FMO DATABASE

FMODB ID: LJ469

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1541940.571579
FMO2-HF: Nuclear repulsion	1481120.87307
FMO2-HF: Total energy	-60819.698509
FMO2-MP2: Total energy	-60998.603266

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.
-9.03	-3.941	4.06	-4.53	-4.619	-0.013

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 : 0.008 / q_NPA : 0.002

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	-0.050	-0.017	3.544	0.436	2.786	-0.004	-1.266	-1.080	0.004
4	A	22	LEU	0	0.012	0.011	5.591	-0.037	-0.037	0.000	0.000	0.000	0.000
5	A	23	PRO	0	0.004	0.002	9.040	0.222	0.222	0.000	0.000	0.000	0.000
6	A	24	ARG	1	0.839	0.902	11.779	0.138	0.138	0.000	0.000	0.000	0.000
7	A	25	LEU	0	0.021	0.028	14.760	-0.011	-0.011	0.000	0.000	0.000	0.000
8	A	26	PRO	0	0.008	0.004	17.368	0.042	0.042	0.000	0.000	0.000	0.000
9	A	27	SER	0	-0.019	-0.017	20.691	0.018	0.018	0.000	0.000	0.000	0.000
10	A	28	GLU	-1	-0.760	-0.891	23.000	-0.200	-0.200	0.000	0.000	0.000	0.000
11	A	29	PRO	0	-0.021	-0.018	26.272	0.010	0.010	0.000	0.000	0.000	0.000
12	A	30	GLY	0	0.001	0.003	29.712	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	31	MET	0	-0.073	-0.001	25.295	0.003	0.003	0.000	0.000	0.000	0.000
14	A	32	THR	0	-0.018	-0.043	22.967	0.009	0.009	0.000	0.000	0.000	0.000
15	A	33	LEU	0	-0.048	-0.024	18.502	-0.021	-0.021	0.000	0.000	0.000	0.000
16	A	34	LEU	0	0.008	0.008	17.465	0.028	0.028	0.000	0.000	0.000	0.000
17	A	35	THR	0	-0.032	-0.035	14.007	-0.036	-0.036	0.000	0.000	0.000	0.000
18	A	36	ILE	0	-0.030	-0.027	13.765	0.030	0.030	0.000	0.000	0.000	0.000
19	A	37	ARG	1	0.923	0.964	12.874	-0.264	-0.264	0.000	0.000	0.000	0.000
20	A	38	ILE	0	-0.012	-0.010	9.562	-0.031	-0.031	0.000	0.000	0.000	0.000
21	A	39	GLU	-1	-0.911	-0.961	12.756	0.410	0.410	0.000	0.000	0.000	0.000
22	A	40	LYS	1	0.936	0.970	14.385	-0.223	-0.223	0.000	0.000	0.000	0.000
23	A	41	ILE	0	0.000	0.008	13.840	-0.070	-0.070	0.000	0.000	0.000	0.000
24	A	42	GLY	0	0.011	0.003	16.579	0.038	0.038	0.000	0.000	0.000	0.000
25	A	43	LEU	0	-0.032	-0.032	16.107	-0.029	-0.029	0.000	0.000	0.000	0.000
26	A	44	LYS	1	0.946	0.973	20.503	-0.168	-0.168	0.000	0.000	0.000	0.000
27	A	45	ASP	-1	-0.773	-0.868	20.861	0.314	0.314	0.000	0.000	0.000	0.000
28	A	46	ALA	0	0.004	0.021	18.089	0.031	0.031	0.000	0.000	0.000	0.000
29	A	47	GLY	0	0.035	0.016	17.479	0.073	0.073	0.000	0.000	0.000	0.000
30	A	48	GLN	0	-0.046	-0.027	19.000	0.010	0.010	0.000	0.000	0.000	0.000
31	A	49	CYS	0	-0.077	-0.007	14.677	-0.040	-0.040	0.000	0.000	0.000	0.000
32	A	50	ILE	0	0.017	0.007	13.162	0.057	0.057	0.000	0.000	0.000	0.000
33	A	51	ASP	-1	-0.873	-0.932	8.825	1.374	1.374	0.000	0.000	0.000	0.000
34	A	52	PRO	0	-0.043	-0.021	9.181	-0.005	-0.005	0.000	0.000	0.000	0.000
35	A	53	TYR	0	-0.011	-0.009	5.301	0.523	0.523	0.000	0.000	0.000	0.000
36	A	54	ILE	0	0.001	-0.007	6.630	-0.480	-0.480	0.000	0.000	0.000	0.000
