FMO DATABASE

FMODB ID: YVG92

Calculation Name: 2FG1-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2FG1

Chain ID: A

ChEMBL ID:

UniProt ID: Q8A8B0

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:

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	157
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1578590.740072
FMO2-HF: Nuclear repulsion	1516562.435466
FMO2-HF: Total energy	-62028.304607
FMO2-MP2: Total energy	-62207.471041

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:ASN)

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

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.
-1.806	0.112	-0.018	-0.774	-1.126	0

Interaction energy analysis for fragmet #1(A:-1:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.028 / q_NPA : -0.032

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].
3	A	1	MET	0	-0.042	-0.011	3.816	-1.579	0.119	-0.016	-0.747	-0.935
4	A	2	GLU	-1	-0.917	-0.964	4.349	-1.672	-1.478	-0.001	-0.023	-0.170
5	A	3	ILE	0	-0.066	-0.034	7.087	-0.010	-0.010	0.000	0.000	0.000
6	A	4	LEU	0	0.022	0.029	10.525	-0.244	-0.244	0.000	0.000	0.000
7	A	5	TYR	0	-0.015	-0.047	12.162	0.152	0.152	0.000	0.000	0.000
8	A	6	ILE	0	-0.007	-0.005	15.791	-0.098	-0.098	0.000	0.000	0.000
9	A	7	LYS	1	0.960	0.980	19.039	0.202	0.202	0.000	0.000	0.000
10	A	8	GLY	0	0.004	-0.003	22.722	-0.020	-0.020	0.000	0.000	0.000
11	A	9	ASP	-1	-0.802	-0.886	24.920	0.108	0.108	0.000	0.000	0.000
12	A	10	ALA	0	0.020	0.010	22.479	-0.009	-0.009	0.000	0.000	0.000
13	A	11	THR	0	-0.086	-0.064	23.763	0.009	0.009	0.000	0.000	0.000
14	A	12	ALA	0	-0.062	-0.037	26.021	-0.007	-0.007	0.000	0.000	0.000
15	A	13	PRO	0	0.015	0.020	21.576	-0.020	-0.020	0.000	0.000	0.000
16	A	14	ILE	0	0.053	0.019	17.816	-0.019	-0.019	0.000	0.000	0.000
17	A	15	GLY	0	0.003	0.005	19.614	0.025	0.025	0.000	0.000	0.000
18	A	16	SER	0	-0.024	-0.017	19.827	0.027	0.027	0.000	0.000	0.000
19	A	17	GLY	0	0.026	0.009	19.922	0.019	0.019	0.000	0.000	0.000
20	A	18	VAL	0	-0.008	-0.005	20.862	-0.010	-0.010	0.000	0.000	0.000
21	A	19	LYS	1	0.816	0.926	19.621	-0.004	-0.004	0.000	0.000	0.000
22	A	20	VAL	0	0.031	0.006	19.413	-0.017	-0.017	0.000	0.000	0.000
23	A	21	ILE	0	0.003	0.003	19.846	0.027	0.027	0.000	0.000	0.000
24	A	22	THR	0	-0.001	0.000	18.664	0.020	0.020	0.000	0.000	0.000
25	A	23	HIS	0	-0.055	-0.054	21.612	-0.009	-0.009	0.000	0.000	0.000
26	A	24	ILE	0	0.016	0.013	21.978	0.012	0.012	0.000	0.000	0.000
27	A	25	CYS	0	-0.052	-0.005	25.474	-0.038	-0.038	0.000	0.000	0.000
28	A	26	ASN	0	-0.002	-0.033	28.865	0.014	0.014	0.000	0.000	0.000
29	A	27	ASP	-1	-0.710	-0.833	31.534	0.256	0.256	0.000	0.000	0.000
30	A	28	ILE	0	-0.020	-0.015	33.394	-0.009	-0.009	0.000	0.000	0.000
31	A	29	GLY	0	0.055	0.042	35.442	-0.012	-0.012	0.000	0.000	0.000
32	A	30	GLY	0	-0.066	-0.020	36.049	-0.013	-0.013	0.000	0.000	0.000
