FMO DATABASE

FMODB ID: 3J47L

Calculation Name: 1QGV-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1QGV

Chain ID: A

ChEMBL ID:

UniProt ID: P83876

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	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1348411.57445
FMO2-HF: Nuclear repulsion	1291079.692236
FMO2-HF: Total energy	-57331.882214
FMO2-MP2: Total energy	-57494.247831

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:2:SER)

Summations of interaction energy for fragment #1(A:2:SER)

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.
0.124	1.692	-0.001	-0.727	-0.839	0.002

Interaction energy analysis for fragmet #1(A:2:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.027 / q_NPA : -0.025

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	4	MET	0	-0.052	-0.010	3.827	1.725	3.073	-0.001	-0.686	-0.660	0.002
4	A	5	LEU	0	-0.011	0.008	6.296	0.085	0.085	0.000	0.000	0.000	0.000
5	A	6	PRO	0	-0.021	-0.003	3.851	-0.733	-0.513	0.000	-0.041	-0.179	0.000
6	A	7	HIS	0	0.049	0.013	6.304	-0.036	-0.036	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.075	-0.024	7.733	-0.205	-0.205	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.000	-0.033	8.387	-0.143	-0.143	0.000	0.000	0.000	0.000
9	A	10	ASN	0	-0.004	-0.001	11.954	0.045	0.045	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.104	0.040	14.458	0.025	0.025	0.000	0.000	0.000	0.000
11	A	12	TRP	0	-0.019	-0.005	11.685	0.010	0.010	0.000	0.000	0.000	0.000
12	A	13	GLN	0	0.035	0.015	9.487	0.053	0.053	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.020	0.024	12.062	0.080	0.080	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.906	-0.963	14.046	0.051	0.051	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.015	-0.022	12.431	0.057	0.057	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.004	0.010	11.029	0.059	0.059	0.000	0.000	0.000	0.000
17	A	18	ILE	0	-0.075	-0.039	12.349	0.094	0.094	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.057	-0.026	15.913	0.030	0.030	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.114	-0.042	12.191	0.035	0.035	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.799	-0.868	11.289	0.835	0.835	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.923	-0.958	15.051	0.184	0.184	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.941	-0.980	17.133	0.294	0.294	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.733	0.859	9.382	-1.075	-1.075	0.000	0.000	0.000	0.000
24	A	25	VAL	0	-0.070	-0.022	16.520	-0.045	-0.045	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.050	0.022	12.998	0.096	0.096	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.047	-0.039	13.912	-0.091	-0.091	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.036	0.009	13.548	0.081	0.081	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.752	0.838	14.646	-0.130	-0.130	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.017	-0.002	16.080	-0.021	-0.021	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.037	-0.015	18.513	0.015	0.015	0.000	0.000	0.000	0.000
31	A	32	HIS	0	0.030	0.042	18.960	-0.036	-0.036	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.757	-0.890	15.170	-0.092	-0.092	0.000	0.000	0.000	0.000
33	A	34	TRP	0	-0.063	-0.027	18.049	0.022	0.022	0.000	0.000	0.000	0.000
34	A	35	ASP	-1	-0.802	-0.899	21.150	0.048	0.048	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.008	-0.012	22.192	0.016	0.016	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.042	-0.032	23.204	0.023	0.023	0.000	0.000	0.000	0.000
