FMO DATABASE

FMODB ID: 4J6NN

Calculation Name: 3EJG-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EJG

Chain ID: A

ChEMBL ID:

UniProt ID: P0C6X1

Base Structure: X-ray

Registration Date: 2023-09-22

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	165
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1627879.420707
FMO2-HF: Nuclear repulsion	1564960.188544
FMO2-HF: Total energy	-62919.232163
FMO2-MP2: Total energy	-63103.433367

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:1:GLU)

Summations of interaction energy for fragment #1(A:1: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.
-17.159	-30.03	61.112	-25.466	-22.778	0.199

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.774 / q_NPA : -0.837

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	-0.035	0.001	3.056	-7.878	-5.105	0.027	-1.172	-1.627	0.002
4	A	4	ASN	0	-0.001	-0.008	2.634	9.941	11.157	0.658	-0.749	-1.126	-0.011
5	A	5	ALA	0	0.044	0.030	4.508	-3.400	-3.144	-0.001	-0.017	-0.239	0.000
6	A	6	PHE	0	-0.074	-0.055	5.973	-4.790	-4.790	0.000	0.000	0.000	0.000
7	A	7	LEU	0	-0.007	-0.017	8.860	-3.217	-3.217	0.000	0.000	0.000	0.000
8	A	8	VAL	0	-0.003	0.000	6.876	3.643	3.643	0.000	0.000	0.000	0.000
9	A	9	HIS	0	-0.034	-0.018	9.614	-2.104	-2.104	0.000	0.000	0.000	0.000
10	A	10	ASP	-1	-0.879	-0.943	12.803	19.284	19.284	0.000	0.000	0.000	0.000
11	A	11	ASN	0	-0.058	-0.038	11.252	1.061	1.061	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.004	0.000	10.039	2.222	2.222	0.000	0.000	0.000	0.000
13	A	13	ALA	0	0.014	0.026	5.461	-0.919	-0.919	0.000	0.000	0.000	0.000
14	A	14	PHE	0	0.016	-0.007	7.491	0.247	0.247	0.000	0.000	0.000	0.000
15	A	15	TYR	0	-0.012	-0.050	1.564	-31.891	-41.265	24.147	-9.763	-5.011	0.085
16	A	16	GLN	0	-0.053	-0.051	8.128	-2.851	-2.851	0.000	0.000	0.000	0.000
17	A	17	GLY	0	0.014	0.002	9.947	1.294	1.294	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.864	-0.907	11.781	20.447	20.447	0.000	0.000	0.000	0.000
19	A	19	VAL	0	0.018	-0.012	11.843	1.626	1.626	0.000	0.000	0.000	0.000
20	A	20	ASP	-1	-0.903	-0.948	11.256	20.687	20.687	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.025	-0.025	8.901	1.411	1.411	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.017	-0.016	7.157	2.974	2.974	0.000	0.000	0.000	0.000
23	A	23	VAL	0	-0.040	-0.025	6.540	4.326	4.326	0.000	0.000	0.000	0.000
24	A	24	ASN	0	-0.083	-0.055	7.332	0.836	0.836	0.000	0.000	0.000	0.000
25	A	25	GLY	0	-0.031	-0.005	4.514	-0.475	-0.278	-0.001	-0.063	-0.133	0.000
26	A	26	VAL	0	-0.047	-0.020	2.357	-2.416	0.521	5.836	-3.964	-4.810	0.010
27	A	27	ASP	-1	-0.934	-0.960	1.758	30.705	23.463	16.127	-4.178	-4.708	0.038
28	A	28	PHE	0	0.008	-0.010	3.712	2.583	3.034	0.011	0.065	-0.527	0.002
29	A	29	ASP	-1	-0.797	-0.873	6.492	26.268	26.268	0.000	0.000	0.000	0.000
30	A	30	PHE	0	-0.067	-0.045	10.250	-2.839	-2.839	0.000	0.000	0.000	0.000
31	A	31	ILE	0	0.000	0.021	10.349	1.676	1.676	0.000	0.000	0.000	0.000
32	A	32	VAL	0	-0.018	-0.019	11.864	-2.477	-2.477	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.028	-0.029	14.697	0.488	0.488	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.012	0.008	17.520	-0.550	-0.550	0.000	0.000	0.000	0.000
35	A	35	ALA	0	-0.011	0.007	19.808	-0.603	-0.603	0.000	0.000	0.000	0.000
