FMO DATABASE

FMODB ID: 15VQZ

Calculation Name: 1GQO-A-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1GQO

Chain ID: A

ChEMBL ID:

UniProt ID: P54517

Base Structure: X-ray

Registration Date: 2025-09-03

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	-1293764.107745
FMO2-HF: Nuclear repulsion	1240029.856262
FMO2-HF: Total energy	-53734.251482
FMO2-MP2: Total energy	-53895.947229

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:PRO)

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

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.
-224.126	-216.668	6.084	-4.425	-9.116	-0.044

Interaction energy analysis for fragmet #1(A:1:PRO)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.858 / q_NPA : 0.919

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	3	PHE	0	0.027	0.017	2.854	-3.847	-0.186	1.292	-1.845	-3.108	-0.018
43	A	43	ILE	0	-0.070	-0.021	2.172	-19.071	-17.166	1.369	-0.998	-2.276	-0.011
44	A	44	GLN	0	0.003	0.004	3.416	7.421	8.211	0.002	-0.264	-0.528	-0.001
68	A	68	SER	0	0.008	-0.006	2.702	-4.728	-3.539	1.203	-0.910	-1.481	-0.010
69	A	69	GLY	0	0.016	-0.009	5.145	0.785	0.836	-0.001	-0.003	-0.047	0.000
139	A	139	LEU	0	-0.042	-0.019	2.359	-5.987	-6.186	2.220	-0.403	-1.619	-0.004
140	A	140	SER	0	-0.141	-0.072	5.010	0.951	1.012	-0.001	-0.002	-0.057	0.000
4	A	4	LEU	0	0.051	0.033	5.576	1.743	1.743	0.000	0.000	0.000	0.000
5	A	5	ILE	0	-0.047	-0.020	9.402	0.702	0.702	0.000	0.000	0.000	0.000
6	A	6	LEU	0	0.026	0.017	11.860	1.130	1.130	0.000	0.000	0.000	0.000
7	A	7	ASN	0	0.029	0.020	14.808	0.669	0.669	0.000	0.000	0.000	0.000
8	A	8	GLY	0	0.113	0.049	18.213	0.294	0.294	0.000	0.000	0.000	0.000
9	A	9	PRO	0	-0.002	0.007	21.531	0.145	0.145	0.000	0.000	0.000	0.000
10	A	10	ASN	0	-0.100	-0.060	25.282	0.336	0.336	0.000	0.000	0.000	0.000
11	A	11	VAL	0	0.016	0.032	19.955	0.221	0.221	0.000	0.000	0.000	0.000
12	A	12	ASN	0	0.050	0.016	23.324	-0.030	-0.030	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.860	0.934	24.511	10.520	10.520	0.000	0.000	0.000	0.000
14	A	14	LEU	0	0.000	0.019	22.481	0.525	0.525	0.000	0.000	0.000	0.000
15	A	15	GLY	0	0.082	0.025	26.465	-0.181	-0.181	0.000	0.000	0.000	0.000
16	A	16	SER	0	-0.128	-0.074	29.244	0.462	0.462	0.000	0.000	0.000	0.000
17	A	17	ARG	1	0.837	0.888	31.207	10.029	10.029	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.808	-0.885	31.690	-9.626	-9.626	0.000	0.000	0.000	0.000
19	A	19	PRO	0	0.056	0.027	30.741	-0.274	-0.274	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.930	-0.963	30.091	-9.488	-9.488	0.000	0.000	0.000	0.000
21	A	21	VAL	0	-0.068	-0.019	29.608	-0.132	-0.132	0.000	0.000	0.000	0.000
22	A	22	PHE	0	-0.064	-0.044	26.374	-0.332	-0.332	0.000	0.000	0.000	0.000
23	A	23	GLY	0	0.028	0.035	25.744	-0.537	-0.537	0.000	0.000	0.000	0.000
24	A	24	ARG	0	-0.028	-0.030	27.217	0.085	0.085	0.000	0.000	0.000	0.000
