FMO DATABASE

FMODB ID: QM63Y

Calculation Name: 6CH2-F-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 6CH2

Chain ID: F

ChEMBL ID:

UniProt ID: P40729

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	146
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1252482.406605
FMO2-HF: Nuclear repulsion	1193440.313049
FMO2-HF: Total energy	-59042.093555
FMO2-MP2: Total energy	-59212.412905

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:4:MET)

Summations of interaction energy for fragment #1(A:4:MET)

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.
-58.448	-56.324	0.045	-0.774	-1.396	-0.002

Interaction energy analysis for fragmet #1(A:4:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.902 / q_NPA : 0.940

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	6	ILE	0	0.070	0.039	3.368	-2.213	-0.585	0.046	-0.713	-0.961	-0.002
5	A	8	GLU	-1	-0.926	-0.963	4.220	-30.068	-29.930	-0.001	-0.009	-0.129	0.000
6	A	9	THR	0	-0.084	-0.051	4.056	1.878	2.111	0.001	-0.030	-0.204	0.000
146	A	173	PRO	-1	-0.935	-0.956	4.599	-62.408	-62.283	-0.001	-0.022	-0.102	0.000
4	A	7	ASP	-1	-0.800	-0.879	5.830	-25.164	-25.164	0.000	0.000	0.000	0.000
7	A	10	VAL	0	0.021	0.005	6.559	3.793	3.793	0.000	0.000	0.000	0.000
8	A	11	ALA	0	-0.007	0.001	9.397	2.484	2.484	0.000	0.000	0.000	0.000
9	A	12	ARG	1	0.986	0.994	5.829	33.430	33.430	0.000	0.000	0.000	0.000
10	A	13	TYR	0	0.040	0.009	8.235	0.845	0.845	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.963	0.983	12.347	20.954	20.954	0.000	0.000	0.000	0.000
12	A	15	ALA	0	0.015	0.020	13.548	1.254	1.254	0.000	0.000	0.000	0.000
13	A	16	GLN	0	0.035	0.012	13.256	0.948	0.948	0.000	0.000	0.000	0.000
14	A	17	PHE	0	-0.008	0.001	15.888	0.852	0.852	0.000	0.000	0.000	0.000
15	A	18	THR	0	0.004	-0.018	18.181	0.838	0.838	0.000	0.000	0.000	0.000
16	A	19	GLN	0	-0.045	-0.006	16.641	1.086	1.086	0.000	0.000	0.000	0.000
17	A	20	LEU	0	0.030	0.012	17.926	0.637	0.637	0.000	0.000	0.000	0.000
18	A	21	ASP	-1	-0.872	-0.933	21.568	-11.323	-11.323	0.000	0.000	0.000	0.000
19	A	22	THR	0	-0.074	-0.043	23.625	0.733	0.733	0.000	0.000	0.000	0.000
20	A	23	MET	0	-0.007	0.010	24.150	0.394	0.394	0.000	0.000	0.000	0.000
21	A	24	MET	0	-0.028	-0.018	25.728	0.530	0.530	0.000	0.000	0.000	0.000
22	A	25	SER	0	-0.047	-0.017	27.622	0.587	0.587	0.000	0.000	0.000	0.000
23	A	26	LYS	1	0.958	0.966	28.095	10.520	10.520	0.000	0.000	0.000	0.000
24	A	27	LEU	0	-0.001	0.010	28.905	0.301	0.301	0.000	0.000	0.000	0.000
25	A	28	ASN	0	-0.027	-0.022	31.706	0.339	0.339	0.000	0.000	0.000	0.000
26	A	29	ASN	0	-0.054	-0.016	34.169	0.375	0.375	0.000	0.000	0.000	0.000
27	A	30	THR	0	0.035	0.010	33.870	0.205	0.205	0.000	0.000	0.000	0.000
28	A	31	SER	0	0.005	0.017	36.458	0.281	0.281	0.000	0.000	0.000	0.000
29	A	32	SER	0	-0.007	-0.009	38.270	0.252	0.252	0.000	0.000	0.000	0.000
