FMO DATABASE

FMODB ID: 3QR4L

Calculation Name: 2QZ5-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QZ5

Chain ID: A

ChEMBL ID:

UniProt ID: Q8C4Q6

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	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	152
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1541344.743747
FMO2-HF: Nuclear repulsion	1480526.002168
FMO2-HF: Total energy	-60818.741579
FMO2-MP2: Total energy	-60997.677928

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:19:GLY)

Summations of interaction energy for fragment #1(A:19:GLY)

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.
-9.32	-4.441	5.088	-5.105	-4.861	-0.015

Interaction energy analysis for fragmet #1(A:19:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.013 / q_NPA : 0.003

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	21	LEU	0	-0.040	-0.016	3.544	0.329	2.705	-0.006	-1.278	-1.092	0.004
4	A	22	LEU	0	0.016	0.006	5.592	-0.015	-0.015	0.000	0.000	0.000	0.000
5	A	23	PRO	0	-0.006	-0.006	9.038	0.225	0.225	0.000	0.000	0.000	0.000
6	A	24	ARG	1	0.890	0.954	11.777	0.131	0.131	0.000	0.000	0.000	0.000
7	A	25	LEU	0	-0.014	0.019	14.760	-0.010	-0.010	0.000	0.000	0.000	0.000
8	A	26	PRO	0	0.008	0.004	17.367	0.044	0.044	0.000	0.000	0.000	0.000
9	A	27	SER	0	-0.035	-0.023	20.690	0.014	0.014	0.000	0.000	0.000	0.000
10	A	28	GLU	-1	-0.828	-0.944	23.000	-0.186	-0.186	0.000	0.000	0.000	0.000
11	A	29	PRO	0	-0.034	-0.023	26.272	0.011	0.011	0.000	0.000	0.000	0.000
12	A	30	GLY	0	0.003	0.005	29.714	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	31	MET	0	-0.058	-0.004	25.353	0.003	0.003	0.000	0.000	0.000	0.000
14	A	32	THR	0	-0.006	-0.031	22.951	0.010	0.010	0.000	0.000	0.000	0.000
15	A	33	LEU	0	-0.059	-0.029	18.801	-0.022	-0.022	0.000	0.000	0.000	0.000
16	A	34	LEU	0	0.025	0.013	17.353	0.028	0.028	0.000	0.000	0.000	0.000
17	A	35	THR	0	-0.011	-0.003	14.081	-0.039	-0.039	0.000	0.000	0.000	0.000
18	A	36	ILE	0	-0.024	-0.028	13.670	0.029	0.029	0.000	0.000	0.000	0.000
19	A	37	ARG	1	0.980	1.013	12.868	-0.293	-0.293	0.000	0.000	0.000	0.000
20	A	38	ILE	0	-0.008	-0.015	9.426	-0.036	-0.036	0.000	0.000	0.000	0.000
21	A	39	GLU	-1	-0.930	-0.968	12.749	0.411	0.411	0.000	0.000	0.000	0.000
22	A	40	LYS	1	0.976	0.981	14.379	-0.208	-0.208	0.000	0.000	0.000	0.000
23	A	41	ILE	0	0.003	0.011	13.893	-0.071	-0.071	0.000	0.000	0.000	0.000
24	A	42	GLY	0	0.026	0.006	16.576	0.038	0.038	0.000	0.000	0.000	0.000
25	A	43	LEU	0	-0.056	-0.042	15.937	-0.031	-0.031	0.000	0.000	0.000	0.000
26	A	44	LYS	1	0.943	0.975	20.502	-0.146	-0.146	0.000	0.000	0.000	0.000
27	A	45	ASP	-1	-0.779	-0.880	20.994	0.277	0.277	0.000	0.000	0.000	0.000
28	A	46	ALA	0	-0.004	0.017	18.083	0.029	0.029	0.000	0.000	0.000	0.000
29	A	47	GLY	0	0.020	0.009	17.466	0.070	0.070	0.000	0.000	0.000	0.000
30	A	48	GLN	0	-0.068	-0.048	18.902	0.008	0.008	0.000	0.000	0.000	0.000
31	A	49	CYS	0	-0.092	-0.024	14.575	-0.032	-0.032	0.000	0.000	0.000	0.000