25	A	25	GLN	0	-0.044	-0.012	20.970	-0.001	-0.001	0.000	0.000	0.000	0.000
26	A	26	THR	0	-0.020	-0.039	24.632	-0.034	-0.034	0.000	0.000	0.000	0.000
27	A	27	LEU	0	0.004	-0.004	18.614	-0.323	-0.323	0.000	0.000	0.000	0.000
28	A	28	THR	0	0.052	0.021	20.060	-0.865	-0.865	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.832	-0.873	20.063	-13.481	-13.481	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.007	0.003	17.132	-0.680	-0.680	0.000	0.000	0.000	0.000
31	A	31	GLU	-1	-0.900	-0.965	15.643	-18.965	-18.965	0.000	0.000	0.000	0.000
32	A	32	THR	0	-0.041	-0.025	15.021	-1.269	-1.269	0.000	0.000	0.000	0.000
33	A	33	ASP	-1	-0.869	-0.941	15.772	-17.526	-17.526	0.000	0.000	0.000	0.000
34	A	34	LEU	0	-0.039	-0.028	11.854	-1.233	-1.233	0.000	0.000	0.000	0.000
35	A	35	PHE	0	-0.015	0.012	11.049	-2.862	-2.862	0.000	0.000	0.000	0.000
36	A	36	GLN	0	0.020	0.011	11.215	-1.483	-1.483	0.000	0.000	0.000	0.000
37	A	37	PHE	0	-0.048	-0.031	8.920	-0.634	-0.634	0.000	0.000	0.000	0.000
38	A	38	ALA	0	0.002	-0.002	7.293	-1.734	-1.734	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.882	-0.953	7.244	-26.137	-26.137	0.000	0.000	0.000	0.000
40	A	40	ALA	0	-0.060	-0.030	9.370	-1.097	-1.097	0.000	0.000	0.000	0.000
41	A	41	LEU	0	-0.071	-0.032	6.822	1.312	1.312	0.000	0.000	0.000	0.000
42	A	42	HIS	0	-0.073	-0.029	5.532	-4.305	-4.305	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.010	-0.005	5.523	-4.260	-4.260	0.000	0.000	0.000	0.000
46	A	46	THR	0	0.002	0.013	8.338	2.962	2.962	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.008	-0.001	11.013	-0.621	-0.621	0.000	0.000	0.000	0.000
48	A	48	PHE	0	0.025	0.012	13.926	0.647	0.647	0.000	0.000	0.000	0.000
49	A	49	GLN	0	-0.069	-0.050	16.607	0.110	0.110	0.000	0.000	0.000	0.000
50	A	50	SER	0	-0.008	-0.026	19.817	0.590	0.590	0.000	0.000	0.000	0.000
51	A	51	ASN	0	-0.023	-0.037	22.764	-0.296	-0.296	0.000	0.000	0.000	0.000
52	A	52	HIS	0	-0.017	0.004	25.136	0.580	0.580	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.828	-0.895	23.965	-11.620	-11.620	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.001	0.003	23.352	-0.399	-0.399	0.000	0.000	0.000	0.000
55	A	55	ASP	-1	-0.731	-0.840	21.725	-13.042	-13.042	0.000	0.000	0.000	0.000
56	A	56	LEU	0	-0.055	-0.028	19.035	-0.734	-0.734	0.000	0.000	0.000	0.000
57	A	57	ILE	0	-0.020	-0.007	18.496	-0.694	-0.694	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.896	-0.941	19.455	-13.481	-13.481	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.002	-0.004	15.909	-0.644	-0.644	0.000	0.000	0.000	0.000
60	A	60	ILE	0	-0.064	-0.036	14.884	-1.394	-1.394	0.000	0.000	0.000	0.000
61	A	61	HIS	0	0.002	-0.006	15.142	-1.152	-1.152	0.000	0.000	0.000	0.000
62	A	62	GLU	-1	-0.954	-0.977	16.061	-16.465	-16.465	0.000	0.000	0.000	0.000
