FMO DATABASE

FMODB ID: MNLQZ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1776758.086141
FMO2-HF: Nuclear repulsion	1711205.738399
FMO2-HF: Total energy	-65552.347742
FMO2-MP2: Total energy	-65746.075641

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.
-19.686	-8.404	9.655	-6.998	-13.936	-0.048

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 : 0.010 / q_NPA : 0.013

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	-0.005	0.001	2.288	-1.324	2.172	1.150	-1.730	-2.917	-0.003
4	A	4	GLY	0	0.053	0.031	4.737	0.218	0.297	-0.001	-0.011	-0.067	0.000
5	A	5	ILE	0	-0.061	-0.032	8.343	0.199	0.199	0.000	0.000	0.000	0.000
6	A	6	ILE	0	0.027	0.016	11.103	0.041	0.041	0.000	0.000	0.000	0.000
7	A	7	GLY	0	0.069	0.032	14.422	0.022	0.022	0.000	0.000	0.000	0.000
8	A	8	ALA	0	0.009	0.026	13.815	0.016	0.016	0.000	0.000	0.000	0.000
9	A	9	THR	0	-0.126	-0.092	15.676	0.022	0.022	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.050	0.041	19.044	0.044	0.044	0.000	0.000	0.000	0.000
11	A	11	ARG	1	0.823	0.894	18.321	0.265	0.265	0.000	0.000	0.000	0.000
12	A	12	ALA	0	0.085	0.021	16.070	-0.039	-0.039	0.000	0.000	0.000	0.000
13	A	13	GLY	0	0.082	0.039	13.706	-0.067	-0.067	0.000	0.000	0.000	0.000
14	A	14	SER	0	-0.052	-0.015	13.584	-0.126	-0.126	0.000	0.000	0.000	0.000
15	A	15	ARG	1	0.835	0.885	14.669	0.551	0.551	0.000	0.000	0.000	0.000
16	A	16	ILE	0	0.034	0.015	9.086	-0.071	-0.071	0.000	0.000	0.000	0.000
17	A	17	LEU	0	0.004	0.014	9.677	-0.268	-0.268	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.837	-0.929	10.939	-1.195	-1.195	0.000	0.000	0.000	0.000
19	A	19	GLU	-1	-0.830	-0.901	9.360	-1.085	-1.085	0.000	0.000	0.000	0.000
20	A	20	ALA	0	-0.011	-0.014	6.540	-0.139	-0.139	0.000	0.000	0.000	0.000
21	A	21	LYS	1	0.814	0.886	7.326	0.664	0.664	0.000	0.000	0.000	0.000
22	A	22	ASN	0	-0.094	-0.063	9.235	0.098	0.098	0.000	0.000	0.000	0.000
23	A	23	ARG	1	0.692	0.807	7.355	1.303	1.303	0.000	0.000	0.000	0.000
24	A	24	GLY	0	-0.022	-0.001	6.521	0.009	0.009	0.000	0.000	0.000	0.000
25	A	25	HIS	0	-0.033	-0.017	2.539	-7.585	-4.270	1.940	-1.843	-3.411	-0.022
26	A	26	GLU	-1	-0.857	-0.918	3.182	-2.491	-1.197	0.019	-0.407	-0.905	0.000
27	A	27	VAL	0	-0.021	-0.007	5.055	0.160	0.194	-0.001	-0.012	-0.021	0.000
28	A	28	THR	0	-0.003	-0.012	8.078	0.578	0.578	0.000	0.000	0.000	0.000
29	A	29	ALA	0	-0.011	-0.007	10.227	0.113	0.113	0.000	0.000	0.000	0.000
30	A	30	ILE	0	0.002	0.008	11.094	0.078	0.078	0.000	0.000	0.000	0.000
31	A	31	VAL	0	-0.024	-0.020	14.760	0.052	0.052	0.000	0.000	0.000	0.000
32	A	32	ARG	1	0.913	0.948	18.450	0.277	0.277	0.000	0.000	0.000	0.000
