FMO DATABASE

FMODB ID: 17V5Z

Calculation Name: 2BQX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2BQX

Chain ID: A

ChEMBL ID:

UniProt ID: P56153

Base Structure: X-ray

Registration Date: 2023-06-26

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	OptH
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	166
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1689105.470805
FMO2-HF: Nuclear repulsion	1624562.854725
FMO2-HF: Total energy	-64542.61608
FMO2-MP2: Total energy	-64732.265458

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:7:GLU)

Summations of interaction energy for fragment #1(A:7:GLU)

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.
108.658	110.053	-0.023	-0.601	-0.771	0.002

Interaction energy analysis for fragmet #1(A:7:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -1.013 / q_NPA : -1.023

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	9	SER	0	-0.072	-0.053	3.799	-3.675	-2.289	-0.022	-0.581	-0.783	0.002
4	A	10	HIS	0	-0.022	-0.037	6.330	-1.804	-1.804	0.000	0.000	0.000	0.000
5	A	11	ASP	-1	-0.889	-0.942	9.466	18.700	18.700	0.000	0.000	0.000	0.000
6	A	12	ALA	0	0.065	0.033	11.420	0.278	0.278	0.000	0.000	0.000	0.000
7	A	13	ASP	-1	-0.895	-0.939	14.113	15.531	15.531	0.000	0.000	0.000	0.000
8	A	14	SER	0	-0.062	-0.070	8.770	0.286	0.286	0.000	0.000	0.000	0.000
9	A	15	LEU	0	-0.025	0.037	9.003	2.411	2.411	0.000	0.000	0.000	0.000
10	A	16	CYM	-1	-0.853	-0.910	5.743	38.549	38.558	-0.001	-0.020	0.012	0.000
11	A	17	VAL	0	-0.015	-0.015	8.319	-1.693	-1.693	0.000	0.000	0.000	0.000
12	A	18	VAL	0	-0.010	0.000	8.659	1.222	1.222	0.000	0.000	0.000	0.000
13	A	19	ILE	0	-0.058	-0.019	10.989	-1.995	-1.995	0.000	0.000	0.000	0.000
14	A	20	GLU	-1	-0.794	-0.916	14.397	17.590	17.590	0.000	0.000	0.000	0.000
15	A	21	ILE	0	-0.034	-0.016	17.024	-0.899	-0.899	0.000	0.000	0.000	0.000
16	A	22	SER	0	-0.027	-0.011	19.588	0.103	0.103	0.000	0.000	0.000	0.000
17	A	23	LYS	1	0.893	0.930	21.015	-12.760	-12.760	0.000	0.000	0.000	0.000
18	A	24	HIS	0	-0.047	-0.044	23.462	-0.255	-0.255	0.000	0.000	0.000	0.000
19	A	25	SER	0	-0.002	0.024	24.363	-0.646	-0.646	0.000	0.000	0.000	0.000
20	A	26	ASN	0	0.054	0.008	26.395	0.219	0.219	0.000	0.000	0.000	0.000
21	A	27	ILE	0	-0.045	-0.021	24.492	-0.303	-0.303	0.000	0.000	0.000	0.000
22	A	28	LYS	1	0.865	0.929	21.696	-12.944	-12.944	0.000	0.000	0.000	0.000
23	A	29	TYR	0	-0.029	-0.028	19.336	-0.509	-0.509	0.000	0.000	0.000	0.000
24	A	30	GLU	-1	-0.919	-0.965	18.475	14.022	14.022	0.000	0.000	0.000	0.000
25	A	31	LEU	0	-0.075	-0.034	11.507	0.043	0.043	0.000	0.000	0.000	0.000
