FMO DATABASE

FMODB ID: 982M2

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	OptAll
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	-1347207.412338
FMO2-HF: Nuclear repulsion	1289874.038413
FMO2-HF: Total energy	-57333.373926
FMO2-MP2: Total energy	-57495.568784

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.
0.894	2.644	-0.01	-0.856	-0.886	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 : -0.019 / q_NPA : -0.024

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	-0.043	-0.006	3.874	0.933	2.482	-0.010	-0.816	-0.724	0.002
4	A	5	LEU	0	-0.005	0.003	6.586	-0.102	-0.102	0.000	0.000	0.000	0.000
5	A	6	PRO	0	-0.026	-0.009	3.749	-0.411	-0.210	0.000	-0.040	-0.162	0.000
6	A	7	HIS	0	0.032	0.004	6.343	-0.218	-0.218	0.000	0.000	0.000	0.000
7	A	8	LEU	0	-0.073	-0.025	7.853	0.122	0.122	0.000	0.000	0.000	0.000
8	A	9	HIS	0	-0.020	-0.020	8.985	0.066	0.066	0.000	0.000	0.000	0.000
9	A	10	ASN	0	-0.030	-0.038	12.483	-0.085	-0.085	0.000	0.000	0.000	0.000
10	A	11	GLY	0	0.068	0.044	14.821	0.012	0.012	0.000	0.000	0.000	0.000
11	A	12	TRP	0	-0.025	-0.012	12.559	-0.010	-0.010	0.000	0.000	0.000	0.000
12	A	13	GLN	0	0.014	0.002	10.211	0.066	0.066	0.000	0.000	0.000	0.000
13	A	14	VAL	0	0.028	0.020	11.941	0.006	0.006	0.000	0.000	0.000	0.000
14	A	15	ASP	-1	-0.932	-0.967	14.089	0.009	0.009	0.000	0.000	0.000	0.000
15	A	16	GLN	0	-0.018	-0.021	12.622	-0.008	-0.008	0.000	0.000	0.000	0.000
16	A	17	ALA	0	0.019	0.020	10.858	-0.031	-0.031	0.000	0.000	0.000	0.000
17	A	18	ILE	0	-0.046	-0.016	12.348	0.011	0.011	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.052	-0.025	16.007	-0.001	-0.001	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.086	-0.035	12.093	-0.029	-0.029	0.000	0.000	0.000	0.000
20	A	21	GLU	-1	-0.788	-0.864	11.159	0.235	0.235	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.941	-0.970	15.176	-0.013	-0.013	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.877	-0.929	17.341	0.080	0.080	0.000	0.000	0.000	0.000
23	A	24	ARG	1	0.718	0.825	9.687	-0.414	-0.414	0.000	0.000	0.000	0.000
24	A	25	VAL	0	-0.070	-0.032	16.848	-0.027	-0.027	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.036	0.015	13.027	0.054	0.054	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.023	-0.017	14.262	-0.041	-0.041	0.000	0.000	0.000	0.000
27	A	28	ILE	0	0.012	0.000	13.476	0.063	0.063	0.000	0.000	0.000	0.000
28	A	29	ARG	1	0.727	0.821	14.490	-0.375	-0.375	0.000	0.000	0.000	0.000
29	A	30	PHE	0	0.018	-0.004	16.000	0.015	0.015	0.000	0.000	0.000	0.000
30	A	31	GLY	0	0.065	0.013	18.767	-0.018	-0.018	0.000	0.000	0.000	0.000
31	A	32	HIS	0	0.013	0.004	19.286	0.015	0.015	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.756	-0.871	14.937	0.307	0.307	0.000	0.000	0.000	0.000
33	A	34	TRP	0	-0.066	-0.025	18.009	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	35	ASP	-1	-0.736	-0.853	21.295	0.141	0.141	0.000	0.000	0.000	0.000
35	A	36	PRO	0	0.003	-0.012	22.037	0.016	0.016	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.074	-0.064	23.348	0.006	0.006	0.000	0.000	0.000	0.000
37	A	38	CYS	0	-0.050	-0.012	18.526	0.028	0.028	0.000	0.000	0.000	0.000
38	A	39	MET	0	-0.040	0.005	18.404	0.024	0.024	0.000	0.000	0.000	0.000
39	A	40	LYS	1	0.883	0.918	18.842	-0.131	-0.131	0.000	0.000	0.000	0.000
40	A	41	MET	0	-0.034	-0.002	17.920	0.023	0.023	0.000	0.000	0.000	0.000
41	A	42	ASP	-1	-0.746	-0.857	14.305	0.418	0.418	0.000	0.000	0.000	0.000
42	A	43	GLU	-1	-0.949	-0.968	14.748	0.278	0.278	0.000	0.000	0.000	0.000