30	A	33	TYR	0	0.035	0.014	39.112	0.210	0.210	0.000	0.000	0.000	0.000
31	A	34	LEU	0	-0.026	-0.026	36.531	0.151	0.151	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.110	-0.048	40.996	0.114	0.114	0.000	0.000	0.000	0.000
33	A	36	GLN	-1	-0.991	-0.972	44.248	-6.503	-6.503	0.000	0.000	0.000	0.000
34	A	61	THR	0	0.019	-0.014	50.325	0.035	0.035	0.000	0.000	0.000	0.000
35	A	62	VAL	0	0.014	0.009	50.772	-0.035	-0.035	0.000	0.000	0.000	0.000
36	A	63	GLU	-1	-0.864	-0.915	46.269	-6.513	-6.513	0.000	0.000	0.000	0.000
37	A	64	PHE	0	0.010	-0.011	46.316	-0.105	-0.105	0.000	0.000	0.000	0.000
38	A	65	ILE	0	0.061	0.014	44.959	-0.146	-0.146	0.000	0.000	0.000	0.000
39	A	66	ASN	0	0.008	-0.005	42.705	-0.201	-0.201	0.000	0.000	0.000	0.000
40	A	67	ARG	1	0.782	0.898	40.717	6.655	6.655	0.000	0.000	0.000	0.000
41	A	68	TRP	0	0.102	0.039	39.669	-0.255	-0.255	0.000	0.000	0.000	0.000
42	A	69	GLN	0	-0.022	-0.005	39.576	-0.216	-0.216	0.000	0.000	0.000	0.000
43	A	70	ARG	1	0.948	0.984	32.742	8.496	8.496	0.000	0.000	0.000	0.000
44	A	71	ILE	0	0.018	0.021	35.023	-0.259	-0.259	0.000	0.000	0.000	0.000
45	A	72	ALA	0	0.045	0.031	34.773	-0.243	-0.243	0.000	0.000	0.000	0.000
46	A	73	LEU	0	-0.015	-0.001	33.170	-0.191	-0.191	0.000	0.000	0.000	0.000
47	A	74	LEU	0	-0.020	-0.017	29.833	-0.288	-0.288	0.000	0.000	0.000	0.000
48	A	75	SER	0	0.018	0.002	29.966	-0.346	-0.346	0.000	0.000	0.000	0.000
49	A	76	GLN	0	0.041	0.023	30.114	-0.087	-0.087	0.000	0.000	0.000	0.000
50	A	77	SER	0	-0.059	-0.022	27.284	-0.399	-0.399	0.000	0.000	0.000	0.000
51	A	78	LEU	0	0.017	-0.003	25.616	-0.441	-0.441	0.000	0.000	0.000	0.000
52	A	79	LEU	0	0.023	0.018	25.138	-0.460	-0.460	0.000	0.000	0.000	0.000
53	A	80	GLU	-1	-0.825	-0.903	25.150	-11.214	-11.214	0.000	0.000	0.000	0.000
54	A	81	LEU	0	-0.031	-0.022	21.072	-0.410	-0.410	0.000	0.000	0.000	0.000
55	A	82	ALA	0	0.003	0.004	20.801	-0.635	-0.635	0.000	0.000	0.000	0.000
56	A	83	GLN	0	-0.062	-0.033	21.356	-0.191	-0.191	0.000	0.000	0.000	0.000
57	A	84	ARG	1	0.794	0.885	19.782	11.755	11.755	0.000	0.000	0.000	0.000
58	A	85	GLY	0	0.016	0.022	17.050	-0.649	-0.649	0.000	0.000	0.000	0.000
59	A	86	GLU	-1	-0.925	-0.959	15.983	-17.134	-17.134	0.000	0.000	0.000	0.000
60	A	87	TRP	0	-0.010	-0.033	15.161	0.730	0.730	0.000	0.000	0.000	0.000
61	A	88	ASP	-1	-0.858	-0.922	13.104	-19.581	-19.581	0.000	0.000	0.000	0.000
62	A	89	LEU	0	0.004	-0.005	16.547	0.749	0.749	0.000	0.000	0.000	0.000
63	A	90	LEU	0	-0.028	-0.002	19.371	0.743	0.743	0.000	0.000	0.000	0.000
64	A	91	LEU	0	0.019	0.006	17.926	0.562	0.562	0.000	0.000	0.000	0.000
65	A	92	GLN	0	-0.059	-0.031	18.279	-0.095	-0.095	0.000	0.000	0.000	0.000
66	A	93	GLN	0	-0.002	0.000	22.062	0.786	0.786	0.000	0.000	0.000	0.000
67	A	94	GLU	-1	-0.864	-0.934	24.470	-11.177	-11.177	0.000	0.000	0.000	0.000
68	A	95	VAL	0	-0.001	0.004	24.856	0.466	0.466	0.000	0.000	0.000	0.000
