FMO DATABASE

FMODB ID: M3LZZ

Calculation Name: 3G7G-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3G7G

Chain ID: A

ChEMBL ID:

UniProt ID: Q97DZ9

Base Structure: X-ray

Registration Date: 2023-03-14

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	151
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1434452.890733
FMO2-HF: Nuclear repulsion	1374300.060254
FMO2-HF: Total energy	-60152.830479
FMO2-MP2: Total energy	-60327.511485

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:8:GLU)

Summations of interaction energy for fragment #1(A:8:GLU)

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.
-4.823	-1.196	0.41	-1.536	-2.5	0.004

Interaction energy analysis for fragmet #1(A:8:GLU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.882 / q_NPA : -0.942

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	10	ASN	0	0.006	0.004	2.824	-2.679	0.839	0.411	-1.522	-2.406	0.004
4	A	11	TYR	0	-0.047	-0.026	4.499	-3.887	-3.778	-0.001	-0.014	-0.094	0.000
5	A	12	GLU	-1	-0.836	-0.900	8.057	21.410	21.410	0.000	0.000	0.000	0.000
6	A	13	GLU	-1	-0.806	-0.875	11.422	17.015	17.015	0.000	0.000	0.000	0.000
7	A	14	VAL	0	-0.028	-0.005	14.347	-0.685	-0.685	0.000	0.000	0.000	0.000
8	A	15	PHE	0	-0.025	-0.026	17.140	-0.884	-0.884	0.000	0.000	0.000	0.000
9	A	16	SER	0	0.000	0.004	19.120	0.760	0.760	0.000	0.000	0.000	0.000
10	A	17	ILE	0	-0.040	-0.025	21.606	-0.542	-0.542	0.000	0.000	0.000	0.000
11	A	18	THR	0	-0.009	0.012	24.892	0.276	0.276	0.000	0.000	0.000	0.000
12	A	19	ILE	0	-0.021	-0.021	26.880	-0.332	-0.332	0.000	0.000	0.000	0.000
13	A	20	THR	0	0.025	0.006	29.846	0.063	0.063	0.000	0.000	0.000	0.000
14	A	21	VAL	0	-0.035	-0.027	32.134	-0.043	-0.043	0.000	0.000	0.000	0.000
15	A	22	ASP	-1	-0.828	-0.901	34.964	7.595	7.595	0.000	0.000	0.000	0.000
16	A	23	LYS	1	0.899	0.938	37.218	-7.001	-7.001	0.000	0.000	0.000	0.000
17	A	24	PRO	0	-0.011	-0.019	36.313	-0.018	-0.018	0.000	0.000	0.000	0.000
18	A	25	ILE	0	-0.001	0.007	38.449	-0.239	-0.239	0.000	0.000	0.000	0.000
19	A	26	LEU	0	-0.026	-0.019	39.710	0.155	0.155	0.000	0.000	0.000	0.000
20	A	27	ILE	0	-0.053	-0.022	39.787	-0.181	-0.181	0.000	0.000	0.000	0.000
21	A	28	GLY	0	0.021	0.006	40.930	-0.221	-0.221	0.000	0.000	0.000	0.000
22	A	29	GLN	0	-0.008	-0.015	39.134	0.304	0.304	0.000	0.000	0.000	0.000
23	A	30	ASP	-1	-0.810	-0.876	40.052	7.584	7.584	0.000	0.000	0.000	0.000
