FMO DATABASE

FMODB ID: YZK72

Calculation Name: 3EES-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EES

Chain ID: A

ChEMBL ID:

UniProt ID: Q6MPX4

Base Structure: X-ray

Registration Date: 2023-09-20

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	131
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1202299.384325
FMO2-HF: Nuclear repulsion	1150289.717531
FMO2-HF: Total energy	-52009.666793
FMO2-MP2: Total energy	-52163.645814

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:20:HIS)

Summations of interaction energy for fragment #1(A:20:HIS)

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.
-12.438	-6.325	1.766	-3.255	-4.623	-0.021

Interaction energy analysis for fragmet #1(A:20:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.002 / q_NPA : -0.005

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	22	ILE	0	-0.027	-0.019	3.829	-0.156	1.644	-0.022	-0.853	-0.925	0.001
4	A	23	PRO	0	0.014	0.005	6.389	-0.271	-0.271	0.000	0.000	0.000	0.000
5	A	24	VAL	0	-0.020	-0.009	9.795	-0.011	-0.011	0.000	0.000	0.000	0.000
6	A	25	VAL	0	0.008	0.019	12.812	0.018	0.018	0.000	0.000	0.000	0.000
7	A	26	ALA	0	0.018	0.002	16.515	-0.050	-0.050	0.000	0.000	0.000	0.000
8	A	27	GLY	0	0.036	0.025	19.540	0.029	0.029	0.000	0.000	0.000	0.000
9	A	28	PHE	0	-0.072	-0.042	23.201	-0.028	-0.028	0.000	0.000	0.000	0.000
10	A	29	LEU	0	0.094	0.046	26.189	0.010	0.010	0.000	0.000	0.000	0.000
11	A	30	ARG	1	0.864	0.923	29.231	-0.073	-0.073	0.000	0.000	0.000	0.000
12	A	31	LYS	1	0.889	0.935	32.432	-0.028	-0.028	0.000	0.000	0.000	0.000
13	A	32	ASP	-1	-0.903	-0.953	35.760	0.030	0.030	0.000	0.000	0.000	0.000
14	A	33	GLY	0	-0.021	-0.001	36.231	-0.006	-0.006	0.000	0.000	0.000	0.000
15	A	34	LYS	1	0.840	0.932	34.134	0.011	0.011	0.000	0.000	0.000	0.000
16	A	35	ILE	0	-0.034	-0.021	27.045	0.012	0.012	0.000	0.000	0.000	0.000
17	A	36	LEU	0	-0.014	0.014	27.775	-0.013	-0.013	0.000	0.000	0.000	0.000
18	A	37	VAL	0	-0.029	-0.015	25.441	0.002	0.002	0.000	0.000	0.000	0.000
19	A	38	GLY	0	0.066	0.019	24.813	0.006	0.006	0.000	0.000	0.000	0.000
20	A	39	GLN	0	-0.061	-0.031	24.253	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	40	ARG	1	0.825	0.879	16.027	0.198	0.198	0.000	0.000	0.000	0.000
22	A	41	PRO	0	0.044	0.024	21.807	-0.015	-0.015	0.000	0.000	0.000	0.000
23	A	42	GLU	-1	-0.900	-0.971	23.520	-0.175	-0.175	0.000	0.000	0.000	0.000
24	A	43	ASN	0	-0.064	-0.039	23.032	-0.011	-0.011	0.000	0.000	0.000	0.000
25	A	44	ASN	0	0.070	0.058	18.638	-0.053	-0.053	0.000	0.000	0.000	0.000
