FMO DATABASE

FMODB ID: LJK79

Calculation Name: 3QFG-A-Xray372

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: 2023-06-20

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	145
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1442416.017483
FMO2-HF: Nuclear repulsion	1383280.821257
FMO2-HF: Total energy	-59135.196226
FMO2-MP2: Total energy	-59309.136761

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:54:ASN)

Summations of interaction energy for fragment #1(A:54: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.
-5.773	-2.868	0.051	-1.081	-1.876	-0.002

Interaction energy analysis for fragmet #1(A:54:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.039 / q_NPA : 0.004

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	56	ASP	-1	-0.831	-0.894	3.883	-0.398	0.686	-0.007	-0.492	-0.585	0.001
4	A	57	ILE	0	-0.034	-0.022	6.747	-0.050	-0.050	0.000	0.000	0.000	0.000
5	A	58	LYS	1	0.883	0.945	9.352	-0.763	-0.763	0.000	0.000	0.000	0.000
6	A	59	ILE	0	0.007	0.005	12.975	-0.024	-0.024	0.000	0.000	0.000	0.000
7	A	60	LYS	1	0.928	0.967	16.272	-0.257	-0.257	0.000	0.000	0.000	0.000
8	A	61	GLY	0	0.007	0.001	19.179	-0.018	-0.018	0.000	0.000	0.000	0.000
9	A	62	ASP	-1	-0.832	-0.892	21.966	0.128	0.128	0.000	0.000	0.000	0.000
10	A	63	THR	0	-0.004	-0.020	18.280	-0.013	-0.013	0.000	0.000	0.000	0.000
11	A	64	ILE	0	0.025	0.026	13.233	0.019	0.019	0.000	0.000	0.000	0.000
12	A	65	VAL	0	-0.051	-0.036	13.797	-0.016	-0.016	0.000	0.000	0.000	0.000
13	A	66	SER	0	0.064	0.029	9.200	0.067	0.067	0.000	0.000	0.000	0.000
14	A	67	ASP	-1	-0.919	-0.972	7.893	0.391	0.391	0.000	0.000	0.000	0.000
15	A	68	LYS	1	0.872	0.908	7.719	-0.672	-0.672	0.000	0.000	0.000	0.000
16	A	69	PHE	0	-0.013	0.000	10.456	-0.081	-0.081	0.000	0.000	0.000	0.000
17	A	70	GLU	-1	-0.805	-0.887	13.730	0.238	0.238	0.000	0.000	0.000	0.000
18	A	71	ALA	0	0.015	0.017	16.459	-0.026	-0.026	0.000	0.000	0.000	0.000
19	A	72	LYS	1	0.873	0.942	18.228	-0.103	-0.103	0.000	0.000	0.000	0.000
20	A	73	ILE	0	-0.040	-0.032	18.476	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	74	LYS	1	0.794	0.887	22.198	-0.082	-0.082	0.000	0.000	0.000	0.000
22	A	75	GLU	-1	-0.878	-0.964	25.169	0.100	0.100	0.000	0.000	0.000	0.000
23	A	76	PRO	0	-0.031	0.004	25.060	-0.006	-0.006	0.000	0.000	0.000	0.000
24	A	77	PHE	0	-0.042	-0.030	27.274	-0.002	-0.002	0.000	0.000	0.000	0.000
25	A	78	ILE	0	0.015	0.018	29.446	0.000	0.000	0.000	0.000	0.000	0.000
26	A	79	ILE	0	0.030	0.033	30.144	-0.002	-0.002	0.000	0.000	0.000	0.000
27	A	80	ASN	0	-0.060	-0.052	33.143	0.000	0.000	0.000	0.000	0.000	0.000
28	A	81	GLU	-1	-0.815	-0.932	34.660	0.018	0.018	0.000	0.000	0.000	0.000
29	A	82	LYS	1	0.892	0.939	36.658	-0.024	-0.024	0.000	0.000	0.000	0.000
30	A	83	ASP	-1	-0.783	-0.869	40.060	0.014	0.014	0.000	0.000	0.000	0.000
31	A	84	GLU	-1	-0.857	-0.904	34.644	0.017	0.017	0.000	0.000	0.000	0.000
