FMO DATABASE

FMODB ID: K3843

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1266384.362081
FMO2-HF: Nuclear repulsion	1213166.764133
FMO2-HF: Total energy	-53217.597948
FMO2-MP2: Total energy	-53376.085107

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.
-115.51	-111.916	27.478	-14.885	-16.188	-0.163

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 : 0.839 / q_NPA : 0.917

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	-0.904	1.693	-126.309	-127.706	15.798	-7.857	-6.544	-0.092
4	A	6	LYS	1	0.855	0.924	4.993	27.206	27.262	-0.001	-0.005	-0.050	0.000
5	A	7	GLU	-1	-0.821	-0.876	8.556	-25.637	-25.637	0.000	0.000	0.000	0.000
6	A	8	ILE	0	-0.011	-0.018	10.434	1.568	1.568	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.879	0.936	13.733	20.448	20.448	0.000	0.000	0.000	0.000
8	A	10	THR	0	-0.033	-0.044	16.861	0.548	0.548	0.000	0.000	0.000	0.000
9	A	11	ASN	0	-0.009	-0.011	19.691	0.101	0.101	0.000	0.000	0.000	0.000
10	A	12	GLN	0	-0.057	-0.011	22.076	0.927	0.927	0.000	0.000	0.000	0.000
11	A	13	ASP	-1	-0.873	-0.937	22.436	-13.059	-13.059	0.000	0.000	0.000	0.000
12	A	14	ILE	0	0.066	0.018	16.432	-0.229	-0.229	0.000	0.000	0.000	0.000
13	A	15	ASP	-1	-0.788	-0.869	19.369	-15.581	-15.581	0.000	0.000	0.000	0.000
14	A	16	VAL	0	-0.053	-0.026	21.387	-0.102	-0.102	0.000	0.000	0.000	0.000
15	A	17	VAL	0	-0.001	-0.004	17.255	-0.136	-0.136	0.000	0.000	0.000	0.000
16	A	18	MET	0	-0.010	0.004	13.776	-0.896	-0.896	0.000	0.000	0.000	0.000
17	A	19	THR	0	-0.031	-0.028	17.802	-0.195	-0.195	0.000	0.000	0.000	0.000
18	A	20	ILE	0	-0.033	-0.002	19.921	0.241	0.241	0.000	0.000	0.000	0.000
19	A	21	PHE	0	0.024	0.008	14.015	-0.222	-0.222	0.000	0.000	0.000	0.000
20	A	22	SER	0	-0.095	-0.033	16.046	-0.435	-0.435	0.000	0.000	0.000	0.000
21	A	23	ASP	-1	-0.734	-0.849	17.890	-12.696	-12.696	0.000	0.000	0.000	0.000
22	A	24	PRO	0	0.015	0.011	17.227	-0.505	-0.505	0.000	0.000	0.000	0.000
23	A	25	ALA	0	0.007	-0.025	18.238	-0.179	-0.179	0.000	0.000	0.000	0.000
24	A	26	PHE	0	-0.034	-0.012	17.232	0.406	0.406	0.000	0.000	0.000	0.000
25	A	27	THR	0	0.008	-0.041	13.280	-0.178	-0.178	0.000	0.000	0.000	0.000
26	A	28	ILE	0	-0.008	-0.004	13.526	-0.914	-0.914	0.000	0.000	0.000	0.000
27	A	29	PRO	0	-0.012	-0.014	15.233	-0.362	-0.362	0.000	0.000	0.000	0.000
28	A	30	GLN	0	0.015	0.037	16.135	-0.347	-0.347	0.000	0.000	0.000	0.000
29	A	31	ILE	0	0.014	0.007	9.967	-0.624	-0.624	0.000	0.000	0.000	0.000
30	A	32	PHE	0	-0.009	0.002	10.561	-0.797	-0.797	0.000	0.000	0.000	0.000
31	A	33	PRO	0	-0.011	-0.009	11.285	0.785	0.785	0.000	0.000	0.000	0.000