26	A	45	SER	0	0.022	-0.004	15.170	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	46	LEU	0	-0.042	-0.022	15.732	-0.042	-0.042	0.000	0.000	0.000	0.000
28	A	47	ALA	0	-0.018	0.008	19.218	0.044	0.044	0.000	0.000	0.000	0.000
29	A	48	GLY	0	0.007	0.007	22.545	-0.013	-0.013	0.000	0.000	0.000	0.000
30	A	49	GLN	0	-0.037	-0.021	20.283	0.002	0.002	0.000	0.000	0.000	0.000
31	A	50	TRP	0	-0.013	-0.017	23.100	0.010	0.010	0.000	0.000	0.000	0.000
32	A	51	GLU	-1	-0.800	-0.881	18.507	-0.143	-0.143	0.000	0.000	0.000	0.000
33	A	52	PHE	0	-0.014	-0.017	21.229	0.010	0.010	0.000	0.000	0.000	0.000
34	A	53	PRO	0	0.027	0.025	20.702	-0.013	-0.013	0.000	0.000	0.000	0.000
35	A	54	GLY	0	0.008	-0.011	18.999	0.023	0.023	0.000	0.000	0.000	0.000
36	A	55	GLY	0	0.027	0.027	15.757	-0.039	-0.039	0.000	0.000	0.000	0.000
37	A	56	LYS	1	0.923	0.961	8.541	-0.263	-0.263	0.000	0.000	0.000	0.000
38	A	57	ILE	0	0.007	0.009	11.973	-0.025	-0.025	0.000	0.000	0.000	0.000
39	A	58	GLU	-1	-0.972	-0.974	11.462	0.706	0.706	0.000	0.000	0.000	0.000
40	A	59	ASN	0	-0.040	-0.048	10.742	0.217	0.217	0.000	0.000	0.000	0.000
41	A	60	GLY	0	-0.042	-0.024	13.298	-0.113	-0.113	0.000	0.000	0.000	0.000
42	A	61	GLU	-1	-0.757	-0.834	15.732	0.460	0.460	0.000	0.000	0.000	0.000
43	A	62	THR	0	-0.046	-0.050	16.157	0.071	0.071	0.000	0.000	0.000	0.000
44	A	63	PRO	0	-0.015	-0.024	16.138	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	64	GLU	-1	-0.802	-0.901	17.680	0.406	0.406	0.000	0.000	0.000	0.000
46	A	65	GLU	-1	-0.841	-0.893	20.083	0.445	0.445	0.000	0.000	0.000	0.000
47	A	66	ALA	0	0.001	0.018	16.392	-0.031	-0.031	0.000	0.000	0.000	0.000
48	A	67	LEU	0	-0.008	-0.010	18.383	-0.053	-0.053	0.000	0.000	0.000	0.000
49	A	68	ALA	0	0.005	0.002	20.367	-0.042	-0.042	0.000	0.000	0.000	0.000
50	A	69	ARG	1	0.758	0.860	16.172	-0.416	-0.416	0.000	0.000	0.000	0.000
51	A	70	GLU	-1	-0.837	-0.919	16.710	0.207	0.207	0.000	0.000	0.000	0.000
52	A	71	LEU	0	-0.007	-0.011	20.971	-0.042	-0.042	0.000	0.000	0.000	0.000
53	A	72	ASN	0	-0.037	-0.006	24.246	-0.040	-0.040	0.000	0.000	0.000	0.000
54	A	73	GLU	-1	-0.872	-0.945	20.628	0.203	0.203	0.000	0.000	0.000	0.000
55	A	74	GLU	-1	-0.806	-0.909	21.125	0.004	0.004	0.000	0.000	0.000	0.000
56	A	75	LEU	0	-0.036	-0.028	24.469	-0.023	-0.023	0.000	0.000	0.000	0.000
57	A	76	GLY	0	-0.046	-0.029	27.749	-0.010	-0.010	0.000	0.000	0.000	0.000
58	A	77	ILE	0	-0.091	-0.022	28.149	-0.003	-0.003	0.000	0.000	0.000	0.000
59	A	78	GLU	-1	-0.863	-0.926	28.592	0.193	0.193	0.000	0.000	0.000	0.000
60	A	79	ALA	0	-0.020	-0.023	26.944	-0.011	-0.011	0.000	0.000	0.000	0.000
61	A	80	GLU	-1	-0.938	-0.965	27.926	0.177	0.177	0.000	0.000	0.000	0.000