37	A	38	CYS	0	-0.032	0.006	18.646	0.038	0.038	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.012	0.015	18.469	0.037	0.037	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.961	0.981	18.884	-0.077	-0.077	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.013	0.002	17.695	0.049	0.049	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.752	-0.858	14.538	0.264	0.264	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.959	-0.964	14.733	0.325	0.325	0.000	0.000	0.000	0.000
43	A	44	VAL	0	0.009	0.004	16.536	0.078	0.078	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.013	0.010	13.594	0.075	0.075	0.000	0.000	0.000	0.000
45	A	46	TYR	0	0.021	0.004	9.372	0.203	0.203	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.083	-0.058	12.759	0.110	0.110	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.088	-0.049	15.077	-0.019	-0.019	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.073	0.038	10.005	0.000	0.000	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.877	-0.945	10.739	1.791	1.791	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.852	0.936	12.471	-0.520	-0.520	0.000	0.000	0.000	0.000
51	A	52	VAL	0	-0.011	-0.008	13.877	-0.075	-0.075	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.935	0.976	8.411	-2.388	-2.388	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.040	-0.027	13.041	0.050	0.050	0.000	0.000	0.000	0.000
54	A	55	PHE	0	-0.031	-0.021	15.848	-0.049	-0.049	0.000	0.000	0.000	0.000
55	A	56	ALA	0	0.013	0.002	14.655	-0.088	-0.088	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.011	0.013	8.670	0.172	0.172	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.026	-0.016	9.935	-0.192	-0.192	0.000	0.000	0.000	0.000
58	A	59	TYR	0	0.019	0.010	6.923	0.347	0.347	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.037	-0.008	10.453	-0.052	-0.052	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.036	0.012	11.728	-0.086	-0.086	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.717	-0.862	14.329	-0.104	-0.104	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.040	-0.030	16.590	-0.023	-0.023	0.000	0.000	0.000	0.000
63	A	64	THR	0	-0.063	-0.022	19.609	0.004	0.004	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.958	-0.985	13.864	-0.440	-0.440	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.078	-0.034	14.723	-0.018	-0.018	0.000	0.000	0.000	0.000
66	A	67	PRO	0	0.002	-0.005	18.031	0.036	0.036	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.904	-0.955	20.044	-0.116	-0.116	0.000	0.000	0.000	0.000
68	A	69	PHE	0	-0.003	-0.011	17.566	0.016	0.016	0.000	0.000	0.000	0.000
69	A	70	ASN	0	0.045	0.035	22.307	0.030	0.030	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.961	1.009	24.552	0.016	0.016	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.117	-0.059	21.363	0.008	0.008	0.000	0.000	0.000	0.000
72	A	73	TYR	0	-0.037	-0.005	21.405	0.016	0.016	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.923	-0.994	26.551	0.006	0.006	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.048	-0.035	24.726	-0.007	-0.007	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.006	-0.020	25.935	0.003	0.003	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.909	-0.948	25.698	-0.009	-0.009	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.029	-0.014	25.022	0.002	0.002	0.000	0.000	0.000	0.000
78	A	80	THR	0	-0.042	-0.006	21.654	0.017	0.017	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.012	0.011	17.679	0.012	0.012	0.000	0.000	0.000	0.000
80	A	82	MET	0	-0.058	-0.007	18.853	-0.025	-0.025	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.035	0.005	18.357	0.044	0.044	0.000	0.000	0.000	0.000
82	A	84	PHE	0	0.064	0.032	17.671	-0.048	-0.048	0.000	0.000	0.000	0.000
83	A	85	PHE	0	-0.027	-0.021	18.547	0.044	0.044	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.883	0.939	19.715	-0.277	-0.277	0.000	0.000	0.000	0.000
85	A	87	ASN	0	0.066	0.029	19.926	-0.016	-0.016	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.924	0.989	21.465	-0.155	-0.155	0.000	0.000	0.000	0.000