24	A	31	ASP	-1	-0.888	-0.953	39.030	7.991	7.991	0.000	0.000	0.000	0.000
25	A	32	ILE	0	-0.065	-0.039	37.901	0.100	0.100	0.000	0.000	0.000	0.000
26	A	33	VAL	0	-0.062	-0.030	36.115	0.289	0.289	0.000	0.000	0.000	0.000
27	A	34	GLY	0	0.050	0.027	35.055	0.360	0.360	0.000	0.000	0.000	0.000
28	A	35	ARG	1	0.885	0.945	35.906	-8.513	-8.513	0.000	0.000	0.000	0.000
29	A	36	ARG	1	0.888	0.954	32.651	-8.878	-8.878	0.000	0.000	0.000	0.000
30	A	37	GLN	0	0.003	-0.015	33.945	-0.469	-0.469	0.000	0.000	0.000	0.000
31	A	38	LEU	0	-0.017	-0.003	35.358	0.266	0.266	0.000	0.000	0.000	0.000
32	A	39	ILE	0	-0.008	-0.003	32.770	-0.188	-0.188	0.000	0.000	0.000	0.000
33	A	40	PRO	0	0.041	0.017	34.524	0.199	0.199	0.000	0.000	0.000	0.000
34	A	41	ILE	0	-0.012	-0.001	30.590	0.112	0.112	0.000	0.000	0.000	0.000
35	A	42	ILE	0	-0.015	0.008	34.622	-0.163	-0.163	0.000	0.000	0.000	0.000
36	A	43	SER	0	-0.063	-0.038	34.805	-0.114	-0.114	0.000	0.000	0.000	0.000
37	A	44	GLY	0	0.103	0.035	30.692	0.219	0.219	0.000	0.000	0.000	0.000
38	A	45	LYS	1	0.904	0.970	29.100	-10.541	-10.541	0.000	0.000	0.000	0.000
39	A	46	VAL	0	0.012	0.005	24.858	0.362	0.362	0.000	0.000	0.000	0.000
40	A	47	SER	0	-0.044	-0.031	24.197	-0.542	-0.542	0.000	0.000	0.000	0.000
41	A	48	GLY	0	0.097	0.042	21.794	0.659	0.659	0.000	0.000	0.000	0.000
42	A	49	ASN	0	0.000	0.016	20.118	-1.142	-1.142	0.000	0.000	0.000	0.000
43	A	50	ASN	0	-0.046	-0.028	22.112	-0.274	-0.274	0.000	0.000	0.000	0.000
44	A	51	PHE	0	0.029	0.016	22.760	-0.167	-0.167	0.000	0.000	0.000	0.000
45	A	52	ASN	0	0.008	-0.006	24.760	0.522	0.522	0.000	0.000	0.000	0.000
46	A	53	GLY	0	0.030	0.018	27.589	-0.253	-0.253	0.000	0.000	0.000	0.000
47	A	54	LYS	1	0.895	0.960	30.304	-8.436	-8.436	0.000	0.000	0.000	0.000
48	A	55	VAL	0	0.012	0.015	29.562	0.091	0.091	0.000	0.000	0.000	0.000
49	A	56	LEU	0	-0.067	-0.031	31.872	-0.340	-0.340	0.000	0.000	0.000	0.000
50	A	57	PRO	0	0.011	-0.016	34.814	0.102	0.102	0.000	0.000	0.000	0.000
51	A	58	GLY	0	0.028	0.017	36.914	0.031	0.031	0.000	0.000	0.000	0.000
52	A	59	GLY	0	-0.016	0.002	33.398	0.072	0.072	0.000	0.000	0.000	0.000
53	A	60	ILE	0	0.001	0.003	33.081	-0.200	-0.200	0.000	0.000	0.000	0.000
54	A	61	ASP	-1	-0.784	-0.895	29.514	11.026	11.026	0.000	0.000	0.000	0.000
55	A	62	SER	0	-0.013	-0.007	31.421	-0.364	-0.364	0.000	0.000	0.000	0.000