62	A	81	VAL	0	-0.043	-0.023	22.799	-0.015	-0.015	0.000	0.000	0.000	0.000
63	A	82	GLY	0	-0.003	-0.003	26.185	0.006	0.006	0.000	0.000	0.000	0.000
64	A	83	GLU	-1	-0.888	-0.954	25.770	0.262	0.262	0.000	0.000	0.000	0.000
65	A	84	LEU	0	-0.017	-0.001	19.350	-0.015	-0.015	0.000	0.000	0.000	0.000
66	A	85	LYS	1	0.796	0.891	22.898	-0.162	-0.162	0.000	0.000	0.000	0.000
67	A	86	LEU	0	-0.051	-0.035	19.604	-0.013	-0.013	0.000	0.000	0.000	0.000
68	A	87	ALA	0	0.050	0.036	15.680	0.018	0.018	0.000	0.000	0.000	0.000
69	A	88	CYS	0	-0.118	-0.051	15.410	-0.029	-0.029	0.000	0.000	0.000	0.000
70	A	89	THR	0	0.055	0.031	10.238	0.069	0.069	0.000	0.000	0.000	0.000
71	A	90	HIS	0	-0.046	-0.016	10.372	-0.054	-0.054	0.000	0.000	0.000	0.000
72	A	91	SER	0	0.024	0.012	7.511	0.061	0.061	0.000	0.000	0.000	0.000
73	A	92	TYR	0	-0.059	-0.039	7.206	0.378	0.378	0.000	0.000	0.000	0.000
74	A	93	GLY	0	0.013	0.003	7.271	-0.595	-0.595	0.000	0.000	0.000	0.000
75	A	94	ASP	-1	-0.935	-0.969	3.989	-8.746	-8.261	0.002	-0.154	-0.333	-0.001
76	A	95	VAL	0	-0.008	0.007	2.393	-7.073	-3.797	1.785	-2.047	-3.014	-0.021
77	A	96	GLY	0	0.006	0.006	3.332	2.196	2.748	0.002	-0.196	-0.358	0.000
78	A	97	ILE	0	-0.009	-0.007	5.367	-0.092	-0.092	-0.001	-0.005	0.007	0.000
79	A	98	LEU	0	0.004	-0.012	8.427	0.132	0.132	0.000	0.000	0.000	0.000
80	A	99	ILE	0	-0.006	0.004	10.656	0.049	0.049	0.000	0.000	0.000	0.000
81	A	100	LEU	0	0.000	0.002	14.125	0.014	0.014	0.000	0.000	0.000	0.000
82	A	101	PHE	0	-0.002	-0.015	16.921	-0.033	-0.033	0.000	0.000	0.000	0.000
83	A	102	TYR	0	0.011	-0.026	18.684	0.025	0.025	0.000	0.000	0.000	0.000
84	A	103	GLU	-1	-0.888	-0.937	23.162	0.110	0.110	0.000	0.000	0.000	0.000
85	A	104	ILE	0	-0.019	0.006	24.390	0.016	0.016	0.000	0.000	0.000	0.000
86	A	105	LEU	0	-0.012	-0.009	28.235	-0.017	-0.017	0.000	0.000	0.000	0.000
87	A	106	TYR	0	-0.003	-0.001	31.411	-0.016	-0.016	0.000	0.000	0.000	0.000
88	A	107	TRP	0	0.029	0.015	30.762	0.013	0.013	0.000	0.000	0.000	0.000
89	A	108	LYS	1	0.924	0.977	32.628	-0.141	-0.141	0.000	0.000	0.000	0.000
90	A	109	GLY	0	0.034	0.011	33.459	0.003	0.003	0.000	0.000	0.000	0.000
91	A	110	GLU	-1	-0.850	-0.934	34.615	0.049	0.049	0.000	0.000	0.000	0.000
92	A	111	PRO	0	-0.016	-0.002	29.889	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	112	ARG	1	0.926	0.964	30.871	-0.050	-0.050	0.000	0.000	0.000	0.000
94	A	113	ALA	0	-0.005	-0.004	28.822	0.008	0.008	0.000	0.000	0.000	0.000
95	A	114	LYS	1	0.782	0.902	27.108	-0.098	-0.098	0.000	0.000	0.000	0.000
96	A	115	HIS	0	-0.048	-0.024	19.859	-0.025	-0.025	0.000	0.000	0.000	0.000
97	A	116	HIS	0	-0.049	-0.040	21.459	-0.013	-0.013	0.000	0.000	0.000	0.000