26	A	32	ASP	-1	-0.763	-0.867	16.023	15.954	15.954	0.000	0.000	0.000	0.000
27	A	33	LYS	1	0.944	0.963	13.737	-17.676	-17.676	0.000	0.000	0.000	0.000
28	A	34	GLU	-1	-1.006	-1.012	14.704	15.064	15.064	0.000	0.000	0.000	0.000
29	A	35	SER	0	-0.071	-0.047	15.998	0.212	0.212	0.000	0.000	0.000	0.000
30	A	36	GLY	0	-0.043	-0.008	13.513	0.534	0.534	0.000	0.000	0.000	0.000
31	A	37	ALA	0	-0.019	-0.002	14.140	0.048	0.048	0.000	0.000	0.000	0.000
32	A	38	LEU	0	-0.001	-0.001	15.946	0.053	0.053	0.000	0.000	0.000	0.000
33	A	39	MET	0	0.005	0.004	18.065	-0.733	-0.733	0.000	0.000	0.000	0.000
34	A	40	VAL	0	-0.033	-0.019	21.330	0.134	0.134	0.000	0.000	0.000	0.000
35	A	41	ASP	-1	-0.842	-0.902	22.908	12.002	12.002	0.000	0.000	0.000	0.000
36	A	42	ARG	1	0.870	0.930	24.888	-10.991	-10.991	0.000	0.000	0.000	0.000
37	A	43	VAL	0	-0.028	0.010	27.018	0.296	0.296	0.000	0.000	0.000	0.000
38	A	44	LEU	0	-0.032	-0.028	28.415	-0.246	-0.246	0.000	0.000	0.000	0.000
39	A	45	TYR	0	0.025	0.009	31.152	-0.252	-0.252	0.000	0.000	0.000	0.000
40	A	46	GLY	0	0.032	0.028	34.248	-0.281	-0.281	0.000	0.000	0.000	0.000
41	A	47	ALA	0	-0.057	-0.021	34.469	0.214	0.214	0.000	0.000	0.000	0.000
42	A	48	GLN	0	-0.032	-0.024	32.020	-0.080	-0.080	0.000	0.000	0.000	0.000
43	A	49	ASN	0	0.003	-0.005	29.015	-0.165	-0.165	0.000	0.000	0.000	0.000
44	A	50	TYR	0	0.058	0.032	24.026	-0.099	-0.099	0.000	0.000	0.000	0.000
45	A	51	PRO	0	-0.047	-0.015	26.247	0.115	0.115	0.000	0.000	0.000	0.000
46	A	52	ALA	0	-0.034	-0.026	22.056	-0.027	-0.027	0.000	0.000	0.000	0.000
47	A	53	ASN	0	0.008	0.023	18.071	-0.258	-0.258	0.000	0.000	0.000	0.000
48	A	54	TYR	0	0.047	0.017	18.846	-0.488	-0.488	0.000	0.000	0.000	0.000
49	A	55	GLY	0	0.046	0.027	14.983	0.338	0.338	0.000	0.000	0.000	0.000
50	A	56	PHE	0	0.069	0.067	10.808	-0.215	-0.215	0.000	0.000	0.000	0.000
51	A	57	VAL	0	0.004	0.015	10.592	1.761	1.761	0.000	0.000	0.000	0.000
52	A	58	PRO	0	0.011	0.020	7.158	-1.097	-1.097	0.000	0.000	0.000	0.000
53	A	59	ASN	0	-0.056	-0.031	6.776	3.241	3.241	0.000	0.000	0.000	0.000
54	A	60	THR	0	0.005	-0.018	10.255	-0.938	-0.938	0.000	0.000	0.000	0.000
55	A	61	LEU	0	-0.042	-0.024	13.438	0.174	0.174	0.000	0.000	0.000	0.000
56	A	62	GLY	0	0.016	0.006	17.072	-0.337	-0.337	0.000	0.000	0.000	0.000
57	A	63	SER	0	-0.093	-0.076	19.733	-0.284	-0.284	0.000	0.000	0.000	0.000
58	A	64	ASP	-1	-0.879	-0.935	21.856	12.838	12.838	0.000	0.000	0.000	0.000
59	A	65	GLY	0	-0.096	-0.045	21.414	-0.165	-0.165	0.000	0.000	0.000	0.000
60	A	66	ASP	-1	-0.867	-0.920	18.637	14.804	14.804	0.000	0.000	0.000	0.000
61	A	67	PRO	0	-0.109	-0.063	13.695	0.151	0.151	0.000	0.000	0.000	0.000
