FMO DATABASE

FMODB ID: 98R12

Calculation Name: 3EW7-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3EW7

Chain ID: A

ChEMBL ID:

UniProt ID: Q8Y8U8

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

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	172
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1771945.604041
FMO2-HF: Nuclear repulsion	1706393.86232
FMO2-HF: Total energy	-65551.741721
FMO2-MP2: Total energy	-65745.562117

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:MET)

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

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.
-22.348	-12.664	14.3	-8.348	-15.633	-0.068

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.006 / q_NPA : 0.006

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	ILE	0	0.016	0.015	2.698	-1.062	2.693	0.436	-1.613	-2.578	-0.001
4	A	4	GLY	0	0.057	0.035	4.898	0.164	0.244	-0.001	-0.009	-0.069	0.000
5	A	5	ILE	0	-0.050	-0.035	8.174	0.218	0.218	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.028	0.020	11.138	0.068	0.068	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.062	0.028	14.446	0.020	0.020	0.000	0.000	0.000	0.000
8	A	8	ALA	0	-0.028	-0.014	14.086	0.011	0.011	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.066	-0.041	15.673	0.010	0.010	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.035	0.028	18.920	0.039	0.039	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.893	0.940	18.597	0.305	0.305	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.080	0.015	16.232	-0.038	-0.038	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.073	0.032	13.882	-0.074	-0.074	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.051	-0.002	13.892	-0.122	-0.122	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.845	0.889	15.075	0.612	0.612	0.000	0.000	0.000	0.000
16	A	16	ILE	0	0.022	0.015	9.403	-0.112	-0.112	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.001	0.013	9.988	-0.282	-0.282	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.884	-0.954	10.777	-1.297	-1.297	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.843	-0.919	10.033	-1.232	-1.232	0.000	0.000	0.000	0.000
20	A	20	ALA	0	0.010	-0.006	6.822	-0.156	-0.156	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.848	0.908	6.855	0.702	0.702	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.053	-0.033	8.391	0.070	0.070	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.675	0.812	7.189	1.560	1.560	0.000	0.000	0.000	0.000
24	A	24	GLY	0	-0.025	-0.011	6.111	0.141	0.141	0.000	0.000	0.000	0.000
25	A	25	HIS	0	-0.051	-0.020	2.332	-10.995	-8.285	5.108	-3.026	-4.791	-0.039
26	A	26	GLU	-1	-0.862	-0.916	3.252	-0.757	0.033	0.008	-0.164	-0.634	0.000
27	A	27	VAL	0	-0.003	-0.005	5.217	-0.168	-0.214	-0.001	-0.013	0.061	0.000
28	A	28	THR	0	-0.004	-0.007	8.154	0.599	0.599	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.026	-0.011	10.503	0.049	0.049	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.011	0.010	11.342	0.103	0.103	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.035	-0.030	14.968	0.035	0.035	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.944	0.967	18.622	0.297	0.297	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.020	-0.016	22.229	0.027	0.027	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.035	0.024	21.243	-0.030	-0.030	0.000	0.000	0.000	0.000
35	A	35	GLY	0	0.009	-0.003	22.232	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.891	0.943	22.643	0.486	0.486	0.000	0.000	0.000	0.000
