FMO DATABASE

FMODB ID: LZ489

Calculation Name: 1Q2Y-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1Q2Y

Chain ID: A

ChEMBL ID:

UniProt ID: O31628

Base Structure: X-ray

Registration Date: 2023-09-20

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	140
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1295388.998832
FMO2-HF: Nuclear repulsion	1240014.544043
FMO2-HF: Total energy	-55374.454789
FMO2-MP2: Total energy	-55534.589619

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:1:MET)

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

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.
-17.117	-10.567	14.301	-7.971	-12.879	-0.044

Interaction energy analysis for fragmet #1(A:1:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.023 / q_NPA : -0.016

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	3	ALA	0	0.019	0.028	3.817	-0.989	0.839	-0.025	-0.877	-0.926	0.002
4	A	4	VAL	0	-0.067	-0.050	6.253	0.015	0.015	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.014	0.018	9.831	0.042	0.042	0.000	0.000	0.000	0.000
6	A	6	ALA	0	-0.022	-0.010	13.209	-0.015	-0.015	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.877	0.915	14.503	-0.088	-0.088	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.013	0.001	15.815	-0.002	-0.002	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.807	-0.908	18.009	0.073	0.073	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.796	-0.891	15.652	0.082	0.082	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.044	0.029	12.497	0.004	0.004	0.000	0.000	0.000	0.000
12	A	12	LEU	0	0.000	-0.005	13.891	0.013	0.013	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.806	0.888	16.578	-0.064	-0.064	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.800	-0.877	11.622	0.103	0.103	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.042	-0.035	12.711	0.027	0.027	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.018	-0.017	13.728	0.034	0.034	0.000	0.000	0.000	0.000
17	A	17	TYR	0	-0.026	0.006	13.133	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.038	-0.029	9.825	0.018	0.018	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.703	0.811	12.994	-0.150	-0.150	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.748	-0.871	15.780	0.123	0.123	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-0.912	-0.939	13.456	0.158	0.158	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.030	-0.021	13.655	0.000	0.000	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.020	-0.029	16.483	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	24	VAL	0	0.004	0.019	19.876	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.768	0.896	16.916	-0.151	-0.151	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.844	-0.916	14.924	0.302	0.302	0.000	0.000	0.000	0.000
27	A	27	GLN	0	-0.066	-0.025	18.245	-0.022	-0.022	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.007	-0.015	22.277	-0.014	-0.014	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.024	0.001	23.538	-0.009	-0.009	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.015	0.002	25.202	0.000	0.000	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.004	-0.012	25.394	0.005	0.005	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.883	-0.942	24.207	0.088	0.088	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.939	-0.966	25.647	0.084	0.084	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.924	-0.979	19.818	0.164	0.164	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.016	-0.005	21.622	0.017	0.017	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.751	-0.842	23.755	0.123	0.123	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.911	-0.966	26.106	0.077	0.077	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.041	-0.024	24.942	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.676	-0.788	21.242	0.157	0.157	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.026	-0.017	22.325	0.005	0.005	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.959	-0.961	24.770	0.081	0.081	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.081	-0.047	20.174	0.005	0.005	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.847	-0.912	16.461	0.106	0.106	0.000	0.000	0.000	0.000
44	A	44	HIS	0	-0.011	-0.025	15.323	0.039	0.039	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.056	-0.032	9.211	-0.021	-0.021	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.030	0.027	8.426	0.071	0.071	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.060	-0.039	3.146	-0.724	-0.017	0.145	-0.170	-0.682	-0.001
48	A	48	TYR	0	-0.051	-0.056	4.422	-0.261	0.134	-0.001	-0.119	-0.275	0.000
49	A	49	ASP	-1	-0.921	-0.956	2.160	-7.309	-6.023	6.599	-4.184	-3.701	-0.034
50	A	50	GLY	0	0.007	0.004	3.480	-0.233	-0.057	0.026	-0.016	-0.186	-0.001
51	A	51	GLU	-1	-0.936	-0.979	6.352	0.070	0.070	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.947	0.989	7.524	-0.115	-0.115	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.005	0.020	6.536	-0.194	-0.194	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.042	-0.052	2.971	-0.396	0.110	0.068	-0.116	-0.458	-0.001
55	A	55	GLY	0	-0.012	-0.022	6.301	0.514	0.514	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.020	0.020	7.759	-0.192	-0.192	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.030	0.021	10.912	0.075	0.075	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.741	0.841	13.490	-0.190	-0.190	0.000	0.000	0.000	0.000
59	A	59	TRP	0	-0.029	-0.018	16.356	0.017	0.017	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.940	0.951	18.650	-0.138	-0.138	0.000	0.000	0.000	0.000
61	A	61	MET	0	0.002	0.029	22.185	0.007	0.007	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.829	0.892	24.900	-0.086	-0.086	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.838	-0.912	27.479	0.077	0.077	0.000	0.000	0.000	0.000
64	A	64	GLY	0	0.009	0.010	28.745	-0.002	-0.002	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.032	0.029	25.039	-0.001	-0.001	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.049	0.019	21.424	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.779	0.885	21.641	-0.132	-0.132	0.000	0.000	0.000	0.000