63	A	63	ALA	0	-0.048	-0.025	11.064	-1.362	-1.362	0.000	0.000	0.000	0.000
64	A	64	GLU	-1	-0.767	-0.867	10.807	-22.885	-22.885	0.000	0.000	0.000	0.000
65	A	65	GLU	-1	-0.973	-0.979	11.472	-18.868	-18.868	0.000	0.000	0.000	0.000
66	A	66	GLN	0	-0.086	-0.036	9.651	-0.653	-0.653	0.000	0.000	0.000	0.000
67	A	67	TYR	0	-0.060	-0.029	6.369	-2.772	-2.772	0.000	0.000	0.000	0.000
70	A	70	ILE	0	-0.013	0.004	6.962	-1.309	-1.309	0.000	0.000	0.000	0.000
71	A	71	VAL	0	-0.037	-0.015	9.096	0.975	0.975	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.032	0.018	11.503	0.422	0.422	0.000	0.000	0.000	0.000
73	A	73	ASN	0	0.014	0.004	15.024	1.252	1.252	0.000	0.000	0.000	0.000
74	A	74	PRO	0	0.044	0.017	18.158	0.242	0.242	0.000	0.000	0.000	0.000
75	A	75	GLY	0	0.054	0.024	20.803	0.681	0.681	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.018	-0.038	23.685	0.073	0.073	0.000	0.000	0.000	0.000
77	A	77	LEU	0	0.011	0.018	23.634	0.292	0.292	0.000	0.000	0.000	0.000
78	A	78	SER	0	-0.001	-0.021	23.240	0.262	0.262	0.000	0.000	0.000	0.000
79	A	79	HIS	0	-0.028	-0.013	24.442	0.137	0.137	0.000	0.000	0.000	0.000
80	A	80	TYR	0	-0.041	-0.021	27.560	0.371	0.371	0.000	0.000	0.000	0.000
81	A	81	SER	0	-0.021	-0.034	24.575	0.078	0.078	0.000	0.000	0.000	0.000
82	A	82	TYR	0	0.008	-0.024	24.871	-0.448	-0.448	0.000	0.000	0.000	0.000
83	A	83	ALA	0	0.028	0.031	25.522	-0.193	-0.193	0.000	0.000	0.000	0.000
84	A	84	ILE	0	0.054	0.019	19.668	-0.360	-0.360	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.862	0.944	20.581	11.121	11.121	0.000	0.000	0.000	0.000
86	A	86	ASP	-1	-0.891	-0.953	21.302	-11.956	-11.956	0.000	0.000	0.000	0.000
87	A	87	ALA	0	-0.004	0.006	20.025	-0.183	-0.183	0.000	0.000	0.000	0.000
88	A	88	VAL	0	0.005	0.005	15.966	-0.650	-0.650	0.000	0.000	0.000	0.000
89	A	89	SER	0	-0.059	-0.042	17.321	-0.437	-0.437	0.000	0.000	0.000	0.000
90	A	90	SER	0	-0.116	-0.065	19.558	0.371	0.371	0.000	0.000	0.000	0.000
91	A	91	ILE	0	-0.029	0.003	12.959	-0.107	-0.107	0.000	0.000	0.000	0.000
92	A	92	SER	0	-0.088	-0.081	12.494	-0.155	-0.155	0.000	0.000	0.000	0.000
93	A	93	LEU	0	-0.036	-0.001	8.469	-1.113	-1.113	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.040	-0.014	7.798	1.912	1.912	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.059	0.030	9.677	-1.778	-1.778	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.024	-0.013	11.665	1.044	1.044	0.000	0.000	0.000	0.000
97	A	97	GLU	-1	-0.673	-0.777	13.762	-14.061	-14.061	0.000	0.000	0.000	0.000
98	A	98	VAL	0	-0.027	-0.029	14.697	0.061	0.061	0.000	0.000	0.000	0.000
99	A	99	HIS	0	-0.054	-0.031	17.745	0.469	0.469	0.000	0.000	0.000	0.000
100	A	100	LEU	0	-0.012	0.001	20.495	0.198	0.198	0.000	0.000	0.000	0.000
101	A	101	SER	0	0.030	0.029	22.465	0.380	0.380	0.000	0.000	0.000	0.000
102	A	102	ASN	0	0.030	-0.017	25.572	-0.328	-0.328	0.000	0.000	0.000	0.000