37	A	37	ILE	0	0.029	0.015	16.470	0.019	0.019	0.000	0.000	0.000	0.000
38	A	38	THR	0	0.106	0.056	19.908	-0.043	-0.043	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.028	-0.009	21.106	-0.020	-0.020	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.031	-0.024	19.514	0.042	0.042	0.000	0.000	0.000	0.000
41	A	41	HIS	0	-0.014	-0.005	14.643	-0.073	-0.073	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.836	0.912	17.395	0.513	0.513	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.821	-0.904	13.507	-1.018	-1.018	0.000	0.000	0.000	0.000
44	A	44	ILE	0	-0.018	0.009	10.921	-0.079	-0.079	0.000	0.000	0.000	0.000
45	A	45	ASN	0	0.030	0.018	10.977	0.382	0.382	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.021	-0.014	12.650	-0.046	-0.046	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.022	0.030	14.250	0.079	0.079	0.000	0.000	0.000	0.000
48	A	48	GLN	0	-0.026	-0.025	16.278	-0.012	-0.012	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.817	0.877	18.471	0.278	0.278	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.809	-0.884	19.067	-0.303	-0.303	0.000	0.000	0.000	0.000
51	A	51	ILE	0	0.016	0.005	17.478	0.010	0.010	0.000	0.000	0.000	0.000
52	A	52	PHE	0	-0.018	-0.028	19.477	0.030	0.030	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.896	-0.929	21.600	-0.176	-0.176	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.066	-0.021	15.180	0.001	0.001	0.000	0.000	0.000	0.000
55	A	55	THR	0	-0.063	-0.040	17.883	0.051	0.051	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.089	0.025	14.504	-0.034	-0.034	0.000	0.000	0.000	0.000
57	A	57	SER	0	-0.007	0.005	14.608	0.021	0.021	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.770	-0.864	14.238	-0.238	-0.238	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.004	0.002	11.667	-0.122	-0.122	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.094	-0.040	9.932	0.013	0.013	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.930	-0.953	9.921	-0.588	-0.588	0.000	0.000	0.000	0.000
62	A	62	GLN	0	-0.058	-0.040	6.090	-0.844	-0.844	0.000	0.000	0.000	0.000
63	A	63	ASN	0	0.015	0.006	2.213	-2.594	-2.549	5.205	-1.777	-3.473	-0.014
64	A	64	VAL	0	-0.014	-0.016	3.184	-0.095	0.890	0.464	-0.243	-1.205	0.001
65	A	65	VAL	0	0.029	0.021	5.552	-0.903	-0.903	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.000	-0.009	7.371	0.165	0.165	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.874	-0.958	9.803	-0.337	-0.337	0.000	0.000	0.000	0.000
68	A	68	ALA	0	-0.025	-0.018	13.533	0.041	0.041	0.000	0.000	0.000	0.000
69	A	69	TYR	0	0.038	0.024	15.217	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.015	-0.001	18.465	0.023	0.023	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.097	-0.060	19.973	-0.020	-0.020	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.048	-0.051	22.724	0.000	0.000	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.023	-0.010	26.399	0.004	0.004	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.753	-0.843	27.924	-0.216	-0.216	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.875	-0.936	22.191	-0.329	-0.329	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.015	-0.009	24.750	0.002	0.002	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.992	-0.993	26.569	-0.121	-0.121	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.827	0.913	25.617	0.214	0.214	0.000	0.000	0.000	0.000
79	A	79	HIS	0	0.024	0.029	21.611	0.006	0.006	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.022	-0.023	22.403	0.006	0.006	0.000	0.000	0.000	0.000