36	A	36	ASN	0	-0.016	-0.036	22.831	-0.533	-0.533	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.786	-0.885	26.595	9.915	9.915	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.029	-0.016	28.991	-0.309	-0.309	0.000	0.000	0.000	0.000
39	A	39	LEU	0	-0.005	0.008	24.005	-0.025	-0.025	0.000	0.000	0.000	0.000
40	A	40	ALA	0	0.028	0.031	26.679	-0.018	-0.018	0.000	0.000	0.000	0.000
41	A	41	HIS	0	0.024	-0.003	23.158	0.130	0.130	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.008	-0.014	25.182	0.088	0.088	0.000	0.000	0.000	0.000
43	A	43	GLY	0	0.005	-0.010	25.503	-0.292	-0.292	0.000	0.000	0.000	0.000
44	A	44	GLY	0	-0.017	-0.005	22.383	0.338	0.338	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.060	0.032	15.081	-0.204	-0.204	0.000	0.000	0.000	0.000
46	A	46	ALA	0	0.054	0.040	18.778	0.338	0.338	0.000	0.000	0.000	0.000
47	A	47	LYS	1	0.855	0.930	20.796	-12.454	-12.454	0.000	0.000	0.000	0.000
48	A	48	ALA	0	0.012	0.004	17.923	-0.124	-0.124	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.049	0.024	14.318	0.246	0.246	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.833	-0.919	17.950	12.853	12.853	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.025	-0.023	20.237	-0.377	-0.377	0.000	0.000	0.000	0.000
52	A	52	TYR	0	0.038	0.043	12.460	-0.223	-0.223	0.000	0.000	0.000	0.000
53	A	53	THR	0	-0.046	-0.024	17.481	-0.307	-0.307	0.000	0.000	0.000	0.000
54	A	54	LYS	1	0.918	0.949	19.245	-15.142	-15.142	0.000	0.000	0.000	0.000
55	A	55	GLY	0	0.017	0.020	22.471	-0.606	-0.606	0.000	0.000	0.000	0.000
56	A	56	LYS	1	0.755	0.856	21.401	-14.183	-14.183	0.000	0.000	0.000	0.000
57	A	57	LEU	0	0.076	0.035	19.312	-0.365	-0.365	0.000	0.000	0.000	0.000
58	A	58	GLN	0	-0.010	0.009	22.446	-0.293	-0.293	0.000	0.000	0.000	0.000
59	A	59	ARG	1	0.822	0.908	25.809	-11.796	-11.796	0.000	0.000	0.000	0.000
60	A	60	LEU	0	0.035	0.012	22.978	-0.410	-0.410	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.002	0.001	24.202	-0.071	-0.071	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.924	0.960	26.475	-9.808	-9.808	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.838	-0.912	29.397	10.355	10.355	0.000	0.000	0.000	0.000
64	A	64	HIS	0	0.053	0.029	27.582	-0.186	-0.186	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.041	-0.023	29.047	-0.308	-0.308	0.000	0.000	0.000	0.000
66	A	66	GLY	0	-0.050	-0.022	31.424	-0.303	-0.303	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.049	-0.020	32.340	-0.336	-0.336	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.021	-0.009	31.326	-0.230	-0.230	0.000	0.000	0.000	0.000
69	A	69	GLY	0	-0.012	0.009	33.454	-0.137	-0.137	0.000	0.000	0.000	0.000
70	A	70	LYS	1	0.802	0.866	31.620	-9.038	-9.038	0.000	0.000	0.000	0.000
71	A	71	VAL	0	0.030	0.022	25.613	-0.086	-0.086	0.000	0.000	0.000	0.000
72	A	72	LYS	1	0.934	0.973	29.092	-10.185	-10.185	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.034	0.016	27.649	0.420	0.420	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.016	-0.014	25.167	-0.342	-0.342	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.080	-0.045	24.764	0.218	0.218	0.000	0.000	0.000	0.000
76	A	76	GLY	0	0.067	0.016	21.747	0.306	0.306	0.000	0.000	0.000	0.000
77	A	77	VAL	0	-0.047	-0.011	22.259	-0.454	-0.454	0.000	0.000	0.000	0.000
78	A	78	MET	0	-0.021	0.016	16.080	0.553	0.553	0.000	0.000	0.000	0.000