37	A	55	THR	0	-0.015	0.000	6.403	0.041	0.041	0.000	0.000	0.000	0.000
38	A	56	VAL	0	0.014	0.002	8.347	0.157	0.157	0.000	0.000	0.000	0.000
39	A	57	SER	0	-0.018	-0.004	10.314	-0.168	-0.168	0.000	0.000	0.000	0.000
40	A	58	VAL	0	0.054	0.021	13.085	0.084	0.084	0.000	0.000	0.000	0.000
41	A	59	LYS	1	0.785	0.910	15.312	0.349	0.349	0.000	0.000	0.000	0.000
42	A	60	ASP	-1	-0.735	-0.868	19.484	-0.154	-0.154	0.000	0.000	0.000	0.000
43	A	61	LEU	0	0.042	0.020	23.169	0.007	0.007	0.000	0.000	0.000	0.000
44	A	62	ASN	0	-0.130	-0.071	25.648	0.023	0.023	0.000	0.000	0.000	0.000
45	A	63	GLY	0	0.027	0.018	21.629	0.004	0.004	0.000	0.000	0.000	0.000
46	A	64	ILE	0	-0.017	-0.010	20.590	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	65	ASP	-1	-0.807	-0.895	15.306	-0.446	-0.446	0.000	0.000	0.000	0.000
48	A	66	LEU	0	0.003	0.008	18.151	0.008	0.008	0.000	0.000	0.000	0.000
49	A	67	THR	0	-0.027	-0.017	14.050	0.043	0.043	0.000	0.000	0.000	0.000
50	A	68	PRO	0	0.001	0.012	11.897	0.014	0.014	0.000	0.000	0.000	0.000
51	A	69	VAL	0	-0.003	-0.007	9.008	0.064	0.064	0.000	0.000	0.000	0.000
52	A	70	GLN	0	0.010	0.018	6.630	-0.301	-0.301	0.000	0.000	0.000	0.000
53	A	71	ASP	-1	-0.791	-0.877	3.395	-1.354	-1.117	0.019	-0.111	-0.145	0.000
54	A	72	THR	0	0.025	0.017	2.458	-4.072	-3.076	2.234	-1.856	-1.374	-0.020
55	A	73	PRO	0	0.029	0.002	2.429	-0.109	1.678	1.753	-1.605	-1.935	0.003
56	A	74	VAL	0	-0.030	-0.015	3.499	-3.788	-4.069	0.058	0.308	-0.085	0.000
57	A	75	ALA	0	-0.025	-0.016	6.571	-0.205	-0.205	0.000	0.000	0.000	0.000
58	A	76	SER	0	0.013	0.022	9.619	-0.107	-0.107	0.000	0.000	0.000	0.000
59	A	77	ARG	1	0.910	0.949	11.682	-0.726	-0.726	0.000	0.000	0.000	0.000
60	A	78	LYS	1	0.823	0.915	14.423	-0.744	-0.744	0.000	0.000	0.000	0.000
61	A	79	GLU	-1	-0.823	-0.904	16.589	0.410	0.410	0.000	0.000	0.000	0.000
62	A	80	ASP	-1	-0.864	-0.932	19.977	0.363	0.363	0.000	0.000	0.000	0.000
63	A	81	THR	0	-0.024	-0.031	21.864	-0.009	-0.009	0.000	0.000	0.000	0.000
64	A	82	TYR	0	-0.010	-0.026	18.678	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	83	VAL	0	-0.034	-0.001	12.474	0.029	0.029	0.000	0.000	0.000	0.000
66	A	84	HIS	0	-0.031	-0.045	14.371	-0.035	-0.035	0.000	0.000	0.000	0.000
67	A	85	PHE	0	-0.031	-0.029	7.989	0.088	0.088	0.000	0.000	0.000	0.000
68	A	86	ASN	0	-0.021	-0.011	10.944	0.022	0.022	0.000	0.000	0.000	0.000
69	A	87	VAL	0	0.013	0.015	6.571	0.048	0.048	0.000	0.000	0.000	0.000
70	A	88	ASP	-1	-0.827	-0.902	10.033	0.150	0.150	0.000	0.000	0.000	0.000
71	A	89	ILE	0	-0.014	-0.005	8.282	-0.068	-0.068	0.000	0.000	0.000	0.000
72	A	90	GLU	-1	-0.722	-0.816	10.612	-0.103	-0.103	0.000	0.000	0.000	0.000
73	A	91	LEU	0	0.028	0.008	12.387	-0.126	-0.126	0.000	0.000	0.000	0.000
74	A	92	GLN	0	-0.032	-0.022	12.140	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	93	LYS	1	0.868	0.909	15.182	0.310	0.310	0.000	0.000	0.000	0.000