32	A	34	GLY	0	0.030	0.037	14.334	0.470	0.470	0.000	0.000	0.000	0.000
33	A	35	ILE	0	-0.037	-0.011	15.732	0.533	0.533	0.000	0.000	0.000	0.000
34	A	36	ALA	0	0.012	-0.003	18.884	0.285	0.285	0.000	0.000	0.000	0.000
35	A	37	SER	0	-0.056	-0.027	21.813	0.676	0.676	0.000	0.000	0.000	0.000
36	A	38	ILE	0	0.009	-0.005	19.053	-0.554	-0.554	0.000	0.000	0.000	0.000
37	A	39	LYS	1	0.792	0.900	22.545	11.199	11.199	0.000	0.000	0.000	0.000
38	A	40	CYS	0	-0.017	-0.016	21.775	-0.484	-0.484	0.000	0.000	0.000	0.000
39	A	41	ILE	0	0.014	0.003	24.531	0.173	0.173	0.000	0.000	0.000	0.000
40	A	42	GLU	-1	-0.786	-0.867	25.469	-11.258	-11.258	0.000	0.000	0.000	0.000
41	A	43	PRO	0	0.016	-0.009	24.538	-0.352	-0.352	0.000	0.000	0.000	0.000
42	A	44	GLU	-1	-0.872	-0.914	20.932	-14.100	-14.100	0.000	0.000	0.000	0.000
43	A	45	ILE	0	-0.024	-0.004	20.179	-0.641	-0.641	0.000	0.000	0.000	0.000
44	A	46	PHE	0	0.011	0.001	14.715	0.212	0.212	0.000	0.000	0.000	0.000
45	A	47	GLU	-1	-0.830	-0.905	19.952	-11.391	-11.391	0.000	0.000	0.000	0.000
46	A	48	ALA	0	-0.002	-0.013	17.807	0.247	0.247	0.000	0.000	0.000	0.000
47	A	49	GLU	-1	-0.840	-0.894	19.330	-11.218	-11.218	0.000	0.000	0.000	0.000
48	A	50	GLY	0	0.060	0.036	17.956	-0.014	-0.014	0.000	0.000	0.000	0.000
49	A	51	LYS	1	0.873	0.951	18.764	11.372	11.372	0.000	0.000	0.000	0.000
50	A	52	PHE	0	0.015	0.019	13.031	-0.287	-0.287	0.000	0.000	0.000	0.000
51	A	53	LEU	0	0.031	0.016	16.702	0.152	0.152	0.000	0.000	0.000	0.000
52	A	54	ALA	0	-0.010	-0.010	19.731	0.342	0.342	0.000	0.000	0.000	0.000
53	A	55	PHE	0	-0.035	-0.029	17.136	0.444	0.444	0.000	0.000	0.000	0.000
54	A	56	SER	0	0.030	0.009	18.403	-0.404	-0.404	0.000	0.000	0.000	0.000
55	A	57	TYR	0	-0.063	-0.047	14.723	-0.256	-0.256	0.000	0.000	0.000	0.000
56	A	58	LYS	1	0.853	0.908	18.269	11.598	11.598	0.000	0.000	0.000	0.000
57	A	59	VAL	0	-0.004	-0.009	13.528	-0.312	-0.312	0.000	0.000	0.000	0.000
58	A	60	LYS	1	0.829	0.907	16.767	13.955	13.955	0.000	0.000	0.000	0.000
59	A	61	GLY	0	0.030	0.007	16.151	-0.761	-0.761	0.000	0.000	0.000	0.000
60	A	62	ARG	1	0.767	0.884	16.279	13.820	13.820	0.000	0.000	0.000	0.000
61	A	63	VAL	0	-0.018	-0.002	15.771	-1.184	-1.184	0.000	0.000	0.000	0.000
62	A	64	TYR	0	-0.016	-0.010	15.394	1.221	1.221	0.000	0.000	0.000	0.000
63	A	65	LYS	1	0.912	0.944	15.865	13.014	13.014	0.000	0.000	0.000	0.000
64	A	66	GLY	0	0.013	0.007	16.755	0.527	0.527	0.000	0.000	0.000	0.000
65	A	67	VAL	0	0.005	-0.008	17.660	0.248	0.248	0.000	0.000	0.000	0.000
66	A	68	ASP	-1	-0.820	-0.895	15.386	-18.161	-18.161	0.000	0.000	0.000	0.000