87	A	89	HIS	0	0.015	0.011	22.559	0.015	0.015	0.000	0.000	0.000	0.000
88	A	90	ILE	0	-0.100	-0.056	22.728	-0.012	-0.012	0.000	0.000	0.000	0.000
89	A	91	MET	0	0.017	0.010	24.544	0.002	0.002	0.000	0.000	0.000	0.000
90	A	92	ILE	0	0.019	-0.007	23.641	0.009	0.009	0.000	0.000	0.000	0.000
91	A	93	ASP	-1	-0.880	-0.935	28.060	0.098	0.098	0.000	0.000	0.000	0.000
92	A	94	LEU	0	0.000	-0.022	27.684	0.010	0.010	0.000	0.000	0.000	0.000
93	A	95	GLY	0	0.008	0.013	31.611	0.000	0.000	0.000	0.000	0.000	0.000
94	A	96	THR	0	0.012	-0.014	32.781	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.010	0.013	35.392	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	98	ASN	0	-0.019	0.009	28.945	-0.013	-0.013	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.021	-0.022	30.888	0.010	0.010	0.000	0.000	0.000	0.000
98	A	100	ASN	0	0.006	0.008	25.379	-0.013	-0.013	0.000	0.000	0.000	0.000
99	A	101	LYN	0	-0.005	0.008	23.703	0.015	0.015	0.000	0.000	0.000	0.000
100	A	102	ILE	0	0.028	0.008	22.483	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	103	ASN	0	-0.011	-0.007	23.160	0.017	0.017	0.000	0.000	0.000	0.000
102	A	104	TRP	0	0.008	0.012	25.167	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	105	ALA	0	0.000	-0.003	23.323	0.019	0.019	0.000	0.000	0.000	0.000
104	A	106	MET	0	-0.023	0.006	22.947	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.924	-0.970	23.931	0.155	0.155	0.000	0.000	0.000	0.000
106	A	108	ASP	-1	-0.906	-0.949	24.266	0.230	0.230	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.957	0.977	18.552	-0.459	-0.459	0.000	0.000	0.000	0.000
108	A	110	GLN	0	-0.045	-0.047	21.174	0.056	0.056	0.000	0.000	0.000	0.000
109	A	111	GLU	-1	-0.780	-0.897	23.462	0.201	0.201	0.000	0.000	0.000	0.000
110	A	112	MET	0	0.062	0.015	18.528	0.000	0.000	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.094	-0.041	18.948	0.028	0.028	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.843	-0.913	20.613	0.283	0.283	0.000	0.000	0.000	0.000
113	A	115	ILE	0	-0.018	0.003	22.562	-0.012	-0.012	0.000	0.000	0.000	0.000
114	A	116	ILE	0	0.038	0.026	16.306	-0.011	-0.011	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.852	-0.913	20.364	0.321	0.321	0.000	0.000	0.000	0.000
116	A	118	THR	0	-0.063	-0.039	22.087	-0.028	-0.028	0.000	0.000	0.000	0.000
117	A	119	VAL	0	0.017	0.000	21.665	-0.021	-0.021	0.000	0.000	0.000	0.000
118	A	120	TYR	0	0.035	0.015	19.969	-0.028	-0.028	0.000	0.000	0.000	0.000
119	A	121	ARG	1	0.786	0.874	22.010	-0.291	-0.291	0.000	0.000	0.000	0.000
120	A	122	GLY	0	-0.031	-0.016	25.261	-0.022	-0.022	0.000	0.000	0.000	0.000
121	A	123	ALA	0	0.058	0.019	23.250	-0.019	-0.019	0.000	0.000	0.000	0.000
122	A	124	ARG	1	0.919	0.975	23.466	-0.297	-0.297	0.000	0.000	0.000	0.000
123	A	125	LYS	1	0.830	0.924	25.177	-0.191	-0.191	0.000	0.000	0.000	0.000
124	A	126	GLY	0	0.016	0.009	27.860	-0.015	-0.015	0.000	0.000	0.000	0.000
125	A	127	ARG	1	0.859	0.944	28.763	-0.153	-0.153	0.000	0.000	0.000	0.000
126	A	128	GLY	0	0.040	0.004	27.596	0.010	0.010	0.000	0.000	0.000	0.000
127	A	129	LEU	0	0.007	0.022	28.444	0.000	0.000	0.000	0.000	0.000	0.000
128	A	130	VAL	0	-0.084	-0.043	25.965	-0.001	-0.001	0.000	0.000	0.000	0.000
129	A	131	VAL	0	0.021	0.006	29.292	-0.004	-0.004	0.000	0.000	0.000	0.000
130	A	132	SER	0	-0.024	-0.015	28.086	0.012	0.012	0.000	0.000	0.000	0.000
131	A	133	PRO	0	0.004	-0.016	30.208	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.847	0.942	27.111	-0.187	-0.187	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.926	-0.952	32.874	0.089	0.089	0.000	0.000	0.000	0.000
134	A	136	TYR	0	-0.014	-0.003	31.113	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	137	SER	0	-0.024	-0.003	37.861	-0.007	-0.007	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:SER)