32	A	85	LYS	1	0.754	0.862	37.811	-0.017	-0.017	0.000	0.000	0.000	0.000
33	A	86	LYS	1	0.877	0.954	31.892	-0.020	-0.020	0.000	0.000	0.000	0.000
34	A	87	LYS	1	0.884	0.938	32.966	-0.035	-0.035	0.000	0.000	0.000	0.000
35	A	88	TYR	0	0.029	0.004	28.240	0.001	0.001	0.000	0.000	0.000	0.000
36	A	89	ILE	0	-0.012	-0.004	24.812	0.000	0.000	0.000	0.000	0.000	0.000
37	A	90	ALA	0	0.003	-0.009	25.957	0.001	0.001	0.000	0.000	0.000	0.000
38	A	91	PHE	0	0.019	-0.012	22.097	0.004	0.004	0.000	0.000	0.000	0.000
39	A	92	LYS	1	0.904	0.983	23.372	-0.053	-0.053	0.000	0.000	0.000	0.000
40	A	93	MET	0	0.002	-0.007	18.316	0.014	0.014	0.000	0.000	0.000	0.000
41	A	94	GLU	-1	-0.811	-0.878	22.460	0.071	0.071	0.000	0.000	0.000	0.000
42	A	95	ILE	0	0.041	0.024	17.151	0.012	0.012	0.000	0.000	0.000	0.000
43	A	96	THR	0	0.030	0.028	18.899	-0.027	-0.027	0.000	0.000	0.000	0.000
44	A	97	ALA	0	-0.051	-0.003	16.552	0.027	0.027	0.000	0.000	0.000	0.000
45	A	98	LYS	1	0.857	0.929	14.062	-0.238	-0.238	0.000	0.000	0.000	0.000
46	A	99	LYS	1	0.853	0.917	10.077	0.089	0.089	0.000	0.000	0.000	0.000
47	A	100	ASP	-1	-0.925	-0.970	14.558	-0.072	-0.072	0.000	0.000	0.000	0.000
48	A	101	ASP	-1	-0.829	-0.921	11.211	0.032	0.032	0.000	0.000	0.000	0.000
49	A	102	LYS	1	0.986	1.004	14.654	0.191	0.191	0.000	0.000	0.000	0.000
50	A	103	ASP	-1	-0.859	-0.925	12.304	0.007	0.007	0.000	0.000	0.000	0.000
51	A	104	LEU	0	-0.114	-0.050	11.904	0.056	0.056	0.000	0.000	0.000	0.000
52	A	105	ASN	0	-0.003	-0.003	15.273	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	106	PRO	0	0.007	-0.011	16.406	0.026	0.026	0.000	0.000	0.000	0.000
54	A	107	SER	0	0.034	0.002	17.252	0.018	0.018	0.000	0.000	0.000	0.000
55	A	108	SER	0	0.019	0.012	14.275	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	109	ILE	0	-0.029	-0.001	12.524	0.047	0.047	0.000	0.000	0.000	0.000
57	A	110	SER	0	-0.027	-0.017	12.593	0.028	0.028	0.000	0.000	0.000	0.000
58	A	111	HIS	0	-0.054	-0.013	13.213	-0.001	-0.001	0.000	0.000	0.000	0.000
59	A	112	ASP	-1	-0.841	-0.938	9.090	0.315	0.315	0.000	0.000	0.000	0.000
60	A	113	TYR	0	-0.105	-0.055	6.052	0.235	0.235	0.000	0.000	0.000	0.000
61	A	114	ILE	0	-0.015	-0.005	10.243	-0.012	-0.012	0.000	0.000	0.000	0.000
62	A	115	ASN	0	0.047	0.027	12.935	-0.034	-0.034	0.000	0.000	0.000	0.000
63	A	116	ILE	0	-0.019	0.010	15.690	0.012	0.012	0.000	0.000	0.000	0.000
64	A	117	THR	0	-0.010	-0.018	18.882	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	118	GLN	0	-0.016	-0.016	21.523	0.003	0.003	0.000	0.000	0.000	0.000
66	A	119	ASP	-1	-0.858	-0.926	25.191	0.090	0.090	0.000	0.000	0.000	0.000
67	A	120	ASP	-1	-0.841	-0.910	27.214	0.045	0.045	0.000	0.000	0.000	0.000
68	A	121	LYS	1	0.908	0.944	30.132	-0.041	-0.041	0.000	0.000	0.000	0.000
69	A	122	ASN	0	-0.019	-0.017	31.480	0.003	0.003	0.000	0.000	0.000	0.000
70	A	123	THR	0	-0.015	0.000	26.962	0.001	0.001	0.000	0.000	0.000	0.000
