FMO DATABASE

FMODB ID: LJM79

Calculation Name: 3QFG-A-Xray318

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3QFG

Chain ID: A

ChEMBL ID:

UniProt ID: Q2G019

Base Structure: X-ray

Registration Date: 2021-09-07

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

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. 1.20200129

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	147
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1446114.400875
FMO2-HF: Nuclear repulsion	1386810.40468
FMO2-HF: Total energy	-59303.996195
FMO2-MP2: Total energy	-59478.506777

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:53:ACE )

Summations of interaction energy for fragment #1(A:53:ACE )

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.
2.387	-0.26	13.902	-7.888	-3.369	-0.044

Interaction energy analysis for fragmet #1(A:53:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.034 / q_NPA : -0.001

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	55	MET	0	-0.063	-0.009	3.810	0.750	1.776	-0.007	-0.478	-0.541	0.000
4	A	56	ASP	-1	-0.893	-0.958	5.524	-0.292	-0.292	0.000	0.000	0.000	0.000
5	A	57	ILE	0	-0.034	-0.017	8.320	0.107	0.107	0.000	0.000	0.000	0.000
6	A	58	LYS	1	0.949	0.979	10.206	0.147	0.147	0.000	0.000	0.000	0.000
7	A	59	ILE	0	0.022	0.020	13.742	0.029	0.029	0.000	0.000	0.000	0.000
8	A	60	LYS	1	0.915	0.958	16.785	0.030	0.030	0.000	0.000	0.000	0.000
9	A	61	GLY	0	0.019	0.011	19.916	0.005	0.005	0.000	0.000	0.000	0.000
10	A	62	ASP	-1	-0.951	-0.984	22.311	0.043	0.043	0.000	0.000	0.000	0.000
11	A	63	THR	0	0.038	0.018	18.775	0.011	0.011	0.000	0.000	0.000	0.000
12	A	64	ILE	0	0.000	0.014	13.511	-0.012	-0.012	0.000	0.000	0.000	0.000
13	A	65	VAL	0	-0.037	-0.032	14.526	-0.012	-0.012	0.000	0.000	0.000	0.000
14	A	66	SER	0	0.051	0.019	9.878	-0.015	-0.015	0.000	0.000	0.000	0.000
15	A	67	ASP	-1	-0.917	-0.963	10.618	-0.304	-0.304	0.000	0.000	0.000	0.000
16	A	68	LYS	1	0.900	0.943	7.145	-0.117	-0.117	0.000	0.000	0.000	0.000
17	A	69	PHE	0	-0.019	-0.009	10.282	0.001	0.001	0.000	0.000	0.000	0.000
18	A	70	GLU	-1	-0.882	-0.940	14.278	-0.006	-0.006	0.000	0.000	0.000	0.000
19	A	71	ALA	0	0.027	0.020	16.891	0.006	0.006	0.000	0.000	0.000	0.000
20	A	72	LYS	1	0.990	1.017	18.308	-0.048	-0.048	0.000	0.000	0.000	0.000
21	A	73	ILE	0	-0.033	-0.027	18.814	0.009	0.009	0.000	0.000	0.000	0.000
22	A	74	LYS	1	0.905	0.960	22.076	-0.064	-0.064	0.000	0.000	0.000	0.000
23	A	75	GLU	-1	-0.918	-0.976	24.858	0.066	0.066	0.000	0.000	0.000	0.000
24	A	76	PRO	0	-0.021	0.008	24.603	0.001	0.001	0.000	0.000	0.000	0.000
25	A	77	PHE	0	-0.046	-0.032	26.709	-0.007	-0.007	0.000	0.000	0.000	0.000
26	A	78	ILE	0	-0.002	0.014	28.584	0.007	0.007	0.000	0.000	0.000	0.000
27	A	79	ILE	0	0.015	0.024	29.028	-0.005	-0.005	0.000	0.000	0.000	0.000
28	A	80	ASN	0	-0.089	-0.073	32.083	0.005	0.005	0.000	0.000	0.000	0.000
29	A	81	GLU	-1	-0.791	-0.909	33.358	0.069	0.069	0.000	0.000	0.000	0.000