33	A	31	TRP	0	0.007	-0.013	30.616	0.016	0.016	0.000	0.000	0.000
34	A	32	GLY	0	0.042	0.005	35.433	-0.011	-0.011	0.000	0.000	0.000
35	A	33	LYS	1	0.922	0.968	34.252	-0.155	-0.155	0.000	0.000	0.000
36	A	34	GLY	0	0.036	0.025	31.207	0.014	0.014	0.000	0.000	0.000
37	A	35	PHE	0	0.085	0.024	25.475	-0.009	-0.009	0.000	0.000	0.000
38	A	36	VAL	0	0.055	0.024	29.287	-0.009	-0.009	0.000	0.000	0.000
39	A	37	LEU	0	-0.031	-0.006	31.474	-0.010	-0.010	0.000	0.000	0.000
40	A	38	ALA	0	-0.028	-0.010	29.820	-0.012	-0.012	0.000	0.000	0.000
41	A	39	LEU	0	0.012	0.006	27.207	-0.010	-0.010	0.000	0.000	0.000
42	A	40	SER	0	-0.024	-0.038	31.110	-0.005	-0.005	0.000	0.000	0.000
43	A	41	LYS	1	0.898	0.959	34.123	-0.074	-0.074	0.000	0.000	0.000
44	A	42	LYS	1	0.830	0.933	29.250	-0.077	-0.077	0.000	0.000	0.000
45	A	43	TRP	0	0.002	-0.016	27.394	0.003	0.003	0.000	0.000	0.000
46	A	44	LYS	1	0.907	0.937	34.326	-0.100	-0.100	0.000	0.000	0.000
47	A	45	MET	0	0.051	0.026	33.002	0.003	0.003	0.000	0.000	0.000
48	A	46	PRO	0	0.007	0.003	30.031	0.006	0.006	0.000	0.000	0.000
49	A	47	GLU	-1	-0.754	-0.827	32.063	0.131	0.131	0.000	0.000	0.000
50	A	48	GLU	-1	-0.868	-0.921	34.771	0.129	0.129	0.000	0.000	0.000
51	A	49	ALA	0	0.027	0.018	33.062	0.001	0.001	0.000	0.000	0.000
52	A	50	TYR	0	0.001	-0.001	31.781	-0.001	-0.001	0.000	0.000	0.000
53	A	51	ARG	1	0.826	0.888	34.079	-0.136	-0.136	0.000	0.000	0.000
54	A	52	GLN	0	-0.073	-0.052	37.736	0.001	0.001	0.000	0.000	0.000
55	A	53	TRP	0	-0.019	0.000	28.719	-0.001	-0.001	0.000	0.000	0.000
56	A	54	TYR	0	-0.006	0.007	36.150	-0.004	-0.004	0.000	0.000	0.000
57	A	55	LYS	1	0.922	0.950	37.535	-0.127	-0.127	0.000	0.000	0.000
58	A	56	SER	0	-0.038	-0.009	37.670	-0.001	-0.001	0.000	0.000	0.000
59	A	57	GLN	0	-0.090	-0.059	37.639	0.005	0.005	0.000	0.000	0.000
60	A	58	GLU	-1	-0.913	-0.944	36.456	0.182	0.182	0.000	0.000	0.000
61	A	59	GLU	-1	-0.926	-0.970	31.216	0.292	0.292	0.000	0.000	0.000
62	A	60	PHE	0	-0.052	-0.005	31.914	0.016	0.016	0.000	0.000	0.000
63	A	61	THR	0	0.021	-0.003	30.392	-0.011	-0.011	0.000	0.000	0.000
64	A	62	LEU	0	-0.025	-0.037	28.309	0.018	0.018	0.000	0.000	0.000
65	A	63	GLY	0	-0.031	-0.033	24.775	0.006	0.006	0.000	0.000	0.000
66	A	64	ALA	0	0.023	0.038	24.874	0.027	0.027	0.000	0.000	0.000
67	A	65	VAL	0	-0.029	-0.028	22.636	0.005	0.005	0.000	0.000	0.000
68	A	66	GLN	0	0.051	0.043	26.090	-0.013	-0.013	0.000	0.000	0.000
69	A	67	PHE	0	-0.029	-0.021	21.579	0.003	0.003	0.000	0.000	0.000
70	A	68	VAL	0	-0.004	0.003	26.994	-0.020	-0.020	0.000	0.000	0.000
71	A	69	ASN	0	-0.061	-0.042	28.070	-0.003	-0.003	0.000	0.000	0.000
72	A	70	VAL	0	-0.009	-0.012	28.149	-0.007	-0.007	0.000	0.000	0.000
73	A	71	GLU	-1	-0.779	-0.878	29.245	0.053	0.053	0.000	0.000	0.000
74	A	72	ASN	0	0.023	0.003	29.241	0.024	0.024	0.000	0.000	0.000