71	A	124	VAL	0	0.011	-0.001	22.570	0.002	0.002	0.000	0.000	0.000	0.000
72	A	125	ASN	0	-0.068	-0.035	23.477	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	126	LYS	1	0.980	0.988	16.382	-0.032	-0.032	0.000	0.000	0.000	0.000
74	A	127	LEU	0	-0.042	-0.030	21.332	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	128	ARG	1	0.837	0.888	21.338	-0.018	-0.018	0.000	0.000	0.000	0.000
76	A	129	ASP	-1	-0.859	-0.912	20.145	0.056	0.056	0.000	0.000	0.000	0.000
77	A	130	GLY	0	-0.043	-0.035	23.003	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	131	TYR	0	-0.018	-0.016	22.950	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	132	LEU	0	-0.010	-0.003	28.527	0.000	0.000	0.000	0.000	0.000	0.000
80	A	133	LEU	0	0.007	0.016	31.701	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	134	SER	0	-0.024	-0.012	34.957	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	135	ASP	-1	-0.829	-0.937	31.132	0.020	0.020	0.000	0.000	0.000	0.000
83	A	136	LYS	1	0.980	0.987	33.986	-0.008	-0.008	0.000	0.000	0.000	0.000
84	A	137	LYS	1	0.779	0.900	35.167	-0.031	-0.031	0.000	0.000	0.000	0.000
85	A	138	TYR	0	0.048	-0.015	30.489	0.001	0.001	0.000	0.000	0.000	0.000
86	A	139	LYS	1	0.949	0.992	30.729	-0.007	-0.007	0.000	0.000	0.000	0.000
87	A	140	ASP	-1	-0.900	-0.958	30.800	0.033	0.033	0.000	0.000	0.000	0.000
88	A	141	TRP	0	-0.050	-0.043	25.969	0.005	0.005	0.000	0.000	0.000	0.000
89	A	142	THR	0	0.008	0.006	26.164	0.006	0.006	0.000	0.000	0.000	0.000
90	A	143	GLU	-1	-0.865	-0.909	26.437	0.013	0.013	0.000	0.000	0.000	0.000
91	A	144	HIS	1	0.824	0.881	24.659	-0.021	-0.021	0.000	0.000	0.000	0.000
92	A	145	ASN	0	0.008	-0.001	22.269	0.007	0.007	0.000	0.000	0.000	0.000
93	A	146	GLN	0	0.039	0.034	21.053	0.016	0.016	0.000	0.000	0.000	0.000
94	A	147	ASP	-1	-0.868	-0.898	21.842	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	148	GLN	0	-0.048	-0.029	18.092	0.000	0.000	0.000	0.000	0.000	0.000
96	A	149	ILE	0	-0.010	-0.005	19.083	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	150	LYS	1	0.954	0.966	19.096	0.025	0.025	0.000	0.000	0.000	0.000
98	A	151	LYS	1	0.999	1.002	16.794	0.101	0.101	0.000	0.000	0.000	0.000
99	A	152	GLY	0	-0.015	-0.009	19.080	0.011	0.011	0.000	0.000	0.000	0.000
100	A	153	LYS	1	0.877	0.944	21.568	-0.003	-0.003	0.000	0.000	0.000	0.000
101	A	154	THR	0	0.063	-0.003	21.508	0.007	0.007	0.000	0.000	0.000	0.000
102	A	155	ALA	0	-0.043	-0.019	22.616	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	156	GLN	0	-0.060	-0.027	23.144	0.013	0.013	0.000	0.000	0.000	0.000
104	A	157	ALA	0	-0.005	0.013	21.356	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	158	MET	0	-0.007	-0.020	23.381	0.002	0.002	0.000	0.000	0.000	0.000
106	A	159	PHE	0	0.005	0.013	18.389	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	160	ILE	0	0.040	0.017	22.533	0.002	0.002	0.000	0.000	0.000	0.000
108	A	161	TYR	0	0.055	0.029	18.293	0.003	0.003	0.000	0.000	0.000	0.000