32	A	50	ILE	0	-0.010	-0.016	13.054	0.062	0.062	0.000	0.000	0.000	0.000
33	A	51	ASP	-1	-0.896	-0.947	8.758	1.281	1.281	0.000	0.000	0.000	0.000
34	A	52	PRO	0	-0.041	-0.022	9.092	-0.025	-0.025	0.000	0.000	0.000	0.000
35	A	53	TYR	0	0.000	-0.003	5.456	0.331	0.331	0.000	0.000	0.000	0.000
36	A	54	ILE	0	0.001	-0.007	6.621	-0.440	-0.440	0.000	0.000	0.000	0.000
37	A	55	THR	0	-0.029	-0.010	6.404	-0.004	-0.004	0.000	0.000	0.000	0.000
38	A	56	VAL	0	0.008	-0.005	8.352	0.183	0.183	0.000	0.000	0.000	0.000
39	A	57	SER	0	0.000	0.002	10.315	-0.161	-0.161	0.000	0.000	0.000	0.000
40	A	58	VAL	0	0.037	0.014	13.087	0.083	0.083	0.000	0.000	0.000	0.000
41	A	59	LYS	1	0.821	0.945	15.798	0.364	0.364	0.000	0.000	0.000	0.000
42	A	60	ASP	-1	-0.751	-0.866	19.487	-0.186	-0.186	0.000	0.000	0.000	0.000
43	A	61	LEU	0	0.026	0.016	23.172	0.006	0.006	0.000	0.000	0.000	0.000
44	A	62	ASN	0	-0.072	-0.073	25.434	0.027	0.027	0.000	0.000	0.000	0.000
45	A	63	GLY	0	0.005	-0.009	21.634	0.004	0.004	0.000	0.000	0.000	0.000
46	A	64	ILE	0	-0.027	-0.014	20.577	-0.023	-0.023	0.000	0.000	0.000	0.000
47	A	65	ASP	-1	-0.869	-0.937	15.391	-0.494	-0.494	0.000	0.000	0.000	0.000
48	A	66	LEU	0	-0.018	-0.009	18.163	0.012	0.012	0.000	0.000	0.000	0.000
49	A	67	THR	0	-0.036	-0.037	14.062	0.011	0.011	0.000	0.000	0.000	0.000
50	A	68	PRO	0	-0.017	0.009	11.949	0.006	0.006	0.000	0.000	0.000	0.000
51	A	69	VAL	0	0.010	0.002	8.842	0.059	0.059	0.000	0.000	0.000	0.000
52	A	70	GLN	0	0.001	0.013	6.615	-0.363	-0.363	0.000	0.000	0.000	0.000
53	A	71	ASP	-1	-0.803	-0.899	3.578	-1.331	-1.056	0.014	-0.118	-0.171	0.000
54	A	72	THR	0	-0.003	0.004	2.457	-4.126	-3.097	2.227	-1.871	-1.385	-0.020
55	A	73	PRO	0	0.030	0.001	2.159	-0.334	1.151	2.793	-2.148	-2.130	0.001
56	A	74	VAL	0	-0.024	-0.011	3.493	-3.756	-4.042	0.060	0.310	-0.083	0.000
57	A	75	ALA	0	-0.025	-0.013	6.571	-0.159	-0.159	0.000	0.000	0.000	0.000
58	A	76	SER	0	0.019	0.023	9.615	0.008	0.008	0.000	0.000	0.000	0.000
59	A	77	ARG	1	0.953	0.976	11.694	-0.756	-0.756	0.000	0.000	0.000	0.000
60	A	78	LYS	1	0.902	0.978	14.259	-0.747	-0.747	0.000	0.000	0.000	0.000
61	A	79	GLU	-1	-0.906	-0.966	16.586	0.367	0.367	0.000	0.000	0.000	0.000
62	A	80	ASP	-1	-0.869	-0.935	19.974	0.349	0.349	0.000	0.000	0.000	0.000
63	A	81	THR	0	-0.020	-0.023	21.904	-0.009	-0.009	0.000	0.000	0.000	0.000
64	A	82	TYR	0	-0.011	-0.021	18.692	-0.035	-0.035	0.000	0.000	0.000	0.000
65	A	83	VAL	0	-0.034	0.001	12.337	0.034	0.034	0.000	0.000	0.000	0.000
66	A	84	HIS	0	-0.007	-0.024	14.366	-0.043	-0.043	0.000	0.000	0.000	0.000
67	A	85	PHE	0	-0.019	-0.025	7.931	0.092	0.092	0.000	0.000	0.000	0.000
68	A	86	ASN	0	-0.033	-0.016	10.958	0.026	0.026	0.000	0.000	0.000	0.000
69	A	87	VAL	0	0.001	0.009	6.625	0.060	0.060	0.000	0.000	0.000	0.000
70	A	88	ASP	-1	-0.859	-0.938	9.996	0.137	0.137	0.000	0.000	0.000	0.000
71	A	89	ILE	0	-0.034	-0.012	8.543	-0.065	-0.065	0.000	0.000	0.000	0.000
72	A	90	GLU	-1	-0.784	-0.888	10.606	-0.102	-0.102	0.000	0.000	0.000	0.000