43	A	44	VAL	0	-0.013	-0.009	16.712	0.036	0.036	0.000	0.000	0.000	0.000
44	A	45	LEU	0	0.018	0.008	13.916	0.025	0.025	0.000	0.000	0.000	0.000
45	A	46	TYR	0	0.035	0.013	9.714	0.103	0.103	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.092	-0.047	12.954	0.040	0.040	0.000	0.000	0.000	0.000
47	A	48	ILE	0	-0.069	-0.043	15.099	-0.046	-0.046	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.068	0.039	10.276	-0.023	-0.023	0.000	0.000	0.000	0.000
49	A	50	GLU	-1	-0.800	-0.898	9.953	1.238	1.238	0.000	0.000	0.000	0.000
50	A	51	LYS	1	0.820	0.911	13.044	-0.332	-0.332	0.000	0.000	0.000	0.000
51	A	52	VAL	0	0.019	0.008	13.975	-0.060	-0.060	0.000	0.000	0.000	0.000
52	A	53	LYS	1	0.877	0.936	8.818	-1.415	-1.415	0.000	0.000	0.000	0.000
53	A	54	ASN	0	-0.041	-0.024	13.096	-0.001	-0.001	0.000	0.000	0.000	0.000
54	A	55	PHE	0	-0.030	-0.019	16.034	-0.044	-0.044	0.000	0.000	0.000	0.000
55	A	56	ALA	0	-0.014	-0.010	14.880	-0.050	-0.050	0.000	0.000	0.000	0.000
56	A	57	VAL	0	-0.019	0.006	8.846	0.094	0.094	0.000	0.000	0.000	0.000
57	A	58	ILE	0	-0.012	-0.013	9.865	-0.109	-0.109	0.000	0.000	0.000	0.000
58	A	59	TYR	0	0.005	0.006	6.716	0.169	0.169	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.026	-0.009	10.316	-0.102	-0.102	0.000	0.000	0.000	0.000
60	A	61	VAL	0	0.038	0.008	11.893	0.020	0.020	0.000	0.000	0.000	0.000
61	A	62	ASP	-1	-0.732	-0.848	14.620	0.154	0.154	0.000	0.000	0.000	0.000
62	A	63	ILE	0	-0.030	-0.023	16.972	-0.014	-0.014	0.000	0.000	0.000	0.000
63	A	64	THR	0	-0.044	-0.021	20.084	-0.026	-0.026	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.918	-0.950	13.994	0.241	0.241	0.000	0.000	0.000	0.000
65	A	66	VAL	0	-0.070	-0.022	14.925	-0.019	-0.019	0.000	0.000	0.000	0.000
66	A	67	PRO	0	0.008	-0.003	18.356	0.003	0.003	0.000	0.000	0.000	0.000
67	A	68	ASP	-1	-0.893	-0.958	19.564	0.073	0.073	0.000	0.000	0.000	0.000
68	A	69	PHE	0	0.011	-0.005	17.414	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	70	ASN	0	0.011	0.033	22.363	0.011	0.011	0.000	0.000	0.000	0.000
70	A	71	LYS	1	0.806	0.871	24.684	-0.062	-0.062	0.000	0.000	0.000	0.000
71	A	72	MET	0	-0.083	-0.040	22.249	-0.005	-0.005	0.000	0.000	0.000	0.000
72	A	73	TYR	0	0.006	-0.014	21.492	0.007	0.007	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.822	-0.893	26.540	0.065	0.065	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.036	-0.014	24.524	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	76	TYR	0	-0.013	-0.017	26.463	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.885	-0.913	25.914	0.098	0.098	0.000	0.000	0.000	0.000
77	A	78	PRO	0	-0.026	-0.017	24.985	0.009	0.009	0.000	0.000	0.000	0.000
78	A	80	THR	0	-0.051	-0.021	21.682	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	81	VAL	0	0.003	-0.002	17.499	0.027	0.027	0.000	0.000	0.000	0.000
80	A	82	MET	0	-0.049	-0.009	18.915	-0.032	-0.032	0.000	0.000	0.000	0.000
81	A	83	PHE	0	0.030	0.005	18.312	0.031	0.031	0.000	0.000	0.000	0.000
82	A	84	PHE	0	0.046	0.020	17.645	-0.032	-0.032	0.000	0.000	0.000	0.000
83	A	85	PHE	0	-0.018	-0.015	18.711	0.018	0.018	0.000	0.000	0.000	0.000
84	A	86	ARG	1	0.848	0.907	19.600	-0.087	-0.087	0.000	0.000	0.000	0.000
85	A	87	ASN	0	0.058	0.026	19.777	-0.009	-0.009	0.000	0.000	0.000	0.000
86	A	88	LYS	1	0.836	0.947	21.136	-0.079	-0.079	0.000	0.000	0.000	0.000
87	A	89	HIS	0	0.019	0.003	22.214	0.003	0.003	0.000	0.000	0.000	0.000
88	A	90	ILE	0	-0.087	-0.050	22.609	-0.012	-0.012	0.000	0.000	0.000	0.000
89	A	91	MET	0	0.018	0.015	24.453	0.008	0.008	0.000	0.000	0.000	0.000
90	A	92	ILE	0	0.000	-0.024	23.452	0.000	0.000	0.000	0.000	0.000	0.000