69	A	96	SER	0	-0.003	-0.011	27.509	0.511	0.511	0.000	0.000	0.000	0.000
70	A	97	TYR	0	-0.092	-0.062	28.997	0.407	0.407	0.000	0.000	0.000	0.000
71	A	98	LEU	0	0.036	0.018	29.095	0.398	0.398	0.000	0.000	0.000	0.000
72	A	99	GLN	0	-0.004	-0.005	30.834	0.060	0.060	0.000	0.000	0.000	0.000
73	A	100	SER	0	-0.132	-0.069	33.366	0.321	0.321	0.000	0.000	0.000	0.000
74	A	101	ILE	0	0.036	0.010	34.558	0.245	0.245	0.000	0.000	0.000	0.000
75	A	102	GLU	-1	-0.881	-0.944	36.336	-8.003	-8.003	0.000	0.000	0.000	0.000
76	A	103	THR	0	-0.054	-0.026	37.552	0.215	0.215	0.000	0.000	0.000	0.000
77	A	104	VAL	0	-0.098	-0.056	39.866	0.245	0.245	0.000	0.000	0.000	0.000
78	A	105	MET	0	0.030	0.023	41.933	0.140	0.140	0.000	0.000	0.000	0.000
79	A	106	GLU	-1	-0.866	-0.921	41.698	-7.113	-7.113	0.000	0.000	0.000	0.000
80	A	107	LYS	1	0.773	0.893	42.977	7.217	7.217	0.000	0.000	0.000	0.000
81	A	108	GLN	0	0.065	0.021	47.318	0.020	0.020	0.000	0.000	0.000	0.000
82	A	109	THR	0	0.013	0.011	49.852	-0.060	-0.060	0.000	0.000	0.000	0.000
83	A	110	PRO	0	0.001	0.013	50.426	0.108	0.108	0.000	0.000	0.000	0.000
84	A	111	PRO	0	0.036	0.004	53.337	0.028	0.028	0.000	0.000	0.000	0.000
85	A	112	GLY	0	-0.014	0.011	55.851	0.107	0.107	0.000	0.000	0.000	0.000
86	A	113	ILE	0	-0.012	-0.009	55.471	-0.077	-0.077	0.000	0.000	0.000	0.000
87	A	114	THR	0	-0.015	-0.009	56.042	0.087	0.087	0.000	0.000	0.000	0.000
88	A	115	ARG	1	0.891	0.923	54.314	5.491	5.491	0.000	0.000	0.000	0.000
89	A	116	SER	0	-0.006	-0.012	53.778	-0.111	-0.111	0.000	0.000	0.000	0.000
90	A	117	ILE	0	0.018	0.013	51.235	-0.100	-0.100	0.000	0.000	0.000	0.000
91	A	118	GLN	0	0.038	0.019	50.465	-0.055	-0.055	0.000	0.000	0.000	0.000
92	A	119	ASP	-1	-0.830	-0.916	49.835	-5.976	-5.976	0.000	0.000	0.000	0.000
93	A	120	MET	0	-0.022	-0.001	46.260	-0.067	-0.067	0.000	0.000	0.000	0.000
94	A	121	VAL	0	-0.010	-0.002	44.848	-0.164	-0.164	0.000	0.000	0.000	0.000
95	A	122	ALA	0	0.017	0.016	44.929	-0.149	-0.149	0.000	0.000	0.000	0.000
96	A	123	GLY	0	0.008	0.008	44.992	-0.098	-0.098	0.000	0.000	0.000	0.000
97	A	124	TYR	0	0.016	0.002	40.825	-0.087	-0.087	0.000	0.000	0.000	0.000
98	A	125	ILE	0	0.011	0.010	40.202	-0.203	-0.203	0.000	0.000	0.000	0.000
99	A	126	LYS	1	0.929	0.961	40.333	6.747	6.747	0.000	0.000	0.000	0.000
100	A	127	GLN	0	0.031	0.011	36.836	0.028	0.028	0.000	0.000	0.000	0.000
101	A	128	THR	0	-0.021	-0.012	35.276	-0.248	-0.248	0.000	0.000	0.000	0.000
102	A	129	LEU	0	0.021	0.012	35.125	-0.236	-0.236	0.000	0.000	0.000	0.000
103	A	130	ASP	-1	-0.905	-0.949	35.517	-7.998	-7.998	0.000	0.000	0.000	0.000
104	A	131	ASN	0	-0.039	-0.032	32.026	-0.193	-0.193	0.000	0.000	0.000	0.000
105	A	132	GLU	-1	-0.819	-0.896	31.038	-9.352	-9.352	0.000	0.000	0.000	0.000
106	A	133	GLN	0	-0.057	-0.021	31.128	-0.340	-0.340	0.000	0.000	0.000	0.000
107	A	134	LEU	0	-0.006	0.000	29.955	-0.255	-0.255	0.000	0.000	0.000	0.000
