FMO DATABASE

FMODB ID: 9R4Z2

Calculation Name: 1V37-A-Xray547

Preferred Name:

Target Type:

Ligand Name: glycerol

Ligand 3-letter code: GOL

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1V37

Chain ID: A

ChEMBL ID:

UniProt ID: Q53WB3

Base Structure: X-ray

Registration Date: 2025-10-05

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	171
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1793170.891876
FMO2-HF: Nuclear repulsion	1728083.296573
FMO2-HF: Total energy	-65087.595303
FMO2-MP2: Total energy	-65283.539194

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:MET)

Summations of interaction energy for fragment #1(A:1: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.
-85.394	-82.365	30.996	-13.939	-20.085	-0.174

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.735 / q_NPA : 0.866

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	LEU	0	-0.024	-0.012	2.793	0.375	4.380	0.662	-1.709	-2.959	-0.013
4	A	4	TRP	0	0.000	-0.023	4.946	2.820	2.879	-0.001	-0.008	-0.050	0.000
124	A	124	LEU	0	-0.039	-0.004	3.888	0.927	1.534	0.093	-0.150	-0.550	0.000
125	A	125	LYS	1	0.876	0.917	2.523	22.780	24.407	0.912	-0.863	-1.675	-0.011
126	A	126	ALA	0	-0.020	-0.012	2.841	-1.925	-1.886	1.935	0.463	-2.437	-0.003
127	A	127	PRO	0	0.020	0.005	2.845	0.806	0.562	3.347	0.135	-3.237	-0.007
128	A	128	ALA	0	0.025	0.014	3.720	4.533	4.596	0.010	0.163	-0.235	0.000
159	A	159	ASP	-1	-0.806	-0.899	1.689	-119.988	-124.531	14.864	-6.424	-3.897	-0.077
160	A	160	TRP	0	0.040	0.040	2.726	7.405	9.250	0.246	-0.712	-1.379	-0.004
161	A	161	PRO	0	-0.030	-0.021	1.872	-37.769	-38.339	8.929	-4.829	-3.531	-0.059
162	A	162	ARG	1	0.907	0.935	4.340	49.649	49.790	-0.001	-0.005	-0.135	0.000
5	A	5	LEU	0	-0.013	0.005	8.368	1.705	1.705	0.000	0.000	0.000	0.000
6	A	6	VAL	0	0.024	0.006	11.076	0.840	0.840	0.000	0.000	0.000	0.000
7	A	7	ARG	1	0.839	0.930	14.661	14.095	14.095	0.000	0.000	0.000	0.000
8	A	8	HIS	0	0.017	-0.016	17.912	0.361	0.361	0.000	0.000	0.000	0.000
9	A	9	GLY	0	0.079	0.039	20.424	0.118	0.118	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.857	-0.873	23.592	-10.131	-10.131	0.000	0.000	0.000	0.000
11	A	11	THR	0	0.032	-0.007	26.533	0.210	0.210	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.056	0.015	29.203	0.004	0.004	0.000	0.000	0.000	0.000
13	A	13	TRP	0	0.049	0.022	30.404	-0.026	-0.026	0.000	0.000	0.000	0.000
14	A	14	ASN	0	-0.018	0.006	27.094	-0.466	-0.466	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.873	0.919	29.605	9.287	9.287	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.858	-0.919	33.022	-8.501	-8.501	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.009	0.023	31.723	0.137	0.137	0.000	0.000	0.000	0.000