56	A	63	GLN	0	0.023	0.008	30.035	0.107	0.107	0.000	0.000	0.000	0.000
57	A	64	ILE	0	-0.027	-0.019	31.017	-0.371	-0.371	0.000	0.000	0.000	0.000
58	A	65	VAL	0	0.014	0.019	31.022	0.387	0.387	0.000	0.000	0.000	0.000
59	A	66	ARG	1	0.781	0.868	30.167	-10.160	-10.160	0.000	0.000	0.000	0.000
60	A	67	PRO	0	0.047	0.018	32.621	0.081	0.081	0.000	0.000	0.000	0.000
61	A	68	ASP	-1	-0.875	-0.935	29.280	10.438	10.438	0.000	0.000	0.000	0.000
62	A	69	GLY	0	0.041	0.023	30.913	0.178	0.178	0.000	0.000	0.000	0.000
63	A	70	LYS	1	0.819	0.908	25.134	-11.031	-11.031	0.000	0.000	0.000	0.000
64	A	71	CYS	0	-0.058	-0.030	27.750	-0.430	-0.430	0.000	0.000	0.000	0.000
65	A	72	GLU	-1	-0.784	-0.853	26.379	11.206	11.206	0.000	0.000	0.000	0.000
66	A	73	LEU	0	-0.061	-0.032	24.983	-0.394	-0.394	0.000	0.000	0.000	0.000
67	A	74	SER	0	-0.014	-0.021	26.547	0.204	0.204	0.000	0.000	0.000	0.000
68	A	75	ALA	0	0.019	0.016	26.713	-0.456	-0.456	0.000	0.000	0.000	0.000
69	A	76	ARG	1	0.880	0.939	27.726	-9.443	-9.443	0.000	0.000	0.000	0.000
70	A	77	TYR	0	0.015	-0.003	25.204	-0.243	-0.243	0.000	0.000	0.000	0.000
71	A	78	ALA	0	0.031	0.018	29.747	0.184	0.184	0.000	0.000	0.000	0.000
72	A	79	ILE	0	-0.014	-0.002	25.789	-0.111	-0.111	0.000	0.000	0.000	0.000
73	A	80	ARG	1	0.862	0.917	30.176	-8.875	-8.875	0.000	0.000	0.000	0.000
74	A	81	LEU	0	-0.022	0.000	26.320	0.054	0.054	0.000	0.000	0.000	0.000
75	A	82	ASP	-1	-0.830	-0.930	29.732	10.058	10.058	0.000	0.000	0.000	0.000
76	A	83	ASP	-1	-0.792	-0.862	29.516	9.968	9.968	0.000	0.000	0.000	0.000
77	A	84	GLY	0	0.017	0.016	32.626	-0.221	-0.221	0.000	0.000	0.000	0.000
78	A	85	ALA	0	-0.036	-0.008	29.908	-0.195	-0.195	0.000	0.000	0.000	0.000
79	A	86	ALA	0	-0.016	-0.027	30.739	-0.072	-0.072	0.000	0.000	0.000	0.000
80	A	87	ILE	0	-0.011	-0.008	24.887	0.121	0.121	0.000	0.000	0.000	0.000
81	A	88	TYR	0	0.022	0.019	28.337	-0.186	-0.186	0.000	0.000	0.000	0.000
82	A	89	ILE	0	-0.033	-0.026	24.144	0.477	0.477	0.000	0.000	0.000	0.000
83	A	90	GLU	-1	-0.762	-0.861	25.334	10.218	10.218	0.000	0.000	0.000	0.000
84	A	91	ASN	0	0.017	0.031	21.765	1.001	1.001	0.000	0.000	0.000	0.000
85	A	92	ASN	0	0.005	0.017	22.998	-0.733	-0.733	0.000	0.000	0.000	0.000
86	A	93	GLY	0	0.017	-0.005	21.890	0.817	0.817	0.000	0.000	0.000	0.000
87	A	94	ILE	0	-0.018	-0.004	20.009	-0.642	-0.642	0.000	0.000	0.000	0.000
88	A	95	ARG	1	0.852	0.909	22.477	-10.592	-10.592	0.000	0.000	0.000	0.000