33	A	33	ASN	0	-0.049	-0.033	21.963	0.030	0.030	0.000	0.000	0.000	0.000
34	A	34	ALA	0	0.073	0.031	20.792	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	35	GLY	0	-0.014	0.010	21.794	-0.019	-0.019	0.000	0.000	0.000	0.000
36	A	36	LYS	1	0.891	0.938	22.487	0.474	0.474	0.000	0.000	0.000	0.000
37	A	37	ILE	0	0.044	0.038	16.332	0.014	0.014	0.000	0.000	0.000	0.000
38	A	38	THR	0	0.076	0.016	20.076	-0.036	-0.036	0.000	0.000	0.000	0.000
39	A	39	GLN	0	-0.052	-0.021	21.253	0.001	0.001	0.000	0.000	0.000	0.000
40	A	40	THR	0	-0.053	-0.039	20.132	0.042	0.042	0.000	0.000	0.000	0.000
41	A	41	HIS	0	-0.017	0.007	14.728	-0.092	-0.092	0.000	0.000	0.000	0.000
42	A	42	LYS	1	0.834	0.908	17.115	0.569	0.569	0.000	0.000	0.000	0.000
43	A	43	ASP	-1	-0.807	-0.888	14.239	-0.957	-0.957	0.000	0.000	0.000	0.000
44	A	44	ILE	0	0.010	0.017	10.786	-0.143	-0.143	0.000	0.000	0.000	0.000
45	A	45	ASN	0	0.013	0.012	10.772	0.433	0.433	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.023	-0.023	12.456	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	47	LEU	0	0.007	0.016	14.167	0.077	0.077	0.000	0.000	0.000	0.000
48	A	48	GLN	0	-0.008	-0.013	16.199	0.010	0.010	0.000	0.000	0.000	0.000
49	A	49	LYS	1	0.806	0.875	18.228	0.329	0.329	0.000	0.000	0.000	0.000
50	A	50	ASP	-1	-0.760	-0.856	19.427	-0.284	-0.284	0.000	0.000	0.000	0.000
51	A	51	ILE	0	-0.012	-0.002	17.494	0.002	0.002	0.000	0.000	0.000	0.000
52	A	52	PHE	0	-0.006	-0.018	19.546	0.025	0.025	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.863	-0.918	21.181	-0.208	-0.208	0.000	0.000	0.000	0.000
54	A	54	LEU	0	-0.062	-0.013	15.168	-0.005	-0.005	0.000	0.000	0.000	0.000
55	A	55	THR	0	-0.033	-0.040	17.430	0.059	0.059	0.000	0.000	0.000	0.000
56	A	56	LEU	0	0.074	0.024	14.380	-0.032	-0.032	0.000	0.000	0.000	0.000
57	A	57	SER	0	0.008	0.012	14.503	0.019	0.019	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.797	-0.869	14.096	-0.314	-0.314	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.005	0.002	11.455	-0.124	-0.124	0.000	0.000	0.000	0.000
60	A	60	SER	0	-0.077	-0.040	9.986	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	61	ASP	-1	-0.888	-0.924	9.482	-0.974	-0.974	0.000	0.000	0.000	0.000
62	A	62	GLN	0	-0.061	-0.045	6.234	-0.924	-0.924	0.000	0.000	0.000	0.000
63	A	63	ASN	0	0.031	0.015	2.303	-3.582	-2.415	3.738	-1.812	-3.093	-0.018
64	A	64	VAL	0	-0.006	0.001	3.406	0.475	1.313	0.587	-0.258	-1.166	0.001
65	A	65	VAL	0	0.014	0.006	5.481	-0.990	-0.990	0.000	0.000	0.000	0.000
66	A	66	VAL	0	0.025	0.010	7.425	0.211	0.211	0.000	0.000	0.000	0.000
67	A	67	ASP	-1	-0.885	-0.957	9.929	-0.319	-0.319	0.000	0.000	0.000	0.000