18	A	18	ARG	1	0.807	0.877	31.880	8.750	8.750	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.043	-0.009	28.077	-0.393	-0.393	0.000	0.000	0.000	0.000
20	A	20	LEU	0	-0.023	0.004	26.353	0.283	0.283	0.000	0.000	0.000	0.000
21	A	21	GLY	0	0.051	0.009	24.747	-0.554	-0.554	0.000	0.000	0.000	0.000
22	A	22	TRP	0	-0.080	-0.049	22.426	-0.001	-0.001	0.000	0.000	0.000	0.000
23	A	23	THR	0	-0.027	-0.023	26.387	0.331	0.331	0.000	0.000	0.000	0.000
24	A	24	ASP	-1	-0.829	-0.912	26.233	-11.605	-11.605	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.018	-0.002	28.250	0.257	0.257	0.000	0.000	0.000	0.000
26	A	26	PRO	0	0.013	0.003	27.545	-0.474	-0.474	0.000	0.000	0.000	0.000
27	A	27	LEU	0	-0.048	-0.012	23.988	-0.028	-0.028	0.000	0.000	0.000	0.000
28	A	28	THR	0	-0.053	-0.047	28.117	0.354	0.354	0.000	0.000	0.000	0.000
29	A	29	ALA	0	0.040	0.009	29.725	-0.241	-0.241	0.000	0.000	0.000	0.000
30	A	30	GLU	-1	-0.797	-0.892	28.970	-10.540	-10.540	0.000	0.000	0.000	0.000
31	A	31	GLY	0	-0.004	0.001	26.350	-0.380	-0.380	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.801	-0.907	25.314	-10.526	-10.526	0.000	0.000	0.000	0.000
33	A	33	ALA	0	-0.035	-0.010	26.337	-0.209	-0.209	0.000	0.000	0.000	0.000
34	A	34	GLN	0	0.121	0.047	23.649	-0.479	-0.479	0.000	0.000	0.000	0.000
35	A	35	ALA	0	0.001	-0.001	21.712	-0.471	-0.471	0.000	0.000	0.000	0.000
36	A	36	ARG	1	0.856	0.913	22.067	10.026	10.026	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.757	0.872	23.884	11.104	11.104	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.003	0.004	17.492	-0.386	-0.386	0.000	0.000	0.000	0.000
39	A	39	LYS	1	0.853	0.950	18.706	11.642	11.642	0.000	0.000	0.000	0.000
40	A	40	GLY	0	-0.032	-0.011	18.940	0.476	0.476	0.000	0.000	0.000	0.000
41	A	41	ALA	0	-0.009	0.008	18.170	-0.193	-0.193	0.000	0.000	0.000	0.000
42	A	42	LEU	0	-0.033	-0.011	13.290	-1.097	-1.097	0.000	0.000	0.000	0.000
43	A	43	PRO	0	0.033	0.024	10.037	1.052	1.052	0.000	0.000	0.000	0.000
44	A	44	SER	0	0.008	-0.007	12.275	-0.102	-0.102	0.000	0.000	0.000	0.000
45	A	45	LEU	0	-0.034	-0.007	6.478	-0.268	-0.268	0.000	0.000	0.000	0.000
46	A	46	PRO	0	0.000	-0.009	8.395	1.449	1.449	0.000	0.000	0.000	0.000
47	A	47	ALA	0	0.030	0.031	9.508	-1.451	-1.451	0.000	0.000	0.000	0.000
48	A	48	PHE	0	-0.022	-0.009	7.769	1.020	1.020	0.000	0.000	0.000	0.000
49	A	49	SER	0	-0.018	-0.032	12.299	-0.214	-0.214	0.000	0.000	0.000	0.000
50	A	50	SER	0	0.011	0.004	15.333	0.422	0.422	0.000	0.000	0.000	0.000
51	A	51	ASP	-1	-0.781	-0.858	17.705	-12.928	-12.928	0.000	0.000	0.000	0.000
52	A	52	LEU	0	0.017	0.028	20.751	0.652	0.652	0.000	0.000	0.000	0.000
53	A	53	LEU	0	-0.008	-0.021	22.310	-0.461	-0.461	0.000	0.000	0.000	0.000
54	A	54	ARG	1	0.815	0.903	22.967	12.041	12.041	0.000	0.000	0.000	0.000