30	A	82	LYS	1	0.955	0.966	35.364	-0.049	-0.049	0.000	0.000	0.000	0.000
31	A	83	ASP	-1	-0.852	-0.924	38.548	0.056	0.056	0.000	0.000	0.000	0.000
32	A	84	GLU	-1	-0.953	-0.976	33.652	0.083	0.083	0.000	0.000	0.000	0.000
33	A	85	LYS	1	0.806	0.904	36.300	-0.052	-0.052	0.000	0.000	0.000	0.000
34	A	86	LYS	1	0.987	0.999	30.753	-0.093	-0.093	0.000	0.000	0.000	0.000
35	A	87	LYS	1	0.923	0.965	31.527	-0.068	-0.068	0.000	0.000	0.000	0.000
36	A	88	TYR	0	0.028	0.027	26.794	0.008	0.008	0.000	0.000	0.000	0.000
37	A	89	ILE	0	-0.004	-0.002	23.782	-0.010	-0.010	0.000	0.000	0.000	0.000
38	A	90	ALA	0	0.003	-0.004	24.893	0.013	0.013	0.000	0.000	0.000	0.000
39	A	91	PHE	0	0.017	-0.014	21.365	-0.010	-0.010	0.000	0.000	0.000	0.000
40	A	92	LYS	1	0.926	0.985	22.663	-0.067	-0.067	0.000	0.000	0.000	0.000
41	A	93	MET	0	-0.003	-0.012	17.809	0.003	0.003	0.000	0.000	0.000	0.000
42	A	94	GLU	-1	-0.959	-0.972	22.327	0.054	0.054	0.000	0.000	0.000	0.000
43	A	95	ILE	0	0.037	0.024	17.078	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	96	THR	0	-0.014	-0.018	19.089	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	97	ALA	0	-0.012	0.011	17.013	0.003	0.003	0.000	0.000	0.000	0.000
46	A	98	LYS	1	0.946	0.984	15.793	0.011	0.011	0.000	0.000	0.000	0.000
47	A	99	LYS	1	0.866	0.919	12.861	0.105	0.105	0.000	0.000	0.000	0.000
48	A	100	ASP	-1	-0.958	-0.987	16.213	0.058	0.058	0.000	0.000	0.000	0.000
49	A	101	ASP	-1	-0.866	-0.945	11.185	0.172	0.172	0.000	0.000	0.000	0.000
50	A	102	LYS	1	0.970	0.988	14.802	-0.089	-0.089	0.000	0.000	0.000	0.000
51	A	103	ASP	-1	-0.850	-0.921	10.521	0.384	0.384	0.000	0.000	0.000	0.000
52	A	104	LEU	0	-0.089	-0.032	12.020	0.029	0.029	0.000	0.000	0.000	0.000
53	A	105	ASN	0	-0.027	-0.010	14.343	-0.037	-0.037	0.000	0.000	0.000	0.000
54	A	106	PRO	0	0.001	-0.013	15.281	0.040	0.040	0.000	0.000	0.000	0.000
55	A	107	SER	0	0.034	-0.028	16.304	0.017	0.017	0.000	0.000	0.000	0.000
56	A	108	SER	0	0.007	0.018	12.598	0.034	0.034	0.000	0.000	0.000	0.000
57	A	109	ILE	0	0.011	0.023	11.574	0.086	0.086	0.000	0.000	0.000	0.000
58	A	110	SER	0	-0.098	-0.060	11.593	0.061	0.061	0.000	0.000	0.000	0.000
59	A	111	HIS	0	-0.014	-0.002	12.488	0.014	0.014	0.000	0.000	0.000	0.000
60	A	112	ASP	-1	-0.867	-0.939	7.872	0.965	0.965	0.000	0.000	0.000	0.000
61	A	113	TYR	0	-0.101	-0.054	5.677	0.273	0.273	0.000	0.000	0.000	0.000
62	A	114	ILE	0	-0.015	-0.009	9.279	-0.130	-0.130	0.000	0.000	0.000	0.000
63	A	115	ASN	0	0.030	0.033	11.434	-0.001	-0.001	0.000	0.000	0.000	0.000
64	A	116	ILE	0	-0.011	0.004	14.545	-0.044	-0.044	0.000	0.000	0.000	0.000
65	A	117	THR	0	-0.034	-0.024	17.902	0.010	0.010	0.000	0.000	0.000	0.000
66	A	118	GLN	0	-0.020	-0.024	20.462	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	119	ASP	-1	-0.873	-0.919	24.192	0.085	0.085	0.000	0.000	0.000	0.000
68	A	120	ASP	-1	-0.849	-0.920	26.315	0.075	0.075	0.000	0.000	0.000	0.000
69	A	121	LYS	1	0.906	0.935	29.104	-0.055	-0.055	0.000	0.000	0.000	0.000
