0.014	28.936	-0.496	-0.496	0.000	0.000	0.000	0.000
58	A	60	GLY	0	-0.041	-0.013	26.234	-0.041	-0.041	0.000	0.000	0.000	0.000
59	A	61	PHE	0	-0.029	-0.013	24.311	-0.580	-0.580	0.000	0.000	0.000	0.000
60	A	62	ILE	0	-0.007	-0.014	24.215	-0.645	-0.645	0.000	0.000	0.000	0.000
61	A	63	VAL	0	0.014	0.023	26.317	0.377	0.377	0.000	0.000	0.000	0.000
62	A	64	GLN	0	-0.011	-0.015	27.421	-0.521	-0.521	0.000	0.000	0.000	0.000
63	A	65	GLY	0	0.033	0.011	29.782	0.301	0.301	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.025	0.017	31.187	-0.164	-0.164	0.000	0.000	0.000	0.000
65	A	67	ASP	-1	-0.722	-0.818	32.424	-7.923	-7.923	0.000	0.000	0.000	0.000
66	A	68	PRO	0	0.008	0.001	35.781	0.072	0.072	0.000	0.000	0.000	0.000
67	A	69	THR	0	-0.055	-0.045	38.512	0.227	0.227	0.000	0.000	0.000	0.000
68	A	70	GLY	0	-0.014	-0.005	38.200	0.132	0.132	0.000	0.000	0.000	0.000
69	A	71	THR	0	0.011	-0.020	39.277	-0.020	-0.020	0.000	0.000	0.000	0.000
70	A	72	GLY	0	0.021	0.005	36.345	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	73	SER	0	-0.053	-0.025	36.485	-0.130	-0.130	0.000	0.000	0.000	0.000
72	A	74	GLY	0	-0.005	0.012	38.600	0.110	0.110	0.000	0.000	0.000	0.000
73	A	75	GLY	0	0.015	-0.004	35.625	-0.239	-0.239	0.000	0.000	0.000	0.000
74	A	76	GLU	-1	-0.994	-0.992	35.713	-7.678	-7.678	0.000	0.000	0.000	0.000
75	A	77	SER	0	-0.044	-0.043	31.732	-0.189	-0.189	0.000	0.000	0.000	0.000
76	A	78	ILE	0	0.027	0.005	30.323	0.204	0.204	0.000	0.000	0.000	0.000
77	A	79	TYR	0	-0.136	-0.079	28.026	0.121	0.121	0.000	0.000	0.000	0.000
78	A	80	GLY	0	0.000	0.013	34.759	0.141	0.141	0.000	0.000	0.000	0.000
79	A	81	ALA	0	0.013	0.009	36.167	0.213	0.213	0.000	0.000	0.000	0.000
80	A	82	PRO	0	0.029	0.047	33.550	-0.247	-0.247	0.000	0.000	0.000	0.000
81	A	83	PHE	0	-0.021	0.000	26.138	-0.026	-0.026	0.000	0.000	0.000	0.000
82	A	84	LYS	1	0.868	0.904	23.467	11.518	11.518	0.000	0.000	0.000	0.000
83	A	85	ASP	-1	-0.740	-0.855	24.102	-11.228	-11.228	0.000	0.000	0.000	0.000
84	A	86	GLU	-1	-0.902	-0.950	21.003	-12.169	-12.169	0.000	0.000	0.000	0.000
85	A	87	PHE	0	0.039	0.022	18.601	-0.464	-0.464	0.000	0.000	0.000	0.000
86	A	88	HIS	0	0.091	0.036	10.503	-0.410	-0.410	0.000	0.000	0.000	0.000
87	A	89	SER	0	-0.015	-0.008	12.316	-0.473	-0.473	0.000	0.000	0.000	0.000
89	A	91	LEU	0	0.024	0.039	10.232	-1.079	-1.079	0.000	0.000	0.000	0.000
90	A	92	ARG	1	0.806	0.888	12.018	18.644	18.644	0.000	0.000	0.000	0.000
91	A	93	PHE	0	0.090	0.048	14.126	-0.799	-0.799	0.000	0.000	0.000	0.000
92	A	94	ASN	0	-0.053	-0.042	10.294	0.742	0.742	0.000	0.000	0.000	0.000
93	A	95	ARG	1	0.782	0.869	11.790	20.727	20.727	0.000	0.000	0.000	0.000
94	A	96	ARG	1	1.012	1.030	15.634	15.013	15.013	0.000	0.000	0.000	0.000
95	A	97	GLY	0	-0.002	-0.007	16.744	-1.047	-1.047	0.000	0.000	0.000	0.000