55	A	55	ALA	0	0.003	0.018	18.452	-0.198	-0.198	0.000	0.000	0.000	0.000
56	A	56	ARG	1	0.909	0.946	19.667	11.720	11.720	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.799	0.883	21.061	10.537	10.537	0.000	0.000	0.000	0.000
58	A	58	THR	0	0.013	-0.023	18.925	0.213	0.213	0.000	0.000	0.000	0.000
59	A	59	ALA	0	0.003	0.007	17.315	-0.141	-0.141	0.000	0.000	0.000	0.000
60	A	60	GLU	-1	-0.853	-0.905	18.651	-11.270	-11.270	0.000	0.000	0.000	0.000
61	A	61	LEU	0	-0.083	-0.037	21.828	0.228	0.228	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.053	0.029	18.268	0.261	0.261	0.000	0.000	0.000	0.000
63	A	63	GLY	0	-0.061	-0.048	19.468	-0.196	-0.196	0.000	0.000	0.000	0.000
64	A	64	PHE	0	-0.015	-0.002	13.337	-0.168	-0.168	0.000	0.000	0.000	0.000
65	A	65	SER	0	-0.009	-0.015	17.497	0.818	0.818	0.000	0.000	0.000	0.000
66	A	66	PRO	0	-0.033	-0.005	14.949	-0.405	-0.405	0.000	0.000	0.000	0.000
67	A	67	ARG	1	0.945	0.976	13.289	17.164	17.164	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.021	-0.022	14.613	-0.729	-0.729	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.021	-0.001	12.728	-0.150	-0.150	0.000	0.000	0.000	0.000
70	A	70	PRO	0	0.021	0.018	16.074	-0.413	-0.413	0.000	0.000	0.000	0.000
71	A	71	GLU	-1	-0.863	-0.940	14.242	-16.803	-16.803	0.000	0.000	0.000	0.000
72	A	72	LEU	0	-0.007	0.013	11.295	-0.572	-0.572	0.000	0.000	0.000	0.000
73	A	73	ARG	1	0.823	0.896	15.288	12.775	12.775	0.000	0.000	0.000	0.000
74	A	74	GLU	-1	-0.770	-0.868	18.465	-15.724	-15.724	0.000	0.000	0.000	0.000
75	A	75	ILE	0	-0.030	0.001	20.604	0.104	0.104	0.000	0.000	0.000	0.000
76	A	76	HIS	0	0.025	0.015	22.270	0.325	0.325	0.000	0.000	0.000	0.000
77	A	77	PHE	0	0.044	-0.001	25.090	0.063	0.063	0.000	0.000	0.000	0.000
78	A	78	GLY	0	0.014	0.014	28.330	0.311	0.311	0.000	0.000	0.000	0.000
79	A	79	ALA	0	-0.043	-0.034	31.005	0.100	0.100	0.000	0.000	0.000	0.000
80	A	80	LEU	0	-0.038	-0.019	31.129	0.213	0.213	0.000	0.000	0.000	0.000
81	A	81	GLU	-1	-0.738	-0.840	27.970	-11.278	-11.278	0.000	0.000	0.000	0.000
82	A	82	GLY	0	0.035	0.009	31.572	0.323	0.323	0.000	0.000	0.000	0.000
83	A	83	ALA	0	-0.033	-0.008	33.450	0.289	0.289	0.000	0.000	0.000	0.000
84	A	84	LEU	0	0.028	0.013	33.417	-0.310	-0.310	0.000	0.000	0.000	0.000
85	A	85	TRP	0	0.029	0.004	28.932	0.039	0.039	0.000	0.000	0.000	0.000
86	A	86	GLU	-1	-0.923	-0.966	33.630	-8.010	-8.010	0.000	0.000	0.000	0.000
87	A	87	THR	0	-0.007	-0.004	36.948	0.118	0.118	0.000	0.000	0.000	0.000
88	A	88	LEU	0	-0.031	0.009	31.470	0.103	0.103	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.771	-0.882	35.942	-8.496	-8.496	0.000	0.000	0.000	0.000
90	A	90	PRO	0	0.054	0.014	34.866	-0.335	-0.335	0.000	0.000	0.000	0.000