62	A	68	VAL	0	0.032	0.021	14.962	-0.625	-0.625	0.000	0.000	0.000	0.000
63	A	69	ASP	-1	-0.776	-0.891	15.704	15.826	15.826	0.000	0.000	0.000	0.000
64	A	70	ALA	0	-0.039	-0.038	15.543	-0.216	-0.216	0.000	0.000	0.000	0.000
65	A	71	LEU	0	-0.028	-0.006	17.605	0.041	0.041	0.000	0.000	0.000	0.000
66	A	72	VAL	0	-0.005	-0.008	15.092	0.137	0.137	0.000	0.000	0.000	0.000
67	A	73	LEU	0	-0.016	-0.027	18.479	-0.391	-0.391	0.000	0.000	0.000	0.000
68	A	74	SER	0	0.067	0.022	20.145	0.209	0.209	0.000	0.000	0.000	0.000
69	A	75	ASP	-1	-0.871	-0.931	22.270	11.330	11.330	0.000	0.000	0.000	0.000
70	A	76	VAL	0	-0.052	-0.028	20.459	-0.447	-0.447	0.000	0.000	0.000	0.000
71	A	77	ALA	0	-0.011	-0.004	21.494	0.254	0.254	0.000	0.000	0.000	0.000
72	A	78	PHE	0	-0.003	-0.004	16.011	0.176	0.176	0.000	0.000	0.000	0.000
73	A	79	GLN	0	0.011	0.015	16.699	-1.230	-1.230	0.000	0.000	0.000	0.000
74	A	80	ALA	0	0.021	0.031	15.881	1.116	1.116	0.000	0.000	0.000	0.000
75	A	81	GLY	0	0.029	0.000	13.801	-0.269	-0.269	0.000	0.000	0.000	0.000
76	A	82	SER	0	-0.123	-0.062	11.735	1.884	1.884	0.000	0.000	0.000	0.000
77	A	83	VAL	0	0.049	0.014	6.379	-0.599	-0.599	0.000	0.000	0.000	0.000
78	A	84	VAL	0	-0.049	-0.018	9.622	0.628	0.628	0.000	0.000	0.000	0.000
79	A	85	LYS	1	0.962	0.989	5.618	-40.079	-40.079	0.000	0.000	0.000	0.000
80	A	86	ALA	0	0.013	-0.013	10.219	-1.642	-1.642	0.000	0.000	0.000	0.000
81	A	87	ARG	1	0.851	0.950	12.857	-14.233	-14.233	0.000	0.000	0.000	0.000
82	A	88	LEU	0	0.029	-0.001	15.576	-0.694	-0.694	0.000	0.000	0.000	0.000
83	A	89	VAL	0	-0.047	-0.028	18.230	-0.289	-0.289	0.000	0.000	0.000	0.000
84	A	90	GLY	0	0.026	-0.002	21.661	-0.672	-0.672	0.000	0.000	0.000	0.000
85	A	91	VAL	0	-0.003	0.010	22.078	0.702	0.702	0.000	0.000	0.000	0.000
86	A	92	LEU	0	-0.055	-0.017	24.039	-0.615	-0.615	0.000	0.000	0.000	0.000
87	A	93	ASN	0	0.040	0.029	25.771	0.583	0.583	0.000	0.000	0.000	0.000
88	A	94	MET	0	-0.029	-0.027	26.664	-0.420	-0.420	0.000	0.000	0.000	0.000
89	A	95	GLU	-1	-0.860	-0.939	29.431	8.684	8.684	0.000	0.000	0.000	0.000
90	A	96	ASP	-1	-0.785	-0.879	28.496	10.166	10.166	0.000	0.000	0.000	0.000
91	A	97	GLU	-1	-0.926	-0.989	31.178	9.490	9.490	0.000	0.000	0.000	0.000
92	A	98	SER	0	-0.061	-0.039	29.304	-0.184	-0.184	0.000	0.000	0.000	0.000
93	A	99	GLY	0	-0.034	-0.007	30.681	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	100	MET	0	-0.106	-0.052	28.840	-0.162	-0.162	0.000	0.000	0.000	0.000
95	A	101	ASP	-1	-0.753	-0.870	23.835	12.512	12.512	0.000	0.000	0.000	0.000
96	A	102	GLU	-1	-0.870	-0.929	21.565	12.381	12.381	0.000	0.000	0.000	0.000
97	A	103	LYS	1	0.803	0.899	21.307	-12.375	-12.375	0.000	0.000	0.000	0.000