89	A	96	THR	0	0.014	0.010	22.580	-0.407	-0.407	0.000	0.000	0.000	0.000
90	A	97	VAL	0	0.008	0.005	24.418	0.359	0.359	0.000	0.000	0.000	0.000
91	A	98	PRO	0	0.020	0.013	24.546	-0.041	-0.041	0.000	0.000	0.000	0.000
92	A	99	ASP	-1	-0.871	-0.946	26.728	9.765	9.765	0.000	0.000	0.000	0.000
93	A	100	GLU	-1	-0.879	-0.918	28.997	10.686	10.686	0.000	0.000	0.000	0.000
94	A	101	TYR	0	-0.056	-0.056	27.887	-0.278	-0.278	0.000	0.000	0.000	0.000
95	A	102	ILE	0	-0.026	0.000	29.622	-0.087	-0.087	0.000	0.000	0.000	0.000
96	A	103	GLU	-1	-0.787	-0.893	32.434	8.510	8.510	0.000	0.000	0.000	0.000
97	A	104	ALA	0	0.046	0.037	34.078	-0.157	-0.157	0.000	0.000	0.000	0.000
98	A	105	VAL	0	-0.038	-0.029	30.283	-0.113	-0.113	0.000	0.000	0.000	0.000
99	A	106	LYS	1	0.793	0.890	33.738	-8.781	-8.781	0.000	0.000	0.000	0.000
100	A	107	SER	0	-0.040	-0.031	36.548	-0.232	-0.232	0.000	0.000	0.000	0.000
101	A	108	GLY	0	-0.079	-0.040	36.451	-0.149	-0.149	0.000	0.000	0.000	0.000
102	A	109	GLU	-1	-0.924	-0.944	37.178	8.065	8.065	0.000	0.000	0.000	0.000
103	A	110	PHE	0	-0.050	-0.032	32.361	0.271	0.271	0.000	0.000	0.000	0.000
104	A	111	VAL	0	0.032	0.017	29.082	0.012	0.012	0.000	0.000	0.000	0.000
105	A	112	ASP	-1	-0.766	-0.883	27.155	11.836	11.836	0.000	0.000	0.000	0.000
106	A	113	PRO	0	-0.061	-0.038	26.113	0.296	0.296	0.000	0.000	0.000	0.000
107	A	114	ASN	0	-0.079	-0.060	23.225	0.971	0.971	0.000	0.000	0.000	0.000
108	A	115	ALA	0	0.022	0.031	22.750	0.593	0.593	0.000	0.000	0.000	0.000
109	A	116	TYR	0	-0.040	-0.020	23.801	-0.109	-0.109	0.000	0.000	0.000	0.000
110	A	117	TYR	0	-0.003	0.017	15.819	1.168	1.168	0.000	0.000	0.000	0.000
111	A	118	PHE	0	0.004	-0.015	20.346	-0.668	-0.668	0.000	0.000	0.000	0.000
112	A	119	ARG	1	0.890	0.949	15.215	-17.590	-17.590	0.000	0.000	0.000	0.000
113	A	120	THR	0	-0.023	-0.038	18.611	-0.515	-0.515	0.000	0.000	0.000	0.000
114	A	121	ILE	0	0.020	0.011	15.901	1.092	1.092	0.000	0.000	0.000	0.000
115	A	122	PRO	0	-0.035	-0.007	17.626	-0.806	-0.806	0.000	0.000	0.000	0.000
116	A	123	THR	0	0.008	0.010	19.718	0.505	0.505	0.000	0.000	0.000	0.000
117	A	124	PHE	0	0.004	-0.012	19.104	-0.478	-0.478	0.000	0.000	0.000	0.000
118	A	125	GLU	-1	-0.857	-0.905	24.058	9.726	9.726	0.000	0.000	0.000	0.000
119	A	126	THR	0	0.004	-0.029	24.858	-0.222	-0.222	0.000	0.000	0.000	0.000
120	A	127	TYR	0	-0.045	-0.051	27.970	-0.070	-0.070	0.000	0.000	0.000	0.000