91	A	91	ARG	1	0.931	0.969	33.976	8.463	8.463	0.000	0.000	0.000	0.000
92	A	92	TYR	0	-0.002	-0.015	31.133	-0.352	-0.352	0.000	0.000	0.000	0.000
93	A	93	LYS	1	0.824	0.907	29.993	8.569	8.569	0.000	0.000	0.000	0.000
94	A	94	GLU	-1	-0.912	-0.953	29.667	-10.262	-10.262	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.001	0.004	27.931	-0.436	-0.436	0.000	0.000	0.000	0.000
96	A	96	LEU	0	0.001	0.006	25.391	-0.648	-0.648	0.000	0.000	0.000	0.000
97	A	97	LEU	0	-0.022	-0.007	24.835	-0.653	-0.653	0.000	0.000	0.000	0.000
98	A	98	ARG	1	0.906	0.941	24.771	10.814	10.814	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.057	-0.014	17.895	-0.594	-0.594	0.000	0.000	0.000	0.000
100	A	100	GLN	0	0.054	0.015	21.853	-0.250	-0.250	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.022	0.013	24.324	0.418	0.418	0.000	0.000	0.000	0.000
102	A	102	PHE	0	0.039	0.025	25.598	0.499	0.499	0.000	0.000	0.000	0.000
103	A	103	HIS	0	0.026	-0.010	26.426	-0.564	-0.564	0.000	0.000	0.000	0.000
104	A	104	PRO	0	-0.006	0.042	28.078	0.427	0.427	0.000	0.000	0.000	0.000
105	A	105	PRO	0	0.024	-0.010	31.100	-0.065	-0.065	0.000	0.000	0.000	0.000
106	A	106	GLY	0	0.024	0.015	32.531	0.055	0.055	0.000	0.000	0.000	0.000
107	A	107	GLY	0	0.007	0.003	28.705	-0.032	-0.032	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.807	-0.871	21.764	-13.970	-13.970	0.000	0.000	0.000	0.000
109	A	109	SER	0	-0.003	0.001	24.622	-0.113	-0.113	0.000	0.000	0.000	0.000
110	A	110	LEU	0	0.008	-0.005	20.906	-0.421	-0.421	0.000	0.000	0.000	0.000
111	A	111	SER	0	0.004	0.004	20.356	-0.510	-0.510	0.000	0.000	0.000	0.000
112	A	112	ALA	0	0.038	0.026	19.553	-0.722	-0.722	0.000	0.000	0.000	0.000
113	A	113	PHE	0	-0.014	-0.002	18.397	-0.654	-0.654	0.000	0.000	0.000	0.000
114	A	114	GLN	0	0.007	-0.011	16.093	-0.306	-0.306	0.000	0.000	0.000	0.000
115	A	115	GLU	-1	-0.881	-0.911	14.775	-17.563	-17.563	0.000	0.000	0.000	0.000
116	A	116	ARG	1	0.691	0.798	14.771	14.541	14.541	0.000	0.000	0.000	0.000
117	A	117	VAL	0	0.020	0.008	11.930	-0.957	-0.957	0.000	0.000	0.000	0.000
118	A	118	PHE	0	-0.024	-0.036	10.337	-1.906	-1.906	0.000	0.000	0.000	0.000
119	A	119	ARG	1	0.881	0.930	9.893	15.272	15.272	0.000	0.000	0.000	0.000
120	A	120	PHE	0	0.009	0.001	9.286	-0.825	-0.825	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.023	-0.026	6.416	-0.916	-0.916	0.000	0.000	0.000	0.000
122	A	122	GLU	-1	-1.004	-0.983	5.615	-33.040	-33.040	0.000	0.000	0.000	0.000
123	A	123	GLY	0	0.057	0.034	5.724	-0.797	-0.797	0.000	0.000	0.000	0.000
129	A	129	VAL	0	0.009	0.013	6.473	-2.263	-2.263	0.000	0.000	0.000	0.000
130	A	130	LEU	0	-0.027	-0.020	7.255	1.401	1.401	0.000	0.000	0.000	0.000
131	A	131	PHE	0	0.030	0.013	10.964	0.287	0.287	0.000	0.000	0.000	0.000
