FMO DATABASE

FMODB ID: 824VY

Calculation Name: 2ESR-A-Xray372

Preferred Name:

Target Type:

Ligand Name: alpha-d-glucopyranose

ligand 3-letter code: GLC

PDB ID: 2ESR

Chain ID: A

ChEMBL ID:

UniProt ID: Q5XAY9

Base Structure: X-ray

Registration Date: 2023-06-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	160
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1571053.861952
FMO2-HF: Nuclear repulsion	1508945.648277
FMO2-HF: Total energy	-62108.213675
FMO2-MP2: Total energy	-62288.242769

3D Structure

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:28:VAL)

Summations of interaction energy for fragment #1(A:28: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.
-9.772	-3.433	1.282	-2.867	-4.757	-0.011

Interaction energy analysis for fragmet #1(A:28:VAL)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.049 / q_NPA : 0.012

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	30	GLY	0	0.002	0.013	3.179	-3.478	-1.365	-0.001	-0.964	-1.149	0.002
4	A	31	ALA	0	-0.022	-0.011	3.362	-0.642	-0.056	0.030	-0.141	-0.475	0.000
5	A	32	ILE	0	0.064	0.030	2.334	-0.340	0.422	0.791	-0.398	-1.155	-0.003
6	A	33	PHE	0	0.020	-0.016	5.488	0.216	0.216	0.000	0.000	0.000	0.000
7	A	34	ASN	0	-0.011	0.010	8.022	0.159	0.159	0.000	0.000	0.000	0.000
8	A	35	MET	0	-0.081	-0.022	8.226	-0.035	-0.035	0.000	0.000	0.000	0.000
9	A	36	ILE	0	0.003	-0.002	9.516	0.048	0.048	0.000	0.000	0.000	0.000
10	A	37	GLY	0	0.019	0.041	11.699	0.044	0.044	0.000	0.000	0.000	0.000
11	A	38	PRO	0	-0.077	-0.039	11.893	-0.020	-0.020	0.000	0.000	0.000	0.000
12	A	39	TYR	0	0.014	0.000	13.059	0.094	0.094	0.000	0.000	0.000	0.000
13	A	40	PHE	0	0.011	-0.009	12.102	-0.045	-0.045	0.000	0.000	0.000	0.000
14	A	41	ASN	0	-0.031	-0.021	17.898	0.019	0.019	0.000	0.000	0.000	0.000
15	A	42	GLY	0	0.027	0.023	20.447	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	43	GLY	0	0.044	0.012	20.703	-0.015	-0.015	0.000	0.000	0.000	0.000
17	A	44	ARG	1	0.875	0.934	20.523	0.010	0.010	0.000	0.000	0.000	0.000
18	A	45	VAL	0	0.022	0.001	14.013	-0.019	-0.019	0.000	0.000	0.000	0.000
19	A	46	LEU	0	-0.018	-0.001	16.471	0.020	0.020	0.000	0.000	0.000	0.000
20	A	47	ASP	-1	-0.852	-0.947	12.310	-0.116	-0.116	0.000	0.000	0.000	0.000
21	A	48	LEU	0	0.027	0.008	14.797	0.038	0.038	0.000	0.000	0.000	0.000
22	A	49	PHE	0	-0.007	-0.018	14.120	-0.040	-0.040	0.000	0.000	0.000	0.000
23	A	50	ALA	0	0.033	0.025	13.084	-0.044	-0.044	0.000	0.000	0.000	0.000
24	A	51	GLY	0	0.078	0.050	12.061	0.025	0.025	0.000	0.000	0.000	0.000