68	A	68	LEU	0	-0.002	-0.001	15.700	0.009	0.009	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.765	-0.877	17.858	0.144	0.144	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.861	0.907	16.899	-0.136	-0.136	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.021	0.013	11.837	0.029	0.029	0.000	0.000	0.000	0.000
72	A	72	CYS	0	-0.049	-0.020	12.700	-0.033	-0.033	0.000	0.000	0.000	0.000
73	A	73	VAL	0	0.005	-0.018	7.718	0.122	0.122	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.050	0.041	8.648	-0.081	-0.081	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.849	0.899	10.524	-0.066	-0.066	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.037	-0.027	9.740	-0.005	-0.005	0.000	0.000	0.000	0.000
77	A	77	HIS	0	0.036	0.026	5.018	-0.258	-0.085	0.000	-0.025	-0.147	0.000
78	A	78	ARG	1	0.897	0.957	6.926	0.125	0.125	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.035	-0.012	8.171	0.093	0.093	0.000	0.000	0.000	0.000
80	A	80	ALA	0	-0.001	0.001	3.684	-0.750	-0.359	0.065	-0.107	-0.349	0.000
81	A	81	GLY	0	-0.002	0.001	2.398	-3.972	-3.046	2.253	-1.218	-1.961	-0.018
82	A	82	VAL	0	0.045	0.011	3.050	0.009	1.050	1.146	-0.466	-1.721	0.003
83	A	83	GLY	0	0.027	0.018	4.505	-1.058	-1.094	0.008	0.051	-0.023	0.000
84	A	84	GLY	0	0.009	-0.004	7.653	-0.231	-0.231	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.051	-0.025	2.471	-0.984	-1.827	4.017	-0.724	-2.450	0.006
86	A	86	ILE	0	0.040	0.030	6.289	-0.473	-0.473	0.000	0.000	0.000	0.000
87	A	87	MET	0	0.011	0.018	8.334	-0.229	-0.229	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.953	0.984	8.120	-0.365	-0.365	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.022	-0.006	8.449	-0.108	-0.108	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.029	0.007	10.507	-0.068	-0.068	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.792	-0.849	13.436	0.178	0.178	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.892	0.956	13.252	-0.084	-0.084	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.008	0.005	14.491	-0.023	-0.023	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.029	0.009	16.161	-0.017	-0.017	0.000	0.000	0.000	0.000
95	A	95	ALA	0	-0.025	-0.021	18.419	-0.015	-0.015	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.927	-0.965	17.531	0.060	0.060	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.044	-0.015	20.400	-0.008	-0.008	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.044	-0.024	22.210	-0.004	-0.004	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.056	-0.029	21.864	-0.002	-0.002	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.035	-0.016	23.943	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.023	0.029	23.912	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	102	PHE	0	-0.030	-0.038	18.948	0.010	0.010	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.003	0.008	22.038	-0.003	-0.003	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.029	-0.016	17.256	0.011	0.011	0.000	0.000	0.000	0.000
105	A	105	ASN	0	0.020	0.021	20.601	-0.026	-0.026	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.004	-0.006	18.904	0.029	0.029	0.000	0.000	0.000	0.000
107	A	107	GLN	0	0.069	0.044	15.651	-0.047	-0.047	0.000	0.000	0.000	0.000
108	A	108	THR	0	0.014	-0.027	20.003	0.015	0.015	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.015	-0.006	19.242	0.012	0.012	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.021	-0.004	15.858	0.005	0.005	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.023	0.008	17.366	0.015	0.015	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.014	-0.019	18.234	-0.003	-0.003	0.000	0.000	0.000	0.000
113	A	113	PHE	0	0.031	0.013	10.210	-0.011	-0.011	0.000	0.000	0.000	0.000
114	A	114	TYR	0	0.082	0.029	14.088	-0.016	-0.016	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.956	1.001	17.173	-0.121	-0.121	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.887	0.962	13.022	-0.122	-0.122	0.000	0.000	0.000	0.000
117	A	117	HIS	0	-0.120	-0.081	11.995	0.014	0.014	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.021	0.011	16.411	0.001	0.001	0.000	0.000	0.000	0.000
119	A	119	TYR	0	-0.050	-0.042	16.874	-0.011	-0.011	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.940	0.957	21.336	-0.083	-0.083	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.009	-0.010	24.699	0.006	0.006	0.000	0.000	0.000	0.000
122	A	122	LEU	0	0.002	0.009	26.204	-0.008	-0.008	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.014	-0.011	28.518	-0.010	-0.010	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.930	-0.963	29.037	0.070	0.070	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.859	0.930	31.024	-0.076	-0.076	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.830	-0.897	27.154	0.112	0.112	0.000	0.000	0.000	0.000
127	A	127	PHE	0	-0.077	-0.038	25.208	-0.010	-0.010	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.005	0.001	27.071	0.008	0.008	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.866	-0.902	23.403	0.160	0.160	0.000	0.000	0.000	0.000
130	A	130	ALA	0	0.097	0.043	22.805	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.027	0.010	24.894	0.001	0.001	0.000	0.000	0.000	0.000
132	A	132	ILE	0	-0.009	-0.006	21.483	-0.004	-0.004	0.000	0.000	0.000	0.000
133	A	133	PRO	0	-0.020	0.003	24.809	0.003	0.003	0.000	0.000	0.000	0.000
134	A	134	HIS	0	-0.040	-0.035	20.689	0.038	0.038	0.000	0.000	0.000	0.000
135	A	135	LEU	0	0.033	0.024	23.356	-0.016	-0.016	0.000	0.000	0.000	0.000
136	A	136	GLN	0	-0.023	-0.011	23.435	0.009	0.009	0.000	0.000	0.000	0.000
137	A	137	MET	0	-0.073	-0.034	21.185	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	138	MET	0	0.018	0.017	23.738	0.003	0.003	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.833	0.907	17.562	-0.176	-0.176	0.000	0.000	0.000	0.000
140	A	140	ASP	-1	-0.907	-0.942	22.873	0.087	0.087	0.000	0.000	0.000	0.000

Top

Graph

Overview

Highlights

Manual

Support

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