FMO DATABASE

FMODB ID: 5Q27Z

Calculation Name: 3MW6-A-Xray549

Preferred Name:

Target Type:

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 3MW6

Chain ID: A

ChEMBL ID:

UniProt ID: Q9JY98

Base Structure: X-ray

Registration Date: 2025-10-12

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	OptH
Protonation	MOE:Protonate 3D
Complement	ac.sh, 23 2024 Oct
Water	No
Procedure	Manual calculation
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-945587.276079
FMO2-HF: Nuclear repulsion	898214.437596
FMO2-HF: Total energy	-47372.838483
FMO2-MP2: Total energy	-47512.211239

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:GLN)

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

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.
94.298	96.1	0.041	-0.951	-0.892	-0.003

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.889 / q_NPA : 0.931

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	THR	0	-0.011	0.004	3.342	-8.659	-6.857	0.041	-0.951	-0.892	-0.003
4	A	6	ALA	0	0.038	0.017	6.112	4.233	4.233	0.000	0.000	0.000	0.000
5	A	7	LEU	0	0.060	0.027	9.208	1.689	1.689	0.000	0.000	0.000	0.000
6	A	8	GLY	0	0.038	0.015	8.409	1.694	1.694	0.000	0.000	0.000	0.000
7	A	9	ALA	0	0.036	0.016	7.892	1.817	1.817	0.000	0.000	0.000	0.000
8	A	10	ALA	0	0.017	0.018	9.686	2.120	2.120	0.000	0.000	0.000	0.000
9	A	11	LEU	0	0.009	0.015	12.490	1.460	1.460	0.000	0.000	0.000	0.000
10	A	12	LYS	1	0.834	0.890	7.993	33.089	33.089	0.000	0.000	0.000	0.000
11	A	13	SER	0	-0.004	-0.009	12.784	1.425	1.425	0.000	0.000	0.000	0.000
12	A	14	ALA	0	0.031	0.017	14.891	1.091	1.091	0.000	0.000	0.000	0.000
13	A	15	VAL	0	0.016	0.011	16.242	0.975	0.975	0.000	0.000	0.000	0.000
14	A	16	GLN	0	-0.034	-0.019	13.433	1.052	1.052	0.000	0.000	0.000	0.000
15	A	17	THR	0	-0.054	-0.047	18.152	0.865	0.865	0.000	0.000	0.000	0.000
16	A	18	MET	0	0.029	0.027	20.906	0.813	0.813	0.000	0.000	0.000	0.000
17	A	19	SER	0	-0.019	0.008	22.135	0.715	0.715	0.000	0.000	0.000	0.000
18	A	20	LYS	0	0.114	0.071	23.782	-0.075	-0.075	0.000	0.000	0.000	0.000
19	A	21	LYS	1	0.927	0.977	24.617	11.048	11.048	0.000	0.000	0.000	0.000
20	A	22	LYS	1	0.959	0.991	17.503	14.382	14.382	0.000	0.000	0.000	0.000
21	A	23	GLN	0	0.063	0.003	21.317	-0.158	-0.158	0.000	0.000	0.000	0.000
22	A	24	THR	0	-0.054	-0.035	22.772	0.204	0.204	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.927	-0.978	21.365	-12.249	-12.249	0.000	0.000	0.000	0.000
24	A	26	MET	0	-0.011	0.002	16.428	0.072	0.072	0.000	0.000	0.000	0.000
25	A	27	ILE	0	0.002	0.008	20.315	-0.088	-0.088	0.000	0.000	0.000	0.000
26	A	28	ALA	0	-0.016	-0.011	23.399	0.179	0.179	0.000	0.000	0.000	0.000
27	A	29	ASP	-1	-0.900	-0.947	19.450	-12.816	-12.816	0.000	0.000	0.000	0.000
28	A	30	HIS	0	-0.028	-0.010	19.848	-0.389	-0.389	0.000	0.000	0.000	0.000
29	A	31	ILE	0	-0.023	-0.013	21.149	0.137	0.137	0.000	0.000	0.000	0.000
30	A	32	TYR	0	-0.052	-0.050	24.624	0.311	0.311	0.000	0.000	0.000	0.000
31	A	33	GLY	0	0.020	0.016	21.179	0.162	0.162	0.000	0.000	0.000	0.000
32	A	34	LYS	1	0.910	0.972	21.758	12.413	12.413	0.000	0.000	0.000	0.000
33	A	35	TYR	0	0.067	0.023	23.202	0.171	0.171	0.000	0.000	0.000	0.000
34	A	36	ASP	-1	-0.791	-0.897	27.000	-10.058	-10.058	0.000	0.000	0.000	0.000