79	A	79	VAL	0	-0.035	-0.026	19.642	-0.885	-0.885	0.000	0.000	0.000	0.000
80	A	80	GLU	-1	-0.906	-0.950	18.283	17.367	17.367	0.000	0.000	0.000	0.000
81	A	81	CYS	0	-0.069	-0.033	17.933	-1.272	-1.272	0.000	0.000	0.000	0.000
82	A	82	ASP	-1	-0.792	-0.881	17.458	15.225	15.225	0.000	0.000	0.000	0.000
83	A	83	SER	0	0.028	0.012	13.064	-0.447	-0.447	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.012	0.013	11.607	1.412	1.412	0.000	0.000	0.000	0.000
85	A	85	ARG	1	0.929	0.979	13.809	-21.282	-21.282	0.000	0.000	0.000	0.000
86	A	86	ILE	0	0.015	-0.003	14.060	1.412	1.412	0.000	0.000	0.000	0.000
87	A	87	PHE	0	0.041	0.004	15.783	-1.516	-1.516	0.000	0.000	0.000	0.000
88	A	88	ASN	0	-0.026	-0.015	17.582	0.439	0.439	0.000	0.000	0.000	0.000
89	A	89	VAL	0	0.050	0.025	18.713	-0.837	-0.837	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.035	0.008	21.035	0.021	0.021	0.000	0.000	0.000	0.000
91	A	91	GLY	0	0.061	0.037	23.501	-0.193	-0.193	0.000	0.000	0.000	0.000
92	A	92	PRO	0	-0.028	-0.016	24.239	-0.478	-0.478	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.921	0.963	26.884	-10.266	-10.266	0.000	0.000	0.000	0.000
94	A	94	LYS	1	0.950	0.982	29.543	-10.388	-10.388	0.000	0.000	0.000	0.000
95	A	95	GLY	0	-0.019	-0.021	30.988	-0.341	-0.341	0.000	0.000	0.000	0.000
96	A	96	LYS	1	0.961	0.972	33.077	-7.835	-7.835	0.000	0.000	0.000	0.000
97	A	97	HIS	0	0.036	0.021	33.469	0.094	0.094	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.837	-0.920	28.964	11.237	11.237	0.000	0.000	0.000	0.000
99	A	99	ARG	1	0.887	0.924	25.792	-11.915	-11.915	0.000	0.000	0.000	0.000
100	A	100	ASP	-1	-0.811	-0.901	27.498	10.801	10.801	0.000	0.000	0.000	0.000
101	A	101	LEU	0	-0.066	-0.038	28.043	0.237	0.237	0.000	0.000	0.000	0.000
102	A	102	LEU	0	0.021	0.008	22.856	0.370	0.370	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.052	0.035	23.114	0.647	0.647	0.000	0.000	0.000	0.000
104	A	104	LYS	1	0.823	0.911	23.721	-10.566	-10.566	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.016	0.013	22.039	0.278	0.278	0.000	0.000	0.000	0.000
106	A	106	TYR	0	0.043	-0.002	17.057	0.938	0.938	0.000	0.000	0.000	0.000
107	A	107	ASN	0	-0.023	-0.018	19.096	0.744	0.744	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.055	-0.027	20.628	0.127	0.127	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.028	-0.008	14.876	0.188	0.188	0.000	0.000	0.000	0.000
110	A	110	ASN	0	0.028	-0.002	16.295	2.036	2.036	0.000	0.000	0.000	0.000
111	A	111	ASN	0	-0.034	-0.034	17.359	0.492	0.492	0.000	0.000	0.000	0.000
112	A	112	GLU	-1	-0.884	-0.918	16.378	16.693	16.693	0.000	0.000	0.000	0.000
113	A	113	GLN	0	-0.038	-0.035	16.118	1.939	1.939	0.000	0.000	0.000	0.000
114	A	114	GLY	0	0.040	0.021	13.068	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	115	THR	0	-0.013	-0.022	6.914	-1.363	-1.363	0.000	0.000	0.000	0.000
116	A	116	PRO	0	-0.027	-0.002	9.401	0.981	0.981	0.000	0.000	0.000	0.000
117	A	117	LEU	0	0.045	0.035	6.430	3.010	3.010	0.000	0.000	0.000	0.000
118	A	118	THR	0	-0.016	-0.041	8.898	-4.030	-4.030	0.000	0.000	0.000	0.000
119	A	119	PRO	0	-0.011	0.023	12.079	1.013	1.013	0.000	0.000	0.000	0.000
120	A	120	ILE	0	0.057	0.023	14.441	-0.466	-0.466	0.000	0.000	0.000	0.000
121	A	121	LEU	0	-0.002	0.001	17.058	-0.976	-0.976	0.000	0.000	0.000	0.000
122	A	122	SER	0	-0.014	-0.034	19.897	-0.197	-0.197	0.000	0.000	0.000	0.000