70	A	122	ASN	0	-0.028	-0.018	30.425	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	123	THR	0	-0.027	-0.017	25.780	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	124	VAL	0	0.041	0.015	21.272	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	125	ASN	0	-0.064	-0.008	22.291	0.015	0.015	0.000	0.000	0.000	0.000
74	A	126	LYS	1	1.034	1.021	16.247	-0.317	-0.317	0.000	0.000	0.000	0.000
75	A	127	LEU	0	-0.035	-0.032	19.989	-0.015	-0.015	0.000	0.000	0.000	0.000
76	A	128	ARG	1	0.901	0.955	19.867	-0.133	-0.133	0.000	0.000	0.000	0.000
77	A	129	ASP	-1	-0.837	-0.894	18.379	0.268	0.268	0.000	0.000	0.000	0.000
78	A	130	GLY	0	-0.041	-0.053	21.457	-0.012	-0.012	0.000	0.000	0.000	0.000
79	A	131	TYR	0	-0.028	-0.020	21.647	0.007	0.007	0.000	0.000	0.000	0.000
80	A	132	LEU	0	-0.005	-0.001	27.027	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	133	LEU	0	0.017	0.022	30.297	0.001	0.001	0.000	0.000	0.000	0.000
82	A	134	SER	0	0.015	-0.007	33.493	-0.003	-0.003	0.000	0.000	0.000	0.000
83	A	135	ASP	-1	-0.906	-0.951	30.246	0.094	0.094	0.000	0.000	0.000	0.000
84	A	136	LYS	1	0.981	0.976	32.826	-0.054	-0.054	0.000	0.000	0.000	0.000
85	A	137	LYS	1	0.845	0.935	34.069	-0.062	-0.062	0.000	0.000	0.000	0.000
86	A	138	TYR	0	0.064	0.008	29.563	-0.002	-0.002	0.000	0.000	0.000	0.000
87	A	139	LYS	1	1.002	1.031	29.879	-0.062	-0.062	0.000	0.000	0.000	0.000
88	A	140	ASP	-1	-0.919	-0.973	29.975	0.065	0.065	0.000	0.000	0.000	0.000
89	A	141	TRP	0	-0.033	-0.031	25.649	0.000	0.000	0.000	0.000	0.000	0.000
90	A	142	THR	0	0.011	0.001	25.298	0.006	0.006	0.000	0.000	0.000	0.000
91	A	143	GLU	-1	-0.938	-0.959	25.343	0.085	0.085	0.000	0.000	0.000	0.000
92	A	144	HIS	1	0.865	0.922	23.631	-0.093	-0.093	0.000	0.000	0.000	0.000
93	A	145	ASN	0	0.018	0.003	21.259	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	146	GLN	0	0.060	0.064	19.764	0.035	0.035	0.000	0.000	0.000	0.000
95	A	147	ASP	-1	-0.885	-0.927	20.238	0.120	0.120	0.000	0.000	0.000	0.000
96	A	148	GLN	0	-0.017	-0.019	17.475	0.002	0.002	0.000	0.000	0.000	0.000
97	A	149	ILE	0	-0.001	-0.004	18.540	-0.019	-0.019	0.000	0.000	0.000	0.000
98	A	150	LYS	1	0.941	0.961	19.217	-0.053	-0.053	0.000	0.000	0.000	0.000
99	A	151	LYS	1	0.996	1.004	19.039	0.032	0.032	0.000	0.000	0.000	0.000
100	A	152	GLY	0	-0.020	-0.008	20.446	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	153	LYS	1	0.887	0.949	22.366	-0.029	-0.029	0.000	0.000	0.000	0.000
102	A	154	THR	0	0.097	0.037	21.973	0.003	0.003	0.000	0.000	0.000	0.000
103	A	155	ALA	0	-0.048	-0.014	22.532	-0.005	-0.005	0.000	0.000	0.000	0.000
104	A	156	GLN	0	-0.028	-0.010	22.904	0.000	0.000	0.000	0.000	0.000	0.000
105	A	157	ALA	0	0.004	0.019	20.744	0.004	0.004	0.000	0.000	0.000	0.000
106	A	158	MET	0	-0.028	-0.026	22.750	-0.014	-0.014	0.000	0.000	0.000	0.000
107	A	159	PHE	0	0.003	0.013	17.798	0.006	0.006	0.000	0.000	0.000	0.000
108	A	160	ILE	0	0.066	0.052	21.509	-0.013	-0.013	0.000	0.000	0.000	0.000