121	A	128	SER	0	0.032	0.012	29.280	-0.250	-0.250	0.000	0.000	0.000	0.000
122	A	129	PRO	0	0.044	0.011	27.411	0.384	0.384	0.000	0.000	0.000	0.000
123	A	130	LYS	1	0.846	0.937	25.713	-10.549	-10.549	0.000	0.000	0.000	0.000
124	A	131	TYR	0	0.041	-0.026	23.809	0.543	0.543	0.000	0.000	0.000	0.000
125	A	132	LYS	1	0.886	0.955	23.898	-10.262	-10.262	0.000	0.000	0.000	0.000
126	A	133	TRP	0	0.049	0.029	17.545	0.301	0.301	0.000	0.000	0.000	0.000
127	A	134	MET	0	-0.008	0.004	19.065	0.469	0.469	0.000	0.000	0.000	0.000
128	A	135	MET	0	-0.062	-0.001	20.757	-0.141	-0.141	0.000	0.000	0.000	0.000
129	A	136	ASN	0	-0.062	-0.033	18.782	-0.252	-0.252	0.000	0.000	0.000	0.000
130	A	137	HIS	0	-0.003	-0.002	13.168	1.137	1.137	0.000	0.000	0.000	0.000
131	A	138	ILE	0	0.020	0.022	12.628	-0.724	-0.724	0.000	0.000	0.000	0.000
132	A	139	PHE	0	0.012	0.000	13.616	0.920	0.920	0.000	0.000	0.000	0.000
133	A	140	VAL	0	0.013	0.010	12.269	-0.339	-0.339	0.000	0.000	0.000	0.000
134	A	141	CYS	0	-0.087	-0.034	14.793	-0.182	-0.182	0.000	0.000	0.000	0.000
135	A	142	CYS	0	-0.019	-0.003	14.652	0.342	0.342	0.000	0.000	0.000	0.000
136	A	143	ALA	0	0.038	0.012	17.638	-0.544	-0.544	0.000	0.000	0.000	0.000
137	A	144	SER	0	-0.024	-0.007	21.361	0.173	0.173	0.000	0.000	0.000	0.000
138	A	145	ARG	1	0.904	0.923	23.750	-11.009	-11.009	0.000	0.000	0.000	0.000
139	A	146	LEU	0	0.014	0.044	27.593	-0.130	-0.130	0.000	0.000	0.000	0.000
140	A	147	PRO	0	0.021	0.008	29.688	0.289	0.289	0.000	0.000	0.000	0.000
141	A	148	GLU	-1	-0.912	-0.972	32.291	8.900	8.900	0.000	0.000	0.000	0.000
142	A	149	ASN	0	-0.039	-0.008	29.946	-0.228	-0.228	0.000	0.000	0.000	0.000
143	A	150	VAL	0	-0.003	0.002	25.814	0.136	0.136	0.000	0.000	0.000	0.000
144	A	151	LEU	0	-0.036	-0.004	22.896	-0.143	-0.143	0.000	0.000	0.000	0.000
145	A	152	LEU	0	-0.012	-0.009	21.666	0.447	0.447	0.000	0.000	0.000	0.000
146	A	153	LYS	1	0.854	0.908	17.531	-16.904	-16.904	0.000	0.000	0.000	0.000
147	A	154	PHE	0	0.036	0.008	17.090	0.386	0.386	0.000	0.000	0.000	0.000
148	A	155	TYR	0	-0.015	-0.035	11.509	0.206	0.206	0.000	0.000	0.000	0.000
149	A	156	LYS	1	0.834	0.922	11.775	-21.455	-21.455	0.000	0.000	0.000	0.000
150	A	157	ILE	0	0.007	-0.011	8.126	1.691	1.691	0.000	0.000	0.000	0.000
151	A	158	SER	0	0.006	0.003	6.336	-2.798	-2.798	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:GLU)