FMO DATABASE

FMODB ID: 5JVYZ

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	OptH
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	-1576829.853365
FMO2-HF: Nuclear repulsion	1514801.815501
FMO2-HF: Total energy	-62028.037864
FMO2-MP2: Total energy	-62207.152162

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.
0.629	2.484	-0.018	-0.755	-1.082	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 : -0.022 / q_NPA : -0.030

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	-0.049	-0.009	3.816	-1.966	-0.369	-0.017	-0.733	-0.847
4	A	2	GLU	-1	-0.903	-0.959	4.355	2.400	2.658	-0.001	-0.022	-0.235
5	A	3	ILE	0	-0.067	-0.034	6.893	-0.515	-0.515	0.000	0.000	0.000
6	A	4	LEU	0	0.020	0.029	10.268	-0.213	-0.213	0.000	0.000	0.000
7	A	5	TYR	0	-0.018	-0.045	12.190	-0.018	-0.018	0.000	0.000	0.000
8	A	6	ILE	0	-0.012	-0.006	15.980	-0.101	-0.101	0.000	0.000	0.000
9	A	7	LYS	1	0.963	0.983	19.324	-0.120	-0.120	0.000	0.000	0.000
10	A	8	GLY	0	0.002	-0.006	23.012	-0.008	-0.008	0.000	0.000	0.000
11	A	9	ASP	-1	-0.803	-0.882	24.945	0.297	0.297	0.000	0.000	0.000
12	A	10	ALA	0	0.029	0.012	22.487	-0.002	-0.002	0.000	0.000	0.000
13	A	11	THR	0	-0.071	-0.048	23.764	0.010	0.010	0.000	0.000	0.000
14	A	12	ALA	0	-0.067	-0.045	26.014	-0.023	-0.023	0.000	0.000	0.000
15	A	13	PRO	0	0.028	0.028	21.669	-0.007	-0.007	0.000	0.000	0.000
16	A	14	ILE	0	0.042	0.013	17.597	-0.042	-0.042	0.000	0.000	0.000
17	A	15	GLY	0	-0.002	0.004	19.620	0.042	0.042	0.000	0.000	0.000
18	A	16	SER	0	-0.024	-0.018	19.838	-0.006	-0.006	0.000	0.000	0.000
19	A	17	GLY	0	0.016	0.001	19.935	0.041	0.041	0.000	0.000	0.000
20	A	18	VAL	0	0.006	0.000	20.855	-0.029	-0.029	0.000	0.000	0.000
21	A	19	LYS	1	0.845	0.943	19.638	-0.292	-0.292	0.000	0.000	0.000
22	A	20	VAL	0	0.038	0.012	19.413	-0.055	-0.055	0.000	0.000	0.000
23	A	21	ILE	0	0.002	0.002	19.858	0.058	0.058	0.000	0.000	0.000
24	A	22	THR	0	0.001	-0.001	18.719	0.002	0.002	0.000	0.000	0.000
25	A	23	HIS	0	-0.060	-0.055	21.622	0.004	0.004	0.000	0.000	0.000
26	A	24	ILE	0	0.020	0.015	22.038	0.005	0.005	0.000	0.000	0.000
27	A	25	CYS	0	-0.040	-0.003	25.480	-0.032	-0.032	0.000	0.000	0.000
28	A	26	ASN	0	-0.002	-0.024	28.872	0.005	0.005	0.000	0.000	0.000
29	A	27	ASP	-1	-0.703	-0.827	31.541	0.295	0.295	0.000	0.000	0.000
30	A	28	ILE	0	-0.011	-0.011	33.403	-0.013	-0.013	0.000	0.000	0.000
31	A	29	GLY	0	0.058	0.039	35.449	-0.013	-0.013	0.000	0.000	0.000
32	A	30	GLY	0	-0.073	-0.027	36.049	-0.012	-0.012	0.000	0.000	0.000
33	A	31	TRP	0	0.009	-0.012	30.706	0.021	0.021	0.000	0.000	0.000
34	A	32	GLY	0	0.043	0.005	35.449	-0.013	-0.013	0.000	0.000	0.000
35	A	33	LYS	1	0.943	0.972	34.139	-0.223	-0.223	0.000	0.000	0.000
36	A	34	GLY	0	0.034	0.027	31.005	0.016	0.016	0.000	0.000	0.000