75	A	73	LYS	1	0.921	0.964	24.779	-0.040	-0.040	0.000	0.000	0.000
76	A	74	LEU	0	0.028	0.029	24.006	0.008	0.008	0.000	0.000	0.000
77	A	75	TYR	0	0.026	0.002	23.796	-0.005	-0.005	0.000	0.000	0.000
78	A	76	VAL	0	-0.018	-0.001	24.368	0.006	0.006	0.000	0.000	0.000
79	A	77	ALA	0	0.019	0.010	22.500	0.000	0.000	0.000	0.000	0.000
80	A	78	ASN	0	-0.028	-0.026	24.576	0.009	0.009	0.000	0.000	0.000
81	A	79	MET	0	0.016	0.015	20.232	0.025	0.025	0.000	0.000	0.000
82	A	80	ILE	0	0.008	0.025	25.221	-0.008	-0.008	0.000	0.000	0.000
83	A	81	GLY	0	0.066	0.021	25.112	0.027	0.027	0.000	0.000	0.000
84	A	82	GLN	0	-0.120	-0.070	26.061	0.018	0.018	0.000	0.000	0.000
85	A	83	HIS	0	-0.046	-0.039	28.862	-0.020	-0.020	0.000	0.000	0.000
86	A	84	GLY	0	0.037	0.018	32.194	-0.009	-0.009	0.000	0.000	0.000
87	A	85	ILE	0	-0.024	-0.024	33.398	0.010	0.010	0.000	0.000	0.000
88	A	86	TYR	0	-0.004	-0.015	34.430	-0.001	-0.001	0.000	0.000	0.000
89	A	87	LYS	1	0.976	0.996	34.378	-0.164	-0.164	0.000	0.000	0.000
90	A	88	ASP	-1	-0.737	-0.850	35.177	0.219	0.219	0.000	0.000	0.000
91	A	89	SER	0	0.008	-0.019	37.150	-0.004	-0.004	0.000	0.000	0.000
92	A	90	LYS	1	0.858	0.929	34.144	-0.255	-0.255	0.000	0.000	0.000
93	A	91	GLY	0	-0.068	-0.029	36.105	0.002	0.002	0.000	0.000	0.000
94	A	92	LEU	0	-0.012	0.000	29.596	0.007	0.007	0.000	0.000	0.000
95	A	93	PRO	0	0.016	0.001	29.082	-0.010	-0.010	0.000	0.000	0.000
96	A	94	PRO	0	0.019	0.028	30.374	0.017	0.017	0.000	0.000	0.000
97	A	95	ILE	0	-0.045	-0.004	23.589	0.014	0.014	0.000	0.000	0.000
98	A	96	ARG	1	0.882	0.943	26.040	-0.337	-0.337	0.000	0.000	0.000
99	A	97	TYR	0	0.068	0.019	20.344	0.012	0.012	0.000	0.000	0.000
100	A	98	ASP	-1	-0.842	-0.919	21.174	0.546	0.546	0.000	0.000	0.000
101	A	99	ALA	0	0.040	0.027	22.466	0.027	0.027	0.000	0.000	0.000
102	A	100	VAL	0	0.027	0.003	19.296	0.009	0.009	0.000	0.000	0.000
103	A	101	ARG	1	0.791	0.872	14.081	-1.267	-1.267	0.000	0.000	0.000
104	A	102	GLN	0	-0.016	0.000	18.730	0.057	0.057	0.000	0.000	0.000
105	A	103	CYS	0	-0.029	0.007	21.141	-0.010	-0.010	0.000	0.000	0.000
106	A	104	LEU	0	0.013	-0.015	15.690	-0.004	-0.004	0.000	0.000	0.000
107	A	105	LYS	1	0.847	0.921	15.965	-1.010	-1.010	0.000	0.000	0.000
108	A	106	GLU	-1	-0.843	-0.920	17.926	0.434	0.434	0.000	0.000	0.000
109	A	107	VAL	0	-0.035	-0.029	17.067	-0.032	-0.032	0.000	0.000	0.000
110	A	108	ALA	0	0.001	0.014	14.321	-0.021	-0.021	0.000	0.000	0.000
111	A	109	LEU	0	0.020	0.016	15.929	-0.015	-0.015	0.000	0.000	0.000
112	A	110	PHE	0	0.030	0.022	18.532	-0.057	-0.057	0.000	0.000	0.000
113	A	111	THR	0	-0.013	-0.026	15.354	-0.088	-0.088	0.000	0.000	0.000
114	A	112	ILE	0	0.023	0.021	13.196	-0.057	-0.057	0.000	0.000	0.000
115	A	113	ALA	0	-0.040	-0.012	16.472	-0.069	-0.069	0.000	0.000	0.000
116	A	114	HIS	1	0.786	0.883	19.956	-0.372	-0.372	0.000	0.000	0.000