68	A	68	ALA	0	0.003	-0.010	13.708	0.050	0.050	0.000	0.000	0.000	0.000
69	A	69	TYR	0	-0.004	-0.002	15.494	-0.008	-0.008	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.013	-0.014	18.692	0.024	0.024	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.112	-0.064	19.789	-0.014	-0.014	0.000	0.000	0.000	0.000
72	A	72	SER	0	-0.047	-0.049	22.643	0.002	0.002	0.000	0.000	0.000	0.000
73	A	73	PRO	0	0.001	-0.017	26.355	0.005	0.005	0.000	0.000	0.000	0.000
74	A	74	ASP	-1	-0.747	-0.840	27.588	-0.206	-0.206	0.000	0.000	0.000	0.000
75	A	75	GLU	-1	-0.847	-0.925	21.863	-0.320	-0.320	0.000	0.000	0.000	0.000
76	A	76	ALA	0	-0.003	-0.002	24.854	0.009	0.009	0.000	0.000	0.000	0.000
77	A	77	GLU	-1	-0.992	-0.986	26.432	-0.105	-0.105	0.000	0.000	0.000	0.000
78	A	78	LYS	1	0.818	0.907	25.242	0.214	0.214	0.000	0.000	0.000	0.000
79	A	79	HIS	0	0.002	0.019	21.348	0.017	0.017	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.039	-0.012	22.757	0.008	0.008	0.000	0.000	0.000	0.000
81	A	81	THR	0	0.036	0.004	24.117	0.011	0.011	0.000	0.000	0.000	0.000
82	A	82	SER	0	0.008	-0.008	21.021	0.004	0.004	0.000	0.000	0.000	0.000
83	A	83	LEU	0	0.033	0.018	17.551	0.003	0.003	0.000	0.000	0.000	0.000
84	A	84	ASP	-1	-0.827	-0.899	20.313	0.032	0.032	0.000	0.000	0.000	0.000
85	A	85	HIS	0	-0.032	0.002	19.824	0.040	0.040	0.000	0.000	0.000	0.000
86	A	86	LEU	0	0.027	0.019	15.205	0.018	0.018	0.000	0.000	0.000	0.000
87	A	87	ILE	0	-0.036	-0.018	17.998	0.044	0.044	0.000	0.000	0.000	0.000
88	A	88	SER	0	-0.091	-0.052	19.816	0.030	0.030	0.000	0.000	0.000	0.000
89	A	89	VAL	0	-0.012	-0.008	16.895	0.022	0.022	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.030	-0.020	13.384	0.010	0.010	0.000	0.000	0.000	0.000
91	A	91	ASN	0	-0.083	-0.051	16.714	0.076	0.076	0.000	0.000	0.000	0.000
92	A	92	GLY	0	0.024	0.020	19.382	-0.010	-0.010	0.000	0.000	0.000	0.000
93	A	93	THR	0	-0.028	-0.001	13.183	0.065	0.065	0.000	0.000	0.000	0.000
94	A	94	VAL	0	0.000	-0.025	10.940	-0.009	-0.009	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.036	-0.012	9.858	0.210	0.210	0.000	0.000	0.000	0.000
96	A	96	PRO	0	0.023	0.032	7.609	0.262	0.262	0.000	0.000	0.000	0.000
97	A	97	ARG	1	0.784	0.843	5.807	-1.066	-1.066	0.000	0.000	0.000	0.000
98	A	98	LEU	0	-0.008	-0.003	8.619	-0.210	-0.210	0.000	0.000	0.000	0.000
99	A	99	LEU	0	-0.006	-0.018	7.476	0.097	0.097	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.020	0.009	10.575	-0.164	-0.164	0.000	0.000	0.000	0.000
101	A	101	VAL	0	-0.007	-0.003	12.779	0.022	0.022	0.000	0.000	0.000	0.000
102	A	102	GLY	0	0.038	0.028	15.338	-0.001	-0.001	0.000	0.000	0.000	0.000
103	A	103	GLY	0	0.017	-0.011	18.538	-0.038	-0.038	0.000	0.000	0.000	0.000