25	A	52	SER	0	-0.041	-0.045	10.178	0.037	0.037	0.000	0.000	0.000	0.000
26	A	53	GLY	0	0.019	0.010	11.868	0.103	0.103	0.000	0.000	0.000	0.000
27	A	54	GLY	0	-0.034	-0.020	8.092	0.068	0.068	0.000	0.000	0.000	0.000
28	A	55	LEU	0	0.024	0.004	4.992	0.311	0.311	0.000	0.000	0.000	0.000
29	A	56	ALA	0	0.090	0.045	8.868	0.040	0.040	0.000	0.000	0.000	0.000
30	A	57	ILE	0	-0.017	-0.010	11.741	0.019	0.019	0.000	0.000	0.000	0.000
31	A	58	GLU	-1	-0.823	-0.881	8.112	1.730	1.730	0.000	0.000	0.000	0.000
32	A	59	ALA	0	0.025	0.000	10.914	-0.052	-0.052	0.000	0.000	0.000	0.000
33	A	60	VAL	0	-0.027	-0.007	12.656	-0.033	-0.033	0.000	0.000	0.000	0.000
34	A	61	SER	0	-0.063	-0.022	13.126	-0.055	-0.055	0.000	0.000	0.000	0.000
35	A	62	ARG	1	0.784	0.880	8.282	-0.797	-0.797	0.000	0.000	0.000	0.000
36	A	63	GLY	0	0.029	0.012	14.772	-0.052	-0.052	0.000	0.000	0.000	0.000
37	A	64	MET	0	-0.065	0.007	15.412	-0.037	-0.037	0.000	0.000	0.000	0.000
38	A	65	SER	0	0.006	-0.003	18.095	0.027	0.027	0.000	0.000	0.000	0.000
39	A	66	ALA	0	-0.029	-0.005	20.412	0.017	0.017	0.000	0.000	0.000	0.000
40	A	67	ALA	0	0.010	0.006	16.712	-0.013	-0.013	0.000	0.000	0.000	0.000
41	A	68	VAL	0	-0.002	0.014	18.731	0.012	0.012	0.000	0.000	0.000	0.000
42	A	69	LEU	0	-0.009	-0.009	14.942	-0.015	-0.015	0.000	0.000	0.000	0.000
43	A	70	VAL	0	0.005	0.006	17.580	0.011	0.011	0.000	0.000	0.000	0.000
44	A	71	GLU	-1	-0.818	-0.903	15.947	-0.143	-0.143	0.000	0.000	0.000	0.000
45	A	72	LYS	1	0.872	0.940	18.746	0.070	0.070	0.000	0.000	0.000	0.000
46	A	73	ASN	0	-0.044	-0.021	18.585	0.036	0.036	0.000	0.000	0.000	0.000
47	A	74	ARG	1	0.964	0.934	20.272	-0.005	-0.005	0.000	0.000	0.000	0.000
48	A	75	LYS	1	0.913	0.949	19.053	0.034	0.034	0.000	0.000	0.000	0.000
49	A	76	ALA	0	0.004	0.018	15.808	0.028	0.028	0.000	0.000	0.000	0.000
50	A	77	GLN	0	0.093	0.038	16.897	0.044	0.044	0.000	0.000	0.000	0.000
51	A	78	ALA	0	-0.025	-0.003	19.421	0.022	0.022	0.000	0.000	0.000	0.000
52	A	79	ILE	0	0.027	0.013	13.623	0.024	0.024	0.000	0.000	0.000	0.000
53	A	80	ILE	0	0.008	0.009	14.575	0.061	0.061	0.000	0.000	0.000	0.000
54	A	81	GLN	0	-0.025	-0.027	16.258	0.017	0.017	0.000	0.000	0.000	0.000
55	A	82	ASP	-1	-0.874	-0.923	17.913	0.241	0.241	0.000	0.000	0.000	0.000
56	A	83	ASN	0	-0.089	-0.065	12.556	0.151	0.151	0.000	0.000	0.000	0.000
57	A	84	ILE	0	0.020	0.011	15.818	0.041	0.041	0.000	0.000	0.000	0.000
58	A	85	ILE	0	0.053	0.058	17.922	0.002	0.002	0.000	0.000	0.000	0.000
59	A	86	MET	0	-0.033	-0.003	15.167	0.006	0.006	0.000	0.000	0.000	0.000