35	A	37	VAL	0	-0.018	-0.004	28.952	0.198	0.198	0.000	0.000	0.000	0.000
36	A	38	PHE	0	0.033	0.019	28.654	0.234	0.234	0.000	0.000	0.000	0.000
37	A	39	LYS	1	0.857	0.921	24.237	11.342	11.342	0.000	0.000	0.000	0.000
38	A	40	ARG	1	0.847	0.896	28.794	9.319	9.319	0.000	0.000	0.000	0.000
39	A	41	PHE	0	-0.074	-0.035	30.879	0.272	0.272	0.000	0.000	0.000	0.000
40	A	42	LYS	1	0.838	0.930	34.522	8.504	8.504	0.000	0.000	0.000	0.000
41	A	43	PRO	0	0.030	0.015	36.507	-0.151	-0.151	0.000	0.000	0.000	0.000
42	A	44	LEU	0	0.030	0.014	33.660	-0.061	-0.061	0.000	0.000	0.000	0.000
43	A	45	ALA	0	0.013	0.013	37.389	0.233	0.233	0.000	0.000	0.000	0.000
44	A	46	LEU	0	0.045	0.016	38.774	-0.102	-0.102	0.000	0.000	0.000	0.000
45	A	47	GLY	0	0.038	0.016	38.723	-0.038	-0.038	0.000	0.000	0.000	0.000
46	A	48	ILE	0	-0.025	-0.008	33.274	-0.210	-0.210	0.000	0.000	0.000	0.000
47	A	49	ASP	-1	-0.830	-0.923	33.339	-8.428	-8.428	0.000	0.000	0.000	0.000
48	A	50	GLN	0	-0.017	-0.016	33.162	-0.343	-0.343	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.895	-0.943	33.032	-8.744	-8.744	0.000	0.000	0.000	0.000
50	A	52	LEU	0	-0.059	-0.045	28.088	-0.372	-0.372	0.000	0.000	0.000	0.000
51	A	53	ILE	0	-0.024	-0.020	28.590	-0.398	-0.398	0.000	0.000	0.000	0.000
52	A	54	ALA	0	-0.002	0.007	29.294	-0.262	-0.262	0.000	0.000	0.000	0.000
53	A	55	ALA	0	-0.041	-0.017	27.043	-0.308	-0.308	0.000	0.000	0.000	0.000
54	A	56	LEU	0	-0.112	-0.046	23.330	-0.552	-0.552	0.000	0.000	0.000	0.000
55	A	57	PRO	0	0.059	0.028	24.320	0.013	0.013	0.000	0.000	0.000	0.000
56	A	58	GLN	0	-0.017	-0.004	19.678	0.242	0.242	0.000	0.000	0.000	0.000
57	A	59	TYR	0	-0.029	-0.028	19.365	-0.544	-0.544	0.000	0.000	0.000	0.000
58	A	60	ASP	-1	-0.793	-0.879	24.570	-10.666	-10.666	0.000	0.000	0.000	0.000
59	A	61	ALA	0	0.039	0.010	27.971	0.126	0.126	0.000	0.000	0.000	0.000
60	A	62	ALA	0	0.014	0.003	30.959	0.188	0.188	0.000	0.000	0.000	0.000
61	A	63	LEU	0	-0.052	-0.029	26.740	0.239	0.239	0.000	0.000	0.000	0.000
62	A	64	ILE	0	0.046	0.025	27.024	0.047	0.047	0.000	0.000	0.000	0.000
63	A	65	ALA	0	0.020	0.016	29.342	0.157	0.157	0.000	0.000	0.000	0.000
64	A	66	ARG	1	0.895	0.935	30.325	9.488	9.488	0.000	0.000	0.000	0.000
65	A	67	VAL	0	-0.011	-0.005	26.760	0.195	0.195	0.000	0.000	0.000	0.000
66	A	68	LEU	0	0.018	0.016	30.173	0.139	0.139	0.000	0.000	0.000	0.000
67	A	69	ALA	0	0.038	0.011	32.740	0.219	0.219	0.000	0.000	0.000	0.000
68	A	70	ASN	0	-0.005	-0.002	31.037	0.453	0.453	0.000	0.000	0.000	0.000
69	A	71	HIS	0	0.022	0.031	31.585	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	72	CYS	0	-0.049	-0.037	33.477	0.168	0.168	0.000	0.000	0.000	0.000
71	A	73	ARG	1	0.937	0.969	35.534	8.220	8.220	0.000	0.000	0.000	0.000
72	A	74	ARG	1	0.892	0.963	29.530	9.196	9.196	0.000	0.000	0.000	0.000
73	A	75	PRO	0	0.084	0.032	36.897	0.028	0.028	0.000	0.000	0.000	0.000
74	A	76	ARG	1	0.888	0.964	31.293	8.786	8.786	0.000	0.000	0.000	0.000
75	A	77	TYR	0	0.019	0.025	36.389	0.003	0.003	0.000	0.000	0.000	0.000
76	A	78	LEU	0	0.049	0.025	38.187	0.118	0.118	0.000	0.000	0.000	0.000
77	A	79	LYS	1	0.930	0.957	39.052	7.433	7.433	0.000	0.000	0.000	0.000
78	A	80	ALA	0	-0.036	-0.011	38.932	0.102	0.102	0.000	0.000	0.000	0.000
79	A	81	LEU	0	-0.013	-0.015	41.083	0.087	0.087	0.000	0.000	0.000	0.000
80	A	82	ALA	0	0.036	0.019	43.601	0.135	0.135	0.000	0.000	0.000	0.000
81	A	83	ARG	1	0.933	0.979	40.022	7.218	7.218	0.000	0.000	0.000	0.000
82	A	84	GLY	0	0.035	0.031	44.781	0.112	0.112	0.000	0.000	0.000	0.000
83	A	85	GLY	0	0.010	0.004	44.487	-0.112	-0.112	0.000	0.000	0.000	0.000
84	A	86	LYS	1	0.843	0.902	42.632	6.566	6.566	0.000	0.000	0.000	0.000
85	A	87	ARG	1	0.804	0.893	40.484	6.910	6.910	0.000	0.000	0.000	0.000
86	A	88	PHE	0	-0.003	-0.015	36.064	0.008	0.008	0.000	0.000	0.000	0.000
87	A	89	ASP	-1	-0.780	-0.897	35.112	-8.595	-8.595	0.000	0.000	0.000	0.000
88	A	90	LEU	0	0.007	-0.005	29.269	-0.105	-0.105	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.049	-0.010	30.153	-0.581	-0.581	0.000	0.000	0.000	0.000
90	A	92	ASN	0	-0.012	-0.008	31.200	0.294	0.294	0.000	0.000	0.000	0.000
91	A	93	ARG	1	0.949	0.980	33.772	8.507	8.507	0.000	0.000	0.000	0.000
92	A	94	PHE	0	-0.002	-0.010	37.226	-0.023	-0.023	0.000	0.000	0.000	0.000
93	A	95	LYS	1	0.909	0.958	37.733	7.993	7.993	0.000	0.000	0.000	0.000
94	A	96	GLY	0	0.065	0.043	41.379	-0.046	-0.046	0.000	0.000	0.000	0.000
95	A	97	GLU	-1	-0.858	-0.935	43.973	-6.581	-6.581	0.000	0.000	0.000	0.000
96	A	98	VAL	0	-0.076	-0.013	43.661	-0.030	-0.030	0.000	0.000	0.000	0.000
97	A	99	THR	0	0.010	-0.005	46.139	0.136	0.136	0.000	0.000	0.000	0.000
98	A	100	PRO	0	0.058	0.001	49.769	-0.050	-0.050	0.000	0.000	0.000	0.000
99	A	101	GLU	-1	-0.910	-0.934	51.910	-5.776	-5.776	0.000	0.000	0.000	0.000
100	A	102	GLU	-1	-0.799	-0.889	46.117	-6.627	-6.627	0.000	0.000	0.000	0.000
101	A	103	GLN	0	-0.049	-0.027	47.920	-0.018	-0.018	0.000	0.000	0.000	0.000
102	A	104	ALA	0	0.027	0.017	48.928	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	105	ILE	0	-0.009	-0.005	48.066	0.013	0.013	0.000	0.000	0.000	0.000
104	A	106	ALA	0	-0.047	-0.021	45.567	-0.048	-0.048	0.000	0.000	0.000	0.000
105	A	107	GLN	0	-0.043	-0.046	47.275	0.043	0.043	0.000	0.000	0.000	0.000
106	A	108	ASN	0	-0.040	-0.009	49.533	0.065	0.065	0.000	0.000	0.000	0.000
107	A	109	HIS	0	0.031	0.030	44.685	0.051	0.051	0.000	0.000	0.000	0.000
108	A	110	PRO	0	0.037	0.006	47.990	-0.059	-0.059	0.000	0.000	0.000	0.000
109	A	111	PHE	0	0.022	-0.001	42.152	-0.040	-0.040	0.000	0.000	0.000	0.000
110	A	112	VAL	0	-0.026	-0.006	43.866	-0.148	-0.148	0.000	0.000	0.000	0.000
111	A	113	GLN	0	0.049	0.027	45.502	-0.046	-0.046	0.000	0.000	0.000	0.000
112	A	114	GLN	0	-0.021	-0.002	43.767	-0.090	-0.090	0.000	0.000	0.000	0.000
113	A	115	ALA	0	0.003	-0.007	41.740	-0.042	-0.042	0.000	0.000	0.000	0.000
114	A	116	LEU	0	-0.017	-0.018	43.400	-0.116	-0.116	0.000	0.000	0.000	0.000
115	A	117	GLN	0	0.012	0.024	46.072	-0.019	-0.019	0.000	0.000	0.000	0.000
116	A	118	GLN	0	-0.006	-0.003	41.737	-0.090	-0.090	0.000	0.000	0.000	0.000
117	A	119	GLN	0	0.005	-0.003	41.306	-0.181	-0.181	0.000	0.000	0.000	0.000
118	A	120	SER	0	-0.046	-0.036	43.031	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	121	ALA	0	0.039	0.019	45.690	0.026	0.026	0.000	0.000	0.000	0.000
120	A	122	GLN	0	-0.098	-0.048	38.960	-0.178	-0.178	0.000	0.000	0.000	0.000
121	A	123	ALA	0	-0.074	-0.035	42.084	-0.126	-0.126	0.000	0.000	0.000	0.000
122	A	124	ALA	-1	-0.932	-0.936	44.325	-6.224	-6.224	0.000	0.000	0.000	0.000

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