104	A	104	ALA	0	-0.026	-0.013	21.329	0.006	0.006	0.000	0.000	0.000	0.000
105	A	105	ALA	0	0.015	0.022	24.063	-0.003	-0.003	0.000	0.000	0.000	0.000
106	A	125	ALA	0	0.009	-0.007	29.164	0.005	0.005	0.000	0.000	0.000	0.000
107	A	126	PRO	0	-0.023	-0.003	25.707	-0.020	-0.020	0.000	0.000	0.000	0.000
108	A	127	TYR	0	-0.009	-0.013	24.603	0.018	0.018	0.000	0.000	0.000	0.000
109	A	128	TYR	0	0.047	0.049	20.743	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	129	PRO	0	0.010	0.001	20.041	0.021	0.021	0.000	0.000	0.000	0.000
111	A	130	THR	0	0.034	0.026	23.164	0.009	0.009	0.000	0.000	0.000	0.000
112	A	131	ALA	0	0.049	0.023	26.141	0.010	0.010	0.000	0.000	0.000	0.000
113	A	132	ARG	1	0.972	0.970	27.108	0.064	0.064	0.000	0.000	0.000	0.000
114	A	133	ALA	0	0.009	0.015	25.611	0.011	0.011	0.000	0.000	0.000	0.000
115	A	134	GLN	0	0.036	0.020	21.208	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	135	ALA	0	-0.027	-0.013	23.522	0.018	0.018	0.000	0.000	0.000	0.000
117	A	136	LYS	1	0.830	0.887	25.787	0.017	0.017	0.000	0.000	0.000	0.000
118	A	137	GLN	0	0.051	0.023	20.539	0.017	0.017	0.000	0.000	0.000	0.000
119	A	138	LEU	0	0.013	0.008	20.137	0.025	0.025	0.000	0.000	0.000	0.000
120	A	139	GLU	-1	-0.853	-0.904	22.648	0.035	0.035	0.000	0.000	0.000	0.000
121	A	140	HIS	1	0.823	0.896	23.911	0.002	0.002	0.000	0.000	0.000	0.000
122	A	141	LEU	0	0.036	0.040	17.707	0.009	0.009	0.000	0.000	0.000	0.000
123	A	142	LYS	1	0.965	0.983	21.268	-0.068	-0.068	0.000	0.000	0.000	0.000
124	A	143	SER	0	-0.100	-0.066	23.282	0.011	0.011	0.000	0.000	0.000	0.000
125	A	144	HIS	1	0.861	0.929	21.476	-0.132	-0.132	0.000	0.000	0.000	0.000
126	A	145	GLN	0	-0.018	-0.010	19.419	0.003	0.003	0.000	0.000	0.000	0.000
127	A	146	ALA	0	0.000	0.003	18.751	0.037	0.037	0.000	0.000	0.000	0.000
128	A	147	GLU	-1	-0.850	-0.906	19.222	0.216	0.216	0.000	0.000	0.000	0.000
129	A	148	PHE	0	0.012	0.008	14.489	-0.010	-0.010	0.000	0.000	0.000	0.000
130	A	149	SER	0	-0.015	0.017	10.718	0.069	0.069	0.000	0.000	0.000	0.000
131	A	150	TRP	0	-0.045	-0.015	12.370	-0.066	-0.066	0.000	0.000	0.000	0.000
132	A	151	THR	0	0.017	0.009	10.979	0.134	0.134	0.000	0.000	0.000	0.000
133	A	152	TYR	0	-0.040	-0.035	12.973	-0.072	-0.072	0.000	0.000	0.000	0.000
134	A	153	ILE	0	0.004	0.014	12.152	0.032	0.032	0.000	0.000	0.000	0.000
135	A	154	SER	0	0.020	0.010	15.303	-0.032	-0.032	0.000	0.000	0.000	0.000
136	A	155	PRO	0	-0.009	-0.002	18.018	0.002	0.002	0.000	0.000	0.000	0.000
137	A	156	SER	0	0.010	0.002	19.617	0.017	0.017	0.000	0.000	0.000	0.000
138	A	157	ALA	0	-0.007	-0.013	21.716	0.018	0.018	0.000	0.000	0.000	0.000