81	A	81	THR	0	0.015	0.002	24.058	0.010	0.010	0.000	0.000	0.000	0.000
82	A	82	SER	0	0.020	0.004	20.946	0.009	0.009	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.027	0.012	17.174	0.009	0.009	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.820	-0.889	20.081	0.008	0.008	0.000	0.000	0.000	0.000
85	A	85	HIS	0	-0.036	-0.012	20.041	0.042	0.042	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.034	0.013	15.236	0.021	0.021	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.024	-0.006	17.829	0.050	0.050	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.085	-0.044	19.550	0.036	0.036	0.000	0.000	0.000	0.000
89	A	89	VAL	0	-0.035	-0.014	17.058	0.027	0.027	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.018	-0.020	13.133	0.025	0.025	0.000	0.000	0.000	0.000
91	A	91	ASN	0	-0.113	-0.062	16.813	0.079	0.079	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.024	0.024	19.376	0.000	0.000	0.000	0.000	0.000	0.000
93	A	93	THR	0	-0.005	0.008	13.446	0.065	0.065	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.010	-0.015	10.960	-0.032	-0.032	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.045	-0.037	10.184	0.218	0.218	0.000	0.000	0.000	0.000
96	A	96	PRO	0	0.023	0.045	7.688	0.274	0.274	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.768	0.837	5.484	-0.523	-0.523	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.012	-0.011	8.526	-0.240	-0.240	0.000	0.000	0.000	0.000
99	A	99	LEU	0	-0.010	-0.011	7.339	0.051	0.051	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.005	-0.003	10.410	-0.114	-0.114	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.000	0.009	12.496	0.012	0.012	0.000	0.000	0.000	0.000
102	A	102	GLY	0	0.029	0.024	14.990	0.018	0.018	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.003	-0.026	18.478	-0.043	-0.043	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.029	-0.010	21.187	0.010	0.010	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.031	0.032	24.240	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	125	ALA	0	-0.001	-0.013	29.782	0.004	0.004	0.000	0.000	0.000	0.000
107	A	126	PRO	0	-0.030	-0.003	25.984	-0.021	-0.021	0.000	0.000	0.000	0.000
108	A	127	TYR	0	0.000	-0.013	24.217	0.017	0.017	0.000	0.000	0.000	0.000
109	A	128	TYR	0	0.035	0.042	20.809	-0.012	-0.012	0.000	0.000	0.000	0.000
110	A	129	PRO	0	0.019	0.006	20.228	0.024	0.024	0.000	0.000	0.000	0.000
111	A	130	THR	0	0.020	0.013	23.318	0.007	0.007	0.000	0.000	0.000	0.000
112	A	131	ALA	0	0.059	0.023	25.689	0.004	0.004	0.000	0.000	0.000	0.000
113	A	132	ARG	1	0.979	0.973	27.276	0.084	0.084	0.000	0.000	0.000	0.000
114	A	133	ALA	0	0.007	0.005	25.544	0.010	0.010	0.000	0.000	0.000	0.000
115	A	134	GLN	0	0.028	0.031	21.064	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	135	ALA	0	0.000	-0.001	23.483	0.015	0.015	0.000	0.000	0.000	0.000
117	A	136	LYS	1	0.834	0.886	25.750	0.042	0.042	0.000	0.000	0.000	0.000
118	A	137	GLN	0	0.054	0.038	20.295	0.013	0.013	0.000	0.000	0.000	0.000
119	A	138	LEU	0	0.030	0.010	19.904	0.025	0.025	0.000	0.000	0.000	0.000
120	A	139	GLU	-1	-0.858	-0.895	22.397	0.007	0.007	0.000	0.000	0.000	0.000
121	A	140	HIS	1	0.809	0.869	23.590	0.029	0.029	0.000	0.000	0.000	0.000
122	A	141	LEU	0	0.009	0.020	17.417	0.014	0.014	0.000	0.000	0.000	0.000
123	A	142	LYS	1	0.958	0.977	20.961	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	143	SER	0	-0.086	-0.039	22.833	0.011	0.011	0.000	0.000	0.000	0.000
125	A	144	HIS	1	0.870	0.940	20.947	-0.103	-0.103	0.000	0.000	0.000	0.000
126	A	145	GLN	0	-0.025	-0.005	18.914	0.003	0.003	0.000	0.000	0.000	0.000