103	A	103	LEU	0	0.015	0.004	24.599	0.464	0.464	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.034	0.015	24.760	0.355	0.355	0.000	0.000	0.000	0.000
105	A	105	ALA	0	-0.064	-0.015	30.603	0.319	0.319	0.000	0.000	0.000	0.000
106	A	106	ARG	1	0.878	0.940	28.741	10.441	10.441	0.000	0.000	0.000	0.000
107	A	107	GLU	-1	-0.761	-0.857	33.195	-9.233	-9.233	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.881	-0.938	33.199	-8.335	-8.335	0.000	0.000	0.000	0.000
109	A	109	PHE	0	-0.041	-0.029	31.520	-0.189	-0.189	0.000	0.000	0.000	0.000
110	A	110	ARG	1	0.813	0.871	28.981	9.726	9.726	0.000	0.000	0.000	0.000
111	A	111	HIS	0	-0.072	-0.035	28.469	-0.410	-0.410	0.000	0.000	0.000	0.000
112	A	112	GLN	0	-0.020	-0.010	28.207	0.016	0.016	0.000	0.000	0.000	0.000
113	A	113	SER	0	-0.017	-0.026	22.299	0.048	0.048	0.000	0.000	0.000	0.000
114	A	114	VAL	0	-0.042	-0.027	25.311	0.137	0.137	0.000	0.000	0.000	0.000
115	A	115	ILE	0	0.017	0.014	19.330	-0.022	-0.022	0.000	0.000	0.000	0.000
116	A	116	ALA	0	0.019	0.003	19.989	-0.400	-0.400	0.000	0.000	0.000	0.000
117	A	117	PRO	0	-0.102	-0.055	20.549	-0.291	-0.291	0.000	0.000	0.000	0.000
118	A	118	VAL	0	-0.041	-0.007	19.832	0.274	0.274	0.000	0.000	0.000	0.000
119	A	119	ALA	0	-0.008	0.024	16.262	-0.690	-0.690	0.000	0.000	0.000	0.000
120	A	120	LYS	1	0.933	0.961	12.389	20.375	20.375	0.000	0.000	0.000	0.000
121	A	121	GLY	0	0.006	0.001	15.522	0.516	0.516	0.000	0.000	0.000	0.000
122	A	122	GLN	0	-0.014	-0.014	16.973	-0.354	-0.354	0.000	0.000	0.000	0.000
123	A	123	ILE	0	-0.029	-0.001	14.944	0.388	0.388	0.000	0.000	0.000	0.000
124	A	124	VAL	0	0.007	-0.002	19.118	0.088	0.088	0.000	0.000	0.000	0.000
125	A	125	GLY	0	-0.026	-0.007	22.471	0.176	0.176	0.000	0.000	0.000	0.000
126	A	126	LEU	0	-0.028	-0.004	18.943	0.237	0.237	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.022	0.009	20.358	-0.449	-0.449	0.000	0.000	0.000	0.000
128	A	128	ALA	0	0.050	0.011	18.780	-0.481	-0.481	0.000	0.000	0.000	0.000
129	A	129	GLU	-1	-0.872	-0.932	16.266	-19.165	-19.165	0.000	0.000	0.000	0.000
130	A	130	GLY	0	0.009	0.001	15.521	-1.072	-1.072	0.000	0.000	0.000	0.000
131	A	131	TYR	0	0.012	-0.008	13.379	-0.335	-0.335	0.000	0.000	0.000	0.000
132	A	132	LYS	1	0.866	0.946	11.318	16.621	16.621	0.000	0.000	0.000	0.000
133	A	133	LEU	0	-0.049	-0.029	10.877	-1.787	-1.787	0.000	0.000	0.000	0.000
134	A	134	ALA	0	0.034	0.018	11.718	-0.757	-0.757	0.000	0.000	0.000	0.000
135	A	135	VAL	0	0.021	0.013	6.041	-1.453	-1.453	0.000	0.000	0.000	0.000
136	A	136	ARG	1	0.913	0.956	6.687	20.126	20.126	0.000	0.000	0.000	0.000
137	A	137	TYR	0	-0.034	-0.003	8.433	-0.835	-0.835	0.000	0.000	0.000	0.000
138	A	138	LEU	0	0.023	0.012	5.720	-0.092	-0.092	0.000	0.000	0.000	0.000
141	A	141	GLN	-1	-0.946	-0.963	5.976	-29.361	-29.361	0.000	0.000	0.000	0.000

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