73	A	91	LEU	0	0.048	0.020	12.384	-0.135	-0.135	0.000	0.000	0.000	0.000
74	A	92	GLN	0	-0.024	-0.020	11.785	0.019	0.019	0.000	0.000	0.000	0.000
75	A	93	LYS	1	0.897	0.925	15.180	0.310	0.310	0.000	0.000	0.000	0.000
76	A	94	HIS	0	0.016	0.022	18.959	0.025	0.025	0.000	0.000	0.000	0.000
77	A	95	VAL	0	0.108	0.049	21.323	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	96	GLU	-1	-0.794	-0.873	22.895	-0.130	-0.130	0.000	0.000	0.000	0.000
79	A	97	LYS	1	0.820	0.909	23.695	0.205	0.205	0.000	0.000	0.000	0.000
80	A	98	LEU	0	-0.073	-0.015	19.498	-0.023	-0.023	0.000	0.000	0.000	0.000
81	A	99	THR	0	-0.006	-0.011	23.616	0.023	0.023	0.000	0.000	0.000	0.000
82	A	100	LYS	1	1.027	0.985	25.439	0.085	0.085	0.000	0.000	0.000	0.000
83	A	101	GLY	0	0.018	-0.001	26.653	0.009	0.009	0.000	0.000	0.000	0.000
84	A	102	ALA	0	-0.016	-0.008	21.263	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	103	ALA	0	0.022	0.016	20.724	0.023	0.023	0.000	0.000	0.000	0.000
86	A	104	ILE	0	-0.024	-0.011	14.996	-0.046	-0.046	0.000	0.000	0.000	0.000
87	A	105	PHE	0	-0.029	-0.018	15.294	0.051	0.051	0.000	0.000	0.000	0.000
88	A	106	PHE	0	0.044	0.021	11.934	-0.055	-0.055	0.000	0.000	0.000	0.000
89	A	107	GLU	-1	-0.849	-0.907	11.679	-0.199	-0.199	0.000	0.000	0.000	0.000
90	A	108	PHE	0	0.054	0.021	10.821	0.036	0.036	0.000	0.000	0.000	0.000
91	A	109	LYS	1	0.929	0.959	8.969	0.364	0.364	0.000	0.000	0.000	0.000
92	A	110	HIS	0	0.020	0.007	10.383	0.225	0.225	0.000	0.000	0.000	0.000
93	A	111	TYR	0	0.057	0.031	11.190	-0.196	-0.196	0.000	0.000	0.000	0.000
94	A	112	LYS	1	0.870	0.925	12.837	-0.176	-0.176	0.000	0.000	0.000	0.000
95	A	113	PRO	0	0.050	0.011	16.574	-0.045	-0.045	0.000	0.000	0.000	0.000
96	A	114	LYS	1	0.971	0.983	18.092	-0.187	-0.187	0.000	0.000	0.000	0.000
97	A	115	LYS	1	0.910	0.950	19.343	-0.074	-0.074	0.000	0.000	0.000	0.000
98	A	116	ARG	1	1.006	1.016	16.871	-0.170	-0.170	0.000	0.000	0.000	0.000
99	A	117	PHE	0	0.061	0.025	14.246	-0.027	-0.027	0.000	0.000	0.000	0.000
100	A	118	THR	0	0.042	0.046	9.303	0.123	0.123	0.000	0.000	0.000	0.000
101	A	119	SER	0	-0.112	-0.047	12.385	-0.093	-0.093	0.000	0.000	0.000	0.000
102	A	120	THR	0	0.074	0.033	13.461	0.071	0.071	0.000	0.000	0.000	0.000
103	A	121	LYS	1	0.743	0.850	14.822	-0.310	-0.310	0.000	0.000	0.000	0.000
104	A	122	CYS	0	-0.052	-0.019	16.115	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	123	PHE	0	0.051	0.033	15.657	0.010	0.010	0.000	0.000	0.000	0.000
106	A	124	ALA	0	0.052	0.034	16.396	0.015	0.015	0.000	0.000	0.000	0.000
107	A	125	PHE	0	-0.039	-0.025	16.874	-0.023	-0.023	0.000	0.000	0.000	0.000
108	A	126	MET	0	0.041	0.040	17.274	0.016	0.016	0.000	0.000	0.000	0.000
109	A	127	GLU	-1	-0.842	-0.936	20.653	-0.092	-0.092	0.000	0.000	0.000	0.000
110	A	128	MET	0	-0.016	0.014	20.960	0.001	0.001	0.000	0.000	0.000	0.000
111	A	129	ASP	-1	-0.927	-0.953	24.297	-0.037	-0.037	0.000	0.000	0.000	0.000
112	A	130	GLU	-1	-0.880	-0.967	23.396	0.011	0.011	0.000	0.000	0.000	0.000
113	A	131	ILE	0	-0.048	-0.032	20.629	0.011	0.011	0.000	0.000	0.000	0.000