98	A	104	LEU	0	0.020	0.003	16.445	-0.430	-0.430	0.000	0.000	0.000	0.000
99	A	105	ILE	0	-0.039	-0.012	20.124	0.032	0.032	0.000	0.000	0.000	0.000
100	A	106	ALA	0	0.017	-0.003	16.724	0.107	0.107	0.000	0.000	0.000	0.000
101	A	107	LEU	0	-0.021	-0.001	17.836	-0.591	-0.591	0.000	0.000	0.000	0.000
102	A	108	PRO	0	0.030	0.018	15.133	0.947	0.947	0.000	0.000	0.000	0.000
103	A	109	ILE	0	-0.011	0.005	10.938	-0.843	-0.843	0.000	0.000	0.000	0.000
104	A	110	ASP	-1	-0.792	-0.932	15.000	15.091	15.091	0.000	0.000	0.000	0.000
105	A	111	LYS	1	0.852	0.926	11.845	-22.369	-22.369	0.000	0.000	0.000	0.000
106	A	112	ILE	0	-0.066	-0.027	11.435	0.330	0.330	0.000	0.000	0.000	0.000
107	A	113	ASP	-1	-0.807	-0.874	15.577	13.874	13.874	0.000	0.000	0.000	0.000
108	A	114	PRO	0	-0.029	-0.001	19.120	-0.087	-0.087	0.000	0.000	0.000	0.000
109	A	115	THR	0	-0.063	-0.052	21.331	-0.809	-0.809	0.000	0.000	0.000	0.000
110	A	116	HIS	0	-0.006	-0.017	22.757	-0.738	-0.738	0.000	0.000	0.000	0.000
111	A	117	SER	0	-0.021	-0.001	21.982	-0.098	-0.098	0.000	0.000	0.000	0.000
112	A	118	TYR	0	-0.096	-0.056	22.965	-0.098	-0.098	0.000	0.000	0.000	0.000
113	A	119	VAL	0	-0.003	0.013	23.848	-0.323	-0.323	0.000	0.000	0.000	0.000
114	A	120	LYS	1	0.856	0.918	23.147	-11.750	-11.750	0.000	0.000	0.000	0.000
115	A	121	ASP	-1	-0.765	-0.880	23.635	11.843	11.843	0.000	0.000	0.000	0.000
116	A	122	ILE	0	-0.012	0.005	25.667	-0.164	-0.164	0.000	0.000	0.000	0.000
117	A	123	ASP	-1	-0.960	-0.987	27.087	9.960	9.960	0.000	0.000	0.000	0.000
118	A	124	ASP	-1	-0.805	-0.887	27.372	10.448	10.448	0.000	0.000	0.000	0.000
119	A	125	LEU	0	-0.067	-0.023	25.079	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	126	SER	0	0.014	0.011	29.058	-0.312	-0.312	0.000	0.000	0.000	0.000
121	A	127	LYS	1	0.924	0.949	32.081	-8.291	-8.291	0.000	0.000	0.000	0.000
122	A	128	HIS	0	-0.023	-0.016	33.695	0.129	0.129	0.000	0.000	0.000	0.000
123	A	129	THR	0	0.001	-0.010	27.966	0.005	0.005	0.000	0.000	0.000	0.000
124	A	130	LEU	0	0.045	0.024	28.596	0.146	0.146	0.000	0.000	0.000	0.000
125	A	131	ASP	-1	-0.844	-0.928	30.867	8.643	8.643	0.000	0.000	0.000	0.000
126	A	132	LYS	1	0.925	0.967	30.665	-9.759	-9.759	0.000	0.000	0.000	0.000
127	A	133	ILE	0	0.015	0.005	25.684	0.011	0.011	0.000	0.000	0.000	0.000
128	A	134	LYS	1	0.982	0.992	29.347	-8.878	-8.878	0.000	0.000	0.000	0.000
129	A	135	HIS	0	0.028	0.008	31.439	-0.098	-0.098	0.000	0.000	0.000	0.000
130	A	136	PHE	0	-0.019	-0.001	26.829	-0.149	-0.149	0.000	0.000	0.000	0.000
131	A	137	PHE	0	0.022	-0.008	24.242	-0.013	-0.013	0.000	0.000	0.000	0.000