139	A	158	MET	0	-0.025	0.011	24.608	-0.004	-0.004	0.000	0.000	0.000	0.000
140	A	159	PHE	0	0.040	0.008	18.998	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	160	GLU	-1	-0.898	-0.932	24.242	-0.167	-0.167	0.000	0.000	0.000	0.000
142	A	161	PRO	0	-0.036	-0.029	25.812	-0.024	-0.024	0.000	0.000	0.000	0.000
143	A	162	GLY	0	0.011	0.025	26.269	0.004	0.004	0.000	0.000	0.000	0.000
144	A	184	PHE	0	-0.034	-0.031	26.469	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	185	ILE	0	-0.015	-0.005	19.479	0.001	0.001	0.000	0.000	0.000	0.000
146	A	186	SER	0	0.024	0.021	20.563	-0.002	-0.002	0.000	0.000	0.000	0.000
147	A	187	MET	0	-0.044	-0.017	17.348	-0.009	-0.009	0.000	0.000	0.000	0.000
148	A	188	GLU	-1	-0.817	-0.897	16.416	-0.579	-0.579	0.000	0.000	0.000	0.000
149	A	189	ASP	-1	-0.786	-0.896	15.301	-0.372	-0.372	0.000	0.000	0.000	0.000
150	A	190	TYR	0	-0.056	-0.037	15.321	-0.003	-0.003	0.000	0.000	0.000	0.000
151	A	191	ALA	0	0.009	0.003	12.234	-0.012	-0.012	0.000	0.000	0.000	0.000
152	A	192	ILE	0	0.014	0.019	10.680	-0.115	-0.115	0.000	0.000	0.000	0.000
153	A	193	ALA	0	-0.020	-0.009	10.540	-0.033	-0.033	0.000	0.000	0.000	0.000
154	A	194	VAL	0	-0.031	-0.026	8.494	0.062	0.062	0.000	0.000	0.000	0.000
155	A	195	LEU	0	0.002	0.004	5.202	-0.012	-0.012	0.000	0.000	0.000	0.000
156	A	196	ASP	-1	-0.794	-0.867	5.772	-0.716	-0.716	0.000	0.000	0.000	0.000
157	A	197	GLU	-1	-0.754	-0.844	7.381	0.526	0.526	0.000	0.000	0.000	0.000
158	A	198	ILE	0	-0.024	-0.006	2.450	0.375	-0.056	2.083	-0.267	-1.385	0.000
159	A	199	GLU	-1	-0.779	-0.861	3.084	-2.877	-1.494	0.140	-0.667	-0.855	-0.006
160	A	200	ARG	1	0.762	0.860	3.967	0.948	1.055	0.000	0.009	-0.116	0.000
161	A	201	PRO	0	-0.016	0.006	5.509	-0.100	-0.100	0.000	0.000	0.000	0.000
162	A	202	ASN	0	-0.085	-0.061	8.236	-0.047	-0.047	0.000	0.000	0.000	0.000
163	A	203	HIS	1	0.796	0.897	11.273	-0.232	-0.232	0.000	0.000	0.000	0.000
164	A	204	LEU	0	0.039	0.028	8.800	-0.013	-0.013	0.000	0.000	0.000	0.000
165	A	205	ASN	0	-0.035	-0.040	12.440	0.028	0.028	0.000	0.000	0.000	0.000
166	A	206	GLU	-1	-0.856	-0.896	15.021	0.181	0.181	0.000	0.000	0.000	0.000
167	A	207	HIS	0	0.002	0.002	15.594	-0.034	-0.034	0.000	0.000	0.000	0.000
168	A	208	PHE	0	-0.021	-0.015	12.160	0.016	0.016	0.000	0.000	0.000	0.000
169	A	209	THR	0	-0.014	-0.016	17.333	-0.027	-0.027	0.000	0.000	0.000	0.000
170	A	210	VAL	0	0.009	0.011	15.225	0.021	0.021	0.000	0.000	0.000	0.000
171	A	211	ALA	0	0.027	0.005	17.670	0.014	0.014	0.000	0.000	0.000	0.000
172	A	212	GLY	0	-0.006	0.003	20.038	-0.028	-0.028	0.000	0.000	0.000	0.000

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