60	A	87	THR	0	-0.056	-0.041	15.691	0.012	0.012	0.000	0.000	0.000	0.000
61	A	88	LYS	1	0.812	0.902	18.230	-0.417	-0.417	0.000	0.000	0.000	0.000
62	A	89	ALA	0	0.012	-0.002	20.303	-0.031	-0.031	0.000	0.000	0.000	0.000
63	A	90	GLU	-1	-0.866	-0.945	20.947	0.176	0.176	0.000	0.000	0.000	0.000
64	A	91	ASN	0	-0.023	-0.012	21.980	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	92	ARG	1	0.816	0.915	20.451	-0.211	-0.211	0.000	0.000	0.000	0.000
66	A	93	PHE	0	0.003	-0.001	15.664	-0.002	-0.002	0.000	0.000	0.000	0.000
67	A	94	THR	0	-0.003	0.009	20.760	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	95	LEU	0	-0.039	-0.003	18.510	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	96	LEU	0	0.014	-0.001	21.400	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	97	LYN	0	0.050	0.045	21.937	-0.009	-0.009	0.000	0.000	0.000	0.000
71	A	98	MET	0	-0.097	-0.053	23.005	0.005	0.005	0.000	0.000	0.000	0.000
72	A	99	GLU	-1	-0.823	-0.915	22.544	-0.096	-0.096	0.000	0.000	0.000	0.000
73	A	100	ALA	0	0.019	0.013	19.678	0.009	0.009	0.000	0.000	0.000	0.000
74	A	101	GLU	-1	-0.896	-0.950	21.736	-0.120	-0.120	0.000	0.000	0.000	0.000
75	A	102	ARG	0	0.121	0.058	24.810	0.009	0.009	0.000	0.000	0.000	0.000
76	A	103	ALA	0	-0.009	-0.017	22.866	0.008	0.008	0.000	0.000	0.000	0.000
77	A	104	ILE	0	0.031	0.010	21.393	0.009	0.009	0.000	0.000	0.000	0.000
78	A	105	ASP	-1	-0.856	-0.925	24.929	-0.065	-0.065	0.000	0.000	0.000	0.000
79	A	106	CYS	0	-0.113	-0.051	27.593	0.009	0.009	0.000	0.000	0.000	0.000
80	A	107	LEU	0	-0.060	-0.010	22.225	0.010	0.010	0.000	0.000	0.000	0.000
81	A	108	THR	0	0.011	-0.010	26.680	-0.001	-0.001	0.000	0.000	0.000	0.000
82	A	109	GLY	0	-0.029	-0.001	26.580	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	110	ARG	1	0.842	0.908	24.989	0.053	0.053	0.000	0.000	0.000	0.000
84	A	111	PHE	0	-0.006	-0.019	19.501	0.016	0.016	0.000	0.000	0.000	0.000
85	A	112	ASP	-1	-0.804	-0.891	19.442	-0.033	-0.033	0.000	0.000	0.000	0.000
86	A	113	LEU	0	-0.045	-0.011	12.092	-0.013	-0.013	0.000	0.000	0.000	0.000
87	A	114	VAL	0	0.015	0.002	15.041	0.031	0.031	0.000	0.000	0.000	0.000
88	A	115	PHE	0	-0.015	-0.009	8.501	-0.029	-0.029	0.000	0.000	0.000	0.000
89	A	116	LEU	0	0.007	-0.013	11.420	0.066	0.066	0.000	0.000	0.000	0.000
90	A	117	ASP	-1	-0.885	-0.946	8.325	-1.067	-1.067	0.000	0.000	0.000	0.000
91	A	118	PRO	0	-0.022	0.012	11.042	0.059	0.059	0.000	0.000	0.000	0.000
92	A	119	PRO	0	0.027	0.008	13.881	-0.048	-0.048	0.000	0.000	0.000	0.000
93	A	120	TYR	0	0.007	-0.008	16.147	0.012	0.012	0.000	0.000	0.000	0.000