76	A	94	HIS	0	0.004	0.017	18.960	0.020	0.020	0.000	0.000	0.000	0.000
77	A	95	VAL	0	0.110	0.046	21.205	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	96	GLU	-1	-0.783	-0.857	22.897	-0.123	-0.123	0.000	0.000	0.000	0.000
79	A	97	LYS	1	0.740	0.847	23.655	0.191	0.191	0.000	0.000	0.000	0.000
80	A	98	LEU	0	-0.070	-0.012	19.575	-0.022	-0.022	0.000	0.000	0.000	0.000
81	A	99	THR	0	0.000	-0.011	23.617	0.020	0.020	0.000	0.000	0.000	0.000
82	A	100	LYS	1	1.024	0.983	25.439	0.079	0.079	0.000	0.000	0.000	0.000
83	A	101	GLY	0	0.006	0.014	26.652	0.009	0.009	0.000	0.000	0.000	0.000
84	A	102	ALA	0	-0.018	-0.003	21.310	0.000	0.000	0.000	0.000	0.000	0.000
85	A	103	ALA	0	0.024	0.019	20.761	0.021	0.021	0.000	0.000	0.000	0.000
86	A	104	ILE	0	-0.018	-0.011	14.996	-0.043	-0.043	0.000	0.000	0.000	0.000
87	A	105	PHE	0	-0.035	-0.020	15.228	0.050	0.050	0.000	0.000	0.000	0.000
88	A	106	PHE	0	0.052	0.019	12.053	-0.049	-0.049	0.000	0.000	0.000	0.000
89	A	107	GLU	-1	-0.809	-0.884	11.626	-0.157	-0.157	0.000	0.000	0.000	0.000
90	A	108	PHE	0	0.050	0.015	10.819	0.055	0.055	0.000	0.000	0.000	0.000
91	A	109	LYS	1	0.833	0.898	9.382	0.158	0.158	0.000	0.000	0.000	0.000
92	A	110	HIS	0	0.018	0.003	10.474	0.240	0.240	0.000	0.000	0.000	0.000
93	A	111	TYR	0	0.063	0.034	11.244	-0.194	-0.194	0.000	0.000	0.000	0.000
94	A	112	LYS	1	0.860	0.922	12.903	-0.239	-0.239	0.000	0.000	0.000	0.000
95	A	113	PRO	0	0.059	0.015	16.636	-0.045	-0.045	0.000	0.000	0.000	0.000
96	A	114	LYS	1	0.962	0.978	18.149	-0.202	-0.202	0.000	0.000	0.000	0.000
97	A	115	LYS	1	0.913	0.950	19.494	-0.092	-0.092	0.000	0.000	0.000	0.000
98	A	116	ARG	1	0.994	1.009	16.889	-0.195	-0.195	0.000	0.000	0.000	0.000
99	A	117	PHE	0	0.057	0.027	14.264	-0.028	-0.028	0.000	0.000	0.000	0.000
100	A	118	THR	0	0.056	0.047	9.249	0.106	0.106	0.000	0.000	0.000	0.000
101	A	119	SER	0	-0.094	-0.030	12.432	-0.101	-0.101	0.000	0.000	0.000	0.000
102	A	120	THR	0	0.072	0.026	13.531	0.080	0.080	0.000	0.000	0.000	0.000
103	A	121	LYS	1	0.714	0.837	14.888	-0.390	-0.390	0.000	0.000	0.000	0.000
104	A	122	CYS	0	-0.055	-0.039	16.112	-0.011	-0.011	0.000	0.000	0.000	0.000
105	A	123	PHE	0	0.048	0.031	15.654	0.016	0.016	0.000	0.000	0.000	0.000
106	A	124	ALA	0	0.048	0.038	16.392	0.010	0.010	0.000	0.000	0.000	0.000
107	A	125	PHE	0	-0.028	-0.026	16.873	-0.019	-0.019	0.000	0.000	0.000	0.000
108	A	126	MET	0	0.053	0.048	17.764	0.012	0.012	0.000	0.000	0.000	0.000
109	A	127	GLU	-1	-0.816	-0.910	20.654	-0.087	-0.087	0.000	0.000	0.000	0.000
110	A	128	MET	0	0.000	0.015	20.534	0.003	0.003	0.000	0.000	0.000	0.000
111	A	129	ASP	-1	-0.921	-0.951	24.298	-0.028	-0.028	0.000	0.000	0.000	0.000
112	A	130	GLU	-1	-0.885	-0.973	23.379	0.025	0.025	0.000	0.000	0.000	0.000
113	A	131	ILE	0	-0.040	-0.024	20.829	0.012	0.012	0.000	0.000	0.000	0.000
114	A	132	LYS	1	0.914	0.976	23.289	-0.023	-0.023	0.000	0.000	0.000	0.000
115	A	133	PRO	0	-0.024	-0.003	23.243	0.009	0.009	0.000	0.000	0.000	0.000
116	A	134	GLY	0	0.031	0.024	23.072	0.001	0.001	0.000	0.000	0.000	0.000
117	A	135	PRO	0	-0.023	-0.027	21.659	0.000	0.000	0.000	0.000	0.000	0.000
118	A	136	ILE	0	-0.007	0.002	20.032	-0.017	-0.017	0.000	0.000	0.000	0.000
119	A	137	VAL	0	-0.048	-0.020	20.610	0.026	0.026	0.000	0.000	0.000	0.000
120	A	138	ILE	0	0.027	0.028	18.014	-0.016	-0.016	0.000	0.000	0.000	0.000
121	A	139	GLU	-1	-0.837	-0.890	20.767	0.106	0.106	0.000	0.000	0.000	0.000
122	A	140	LEU	0	-0.008	-0.013	17.814	0.000	0.000	0.000	0.000	0.000	0.000
123	A	141	TYR	0	-0.012	-0.056	20.378	-0.005	-0.005	0.000	0.000	0.000	0.000
124	A	142	LYS	1	0.853	0.925	20.340	-0.078	-0.078	0.000	0.000	0.000	0.000
125	A	143	LYS	1	0.928	1.019	18.829	-0.108	-0.108	0.000	0.000	0.000	0.000
126	A	144	PRO	0	-0.056	-0.056	19.928	0.010	0.010	0.000	0.000	0.000	0.000
127	A	145	THR	0	0.015	-0.043	16.096	0.027	0.027	0.000	0.000	0.000	0.000
128	A	146	ASP	-1	-0.781	-0.863	19.307	-0.087	-0.087	0.000	0.000	0.000	0.000
129	A	147	PHE	0	0.046	0.000	15.305	0.004	0.004	0.000	0.000	0.000	0.000
130	A	148	LYS	1	0.835	0.919	20.820	0.122	0.122	0.000	0.000	0.000	0.000
131	A	149	ARG	1	0.728	0.842	22.165	0.102	0.102	0.000	0.000	0.000	0.000
132	A	150	LYS	1	0.894	0.948	24.383	0.079	0.079	0.000	0.000	0.000	0.000
133	A	151	LYS	1	0.922	0.964	26.965	0.024	0.024	0.000	0.000	0.000	0.000
134	A	152	LEU	0	0.031	0.027	23.752	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	153	GLN	0	-0.029	-0.017	25.562	0.009	0.009	0.000	0.000	0.000	0.000
136	A	154	LEU	0	0.053	0.037	25.140	0.009	0.009	0.000	0.000	0.000	0.000
137	A	155	LEU	0	-0.019	-0.021	20.277	0.000	0.000	0.000	0.000	0.000	0.000
138	A	156	THR	0	-0.045	-0.051	23.981	0.001	0.001	0.000	0.000	0.000	0.000
139	A	157	LYS	1	0.997	1.006	26.530	-0.075	-0.075	0.000	0.000	0.000	0.000
140	A	158	LYS	1	0.933	0.975	26.847	-0.171	-0.171	0.000	0.000	0.000	0.000
141	A	159	PRO	0	0.057	0.033	26.419	0.003	0.003	0.000	0.000	0.000	0.000
142	A	160	LEU	0	-0.091	-0.035	22.285	0.013	0.013	0.000	0.000	0.000	0.000
143	A	161	TYR	0	0.048	0.026	21.214	-0.008	-0.008	0.000	0.000	0.000	0.000
144	A	162	LEU	0	0.018	0.019	13.970	0.059	0.059	0.000	0.000	0.000	0.000
145	A	163	HIS	0	-0.033	-0.025	17.138	-0.037	-0.037	0.000	0.000	0.000	0.000
146	A	164	LEU	0	0.030	0.021	14.512	0.058	0.058	0.000	0.000	0.000	0.000
147	A	165	HIS	0	0.070	0.036	17.104	-0.020	-0.020	0.000	0.000	0.000	0.000
148	A	166	GLN	0	-0.026	-0.004	17.442	-0.018	-0.018	0.000	0.000	0.000	0.000
149	A	167	SER	0	-0.012	-0.025	18.472	0.014	0.014	0.000	0.000	0.000	0.000
150	A	168	LEU	0	0.017	0.015	19.776	-0.024	-0.024	0.000	0.000	0.000	0.000
151	A	169	HIS	0	-0.063	-0.042	18.198	0.016	0.016	0.000	0.000	0.000	0.000
152	A	170	LYS	1	1.003	1.010	23.214	0.099	0.099	0.000	0.000	0.000	0.000

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