98	A	117	MET	0	-0.035	-0.005	25.488	0.008	0.008	0.000	0.000	0.000	0.000
99	A	118	MET	0	-0.050	-0.021	28.007	0.007	0.007	0.000	0.000	0.000	0.000
100	A	119	LEU	0	0.009	0.016	27.195	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	120	GLU	-1	-0.814	-0.881	29.932	-0.060	-0.060	0.000	0.000	0.000	0.000
102	A	121	TRP	0	0.017	0.015	30.653	0.003	0.003	0.000	0.000	0.000	0.000
103	A	122	ILE	0	-0.017	-0.016	28.626	-0.004	-0.004	0.000	0.000	0.000	0.000
104	A	123	HIS	0	0.034	0.003	32.783	0.014	0.014	0.000	0.000	0.000	0.000
105	A	124	PRO	0	0.066	0.033	30.307	-0.010	-0.010	0.000	0.000	0.000	0.000
106	A	125	GLU	-1	-0.844	-0.925	30.402	-0.007	-0.007	0.000	0.000	0.000	0.000
107	A	126	GLU	-1	-0.834	-0.927	32.113	-0.049	-0.049	0.000	0.000	0.000	0.000
108	A	127	LEU	0	-0.023	-0.006	25.084	-0.014	-0.014	0.000	0.000	0.000	0.000
109	A	128	LYS	1	0.830	0.904	27.716	0.021	0.021	0.000	0.000	0.000	0.000
110	A	129	HIS	0	0.004	0.009	28.527	-0.026	-0.026	0.000	0.000	0.000	0.000
111	A	130	ARG	1	0.761	0.873	27.996	0.061	0.061	0.000	0.000	0.000	0.000
112	A	131	ASN	0	0.010	0.005	25.363	-0.025	-0.025	0.000	0.000	0.000	0.000
113	A	132	ILE	0	-0.004	0.005	22.666	0.000	0.000	0.000	0.000	0.000	0.000
114	A	133	PRO	0	0.053	0.028	17.799	-0.025	-0.025	0.000	0.000	0.000	0.000
115	A	134	GLU	-1	-0.844	-0.916	17.425	-0.454	-0.454	0.000	0.000	0.000	0.000
116	A	135	ALA	0	0.026	0.007	14.497	0.028	0.028	0.000	0.000	0.000	0.000
117	A	136	ASN	0	0.035	0.001	16.475	0.026	0.026	0.000	0.000	0.000	0.000
118	A	137	ARG	1	0.860	0.935	19.063	0.227	0.227	0.000	0.000	0.000	0.000
119	A	138	LYS	1	0.827	0.912	16.506	0.446	0.446	0.000	0.000	0.000	0.000
120	A	139	ILE	0	-0.017	-0.005	16.747	0.033	0.033	0.000	0.000	0.000	0.000
121	A	140	LEU	0	0.015	0.014	19.995	0.035	0.035	0.000	0.000	0.000	0.000
122	A	141	HIS	0	0.045	0.022	21.057	0.017	0.017	0.000	0.000	0.000	0.000
123	A	142	LYS	1	0.927	0.962	18.046	-0.088	-0.088	0.000	0.000	0.000	0.000
124	A	143	ILE	0	0.042	0.027	20.659	0.021	0.021	0.000	0.000	0.000	0.000
125	A	144	TYR	0	0.013	-0.028	24.180	0.006	0.006	0.000	0.000	0.000	0.000
126	A	145	LYS	1	0.958	0.980	26.321	-0.100	-0.100	0.000	0.000	0.000	0.000
127	A	146	ALA	0	-0.029	-0.011	24.572	0.010	0.010	0.000	0.000	0.000	0.000
128	A	147	LEU	0	-0.045	-0.010	26.700	0.009	0.009	0.000	0.000	0.000	0.000
129	A	148	GLY	0	-0.024	0.005	29.239	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	149	LEU	0	-0.020	0.000	30.050	-0.008	-0.008	0.000	0.000	0.000	0.000
131	A	150	GLU	-1	-0.910	-0.940	30.415	-0.018	-0.018	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:20:HIS)