37	A	35	PHE	0	0.083	0.025	25.491	-0.011	-0.011	0.000	0.000	0.000
38	A	36	VAL	0	0.060	0.024	29.288	-0.006	-0.006	0.000	0.000	0.000
39	A	37	LEU	0	-0.034	-0.010	31.478	-0.012	-0.012	0.000	0.000	0.000
40	A	38	ALA	0	-0.029	-0.008	29.812	-0.015	-0.015	0.000	0.000	0.000
41	A	39	LEU	0	0.019	0.008	27.336	-0.009	-0.009	0.000	0.000	0.000
42	A	40	SER	0	-0.055	-0.049	31.115	-0.006	-0.006	0.000	0.000	0.000
43	A	41	LYS	1	0.912	0.967	34.286	-0.202	-0.202	0.000	0.000	0.000
44	A	42	LYS	1	0.888	0.963	29.058	-0.260	-0.260	0.000	0.000	0.000
45	A	43	TRP	0	0.007	-0.009	27.751	0.005	0.005	0.000	0.000	0.000
46	A	44	LYS	1	0.925	0.949	34.336	-0.195	-0.195	0.000	0.000	0.000
47	A	45	MET	0	0.051	0.029	33.037	-0.002	-0.002	0.000	0.000	0.000
48	A	46	PRO	0	0.006	0.004	30.091	0.002	0.002	0.000	0.000	0.000
49	A	47	GLU	-1	-0.766	-0.857	32.075	0.215	0.215	0.000	0.000	0.000
50	A	48	GLU	-1	-0.854	-0.916	34.782	0.193	0.193	0.000	0.000	0.000
51	A	49	ALA	0	0.012	0.011	33.055	-0.004	-0.004	0.000	0.000	0.000
52	A	50	TYR	0	-0.005	-0.006	31.706	-0.006	-0.006	0.000	0.000	0.000
53	A	51	ARG	1	0.820	0.893	34.092	-0.216	-0.216	0.000	0.000	0.000
54	A	52	GLN	0	-0.075	-0.050	37.748	-0.005	-0.005	0.000	0.000	0.000
55	A	53	TRP	0	-0.033	-0.003	28.840	-0.001	-0.001	0.000	0.000	0.000
56	A	54	TYR	0	-0.004	0.001	36.166	-0.005	-0.005	0.000	0.000	0.000
57	A	55	LYS	1	0.915	0.937	37.548	-0.180	-0.180	0.000	0.000	0.000
58	A	56	SER	0	-0.032	0.002	37.628	-0.004	-0.004	0.000	0.000	0.000
59	A	57	GLN	0	-0.073	-0.043	37.629	-0.001	-0.001	0.000	0.000	0.000
60	A	58	GLU	-1	-0.924	-0.950	36.559	0.220	0.220	0.000	0.000	0.000
61	A	59	GLU	-1	-0.923	-0.967	31.107	0.338	0.338	0.000	0.000	0.000
62	A	60	PHE	0	-0.059	-0.009	31.931	0.023	0.023	0.000	0.000	0.000
63	A	61	THR	0	0.022	-0.002	30.241	-0.016	-0.016	0.000	0.000	0.000
64	A	62	LEU	0	-0.031	-0.042	28.258	0.024	0.024	0.000	0.000	0.000
65	A	63	GLY	0	-0.025	-0.027	24.786	-0.002	-0.002	0.000	0.000	0.000
66	A	64	ALA	0	0.029	0.042	24.890	0.032	0.032	0.000	0.000	0.000
67	A	65	VAL	0	-0.026	-0.029	22.661	0.017	0.017	0.000	0.000	0.000
68	A	66	GLN	0	0.066	0.053	26.106	-0.013	-0.013	0.000	0.000	0.000
69	A	67	PHE	0	-0.032	-0.024	21.660	0.019	0.019	0.000	0.000	0.000
70	A	68	VAL	0	-0.007	0.002	27.012	-0.029	-0.029	0.000	0.000	0.000
71	A	69	ASN	0	-0.062	-0.037	28.086	0.001	0.001	0.000	0.000	0.000
72	A	70	VAL	0	-0.010	-0.014	28.207	-0.016	-0.016	0.000	0.000	0.000
73	A	71	GLU	-1	-0.833	-0.910	29.337	0.221	0.221	0.000	0.000	0.000
74	A	72	ASN	0	0.029	0.000	29.257	0.028	0.028	0.000	0.000	0.000
75	A	73	LYS	1	0.885	0.948	24.765	-0.263	-0.263	0.000	0.000	0.000
76	A	74	LEU	0	0.022	0.026	24.114	0.034	0.034	0.000	0.000	0.000
77	A	75	TYR	0	0.025	0.003	23.902	-0.028	-0.028	0.000	0.000	0.000