109	A	161	TYR	0	0.040	0.021	16.929	0.000	0.000	0.000	0.000	0.000	0.000
110	A	162	GLU	-1	-0.933	-0.965	23.216	0.117	0.117	0.000	0.000	0.000	0.000
111	A	163	LEU	0	-0.038	-0.033	25.450	0.004	0.004	0.000	0.000	0.000	0.000
112	A	164	ARG	1	0.847	0.926	23.668	-0.137	-0.137	0.000	0.000	0.000	0.000
113	A	165	GLY	0	0.041	0.030	28.533	0.000	0.000	0.000	0.000	0.000	0.000
114	A	166	ASP	-1	-0.955	-0.988	30.860	0.065	0.065	0.000	0.000	0.000	0.000
115	A	167	GLY	0	0.022	0.035	29.195	-0.006	-0.006	0.000	0.000	0.000	0.000
116	A	168	ASN	0	-0.026	-0.042	27.031	0.002	0.002	0.000	0.000	0.000	0.000
117	A	169	ILE	0	0.030	0.022	22.274	0.005	0.005	0.000	0.000	0.000	0.000
118	A	170	ASN	0	-0.041	-0.028	20.011	-0.021	-0.021	0.000	0.000	0.000	0.000
119	A	171	LEU	0	-0.017	0.000	15.623	0.013	0.013	0.000	0.000	0.000	0.000
120	A	172	ASN	0	0.001	-0.014	14.016	-0.047	-0.047	0.000	0.000	0.000	0.000
121	A	173	VAL	0	0.069	0.020	10.513	0.028	0.028	0.000	0.000	0.000	0.000
122	A	174	HIS	0	-0.026	0.006	6.523	-0.355	-0.355	0.000	0.000	0.000	0.000
123	A	175	LYS	1	0.934	0.963	3.461	0.696	0.843	0.011	-0.052	-0.107	0.000
124	A	176	TYR	0	0.004	0.001	2.373	0.309	0.295	2.846	-1.886	-0.947	-0.010
125	A	177	SER	0	0.016	0.021	1.914	1.687	-2.943	10.492	-4.631	-1.231	-0.025
126	A	178	GLU	-1	-0.930	-0.971	3.009	-2.349	-1.525	0.560	-0.841	-0.543	-0.009
127	A	179	ASP	-1	-0.865	-0.938	5.642	0.474	0.474	0.000	0.000	0.000	0.000
128	A	180	LYS	1	0.893	0.944	8.540	-0.132	-0.132	0.000	0.000	0.000	0.000
129	A	181	THR	0	-0.038	-0.023	9.336	0.013	0.013	0.000	0.000	0.000	0.000
130	A	182	VAL	0	-0.095	-0.047	8.237	-0.063	-0.063	0.000	0.000	0.000	0.000
131	A	183	ASP	-1	-0.852	-0.942	11.500	-0.032	-0.032	0.000	0.000	0.000	0.000
132	A	184	SER	0	-0.043	-0.032	14.455	0.040	0.040	0.000	0.000	0.000	0.000
133	A	185	LYS	1	0.950	0.988	17.186	-0.078	-0.078	0.000	0.000	0.000	0.000
134	A	186	SER	0	0.023	0.015	20.463	0.013	0.013	0.000	0.000	0.000	0.000
135	A	187	PHE	0	-0.035	-0.019	21.709	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	188	LYS	1	0.925	0.955	26.304	-0.036	-0.036	0.000	0.000	0.000	0.000
137	A	189	PHE	0	0.112	0.060	29.029	-0.001	-0.001	0.000	0.000	0.000	0.000
138	A	190	SER	0	-0.016	-0.019	30.642	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	191	LYS	1	0.876	0.930	32.708	-0.037	-0.037	0.000	0.000	0.000	0.000
140	A	192	LEU	0	0.036	0.051	28.066	-0.002	-0.002	0.000	0.000	0.000	0.000
141	A	193	LYS	1	0.942	0.967	32.217	-0.044	-0.044	0.000	0.000	0.000	0.000
142	A	194	THR	0	0.016	0.003	32.822	0.006	0.006	0.000	0.000	0.000	0.000
143	A	195	GLU	-1	-0.947	-0.981	33.267	0.059	0.059	0.000	0.000	0.000	0.000
144	A	196	ASP	-1	-0.880	-0.924	35.141	0.058	0.058	0.000	0.000	0.000	0.000
145	A	197	PHE	0	-0.040	-0.043	34.539	0.002	0.002	0.000	0.000	0.000	0.000
146	A	198	SER	0	-0.051	-0.018	37.719	-0.002	-0.002	0.000	0.000	0.000	0.000
147	A	199	NME	0	-0.002	0.024	37.900	-0.002	-0.002	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:53:ACE )