108	A	135	LEU	0	0.002	0.006	25.227	-0.392	-0.392	0.000	0.000	0.000	0.000
109	A	136	LYS	1	0.926	0.965	26.362	9.364	9.364	0.000	0.000	0.000	0.000
110	A	137	GLY	0	-0.001	0.002	27.218	-0.260	-0.260	0.000	0.000	0.000	0.000
111	A	138	LEU	0	-0.009	-0.010	23.274	-0.296	-0.296	0.000	0.000	0.000	0.000
112	A	139	LEU	0	-0.022	-0.010	22.061	-0.625	-0.625	0.000	0.000	0.000	0.000
113	A	140	GLN	0	0.000	-0.008	22.636	-0.312	-0.312	0.000	0.000	0.000	0.000
114	A	141	GLN	0	-0.009	-0.003	21.896	-0.665	-0.665	0.000	0.000	0.000	0.000
115	A	142	ARG	1	0.854	0.926	12.484	18.200	18.200	0.000	0.000	0.000	0.000
116	A	143	LEU	0	0.016	0.011	18.316	-1.076	-1.076	0.000	0.000	0.000	0.000
117	A	144	ASP	-1	-0.840	-0.912	19.906	-13.185	-13.185	0.000	0.000	0.000	0.000
118	A	145	GLU	-1	-0.895	-0.936	15.416	-18.350	-18.350	0.000	0.000	0.000	0.000
119	A	146	LEU	0	-0.033	-0.019	13.651	-1.393	-1.393	0.000	0.000	0.000	0.000
120	A	147	SER	0	-0.035	-0.020	15.374	-0.952	-0.952	0.000	0.000	0.000	0.000
121	A	148	SER	0	-0.019	-0.007	16.312	-0.245	-0.245	0.000	0.000	0.000	0.000
122	A	149	LEU	0	-0.003	0.006	10.805	-0.809	-0.809	0.000	0.000	0.000	0.000
123	A	150	ILE	0	0.015	0.021	12.173	-2.089	-2.089	0.000	0.000	0.000	0.000
124	A	151	GLY	0	0.019	0.020	13.669	-0.507	-0.507	0.000	0.000	0.000	0.000
125	A	152	GLN	0	-0.054	-0.035	12.391	-0.999	-0.999	0.000	0.000	0.000	0.000
126	A	153	SER	0	0.013	-0.008	9.299	-1.793	-1.793	0.000	0.000	0.000	0.000
127	A	154	THR	0	-0.041	-0.039	10.719	-0.757	-0.757	0.000	0.000	0.000	0.000
128	A	155	ARG	1	0.970	1.000	13.495	18.444	18.444	0.000	0.000	0.000	0.000
129	A	156	GLN	0	0.049	0.035	8.507	-0.136	-0.136	0.000	0.000	0.000	0.000
130	A	157	LYS	1	0.853	0.902	10.629	24.614	24.614	0.000	0.000	0.000	0.000
131	A	158	SER	0	-0.020	-0.020	11.431	1.075	1.075	0.000	0.000	0.000	0.000
132	A	159	LEU	0	0.006	0.007	13.203	0.936	0.936	0.000	0.000	0.000	0.000
133	A	160	ASN	0	0.037	0.009	8.449	2.404	2.404	0.000	0.000	0.000	0.000
134	A	161	ASN	0	-0.047	-0.024	12.125	1.186	1.186	0.000	0.000	0.000	0.000
135	A	162	ALA	0	0.005	0.019	14.578	1.219	1.219	0.000	0.000	0.000	0.000
136	A	163	TYR	0	0.049	0.003	14.869	0.934	0.934	0.000	0.000	0.000	0.000
137	A	164	GLY	0	0.002	0.008	14.847	0.436	0.436	0.000	0.000	0.000	0.000
138	A	165	ARG	1	0.784	0.875	15.422	17.226	17.226	0.000	0.000	0.000	0.000
139	A	166	LEU	0	-0.027	0.001	18.675	0.830	0.830	0.000	0.000	0.000	0.000
140	A	167	SER	0	0.000	-0.010	18.302	0.970	0.970	0.000	0.000	0.000	0.000
141	A	168	GLY	0	-0.001	0.010	18.637	-0.460	-0.460	0.000	0.000	0.000	0.000
142	A	169	MET	0	-0.036	-0.008	14.454	-0.287	-0.287	0.000	0.000	0.000	0.000
143	A	170	LEU	0	0.015	-0.006	12.117	0.507	0.507	0.000	0.000	0.000	0.000
144	A	171	LEU	0	-0.020	-0.009	11.017	-0.196	-0.196	0.000	0.000	0.000	0.000
145	A	172	VAL	0	-0.035	-0.008	6.330	1.483	1.483	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:MET)