67	A	69	GLU	-1	-0.791	-0.874	10.304	-29.697	-29.697	0.000	0.000	0.000	0.000
68	A	70	VAL	0	-0.014	0.012	12.784	1.752	1.752	0.000	0.000	0.000	0.000
69	A	71	ARG	1	0.862	0.910	10.289	22.093	22.093	0.000	0.000	0.000	0.000
70	A	72	ILE	0	0.004	-0.003	11.141	1.887	1.887	0.000	0.000	0.000	0.000
71	A	73	ILE	0	-0.003	0.003	11.044	-1.652	-1.652	0.000	0.000	0.000	0.000
72	A	74	TYR	0	-0.033	-0.043	7.828	0.806	0.806	0.000	0.000	0.000	0.000
73	A	75	ASP	-1	-0.802	-0.882	12.820	-15.015	-15.015	0.000	0.000	0.000	0.000
74	A	76	SER	0	0.034	-0.011	13.347	0.429	0.429	0.000	0.000	0.000	0.000
75	A	77	ASP	-1	-0.791	-0.881	15.748	-13.437	-13.437	0.000	0.000	0.000	0.000
76	A	78	ARG	1	0.833	0.908	13.875	13.302	13.302	0.000	0.000	0.000	0.000
77	A	79	GLY	0	0.016	0.019	11.496	-0.788	-0.788	0.000	0.000	0.000	0.000
78	A	80	ASN	0	-0.017	-0.015	11.341	1.091	1.091	0.000	0.000	0.000	0.000
79	A	81	GLY	0	0.025	0.014	8.134	-1.227	-1.227	0.000	0.000	0.000	0.000
80	A	82	ILE	0	-0.029	-0.003	7.355	2.185	2.185	0.000	0.000	0.000	0.000
81	A	83	LEU	0	-0.018	-0.004	6.334	-3.640	-3.640	0.000	0.000	0.000	0.000
82	A	84	TYR	0	-0.056	-0.048	5.234	4.556	4.556	0.000	0.000	0.000	0.000
83	A	85	ILE	0	0.009	0.002	8.427	-1.920	-1.920	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.867	0.929	5.070	40.541	40.541	0.000	0.000	0.000	0.000
85	A	87	LYS	1	0.837	0.888	10.755	15.398	15.398	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.732	0.849	9.139	29.633	29.633	0.000	0.000	0.000	0.000
87	A	89	ASP	-1	-0.809	-0.890	13.292	-18.421	-18.421	0.000	0.000	0.000	0.000
88	A	90	ASN	0	-0.027	-0.034	17.028	-0.097	-0.097	0.000	0.000	0.000	0.000
89	A	91	ASN	0	-0.035	-0.013	18.541	0.803	0.803	0.000	0.000	0.000	0.000
90	A	92	THR	0	-0.014	-0.003	12.806	-0.284	-0.284	0.000	0.000	0.000	0.000
91	A	93	LEU	0	0.015	0.016	11.861	0.008	0.008	0.000	0.000	0.000	0.000
92	A	94	GLN	0	-0.011	-0.020	5.441	5.202	5.202	0.000	0.000	0.000	0.000
93	A	95	ILE	0	0.023	0.018	7.785	1.080	1.080	0.000	0.000	0.000	0.000
94	A	96	ILE	0	-0.020	-0.014	2.440	-7.344	-6.558	2.603	-0.785	-2.604	-0.006
95	A	97	LEU	0	0.015	0.014	3.815	4.708	5.144	0.001	-0.126	-0.312	0.000
96	A	98	GLU	-1	-0.865	-0.943	2.112	-69.185	-65.548	9.062	-6.146	-6.553	-0.065
97	A	99	HIS	0	-0.032	0.007	3.575	2.628	2.704	0.015	0.034	-0.125	0.000
98	A	100	ASP	-1	-0.806	-0.895	5.813	-20.035	-20.035	0.000	0.000	0.000	0.000
99	A	101	ASN	0	0.007	0.017	8.320	1.006	1.006	0.000	0.000	0.000	0.000
100	A	102	LYS	1	1.012	0.984	7.996	19.714	19.714	0.000	0.000	0.000	0.000