91	A	93	ASP	-1	-0.835	-0.902	28.046	0.085	0.085	0.000	0.000	0.000	0.000
92	A	94	LEU	0	-0.012	-0.020	27.931	0.006	0.006	0.000	0.000	0.000	0.000
93	A	95	GLY	0	-0.004	-0.002	32.111	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	96	THR	0	-0.006	-0.028	32.729	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	97	GLY	0	0.023	0.023	35.333	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	98	ASN	0	0.006	0.020	28.728	-0.009	-0.009	0.000	0.000	0.000	0.000
97	A	99	ASN	0	-0.035	-0.029	30.530	0.004	0.004	0.000	0.000	0.000	0.000
98	A	100	ASN	0	0.006	-0.002	25.035	-0.009	-0.009	0.000	0.000	0.000	0.000
99	A	101	LYN	0	-0.006	0.019	23.527	0.015	0.015	0.000	0.000	0.000	0.000
100	A	102	ILE	0	0.002	-0.002	22.119	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	103	ASN	0	-0.002	0.001	23.255	0.014	0.014	0.000	0.000	0.000	0.000
102	A	104	TRP	0	0.014	0.020	25.265	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	105	ALA	0	0.027	0.014	23.692	0.015	0.015	0.000	0.000	0.000	0.000
104	A	106	MET	0	-0.031	0.000	23.073	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	107	GLU	-1	-0.793	-0.887	24.016	0.160	0.160	0.000	0.000	0.000	0.000
106	A	108	ASP	-1	-0.902	-0.946	24.785	0.165	0.165	0.000	0.000	0.000	0.000
107	A	109	LYS	1	0.877	0.922	18.725	-0.311	-0.311	0.000	0.000	0.000	0.000
108	A	110	GLN	0	-0.001	-0.010	21.152	0.042	0.042	0.000	0.000	0.000	0.000
109	A	111	GLU	-1	-0.787	-0.896	23.546	0.150	0.150	0.000	0.000	0.000	0.000
110	A	112	MET	0	0.067	0.020	18.640	-0.002	-0.002	0.000	0.000	0.000	0.000
111	A	113	VAL	0	-0.057	-0.022	18.888	0.011	0.011	0.000	0.000	0.000	0.000
112	A	114	ASP	-1	-0.837	-0.905	21.000	0.172	0.172	0.000	0.000	0.000	0.000
113	A	115	ILE	0	-0.030	0.008	22.203	-0.014	-0.014	0.000	0.000	0.000	0.000
114	A	116	ILE	0	0.025	0.009	16.571	-0.012	-0.012	0.000	0.000	0.000	0.000
115	A	117	GLU	-1	-0.870	-0.929	20.457	0.180	0.180	0.000	0.000	0.000	0.000
116	A	118	THR	0	-0.056	-0.048	22.332	-0.023	-0.023	0.000	0.000	0.000	0.000
117	A	119	VAL	0	0.004	0.000	21.473	-0.017	-0.017	0.000	0.000	0.000	0.000
118	A	120	TYR	0	0.020	0.028	20.212	-0.020	-0.020	0.000	0.000	0.000	0.000
119	A	121	ARG	1	0.821	0.886	22.254	-0.163	-0.163	0.000	0.000	0.000	0.000
120	A	122	GLY	0	-0.023	-0.010	25.707	-0.015	-0.015	0.000	0.000	0.000	0.000
121	A	123	ALA	0	0.021	0.006	23.378	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	124	ARG	1	0.908	0.963	23.217	-0.143	-0.143	0.000	0.000	0.000	0.000
123	A	125	LYS	1	0.840	0.932	25.190	-0.098	-0.098	0.000	0.000	0.000	0.000
124	A	126	GLY	0	0.034	0.020	27.988	-0.006	-0.006	0.000	0.000	0.000	0.000
125	A	127	ARG	1	0.889	0.948	28.957	-0.081	-0.081	0.000	0.000	0.000	0.000
126	A	128	GLY	0	0.061	0.020	27.658	0.004	0.004	0.000	0.000	0.000	0.000
127	A	129	LEU	0	0.013	0.031	28.379	0.003	0.003	0.000	0.000	0.000	0.000
128	A	130	VAL	0	-0.066	-0.032	26.303	-0.006	-0.006	0.000	0.000	0.000	0.000
129	A	131	VAL	0	0.021	0.000	29.585	0.000	0.000	0.000	0.000	0.000	0.000
130	A	132	SER	0	-0.008	-0.006	28.128	0.004	0.004	0.000	0.000	0.000	0.000
131	A	133	PRO	0	-0.033	-0.009	30.211	0.002	0.002	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.894	0.940	27.475	-0.137	-0.137	0.000	0.000	0.000	0.000
133	A	135	ASP	-1	-0.859	-0.890	33.260	0.073	0.073	0.000	0.000	0.000	0.000
134	A	136	TYR	0	-0.067	-0.035	30.617	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	137	SER	0	-0.098	-0.062	37.675	-0.006	-0.006	0.000	0.000	0.000	0.000

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