127	A	146	ALA	0	0.002	-0.010	18.517	0.030	0.030	0.000	0.000	0.000	0.000
128	A	147	GLU	-1	-0.851	-0.906	19.244	0.204	0.204	0.000	0.000	0.000	0.000
129	A	148	PHE	0	0.044	0.013	14.506	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	149	SER	0	-0.006	0.028	10.725	0.043	0.043	0.000	0.000	0.000	0.000
131	A	150	TRP	0	-0.027	-0.003	12.093	-0.064	-0.064	0.000	0.000	0.000	0.000
132	A	151	THR	0	0.007	0.016	10.570	0.080	0.080	0.000	0.000	0.000	0.000
133	A	152	TYR	0	-0.034	-0.015	12.587	-0.077	-0.077	0.000	0.000	0.000	0.000
134	A	153	ILE	0	0.014	0.006	11.786	0.028	0.028	0.000	0.000	0.000	0.000
135	A	154	SER	0	0.000	-0.009	14.866	-0.028	-0.028	0.000	0.000	0.000	0.000
136	A	155	PRO	0	-0.010	0.007	17.701	-0.003	-0.003	0.000	0.000	0.000	0.000
137	A	156	SER	0	0.008	-0.003	19.205	0.022	0.022	0.000	0.000	0.000	0.000
138	A	157	ALA	0	-0.030	-0.013	21.518	0.022	0.022	0.000	0.000	0.000	0.000
139	A	158	MET	0	0.013	0.020	24.490	0.005	0.005	0.000	0.000	0.000	0.000
140	A	159	PHE	0	0.030	-0.006	19.215	-0.013	-0.013	0.000	0.000	0.000	0.000
141	A	160	GLU	-1	-0.889	-0.948	24.544	-0.178	-0.178	0.000	0.000	0.000	0.000
142	A	161	PRO	0	-0.089	-0.051	26.018	-0.019	-0.019	0.000	0.000	0.000	0.000
143	A	162	GLY	0	0.029	0.035	25.846	0.007	0.007	0.000	0.000	0.000	0.000
144	A	184	PHE	0	-0.044	-0.040	26.327	0.003	0.003	0.000	0.000	0.000	0.000
145	A	185	ILE	0	-0.049	-0.017	19.816	-0.009	-0.009	0.000	0.000	0.000	0.000
146	A	186	SER	0	0.074	0.057	20.928	0.000	0.000	0.000	0.000	0.000	0.000
147	A	187	MET	0	-0.048	-0.015	17.604	-0.019	-0.019	0.000	0.000	0.000	0.000
148	A	188	GLU	-1	-0.808	-0.912	16.531	-0.617	-0.617	0.000	0.000	0.000	0.000
149	A	189	ASP	-1	-0.817	-0.902	15.764	-0.438	-0.438	0.000	0.000	0.000	0.000
150	A	190	TYR	0	-0.053	-0.048	15.524	-0.024	-0.024	0.000	0.000	0.000	0.000
151	A	191	ALA	0	0.000	0.000	12.437	-0.034	-0.034	0.000	0.000	0.000	0.000
152	A	192	ILE	0	0.023	0.027	10.947	-0.168	-0.168	0.000	0.000	0.000	0.000
153	A	193	ALA	0	-0.002	0.005	11.029	-0.029	-0.029	0.000	0.000	0.000	0.000
154	A	194	VAL	0	-0.032	-0.028	8.579	-0.009	-0.009	0.000	0.000	0.000	0.000
155	A	195	LEU	0	0.004	-0.005	5.614	-0.116	-0.116	0.000	0.000	0.000	0.000
156	A	196	ASP	-1	-0.811	-0.870	6.201	-0.867	-0.867	0.000	0.000	0.000	0.000
157	A	197	GLU	-1	-0.749	-0.844	7.160	0.137	0.137	0.000	0.000	0.000	0.000
158	A	198	ILE	0	-0.034	-0.010	2.491	0.456	-0.268	2.535	-0.340	-1.471	0.000
159	A	199	GLU	-1	-0.775	-0.857	2.704	-5.040	-3.062	0.547	-1.164	-1.361	-0.015
160	A	200	ARG	1	0.763	0.861	4.139	1.264	1.375	-0.001	0.001	-0.112	0.000
161	A	201	PRO	0	-0.009	0.005	5.356	-0.021	-0.021	0.000	0.000	0.000	0.000
162	A	202	ASN	0	-0.087	-0.057	8.099	0.052	0.052	0.000	0.000	0.000	0.000
163	A	203	HIS	1	0.770	0.880	10.892	-0.049	-0.049	0.000	0.000	0.000	0.000
164	A	204	LEU	0	0.041	0.026	8.313	-0.028	-0.028	0.000	0.000	0.000	0.000
165	A	205	ASN	0	-0.022	-0.036	11.879	0.050	0.050	0.000	0.000	0.000	0.000
166	A	206	GLU	-1	-0.850	-0.899	14.411	0.110	0.110	0.000	0.000	0.000	0.000
167	A	207	HIS	0	-0.006	0.001	15.034	-0.051	-0.051	0.000	0.000	0.000	0.000
168	A	208	PHE	0	-0.019	-0.013	11.964	0.024	0.024	0.000	0.000	0.000	0.000
169	A	209	THR	0	0.001	-0.002	16.734	-0.034	-0.034	0.000	0.000	0.000	0.000
170	A	210	VAL	0	-0.006	-0.001	15.015	0.018	0.018	0.000	0.000	0.000	0.000
171	A	211	ALA	0	0.014	-0.008	17.517	0.021	0.021	0.000	0.000	0.000	0.000
172	A	212	GLY	0	-0.002	0.014	19.874	-0.022	-0.022	0.000	0.000	0.000	0.000

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