94	A	121	ALA	0	0.043	0.035	13.483	0.020	0.020	0.000	0.000	0.000	0.000
95	A	122	LYS	1	0.892	0.932	15.325	0.274	0.274	0.000	0.000	0.000	0.000
96	A	123	GLU	-1	-0.837	-0.912	17.557	-0.228	-0.228	0.000	0.000	0.000	0.000
97	A	124	THR	0	0.017	-0.013	17.517	0.033	0.033	0.000	0.000	0.000	0.000
98	A	125	ILE	0	-0.014	0.005	12.985	0.015	0.015	0.000	0.000	0.000	0.000
99	A	126	VAL	0	0.023	0.008	17.434	0.020	0.020	0.000	0.000	0.000	0.000
100	A	127	ALA	0	0.017	0.014	20.755	0.019	0.019	0.000	0.000	0.000	0.000
101	A	128	THR	0	-0.017	-0.026	18.420	0.024	0.024	0.000	0.000	0.000	0.000
102	A	129	ILE	0	-0.008	-0.009	16.544	0.017	0.017	0.000	0.000	0.000	0.000
103	A	130	GLU	-1	-0.867	-0.940	20.731	-0.135	-0.135	0.000	0.000	0.000	0.000
104	A	131	ALA	0	-0.018	0.000	23.838	0.017	0.017	0.000	0.000	0.000	0.000
105	A	132	LEU	0	-0.034	-0.032	19.199	0.015	0.015	0.000	0.000	0.000	0.000
106	A	133	ALA	0	0.011	0.004	23.543	0.014	0.014	0.000	0.000	0.000	0.000
107	A	134	ALA	0	0.001	0.010	25.363	0.012	0.012	0.000	0.000	0.000	0.000
108	A	135	LYS	1	0.792	0.897	26.771	0.075	0.075	0.000	0.000	0.000	0.000
109	A	136	ASN	0	-0.062	-0.023	27.539	0.009	0.009	0.000	0.000	0.000	0.000
110	A	137	LEU	0	0.021	0.015	23.723	0.008	0.008	0.000	0.000	0.000	0.000
111	A	138	LEU	0	-0.010	0.007	20.010	0.001	0.001	0.000	0.000	0.000	0.000
112	A	139	SER	0	-0.027	-0.022	22.283	0.002	0.002	0.000	0.000	0.000	0.000
113	A	140	GLU	-1	-0.798	-0.913	23.267	-0.078	-0.078	0.000	0.000	0.000	0.000
114	A	141	GLN	0	-0.049	-0.021	21.940	-0.016	-0.016	0.000	0.000	0.000	0.000
115	A	142	VAL	0	-0.031	0.013	18.136	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	143	MET	0	-0.042	-0.011	14.259	-0.025	-0.025	0.000	0.000	0.000	0.000
117	A	144	VAL	0	0.040	0.018	14.790	0.008	0.008	0.000	0.000	0.000	0.000
118	A	145	VAL	0	-0.050	-0.026	8.351	-0.050	-0.050	0.000	0.000	0.000	0.000
119	A	146	CYS	0	-0.001	0.007	10.634	0.036	0.036	0.000	0.000	0.000	0.000
120	A	147	GLU	-1	-0.886	-0.928	3.058	-7.130	-5.194	0.200	-1.094	-1.043	-0.009
121	A	148	THR	0	0.041	0.013	7.698	0.179	0.179	0.000	0.000	0.000	0.000
122	A	149	ASP	-1	-0.864	-0.933	7.988	-1.038	-1.038	0.000	0.000	0.000	0.000
123	A	150	LYS	1	0.861	0.916	9.669	0.770	0.770	0.000	0.000	0.000	0.000
124	A	151	THR	0	-0.023	-0.018	10.892	0.045	0.045	0.000	0.000	0.000	0.000
125	A	152	VAL	0	-0.005	0.021	12.875	0.081	0.081	0.000	0.000	0.000	0.000
126	A	153	LEU	0	-0.032	-0.013	14.433	-0.027	-0.027	0.000	0.000	0.000	0.000
127	A	154	LEU	0	0.003	0.000	13.388	0.023	0.023	0.000	0.000	0.000	0.000