78	A	76	VAL	0	-0.018	0.000	24.382	0.026	0.026	0.000	0.000	0.000
79	A	77	ALA	0	0.015	0.007	22.530	-0.012	-0.012	0.000	0.000	0.000
80	A	78	ASN	0	-0.026	-0.024	24.590	0.024	0.024	0.000	0.000	0.000
81	A	79	MET	0	0.012	0.014	20.241	0.023	0.023	0.000	0.000	0.000
82	A	80	ILE	0	0.013	0.027	25.231	-0.007	-0.007	0.000	0.000	0.000
83	A	81	GLY	0	0.062	0.018	25.117	0.020	0.020	0.000	0.000	0.000
84	A	82	GLN	0	-0.113	-0.062	26.068	0.025	0.025	0.000	0.000	0.000
85	A	83	HIS	0	-0.056	-0.044	28.867	-0.022	-0.022	0.000	0.000	0.000
86	A	84	GLY	0	0.033	0.015	32.185	-0.011	-0.011	0.000	0.000	0.000
87	A	85	ILE	0	-0.037	-0.032	33.315	0.016	0.016	0.000	0.000	0.000
88	A	86	TYR	0	-0.024	-0.024	34.285	0.004	0.004	0.000	0.000	0.000
89	A	87	LYS	1	0.984	0.996	34.349	-0.182	-0.182	0.000	0.000	0.000
90	A	88	ASP	-1	-0.737	-0.850	35.200	0.223	0.223	0.000	0.000	0.000
91	A	89	SER	0	0.009	-0.019	37.172	-0.003	-0.003	0.000	0.000	0.000
92	A	90	LYS	1	0.853	0.930	33.811	-0.250	-0.250	0.000	0.000	0.000
93	A	91	GLY	0	-0.065	-0.021	36.155	0.000	0.000	0.000	0.000	0.000
94	A	92	LEU	0	-0.024	-0.015	29.682	0.008	0.008	0.000	0.000	0.000
95	A	93	PRO	0	0.010	-0.003	29.049	-0.007	-0.007	0.000	0.000	0.000
96	A	94	PRO	0	0.019	0.020	30.318	0.013	0.013	0.000	0.000	0.000
97	A	95	ILE	0	-0.042	-0.002	23.498	0.015	0.015	0.000	0.000	0.000
98	A	96	ARG	1	0.909	0.961	26.036	-0.363	-0.363	0.000	0.000	0.000
99	A	97	TYR	0	0.074	0.026	20.324	0.023	0.023	0.000	0.000	0.000
100	A	98	ASP	-1	-0.858	-0.926	21.221	0.543	0.543	0.000	0.000	0.000
101	A	99	ALA	0	0.037	0.028	22.476	0.032	0.032	0.000	0.000	0.000
102	A	100	VAL	0	0.025	0.001	19.297	0.021	0.021	0.000	0.000	0.000
103	A	101	ARG	1	0.803	0.886	14.296	-1.126	-1.126	0.000	0.000	0.000
104	A	102	GLN	0	-0.016	-0.001	18.743	0.053	0.053	0.000	0.000	0.000
105	A	103	CYS	0	-0.017	0.009	21.157	-0.001	-0.001	0.000	0.000	0.000
106	A	104	LEU	0	0.014	-0.014	15.658	0.014	0.014	0.000	0.000	0.000
107	A	105	LYS	1	0.872	0.940	16.889	-0.853	-0.853	0.000	0.000	0.000
108	A	106	GLU	-1	-0.859	-0.923	17.945	0.531	0.531	0.000	0.000	0.000
109	A	107	VAL	0	-0.045	-0.035	17.039	-0.019	-0.019	0.000	0.000	0.000
110	A	108	ALA	0	0.011	0.007	14.354	0.009	0.009	0.000	0.000	0.000
111	A	109	LEU	0	0.015	0.013	15.951	0.003	0.003	0.000	0.000	0.000
112	A	110	PHE	0	0.012	0.015	18.497	-0.049	-0.049	0.000	0.000	0.000
113	A	111	THR	0	-0.013	-0.018	15.052	-0.084	-0.084	0.000	0.000	0.000
114	A	112	ILE	0	0.028	0.021	13.355	-0.038	-0.038	0.000	0.000	0.000
115	A	113	ALA	0	-0.036	-0.011	16.472	-0.067	-0.067	0.000	0.000	0.000
116	A	114	HIS	1	0.804	0.899	19.960	-0.553	-0.553	0.000	0.000	0.000
117	A	115	LYS	1	0.938	0.974	16.989	-0.555	-0.555	0.000	0.000	0.000
118	A	116	ALA	0	-0.042	-0.011	17.663	-0.046	-0.046	0.000	0.000	0.000