109	A	162	GLU	-1	-0.852	-0.885	24.525	0.025	0.025	0.000	0.000	0.000	0.000
110	A	163	LEU	0	-0.045	-0.035	26.839	0.002	0.002	0.000	0.000	0.000	0.000
111	A	164	ARG	1	0.894	0.953	25.432	-0.047	-0.047	0.000	0.000	0.000	0.000
112	A	165	GLY	0	0.027	0.021	29.784	0.002	0.002	0.000	0.000	0.000	0.000
113	A	166	ASP	-1	-0.950	-0.989	31.992	0.049	0.049	0.000	0.000	0.000	0.000
114	A	167	GLY	0	0.018	0.033	30.095	0.001	0.001	0.000	0.000	0.000	0.000
115	A	168	ASN	0	-0.044	-0.046	27.779	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	169	ILE	0	0.026	0.018	23.267	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	170	ASN	0	-0.012	0.005	20.487	0.012	0.012	0.000	0.000	0.000	0.000
118	A	171	LEU	0	-0.018	0.000	16.321	-0.008	-0.008	0.000	0.000	0.000	0.000
119	A	172	ASN	0	-0.014	-0.022	14.796	0.023	0.023	0.000	0.000	0.000	0.000
120	A	173	VAL	0	0.062	0.025	10.425	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	174	HIS	0	-0.009	0.026	8.090	0.037	0.037	0.000	0.000	0.000	0.000
122	A	175	LYS	1	0.833	0.889	3.097	-1.578	-0.926	0.041	-0.159	-0.534	-0.001
123	A	176	TYR	0	-0.028	-0.016	3.617	-0.273	0.157	0.013	-0.135	-0.308	0.000
124	A	177	SER	0	-0.017	0.016	3.883	-0.117	-0.014	-0.001	-0.014	-0.088	0.000
125	A	178	GLU	-1	-0.914	-0.971	3.671	-3.001	-2.365	0.005	-0.281	-0.361	-0.002
126	A	179	ASP	-1	-0.872	-0.946	7.034	0.029	0.029	0.000	0.000	0.000	0.000
127	A	180	LYS	1	0.904	0.952	9.513	-0.323	-0.323	0.000	0.000	0.000	0.000
128	A	181	THR	0	-0.031	-0.021	9.815	-0.012	-0.012	0.000	0.000	0.000	0.000
129	A	182	VAL	0	-0.089	-0.046	7.841	0.032	0.032	0.000	0.000	0.000	0.000
130	A	183	ASP	-1	-0.826	-0.916	11.290	0.355	0.355	0.000	0.000	0.000	0.000
131	A	184	SER	0	-0.043	-0.041	14.360	-0.028	-0.028	0.000	0.000	0.000	0.000
132	A	185	LYS	1	0.943	0.996	17.260	-0.123	-0.123	0.000	0.000	0.000	0.000
133	A	186	SER	0	-0.008	-0.004	20.564	-0.005	-0.005	0.000	0.000	0.000	0.000
134	A	187	PHE	0	-0.042	-0.027	21.948	0.000	0.000	0.000	0.000	0.000	0.000
135	A	188	LYS	1	0.937	0.965	26.688	-0.090	-0.090	0.000	0.000	0.000	0.000
136	A	189	PHE	0	0.109	0.057	29.873	-0.002	-0.002	0.000	0.000	0.000	0.000
137	A	190	SER	0	-0.012	-0.015	31.304	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	191	LYS	1	0.902	0.947	33.250	-0.067	-0.067	0.000	0.000	0.000	0.000
139	A	192	LEU	0	0.006	0.033	28.825	0.000	0.000	0.000	0.000	0.000	0.000
140	A	193	LYS	1	0.950	0.970	32.792	-0.056	-0.056	0.000	0.000	0.000	0.000
141	A	194	THR	0	0.024	0.002	33.545	0.002	0.002	0.000	0.000	0.000	0.000
142	A	195	GLU	-1	-0.868	-0.921	34.117	0.037	0.037	0.000	0.000	0.000	0.000
143	A	196	ASP	-1	-0.795	-0.882	36.141	0.028	0.028	0.000	0.000	0.000	0.000
144	A	197	PHE	0	-0.038	-0.026	35.252	0.001	0.001	0.000	0.000	0.000	0.000
145	A	198	SER	0	-0.045	-0.015	38.878	-0.001	-0.001	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

Interactive mode: IFIE and PIEDA for fragment #1(A:54:ASN)