96	A	98	LEU	0	-0.057	-0.023	13.947	-0.688	-0.688	0.000	0.000	0.000	0.000
97	A	99	VAL	0	0.024	0.008	17.935	0.687	0.687	0.000	0.000	0.000	0.000
98	A	100	ALA	0	-0.003	-0.010	20.031	-0.530	-0.530	0.000	0.000	0.000	0.000
99	A	101	MET	0	-0.015	0.011	22.298	0.272	0.272	0.000	0.000	0.000	0.000
100	A	102	ALA	0	-0.024	-0.016	25.617	-0.161	-0.161	0.000	0.000	0.000	0.000
101	A	103	ASN	0	-0.053	-0.032	27.020	0.158	0.158	0.000	0.000	0.000	0.000
102	A	104	ALA	0	0.030	0.017	30.440	-0.033	-0.033	0.000	0.000	0.000	0.000
103	A	105	GLY	0	-0.007	-0.012	31.418	0.199	0.199	0.000	0.000	0.000	0.000
104	A	106	SER	0	-0.030	-0.026	28.787	-0.230	-0.230	0.000	0.000	0.000	0.000
105	A	107	HIS	0	-0.080	-0.041	27.025	0.168	0.168	0.000	0.000	0.000	0.000
106	A	108	ASP	-1	-0.822	-0.897	30.116	-8.584	-8.584	0.000	0.000	0.000	0.000
107	A	109	ASN	0	-0.071	-0.048	26.890	-0.250	-0.250	0.000	0.000	0.000	0.000
108	A	110	GLY	0	0.093	0.040	29.980	0.196	0.196	0.000	0.000	0.000	0.000
109	A	111	SER	0	0.024	0.003	30.857	-0.181	-0.181	0.000	0.000	0.000	0.000
110	A	112	GLN	0	-0.032	-0.012	30.288	-0.481	-0.481	0.000	0.000	0.000	0.000
111	A	113	PHE	0	-0.022	-0.003	25.493	-0.292	-0.292	0.000	0.000	0.000	0.000
112	A	114	PHE	0	-0.007	-0.010	22.908	0.215	0.215	0.000	0.000	0.000	0.000
113	A	115	PHE	0	0.034	0.011	22.117	-0.531	-0.531	0.000	0.000	0.000	0.000
114	A	116	THR	0	-0.004	-0.006	18.529	0.341	0.341	0.000	0.000	0.000	0.000
115	A	117	LEU	0	0.014	0.009	21.336	-0.543	-0.543	0.000	0.000	0.000	0.000
116	A	118	GLY	0	-0.001	-0.011	21.147	-0.254	-0.254	0.000	0.000	0.000	0.000
117	A	119	ARG	1	0.720	0.829	14.304	17.174	17.174	0.000	0.000	0.000	0.000
118	A	120	ALA	0	0.101	0.048	19.318	0.611	0.611	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.834	-0.885	16.872	-16.791	-16.791	0.000	0.000	0.000	0.000
120	A	122	GLU	-1	-0.845	-0.937	19.617	-12.696	-12.696	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.026	0.013	21.789	0.391	0.391	0.000	0.000	0.000	0.000
122	A	124	ASN	0	-0.035	-0.011	16.760	-0.700	-0.700	0.000	0.000	0.000	0.000
123	A	125	ASN	0	-0.051	-0.030	18.725	-0.228	-0.228	0.000	0.000	0.000	0.000
124	A	126	LYS	1	0.924	0.981	21.169	11.710	11.710	0.000	0.000	0.000	0.000
125	A	127	HIS	0	0.060	0.052	22.627	0.355	0.355	0.000	0.000	0.000	0.000
126	A	128	THR	0	0.004	0.003	21.300	-0.703	-0.703	0.000	0.000	0.000	0.000
127	A	129	ILE	0	-0.044	-0.007	15.914	0.134	0.134	0.000	0.000	0.000	0.000
128	A	130	PHE	0	-0.001	-0.015	18.455	-0.434	-0.434	0.000	0.000	0.000	0.000
129	A	131	GLY	0	0.057	0.017	17.039	-0.061	-0.061	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.840	0.944	10.647	22.451	22.451	0.000	0.000	0.000	0.000
131	A	133	VAL	0	0.029	0.022	16.758	0.387	0.387	0.000	0.000	0.000	0.000
132	A	134	THR	0	-0.043	-0.016	16.915	-0.900	-0.900	0.000	0.000	0.000	0.000