117	A	115	LYS	1	0.937	0.971	16.987	-0.339	-0.339	0.000	0.000	0.000
118	A	116	ALA	0	-0.048	-0.012	17.632	-0.063	-0.063	0.000	0.000	0.000
119	A	117	SER	0	0.041	0.029	14.978	0.054	0.054	0.000	0.000	0.000
120	A	118	VAL	0	0.027	0.000	14.795	-0.032	-0.032	0.000	0.000	0.000
121	A	119	HIS	0	0.010	0.030	16.089	-0.048	-0.048	0.000	0.000	0.000
122	A	120	MET	0	-0.004	0.010	15.981	0.021	0.021	0.000	0.000	0.000
123	A	121	PRO	0	0.050	0.031	19.986	-0.037	-0.037	0.000	0.000	0.000
124	A	122	ARG	1	0.883	0.923	16.978	-0.182	-0.182	0.000	0.000	0.000
125	A	123	ILE	0	-0.017	-0.012	18.379	-0.021	-0.021	0.000	0.000	0.000
126	A	124	GLY	0	0.075	0.023	21.395	0.040	0.040	0.000	0.000	0.000
127	A	125	CYS	0	-0.056	-0.003	21.923	-0.013	-0.013	0.000	0.000	0.000
128	A	126	GLY	0	0.012	0.007	24.759	-0.020	-0.020	0.000	0.000	0.000
129	A	127	LEU	0	-0.008	-0.029	28.472	0.009	0.009	0.000	0.000	0.000
130	A	128	ALA	0	0.027	0.029	27.047	-0.001	-0.001	0.000	0.000	0.000
131	A	129	GLY	0	0.021	0.004	27.790	0.012	0.012	0.000	0.000	0.000
132	A	130	GLY	0	-0.012	-0.001	23.497	0.015	0.015	0.000	0.000	0.000
133	A	131	LYS	1	0.853	0.922	21.041	-0.368	-0.368	0.000	0.000	0.000
134	A	132	TRP	0	0.075	0.023	15.189	0.040	0.040	0.000	0.000	0.000
135	A	133	GLU	-1	-0.847	-0.928	15.896	0.505	0.505	0.000	0.000	0.000
136	A	134	LEU	0	-0.038	-0.009	15.210	0.132	0.132	0.000	0.000	0.000
137	A	135	MET	0	0.011	-0.008	15.781	0.138	0.138	0.000	0.000	0.000
138	A	136	GLU	-1	-0.794	-0.858	11.656	0.964	0.964	0.000	0.000	0.000
139	A	137	GLN	0	0.002	-0.011	8.907	0.155	0.155	0.000	0.000	0.000
140	A	138	ILE	0	-0.017	-0.009	11.591	0.268	0.268	0.000	0.000	0.000
141	A	139	ILE	0	0.007	0.000	11.875	0.093	0.093	0.000	0.000	0.000
142	A	140	LYS	1	0.884	0.934	7.384	-1.832	-1.832	0.000	0.000	0.000
143	A	141	GLU	-1	-0.785	-0.862	8.259	2.333	2.333	0.000	0.000	0.000
144	A	142	GLU	-1	-0.808	-0.895	10.089	1.318	1.318	0.000	0.000	0.000
145	A	143	LEU	0	0.006	0.002	10.769	-0.194	-0.194	0.000	0.000	0.000
146	A	144	ILE	0	0.030	0.030	4.990	0.040	0.040	0.000	0.000	0.000
147	A	145	THR	0	-0.048	-0.029	4.824	0.227	0.227	0.000	0.000	0.000
148	A	146	LYS	1	0.793	0.904	5.914	-1.385	-1.385	0.000	0.000	0.000
149	A	147	GLU	-1	-0.936	-0.967	5.150	2.089	2.115	-0.001	-0.004	-0.021
150	A	148	ILE	0	-0.055	-0.001	7.935	-0.613	-0.613	0.000	0.000	0.000
151	A	149	ALA	0	0.031	0.001	9.966	0.102	0.102	0.000	0.000	0.000
152	A	150	VAL	0	-0.002	-0.012	11.110	0.033	0.033	0.000	0.000	0.000
153	A	151	THR	0	-0.016	0.002	12.769	-0.137	-0.137	0.000	0.000	0.000
154	A	152	VAL	0	-0.027	-0.020	15.224	0.058	0.058	0.000	0.000	0.000
155	A	153	TYR	0	-0.070	-0.045	17.615	-0.092	-0.092	0.000	0.000	0.000
156	A	154	ASP	-1	-0.831	-0.900	19.632	0.134	0.134	0.000	0.000	0.000
157	A	155	LEU	0	-0.024	-0.018	22.465	-0.021	-0.021	0.000	0.000	0.000

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