123	A	123	CYS	0	0.029	0.045	21.097	-0.633	-0.633	0.000	0.000	0.000	0.000
124	A	124	GLY	0	0.028	0.011	23.124	-0.139	-0.139	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.028	-0.006	25.014	-0.470	-0.470	0.000	0.000	0.000	0.000
126	A	126	PHE	0	-0.077	-0.025	25.200	-0.637	-0.637	0.000	0.000	0.000	0.000
127	A	127	GLY	0	0.027	0.017	27.296	-0.367	-0.367	0.000	0.000	0.000	0.000
128	A	128	ILE	0	-0.032	-0.012	25.380	-0.367	-0.367	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.888	0.963	25.192	-11.593	-11.593	0.000	0.000	0.000	0.000
130	A	130	LEU	0	0.077	0.029	18.511	0.012	0.012	0.000	0.000	0.000	0.000
131	A	131	GLU	-1	-0.755	-0.899	21.155	13.744	13.744	0.000	0.000	0.000	0.000
132	A	132	THR	0	-0.019	0.000	22.479	0.037	0.037	0.000	0.000	0.000	0.000
133	A	133	SER	0	-0.012	-0.030	21.167	0.183	0.183	0.000	0.000	0.000	0.000
134	A	134	LEU	0	0.009	0.005	15.730	0.381	0.381	0.000	0.000	0.000	0.000
135	A	135	GLU	-1	-0.801	-0.878	18.865	13.134	13.134	0.000	0.000	0.000	0.000
136	A	136	VAL	0	-0.039	-0.015	21.257	-0.051	-0.051	0.000	0.000	0.000	0.000
137	A	137	LEU	0	-0.040	-0.009	14.097	0.083	0.083	0.000	0.000	0.000	0.000
138	A	138	LEU	0	0.037	0.002	14.529	0.593	0.593	0.000	0.000	0.000	0.000
139	A	139	ASP	-1	-0.891	-0.928	17.667	13.849	13.849	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.120	-0.065	19.616	-0.369	-0.369	0.000	0.000	0.000	0.000
141	A	141	CYS	0	-0.067	-0.025	14.966	-0.062	-0.062	0.000	0.000	0.000	0.000
142	A	142	ASN	0	0.012	0.016	15.706	1.222	1.222	0.000	0.000	0.000	0.000
143	A	143	THR	0	-0.001	-0.007	16.592	-0.402	-0.402	0.000	0.000	0.000	0.000
144	A	144	LYS	1	0.790	0.936	13.336	-21.152	-21.152	0.000	0.000	0.000	0.000
145	A	145	GLU	-1	-0.873	-0.939	5.672	51.488	51.488	0.000	0.000	0.000	0.000
146	A	146	VAL	0	-0.049	-0.031	9.949	-0.699	-0.699	0.000	0.000	0.000	0.000
147	A	147	LYS	1	0.816	0.921	1.774	-118.244	-122.329	14.308	-5.625	-4.597	0.073
148	A	148	VAL	0	0.013	0.005	7.808	-4.251	-4.251	0.000	0.000	0.000	0.000
149	A	149	PHE	0	-0.026	-0.019	9.096	2.282	2.282	0.000	0.000	0.000	0.000
150	A	150	VAL	0	-0.044	-0.018	10.823	-2.574	-2.574	0.000	0.000	0.000	0.000
151	A	151	TYR	0	-0.006	0.002	13.331	0.748	0.748	0.000	0.000	0.000	0.000
152	A	152	THR	0	-0.023	-0.055	15.883	-0.192	-0.192	0.000	0.000	0.000	0.000
153	A	153	ASP	-1	-0.795	-0.901	17.472	17.453	17.453	0.000	0.000	0.000	0.000
154	A	154	THR	0	-0.033	-0.019	18.555	-0.292	-0.292	0.000	0.000	0.000	0.000
155	A	155	GLU	-1	-0.813	-0.880	17.336	17.755	17.755	0.000	0.000	0.000	0.000
156	A	156	VAL	0	0.016	0.012	13.837	0.243	0.243	0.000	0.000	0.000	0.000
157	A	157	CYS	0	-0.066	-0.032	16.173	0.125	0.125	0.000	0.000	0.000	0.000
158	A	158	LYS	1	0.888	0.937	19.212	-13.815	-13.815	0.000	0.000	0.000	0.000
159	A	159	VAL	0	-0.021	0.002	13.650	-0.376	-0.376	0.000	0.000	0.000	0.000
160	A	160	LYS	1	0.929	0.970	14.103	-20.667	-20.667	0.000	0.000	0.000	0.000
161	A	161	ASP	-1	-0.909	-0.952	17.137	13.913	13.913	0.000	0.000	0.000	0.000
162	A	162	PHE	0	-0.080	-0.047	18.874	-0.599	-0.599	0.000	0.000	0.000	0.000
163	A	163	VAL	0	-0.018	-0.004	15.161	-0.299	-0.299	0.000	0.000	0.000	0.000
164	A	164	SER	0	-0.042	-0.027	16.884	0.118	0.118	0.000	0.000	0.000	0.000
165	A	165	GLY	0	-0.053	0.000	19.204	-0.639	-0.639	0.000	0.000	0.000	0.000

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