132	A	138	GLU	-1	-0.895	-0.943	30.215	8.618	8.618	0.000	0.000	0.000	0.000
133	A	139	THR	0	0.002	0.000	33.615	-0.162	-0.162	0.000	0.000	0.000	0.000
134	A	140	TYR	0	-0.078	-0.025	26.352	-0.110	-0.110	0.000	0.000	0.000	0.000
135	A	141	LYS	1	0.952	0.977	27.680	-10.475	-10.475	0.000	0.000	0.000	0.000
136	A	142	ASP	-1	-0.887	-0.932	33.318	8.105	8.105	0.000	0.000	0.000	0.000
137	A	143	LEU	0	-0.093	-0.062	36.724	-0.185	-0.185	0.000	0.000	0.000	0.000
138	A	144	GLU	-1	-0.923	-0.957	31.344	9.786	9.786	0.000	0.000	0.000	0.000
139	A	145	PRO	0	-0.001	0.000	35.892	-0.079	-0.079	0.000	0.000	0.000	0.000
140	A	146	ASN	0	-0.078	-0.057	36.557	0.004	0.004	0.000	0.000	0.000	0.000
141	A	147	LYS	1	0.927	0.981	30.023	-9.675	-9.675	0.000	0.000	0.000	0.000
142	A	148	TRP	0	-0.017	0.003	33.846	-0.262	-0.262	0.000	0.000	0.000	0.000
143	A	149	VAL	0	0.044	0.019	30.284	0.220	0.220	0.000	0.000	0.000	0.000
144	A	150	LYS	1	0.837	0.937	33.162	-8.319	-8.319	0.000	0.000	0.000	0.000
145	A	151	VAL	0	-0.013	-0.017	30.798	0.229	0.229	0.000	0.000	0.000	0.000
146	A	152	LYS	1	0.809	0.921	31.817	-9.022	-9.022	0.000	0.000	0.000	0.000
147	A	153	GLY	0	-0.036	-0.030	31.376	-0.304	-0.304	0.000	0.000	0.000	0.000
148	A	154	PHE	0	-0.019	-0.011	26.573	0.157	0.157	0.000	0.000	0.000	0.000
149	A	155	GLU	-1	-0.896	-0.906	27.062	9.973	9.973	0.000	0.000	0.000	0.000
150	A	156	ASN	0	0.034	-0.001	26.638	0.526	0.526	0.000	0.000	0.000	0.000
151	A	157	LYS	1	0.889	0.930	19.256	-14.177	-14.177	0.000	0.000	0.000	0.000
152	A	158	GLU	-1	-0.964	-0.970	22.388	11.104	11.104	0.000	0.000	0.000	0.000
153	A	159	SER	0	-0.070	-0.075	23.760	0.331	0.331	0.000	0.000	0.000	0.000
154	A	160	ALA	0	0.043	0.020	20.735	0.203	0.203	0.000	0.000	0.000	0.000
155	A	161	ILE	0	0.011	0.003	18.497	0.595	0.595	0.000	0.000	0.000	0.000
156	A	162	LYS	1	0.903	0.961	19.167	-11.088	-11.088	0.000	0.000	0.000	0.000
157	A	163	VAL	0	-0.001	0.008	19.961	0.132	0.132	0.000	0.000	0.000	0.000
158	A	164	LEU	0	0.018	0.012	13.310	0.212	0.212	0.000	0.000	0.000	0.000
159	A	165	GLU	-1	-0.924	-0.971	16.118	15.184	15.184	0.000	0.000	0.000	0.000
160	A	166	LYS	1	0.895	0.950	17.282	-11.619	-11.619	0.000	0.000	0.000	0.000
161	A	167	ALA	0	0.062	0.036	16.390	-0.101	-0.101	0.000	0.000	0.000	0.000
162	A	168	ILE	0	-0.007	-0.001	12.118	0.454	0.454	0.000	0.000	0.000	0.000
163	A	169	LYS	1	0.902	0.940	14.353	-12.711	-12.711	0.000	0.000	0.000	0.000
164	A	170	ALA	0	-0.048	-0.016	16.882	-0.198	-0.198	0.000	0.000	0.000	0.000
165	A	171	TYR	0	-0.010	0.014	10.910	0.829	0.829	0.000	0.000	0.000	0.000
166	A	172	GLN	0	-0.072	-0.023	11.728	-1.305	-1.305	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLU)