FMO DATABASE

FMODB ID: 4361N

Calculation Name: 2EJX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2EJX

Chain ID: A

ChEMBL ID:

UniProt ID: Q973T5

Base Structure: X-ray

Registration Date: 2023-03-13

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	OptAll
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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1267828.738783
FMO2-HF: Nuclear repulsion	1214610.900605
FMO2-HF: Total energy	-53217.838178
FMO2-MP2: Total energy	-53376.291636

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:3:LYS)

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

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.
-122.323	-117.958	25.246	-13.835	-15.774	-0.158

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.876 / q_NPA : 0.935

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	GLU	-1	-0.825	-0.894	1.685	-127.129	-128.831	16.696	-8.195	-6.799	-0.094
4	A	6	LYS	1	0.846	0.925	4.855	27.035	27.088	-0.001	-0.007	-0.044	0.000
5	A	7	GLU	-1	-0.786	-0.864	8.216	-25.346	-25.346	0.000	0.000	0.000	0.000
6	A	8	ILE	0	-0.019	-0.020	10.262	1.528	1.528	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.851	0.925	13.542	21.131	21.131	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.052	-0.050	16.681	0.317	0.317	0.000	0.000	0.000	0.000
9	A	11	ASN	0	-0.009	-0.030	19.487	0.254	0.254	0.000	0.000	0.000	0.000
10	A	12	GLN	0	-0.079	-0.026	21.783	0.859	0.859	0.000	0.000	0.000	0.000
11	A	13	ASP	-1	-0.818	-0.914	22.457	-12.941	-12.941	0.000	0.000	0.000	0.000
12	A	14	ILE	0	0.075	0.039	16.226	-0.234	-0.234	0.000	0.000	0.000	0.000
13	A	15	ASP	-1	-0.786	-0.870	18.997	-16.194	-16.194	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.028	0.001	21.068	-0.056	-0.056	0.000	0.000	0.000	0.000
15	A	17	VAL	0	-0.014	-0.011	17.011	-0.136	-0.136	0.000	0.000	0.000	0.000
16	A	18	MET	0	-0.027	-0.007	13.668	-0.865	-0.865	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.033	-0.030	17.668	-0.136	-0.136	0.000	0.000	0.000	0.000
18	A	20	ILE	0	-0.035	-0.005	20.016	0.230	0.230	0.000	0.000	0.000	0.000
19	A	21	PHE	0	0.029	0.000	14.493	-0.265	-0.265	0.000	0.000	0.000	0.000
20	A	22	SER	0	-0.089	-0.035	16.338	-0.576	-0.576	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.739	-0.851	18.281	-12.987	-12.987	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.007	0.002	17.387	-0.558	-0.558	0.000	0.000	0.000	0.000
23	A	25	ALA	0	0.003	-0.024	18.396	-0.171	-0.171	0.000	0.000	0.000	0.000
24	A	26	PHE	0	-0.024	-0.006	17.451	0.478	0.478	0.000	0.000	0.000	0.000
25	A	27	THR	0	0.013	-0.033	13.513	-0.208	-0.208	0.000	0.000	0.000	0.000
26	A	28	ILE	0	-0.003	0.009	13.635	-1.019	-1.019	0.000	0.000	0.000	0.000
27	A	29	PRO	0	-0.014	-0.018	15.408	-0.502	-0.502	0.000	0.000	0.000	0.000
28	A	30	GLN	0	0.025	0.038	16.172	-0.274	-0.274	0.000	0.000	0.000	0.000
29	A	31	ILE	0	-0.003	-0.001	10.058	-0.820	-0.820	0.000	0.000	0.000	0.000
30	A	32	PHE	0	0.007	0.005	11.063	-0.790	-0.790	0.000	0.000	0.000	0.000
31	A	33	PRO	0	-0.013	-0.012	11.276	0.915	0.915	0.000	0.000	0.000	0.000
32	A	34	GLY	0	0.041	0.041	14.213	0.529	0.529	0.000	0.000	0.000	0.000
33	A	35	ILE	0	-0.046	-0.012	16.099	0.575	0.575	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.001	-0.005	18.997	0.285	0.285	0.000	0.000	0.000	0.000
35	A	37	SER	0	-0.035	-0.021	22.048	0.725	0.725	0.000	0.000	0.000	0.000
36	A	38	ILE	0	-0.011	-0.008	19.447	-0.574	-0.574	0.000	0.000	0.000	0.000
37	A	39	LYS	1	0.812	0.906	22.995	11.487	11.487	0.000	0.000	0.000	0.000
38	A	40	CYS	0	-0.030	-0.008	21.723	-0.403	-0.403	0.000	0.000	0.000	0.000
39	A	41	ILE	0	0.020	0.007	24.321	0.186	0.186	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.759	-0.863	25.426	-11.419	-11.419	0.000	0.000	0.000	0.000
41	A	43	PRO	0	0.008	0.001	24.281	-0.454	-0.454	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.846	-0.903	20.961	-14.590	-14.590	0.000	0.000	0.000	0.000
43	A	45	ILE	0	-0.035	-0.001	20.105	-0.742	-0.742	0.000	0.000	0.000	0.000
44	A	46	PHE	0	0.000	-0.009	14.845	0.236	0.236	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.822	-0.896	20.091	-11.635	-11.635	0.000	0.000	0.000	0.000
46	A	48	ALA	0	0.006	-0.008	18.298	0.260	0.260	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.844	-0.903	19.687	-11.423	-11.423	0.000	0.000	0.000	0.000
48	A	50	GLY	0	0.068	0.036	18.364	-0.053	-0.053	0.000	0.000	0.000	0.000
49	A	51	LYS	1	0.800	0.893	18.854	11.777	11.777	0.000	0.000	0.000	0.000
50	A	52	PHE	0	0.011	0.014	12.939	-0.334	-0.334	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.031	0.015	16.196	0.180	0.180	0.000	0.000	0.000	0.000
52	A	54	ALA	0	0.036	0.016	19.242	0.338	0.338	0.000	0.000	0.000	0.000
53	A	55	PHE	0	-0.024	-0.007	16.736	0.503	0.503	0.000	0.000	0.000	0.000
54	A	56	SER	0	0.010	0.005	18.445	-0.352	-0.352	0.000	0.000	0.000	0.000
55	A	57	TYR	0	-0.081	-0.056	14.804	-0.268	-0.268	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.852	0.907	18.540	11.739	11.739	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.007	-0.008	13.816	-0.244	-0.244	0.000	0.000	0.000	0.000
58	A	60	LYS	1	0.811	0.889	16.917	14.243	14.243	0.000	0.000	0.000	0.000
59	A	61	GLY	0	0.045	0.018	16.268	-0.867	-0.867	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.742	0.858	16.644	14.222	14.222	0.000	0.000	0.000	0.000
61	A	63	VAL	0	-0.031	-0.018	15.937	-1.255	-1.255	0.000	0.000	0.000	0.000
62	A	64	TYR	0	0.013	0.010	15.276	1.284	1.284	0.000	0.000	0.000	0.000
63	A	65	LYS	1	0.872	0.918	15.780	13.484	13.484	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.017	0.008	16.785	0.619	0.619	0.000	0.000	0.000	0.000
65	A	67	VAL	0	0.001	-0.006	17.534	0.073	0.073	0.000	0.000	0.000	0.000
66	A	68	ASP	-1	-0.811	-0.889	15.052	-18.542	-18.542	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.780	-0.857	9.893	-30.954	-30.954	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.010	0.005	12.737	1.759	1.759	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.855	0.898	10.211	22.449	22.449	0.000	0.000	0.000	0.000
70	A	72	ILE	0	0.022	0.007	11.536	1.899	1.899	0.000	0.000	0.000	0.000
71	A	73	ILE	0	-0.010	0.003	11.238	-1.858	-1.858	0.000	0.000	0.000	0.000
72	A	74	TYR	0	-0.050	-0.052	8.220	0.895	0.895	0.000	0.000	0.000	0.000
73	A	75	ASP	-1	-0.787	-0.872	13.189	-15.399	-15.399	0.000	0.000	0.000	0.000
74	A	76	SER	0	0.047	-0.006	13.514	0.311	0.311	0.000	0.000	0.000	0.000
75	A	77	ASP	-1	-0.782	-0.868	15.984	-13.573	-13.573	0.000	0.000	0.000	0.000
76	A	78	ARG	1	0.840	0.910	13.599	13.597	13.597	0.000	0.000	0.000	0.000
77	A	79	GLY	0	0.017	0.026	11.719	-0.840	-0.840	0.000	0.000	0.000	0.000
78	A	80	ASN	0	-0.020	-0.028	11.381	1.101	1.101	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.018	0.009	8.589	-1.280	-1.280	0.000	0.000	0.000	0.000
80	A	82	ILE	0	-0.033	-0.009	7.410	2.366	2.366	0.000	0.000	0.000	0.000
81	A	83	LEU	0	0.001	0.006	6.477	-3.883	-3.883	0.000	0.000	0.000	0.000
82	A	84	TYR	0	-0.053	-0.054	4.886	4.921	4.921	0.000	0.000	0.000	0.000
83	A	85	ILE	0	-0.011	-0.010	8.357	-1.931	-1.931	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.841	0.912	5.031	40.801	40.801	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.841	0.888	10.654	15.448	15.448	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.743	0.854	9.264	28.936	28.936	0.000	0.000	0.000	0.000
87	A	89	ASP	-1	-0.808	-0.893	13.825	-18.256	-18.256	0.000	0.000	0.000	0.000
88	A	90	ASN	0	-0.026	-0.032	17.429	-0.070	-0.070	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.023	-0.002	18.917	0.799	0.799	0.000	0.000	0.000	0.000
90	A	92	THR	0	-0.020	-0.008	12.921	-0.436	-0.436	0.000	0.000	0.000	0.000
91	A	93	LEU	0	0.022	0.010	11.731	0.043	0.043	0.000	0.000	0.000	0.000
92	A	94	GLN	0	-0.014	-0.015	5.387	5.638	5.638	0.000	0.000	0.000	0.000
93	A	95	ILE	0	0.016	0.013	7.833	1.175	1.175	0.000	0.000	0.000	0.000
94	A	96	ILE	0	-0.023	-0.020	2.234	-7.134	-6.816	2.431	-0.596	-2.152	-0.005
95	A	97	LEU	0	0.002	0.010	3.768	5.619	5.989	0.000	-0.083	-0.287	0.000
96	A	98	GLU	-1	-0.871	-0.936	2.357	-77.757	-72.857	6.114	-4.787	-6.226	-0.059
97	A	99	HIS	0	-0.030	0.006	3.836	3.006	3.117	0.007	-0.030	-0.089	0.000
98	A	100	ASP	-1	-0.786	-0.876	5.914	-20.181	-20.181	0.000	0.000	0.000	0.000
99	A	101	ASN	0	0.001	0.006	8.613	0.397	0.397	0.000	0.000	0.000	0.000
100	A	102	LYS	1	1.017	0.988	7.525	19.822	19.822	0.000	0.000	0.000	0.000
101	A	103	LEU	0	0.006	0.015	8.641	-0.218	-0.218	0.000	0.000	0.000	0.000
102	A	104	THR	0	-0.012	-0.030	10.005	0.468	0.468	0.000	0.000	0.000	0.000
103	A	105	ALA	0	-0.001	0.006	5.000	-0.236	-0.236	0.000	0.000	0.000	0.000
104	A	106	PHE	0	-0.064	-0.035	7.019	-0.593	-0.593	0.000	0.000	0.000	0.000
105	A	107	LEU	0	-0.005	-0.005	9.080	0.084	0.084	0.000	0.000	0.000	0.000
106	A	108	GLY	0	0.044	0.023	10.000	0.723	0.723	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.888	0.947	4.153	34.868	35.183	-0.001	-0.137	-0.177	0.000
108	A	110	PRO	0	0.017	0.013	8.341	-0.935	-0.935	0.000	0.000	0.000	0.000
109	A	111	TYR	0	0.021	0.004	11.839	0.736	0.736	0.000	0.000	0.000	0.000
110	A	112	VAL	0	0.008	0.008	7.231	0.024	0.024	0.000	0.000	0.000	0.000
111	A	113	SER	0	0.001	-0.008	9.365	-0.379	-0.379	0.000	0.000	0.000	0.000
112	A	114	SER	0	0.011	0.022	10.698	0.587	0.587	0.000	0.000	0.000	0.000
113	A	115	ASN	0	0.017	0.009	13.132	1.570	1.570	0.000	0.000	0.000	0.000
114	A	116	LEU	0	0.005	-0.008	8.154	0.215	0.215	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.880	-0.929	12.278	-22.958	-22.958	0.000	0.000	0.000	0.000
116	A	118	ARG	1	0.896	0.946	14.322	17.050	17.050	0.000	0.000	0.000	0.000
117	A	119	LEU	0	-0.064	-0.026	13.497	0.760	0.760	0.000	0.000	0.000	0.000
118	A	120	ALA	0	-0.014	-0.027	13.951	0.444	0.444	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.970	-0.984	15.993	-15.788	-15.788	0.000	0.000	0.000	0.000
120	A	122	ASN	0	-0.056	-0.017	19.349	1.473	1.473	0.000	0.000	0.000	0.000
121	A	123	ILE	0	0.035	0.029	16.719	0.482	0.482	0.000	0.000	0.000	0.000
122	A	124	ASP	-1	-0.714	-0.833	19.716	-14.119	-14.119	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.908	-0.963	22.818	-12.376	-12.376	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.006	-0.007	20.229	0.495	0.495	0.000	0.000	0.000	0.000
125	A	127	ILE	0	0.016	0.009	19.276	0.463	0.463	0.000	0.000	0.000	0.000
126	A	128	ARG	1	0.975	0.989	23.067	11.183	11.183	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.032	-0.012	26.478	0.517	0.517	0.000	0.000	0.000	0.000
128	A	130	GLU	-1	-0.767	-0.863	22.767	-12.131	-12.131	0.000	0.000	0.000	0.000
129	A	131	ARG	1	0.835	0.905	25.164	12.188	12.188	0.000	0.000	0.000	0.000
130	A	132	ILE	0	-0.032	-0.007	27.588	0.376	0.376	0.000	0.000	0.000	0.000
131	A	133	LYS	1	0.817	0.903	25.441	12.080	12.080	0.000	0.000	0.000	0.000
132	A	134	ARG	1	0.751	0.840	23.308	13.039	13.039	0.000	0.000	0.000	0.000
133	A	135	LYS	1	0.915	0.968	29.675	9.190	9.190	0.000	0.000	0.000	0.000
134	A	136	ILE	0	0.011	0.029	25.282	-0.165	-0.165	0.000	0.000	0.000	0.000

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