132	A	132	THR	0	0.009	-0.026	13.642	0.557	0.557	0.000	0.000	0.000	0.000
133	A	133	HIS	0	0.023	0.023	16.368	0.801	0.801	0.000	0.000	0.000	0.000
134	A	134	GLY	0	0.012	0.016	17.604	-0.841	-0.841	0.000	0.000	0.000	0.000
135	A	135	GLY	0	0.013	-0.014	18.778	-0.542	-0.542	0.000	0.000	0.000	0.000
136	A	136	VAL	0	-0.008	-0.002	13.560	-0.517	-0.517	0.000	0.000	0.000	0.000
137	A	137	VAL	0	0.008	0.006	13.865	-1.434	-1.434	0.000	0.000	0.000	0.000
138	A	138	ARG	1	0.846	0.929	14.362	13.306	13.306	0.000	0.000	0.000	0.000
139	A	139	ALA	0	-0.012	-0.016	15.018	-0.062	-0.062	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.001	0.003	9.066	-0.652	-0.652	0.000	0.000	0.000	0.000
141	A	141	LEU	0	-0.014	-0.005	11.258	-1.338	-1.338	0.000	0.000	0.000	0.000
142	A	142	ARG	1	0.917	0.962	13.180	15.717	15.717	0.000	0.000	0.000	0.000
143	A	143	ALA	0	-0.048	-0.013	11.432	0.502	0.502	0.000	0.000	0.000	0.000
144	A	144	LEU	0	-0.056	-0.023	7.138	-1.389	-1.389	0.000	0.000	0.000	0.000
145	A	145	GLY	0	-0.009	0.008	11.259	0.254	0.254	0.000	0.000	0.000	0.000
146	A	146	GLU	-1	-0.857	-0.912	13.753	-20.986	-20.986	0.000	0.000	0.000	0.000
147	A	147	ASP	-1	-0.864	-0.947	16.223	-14.753	-14.753	0.000	0.000	0.000	0.000
148	A	148	GLY	0	0.006	-0.008	16.967	-0.967	-0.967	0.000	0.000	0.000	0.000
149	A	149	LEU	0	-0.051	-0.023	17.948	-0.019	-0.019	0.000	0.000	0.000	0.000
150	A	150	VAL	0	0.034	0.014	16.923	-0.366	-0.366	0.000	0.000	0.000	0.000
151	A	151	PRO	0	0.051	0.028	20.353	0.489	0.489	0.000	0.000	0.000	0.000
152	A	152	PRO	0	-0.069	-0.020	21.151	-0.669	-0.669	0.000	0.000	0.000	0.000
153	A	153	GLY	0	0.017	0.012	20.773	0.267	0.267	0.000	0.000	0.000	0.000
154	A	154	SER	0	-0.069	-0.030	18.953	-0.144	-0.144	0.000	0.000	0.000	0.000
155	A	155	ALA	0	0.040	0.003	13.672	-0.452	-0.452	0.000	0.000	0.000	0.000
156	A	156	VAL	0	-0.012	-0.007	11.655	0.695	0.695	0.000	0.000	0.000	0.000
157	A	157	ALA	0	0.016	0.037	9.104	-1.335	-1.335	0.000	0.000	0.000	0.000
158	A	158	VAL	0	-0.001	-0.012	5.779	2.019	2.019	0.000	0.000	0.000	0.000
163	A	163	ARG	1	0.931	0.944	6.231	35.447	35.447	0.000	0.000	0.000	0.000
164	A	164	VAL	0	0.064	0.044	7.281	-5.136	-5.136	0.000	0.000	0.000	0.000
165	A	165	LEU	0	-0.095	-0.030	5.831	0.986	0.986	0.000	0.000	0.000	0.000
166	A	166	VAL	0	0.032	0.007	9.895	2.403	2.403	0.000	0.000	0.000	0.000
167	A	167	ARG	1	0.799	0.875	13.120	18.299	18.299	0.000	0.000	0.000	0.000
168	A	168	LEU	0	0.000	0.006	15.909	0.716	0.716	0.000	0.000	0.000	0.000
169	A	169	ALA	0	-0.001	-0.009	17.723	-0.066	-0.066	0.000	0.000	0.000	0.000
170	A	170	LEU	0	-0.037	-0.025	20.451	-0.061	-0.061	0.000	0.000	0.000	0.000
171	A	171	ASP	-2	-1.762	-1.859	23.480	-22.660	-22.660	0.000	0.000	0.000	0.000

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