128	A	155	PRO	0	0.009	0.017	17.539	0.008	0.008	0.000	0.000	0.000	0.000
129	A	156	LYS	1	1.001	0.987	19.607	0.214	0.214	0.000	0.000	0.000	0.000
130	A	157	GLU	-1	-0.923	-0.953	21.160	-0.162	-0.162	0.000	0.000	0.000	0.000
131	A	158	ILE	0	-0.039	-0.016	18.802	-0.007	-0.007	0.000	0.000	0.000	0.000
132	A	159	ALA	0	0.038	0.037	22.871	0.003	0.003	0.000	0.000	0.000	0.000
133	A	160	THR	0	-0.007	0.000	25.194	0.001	0.001	0.000	0.000	0.000	0.000
134	A	161	LEU	0	-0.070	-0.033	19.375	0.000	0.000	0.000	0.000	0.000	0.000
135	A	162	GLY	0	0.079	0.031	21.014	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	163	ILE	0	-0.093	-0.037	15.539	-0.008	-0.008	0.000	0.000	0.000	0.000
137	A	164	TRP	0	-0.004	0.005	14.166	0.016	0.016	0.000	0.000	0.000	0.000
138	A	165	LYS	1	0.834	0.902	12.820	0.278	0.278	0.000	0.000	0.000	0.000
139	A	166	GLU	-1	-0.831	-0.912	11.721	-0.483	-0.483	0.000	0.000	0.000	0.000
140	A	167	LYS	1	0.881	0.953	8.421	0.651	0.651	0.000	0.000	0.000	0.000
141	A	168	ILE	0	0.038	0.020	8.233	-0.165	-0.165	0.000	0.000	0.000	0.000
142	A	169	TYR	0	-0.020	-0.025	2.702	-0.043	0.639	0.260	-0.228	-0.714	-0.001
143	A	170	GLY	0	0.023	0.030	5.393	-0.318	-0.318	0.000	0.000	0.000	0.000
144	A	171	ILE	0	-0.039	-0.054	6.133	0.231	0.231	0.000	0.000	0.000	0.000
145	A	172	SER	0	-0.014	-0.005	3.474	0.117	0.311	0.003	-0.039	-0.159	0.000
146	A	173	LYS	1	0.884	0.931	6.471	0.796	0.796	0.000	0.000	0.000	0.000
147	A	174	VAL	0	0.005	0.019	4.743	-0.152	-0.086	-0.001	-0.003	-0.062	0.000
148	A	175	THR	0	0.000	-0.008	7.902	0.164	0.164	0.000	0.000	0.000	0.000
149	A	176	VAL	0	-0.017	-0.012	10.753	-0.010	-0.010	0.000	0.000	0.000	0.000
150	A	177	TYR	0	0.014	-0.018	13.043	0.012	0.012	0.000	0.000	0.000	0.000
151	A	178	VAL	0	-0.033	-0.015	16.645	0.006	0.006	0.000	0.000	0.000	0.000
152	A	179	ASN	0	0.041	0.005	19.266	-0.009	-0.009	0.000	0.000	0.000	0.000
153	A	180	GLU	-1	-0.882	-0.949	23.036	-0.101	-0.101	0.000	0.000	0.000	0.000
154	A	181	GLY	0	-0.004	0.003	25.629	0.003	0.003	0.000	0.000	0.000	0.000
155	A	182	HIS	0	-0.043	0.006	18.783	0.007	0.007	0.000	0.000	0.000	0.000
156	A	183	HIS	0	0.033	0.016	23.238	-0.004	-0.004	0.000	0.000	0.000	0.000
157	A	184	HIS	0	-0.006	-0.004	21.773	-0.017	-0.017	0.000	0.000	0.000	0.000
158	A	185	HIS	1	0.838	0.895	16.496	0.123	0.123	0.000	0.000	0.000	0.000
159	A	186	HIS	0	-0.011	0.009	18.068	-0.020	-0.020	0.000	0.000	0.000	0.000
160	A	187	HIS	0	0.021	0.005	18.417	-0.005	-0.005	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:28:VAL)