114	A	132	LYS	1	0.924	0.972	23.286	-0.014	-0.014	0.000	0.000	0.000	0.000
115	A	133	PRO	0	-0.030	-0.004	23.246	0.008	0.008	0.000	0.000	0.000	0.000
116	A	134	GLY	0	0.028	0.019	23.052	0.001	0.001	0.000	0.000	0.000	0.000
117	A	135	PRO	0	-0.029	-0.029	21.653	-0.001	-0.001	0.000	0.000	0.000	0.000
118	A	136	ILE	0	0.016	0.011	20.068	-0.017	-0.017	0.000	0.000	0.000	0.000
119	A	137	VAL	0	-0.052	-0.019	20.605	0.024	0.024	0.000	0.000	0.000	0.000
120	A	138	ILE	0	0.035	0.029	18.193	-0.016	-0.016	0.000	0.000	0.000	0.000
121	A	139	GLU	-1	-0.830	-0.903	20.765	0.090	0.090	0.000	0.000	0.000	0.000
122	A	140	LEU	0	-0.012	-0.018	17.728	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	141	TYR	0	-0.004	-0.039	20.385	-0.002	-0.002	0.000	0.000	0.000	0.000
124	A	142	LYS	1	0.858	0.929	20.343	-0.068	-0.068	0.000	0.000	0.000	0.000
125	A	143	LYS	1	0.930	1.019	18.894	-0.092	-0.092	0.000	0.000	0.000	0.000
126	A	144	PRO	0	-0.073	-0.064	19.932	0.012	0.012	0.000	0.000	0.000	0.000
127	A	145	THR	0	0.018	-0.048	16.108	0.030	0.030	0.000	0.000	0.000	0.000
128	A	146	ASP	-1	-0.792	-0.871	19.312	-0.105	-0.105	0.000	0.000	0.000	0.000
129	A	147	PHE	0	0.036	-0.004	15.360	0.005	0.005	0.000	0.000	0.000	0.000
130	A	148	LYS	1	0.836	0.966	20.824	0.134	0.134	0.000	0.000	0.000	0.000
131	A	149	ARG	1	0.757	0.883	22.506	0.116	0.116	0.000	0.000	0.000	0.000
132	A	150	LYS	1	0.939	0.970	24.387	0.088	0.088	0.000	0.000	0.000	0.000
133	A	151	LYS	1	0.926	0.963	26.975	0.036	0.036	0.000	0.000	0.000	0.000
134	A	152	LEU	0	0.028	0.023	23.942	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	153	GLN	0	-0.013	-0.003	25.560	0.011	0.011	0.000	0.000	0.000	0.000
136	A	154	LEU	0	0.046	0.033	25.143	0.007	0.007	0.000	0.000	0.000	0.000
137	A	155	LEU	0	-0.024	-0.027	20.319	0.001	0.001	0.000	0.000	0.000	0.000
138	A	156	THR	0	-0.066	-0.059	24.186	0.002	0.002	0.000	0.000	0.000	0.000
139	A	157	LYS	1	1.006	1.007	26.530	-0.065	-0.065	0.000	0.000	0.000	0.000
140	A	158	LYS	1	0.922	0.971	26.778	-0.161	-0.161	0.000	0.000	0.000	0.000
141	A	159	PRO	0	0.067	0.040	26.418	0.002	0.002	0.000	0.000	0.000	0.000
142	A	160	LEU	0	-0.081	-0.026	22.218	0.013	0.013	0.000	0.000	0.000	0.000
143	A	161	TYR	0	0.028	0.018	21.196	-0.008	-0.008	0.000	0.000	0.000	0.000
144	A	162	LEU	0	0.017	0.020	13.908	0.058	0.058	0.000	0.000	0.000	0.000
145	A	163	HIS	0	-0.033	-0.028	17.117	-0.036	-0.036	0.000	0.000	0.000	0.000
146	A	164	LEU	0	0.024	0.025	14.285	0.056	0.056	0.000	0.000	0.000	0.000
147	A	165	HIS	0	0.074	0.040	17.097	-0.017	-0.017	0.000	0.000	0.000	0.000
148	A	166	GLN	0	-0.022	0.003	17.436	-0.017	-0.017	0.000	0.000	0.000	0.000
149	A	167	SER	0	-0.016	-0.026	18.696	0.015	0.015	0.000	0.000	0.000	0.000
150	A	168	LEU	0	0.011	0.017	19.770	-0.024	-0.024	0.000	0.000	0.000	0.000
151	A	169	HIS	0	-0.058	-0.038	18.146	0.017	0.017	0.000	0.000	0.000	0.000
152	A	170	LYS	1	1.012	1.019	23.220	0.087	0.087	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:19:GLY)