133	A	135	GLY	0	-0.019	-0.022	16.690	0.441	0.441	0.000	0.000	0.000	0.000
134	A	136	ASP	-1	-0.871	-0.918	17.711	-14.188	-14.188	0.000	0.000	0.000	0.000
135	A	137	THR	0	0.008	0.000	20.866	0.744	0.744	0.000	0.000	0.000	0.000
136	A	138	VAL	0	-0.005	-0.010	18.254	0.466	0.466	0.000	0.000	0.000	0.000
137	A	139	TYR	0	-0.014	-0.005	21.611	0.376	0.376	0.000	0.000	0.000	0.000
138	A	140	ASN	0	0.002	-0.017	24.763	0.515	0.515	0.000	0.000	0.000	0.000
139	A	141	MET	0	-0.001	0.012	21.620	0.069	0.069	0.000	0.000	0.000	0.000
140	A	142	LEU	0	-0.045	-0.022	22.798	0.090	0.090	0.000	0.000	0.000	0.000
141	A	143	ARG	1	0.925	0.990	26.215	10.323	10.323	0.000	0.000	0.000	0.000
142	A	144	LEU	0	-0.059	-0.019	27.166	0.388	0.388	0.000	0.000	0.000	0.000
143	A	145	SER	0	-0.047	-0.045	28.842	0.198	0.198	0.000	0.000	0.000	0.000
144	A	146	GLU	-1	-0.980	-0.984	30.970	-9.901	-9.901	0.000	0.000	0.000	0.000
145	A	147	VAL	0	-0.074	-0.042	33.216	0.207	0.207	0.000	0.000	0.000	0.000
146	A	148	ASP	-1	-0.907	-0.950	36.276	-7.670	-7.670	0.000	0.000	0.000	0.000
147	A	149	ILE	0	-0.079	-0.049	34.337	-0.100	-0.100	0.000	0.000	0.000	0.000
148	A	150	ASP	-1	-0.822	-0.894	38.820	-7.481	-7.481	0.000	0.000	0.000	0.000
149	A	151	ASP	-1	-0.946	-0.989	39.440	-7.290	-7.290	0.000	0.000	0.000	0.000
150	A	152	ASP	-1	-0.949	-0.959	40.031	-7.323	-7.323	0.000	0.000	0.000	0.000
151	A	153	GLU	-1	-0.903	-0.933	33.925	-9.325	-9.325	0.000	0.000	0.000	0.000
152	A	154	ARG	1	0.901	0.946	35.673	7.348	7.348	0.000	0.000	0.000	0.000
153	A	155	PRO	0	-0.048	-0.027	35.374	0.119	0.119	0.000	0.000	0.000	0.000
154	A	156	HIS	0	0.036	0.017	38.142	0.119	0.119	0.000	0.000	0.000	0.000
155	A	157	ASN	0	-0.074	-0.046	40.024	0.277	0.277	0.000	0.000	0.000	0.000
156	A	158	PRO	0	-0.014	-0.002	36.882	-0.213	-0.213	0.000	0.000	0.000	0.000
157	A	159	HIS	0	0.068	0.062	33.269	0.152	0.152	0.000	0.000	0.000	0.000
158	A	160	LYS	1	0.885	0.921	35.026	7.630	7.630	0.000	0.000	0.000	0.000
159	A	161	ILE	0	0.004	0.013	30.502	-0.245	-0.245	0.000	0.000	0.000	0.000
160	A	162	LYS	1	0.866	0.929	33.406	8.805	8.805	0.000	0.000	0.000	0.000
161	A	163	SER	0	0.001	-0.018	33.401	0.314	0.314	0.000	0.000	0.000	0.000
162	A	165	GLU	-1	-0.797	-0.889	29.120	-9.400	-9.400	0.000	0.000	0.000	0.000
163	A	166	VAL	0	0.021	-0.001	25.692	-0.443	-0.443	0.000	0.000	0.000	0.000
164	A	167	LEU	0	-0.018	0.001	24.375	0.130	0.130	0.000	0.000	0.000	0.000
165	A	168	PHE	0	-0.037	-0.020	20.968	-0.127	-0.127	0.000	0.000	0.000	0.000
166	A	169	ASN	0	0.069	0.026	23.466	-0.634	-0.634	0.000	0.000	0.000	0.000
167	A	170	PRO	0	-0.080	-0.025	20.837	0.001	0.001	0.000	0.000	0.000	0.000
168	A	171	PHE	0	-0.121	-0.079	22.851	-0.237	-0.237	0.000	0.000	0.000	0.000
169	A	172	ASP	-2	-1.793	-1.870	26.021	-20.287	-20.287	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:VAL)