101	A	103	LEU	0	0.007	0.013	9.046	-0.282	-0.282	0.000	0.000	0.000	0.000
102	A	104	THR	0	0.000	-0.031	10.455	0.273	0.273	0.000	0.000	0.000	0.000
103	A	105	ALA	0	0.015	0.011	5.809	-0.158	-0.158	0.000	0.000	0.000	0.000
104	A	106	PHE	0	-0.079	-0.041	7.759	-0.600	-0.600	0.000	0.000	0.000	0.000
105	A	107	LEU	0	-0.008	0.003	9.992	0.176	0.176	0.000	0.000	0.000	0.000
106	A	108	GLY	0	0.042	0.016	10.437	0.502	0.502	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.940	0.975	5.104	33.176	33.176	0.000	0.000	0.000	0.000
108	A	110	PRO	0	0.016	0.010	8.998	-0.927	-0.927	0.000	0.000	0.000	0.000
109	A	111	TYR	0	0.014	0.008	12.249	0.733	0.733	0.000	0.000	0.000	0.000
110	A	112	VAL	0	0.015	0.007	7.206	0.040	0.040	0.000	0.000	0.000	0.000
111	A	113	SER	0	0.014	-0.008	9.591	-0.506	-0.506	0.000	0.000	0.000	0.000
112	A	114	SER	0	-0.002	0.019	10.734	0.522	0.522	0.000	0.000	0.000	0.000
113	A	115	ASN	0	0.001	0.001	12.849	1.440	1.440	0.000	0.000	0.000	0.000
114	A	116	LEU	0	-0.020	-0.016	8.029	0.089	0.089	0.000	0.000	0.000	0.000
115	A	117	ASP	-1	-0.866	-0.918	12.480	-22.584	-22.584	0.000	0.000	0.000	0.000
116	A	118	ARG	1	0.890	0.943	14.636	16.782	16.782	0.000	0.000	0.000	0.000
117	A	119	LEU	0	-0.043	-0.026	13.746	0.708	0.708	0.000	0.000	0.000	0.000
118	A	120	ALA	0	-0.028	-0.036	13.972	0.444	0.444	0.000	0.000	0.000	0.000
119	A	121	GLU	-1	-0.970	-0.974	16.018	-15.606	-15.606	0.000	0.000	0.000	0.000
120	A	122	ASN	0	-0.054	-0.024	19.337	1.412	1.412	0.000	0.000	0.000	0.000
121	A	123	ILE	0	0.008	0.027	17.189	0.552	0.552	0.000	0.000	0.000	0.000
122	A	124	ASP	-1	-0.708	-0.849	20.001	-13.957	-13.957	0.000	0.000	0.000	0.000
123	A	125	GLU	-1	-0.921	-0.970	23.019	-12.191	-12.191	0.000	0.000	0.000	0.000
124	A	126	ILE	0	-0.005	-0.005	20.126	0.441	0.441	0.000	0.000	0.000	0.000
125	A	127	ILE	0	0.007	-0.001	19.753	0.486	0.486	0.000	0.000	0.000	0.000
126	A	128	ARG	1	0.968	0.988	23.567	11.024	11.024	0.000	0.000	0.000	0.000
127	A	129	LEU	0	-0.022	-0.016	26.754	0.514	0.514	0.000	0.000	0.000	0.000
128	A	130	GLU	-1	-0.773	-0.862	22.691	-12.011	-12.011	0.000	0.000	0.000	0.000
129	A	131	ARG	1	0.891	0.931	25.581	11.949	11.949	0.000	0.000	0.000	0.000
130	A	132	ILE	0	-0.040	-0.011	28.123	0.371	0.371	0.000	0.000	0.000	0.000
131	A	133	LYS	1	0.820	0.906	25.258	11.922	11.922	0.000	0.000	0.000	0.000
132	A	134	ARG	1	0.750	0.831	22.989	12.845	12.845	0.000	0.000	0.000	0.000
133	A	135	LYS	1	0.929	0.978	29.557	8.977	8.977	0.000	0.000	0.000	0.000
134	A	136	ILE	0	0.005	0.040	25.428	-0.084	-0.084	0.000	0.000	0.000	0.000

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