119	A	117	SER	0	0.036	0.025	14.996	0.091	0.091	0.000	0.000	0.000
120	A	118	VAL	0	0.033	0.003	14.783	-0.100	-0.100	0.000	0.000	0.000
121	A	119	HIS	0	0.007	0.034	16.096	0.004	0.004	0.000	0.000	0.000
122	A	120	MET	0	-0.006	0.008	15.853	-0.033	-0.033	0.000	0.000	0.000
123	A	121	PRO	0	0.049	0.032	19.975	-0.014	-0.014	0.000	0.000	0.000
124	A	122	ARG	1	0.920	0.953	17.583	-0.468	-0.468	0.000	0.000	0.000
125	A	123	ILE	0	-0.016	-0.013	18.581	-0.059	-0.059	0.000	0.000	0.000
126	A	124	GLY	0	0.074	0.026	21.168	0.035	0.035	0.000	0.000	0.000
127	A	125	CYS	0	-0.048	-0.002	21.643	-0.034	-0.034	0.000	0.000	0.000
128	A	126	GLY	0	0.007	0.006	24.531	-0.017	-0.017	0.000	0.000	0.000
129	A	127	LEU	0	-0.005	-0.029	28.244	0.001	0.001	0.000	0.000	0.000
130	A	128	ALA	0	0.020	0.028	26.879	-0.009	-0.009	0.000	0.000	0.000
131	A	129	GLY	0	0.009	-0.003	27.696	0.003	0.003	0.000	0.000	0.000
132	A	130	GLY	0	-0.020	0.002	23.387	0.004	0.004	0.000	0.000	0.000
133	A	131	LYS	1	0.902	0.930	21.086	-0.400	-0.400	0.000	0.000	0.000
134	A	132	TRP	0	0.074	0.022	14.919	-0.005	-0.005	0.000	0.000	0.000
135	A	133	GLU	-1	-0.853	-0.927	15.838	0.591	0.591	0.000	0.000	0.000
136	A	134	LEU	0	-0.044	-0.010	15.244	0.102	0.102	0.000	0.000	0.000
137	A	135	MET	0	-0.003	-0.014	15.811	0.123	0.123	0.000	0.000	0.000
138	A	136	GLU	-1	-0.857	-0.902	11.421	1.400	1.400	0.000	0.000	0.000
139	A	137	GLN	0	-0.021	-0.019	9.462	0.330	0.330	0.000	0.000	0.000
140	A	138	ILE	0	-0.019	-0.014	11.652	0.241	0.241	0.000	0.000	0.000
141	A	139	ILE	0	0.010	0.002	11.826	0.090	0.090	0.000	0.000	0.000
142	A	140	LYS	1	0.956	0.975	7.314	-2.360	-2.360	0.000	0.000	0.000
143	A	141	GLU	-1	-0.795	-0.874	8.267	2.061	2.061	0.000	0.000	0.000
144	A	142	GLU	-1	-0.814	-0.907	10.098	1.296	1.296	0.000	0.000	0.000
145	A	143	LEU	0	-0.011	-0.002	10.798	-0.200	-0.200	0.000	0.000	0.000
146	A	144	ILE	0	0.026	0.028	4.993	-0.009	-0.009	0.000	0.000	0.000
147	A	145	THR	0	-0.055	-0.034	4.849	0.520	0.520	0.000	0.000	0.000
148	A	146	LYS	1	0.814	0.919	5.935	-1.720	-1.720	0.000	0.000	0.000
149	A	147	GLU	-1	-0.950	-0.973	5.573	2.789	2.789	0.000	0.000	0.000
150	A	148	ILE	0	-0.056	-0.004	7.935	-0.717	-0.717	0.000	0.000	0.000
151	A	149	ALA	0	0.036	0.000	9.980	0.212	0.212	0.000	0.000	0.000
152	A	150	VAL	0	-0.003	-0.010	11.239	-0.132	-0.132	0.000	0.000	0.000
153	A	151	THR	0	-0.016	0.001	12.769	-0.018	-0.018	0.000	0.000	0.000
154	A	152	VAL	0	-0.026	-0.019	15.155	-0.022	-0.022	0.000	0.000	0.000
155	A	153	TYR	0	-0.077	-0.053	17.449	-0.078	-0.078	0.000	0.000	0.000
156	A	154	ASP	-1	-0.857	-0.925	20.173	0.425	0.425	0.000	0.000	0.000
157	A	155	LEU	0	-0.037	-0.030	22.511	-0.030	-0.030	0.000	0.000	0.000

Top

Graph

Manual

About

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