FMO DATABASE

FMODB ID: 39RYL

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:

Apendix: None

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	140
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1294752.978451
FMO2-HF: Nuclear repulsion	1239379.345978
FMO2-HF: Total energy	-55373.632472
FMO2-MP2: Total energy	-55533.748577

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.
-16.222	-10.604	14.136	-7.543	-12.214	-0.047

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 : -0.024 / q_NPA : -0.015

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	0.009	0.024	3.817	-1.032	0.760	-0.025	-0.862	-0.904	0.002
4	A	4	VAL	0	-0.058	-0.052	6.239	0.041	0.041	0.000	0.000	0.000	0.000
5	A	5	ILE	0	0.030	0.028	9.822	0.025	0.025	0.000	0.000	0.000	0.000
6	A	6	ALA	0	-0.020	-0.010	13.214	-0.013	-0.013	0.000	0.000	0.000	0.000
7	A	7	LYS	1	0.944	0.963	14.486	-0.121	-0.121	0.000	0.000	0.000	0.000
8	A	8	ASN	0	-0.003	0.015	15.686	-0.009	-0.009	0.000	0.000	0.000	0.000
9	A	9	GLU	-1	-0.822	-0.930	18.003	0.060	0.060	0.000	0.000	0.000	0.000
10	A	10	GLU	-1	-0.845	-0.936	15.574	0.062	0.062	0.000	0.000	0.000	0.000
11	A	11	GLN	0	0.005	0.002	12.297	-0.005	-0.005	0.000	0.000	0.000	0.000
12	A	12	LEU	0	-0.001	-0.008	13.874	0.007	0.007	0.000	0.000	0.000	0.000
13	A	13	LYS	1	0.898	0.961	16.560	-0.048	-0.048	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.806	-0.880	11.622	0.058	0.058	0.000	0.000	0.000	0.000
15	A	15	ALA	0	-0.038	-0.035	12.856	0.009	0.009	0.000	0.000	0.000	0.000
16	A	16	PHE	0	-0.026	-0.019	13.881	0.023	0.023	0.000	0.000	0.000	0.000
17	A	17	TYR	0	0.013	0.041	13.293	-0.007	-0.007	0.000	0.000	0.000	0.000
18	A	18	VAL	0	-0.042	-0.029	10.225	0.001	0.001	0.000	0.000	0.000	0.000
19	A	19	ARG	1	0.744	0.835	13.116	-0.134	-0.134	0.000	0.000	0.000	0.000
20	A	20	GLU	-1	-0.807	-0.908	15.867	0.046	0.046	0.000	0.000	0.000	0.000
21	A	21	GLU	-1	-1.030	-1.015	13.399	0.007	0.007	0.000	0.000	0.000	0.000
22	A	22	VAL	0	-0.018	-0.016	13.762	-0.002	-0.002	0.000	0.000	0.000	0.000
23	A	23	PHE	0	-0.020	-0.027	16.518	-0.008	-0.008	0.000	0.000	0.000	0.000
24	A	24	VAL	0	-0.002	0.015	19.944	-0.010	-0.010	0.000	0.000	0.000	0.000
25	A	25	LYS	1	0.856	0.946	18.059	-0.044	-0.044	0.000	0.000	0.000	0.000
26	A	26	GLU	-1	-0.889	-0.932	15.028	0.113	0.113	0.000	0.000	0.000	0.000
27	A	27	GLN	0	-0.089	-0.028	19.068	-0.016	-0.016	0.000	0.000	0.000	0.000
28	A	28	ASN	0	-0.011	-0.021	22.288	-0.013	-0.013	0.000	0.000	0.000	0.000
29	A	29	VAL	0	-0.030	-0.001	23.504	-0.004	-0.004	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.001	-0.005	25.269	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	31	ALA	0	0.005	-0.014	25.514	0.005	0.005	0.000	0.000	0.000	0.000
32	A	32	GLU	-1	-0.864	-0.931	24.310	0.057	0.057	0.000	0.000	0.000	0.000
33	A	33	GLU	-1	-0.941	-0.968	25.755	0.061	0.061	0.000	0.000	0.000	0.000
34	A	34	GLU	-1	-0.924	-0.973	20.015	0.102	0.102	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.048	-0.030	21.845	0.018	0.018	0.000	0.000	0.000	0.000
36	A	36	ASP	-1	-0.767	-0.846	23.846	0.111	0.111	0.000	0.000	0.000	0.000
37	A	37	GLU	-1	-0.919	-0.974	26.198	0.069	0.069	0.000	0.000	0.000	0.000
38	A	38	LEU	0	-0.044	-0.020	24.917	0.000	0.000	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.680	-0.826	21.185	0.142	0.142	0.000	0.000	0.000	0.000
40	A	40	ASN	0	-0.011	-0.013	22.336	0.008	0.008	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.969	-0.967	24.780	0.088	0.088	0.000	0.000	0.000	0.000
42	A	42	SER	0	-0.080	-0.039	20.177	0.008	0.008	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.882	-0.922	16.334	0.159	0.159	0.000	0.000	0.000	0.000
44	A	44	HIS	0	-0.028	-0.031	15.241	0.035	0.035	0.000	0.000	0.000	0.000
45	A	45	ILE	0	-0.043	-0.026	9.235	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	46	VAL	0	0.023	0.023	8.271	0.049	0.049	0.000	0.000	0.000	0.000
47	A	47	VAL	0	-0.058	-0.036	3.087	-0.641	0.017	0.120	-0.150	-0.628	-0.001
48	A	48	TYR	0	-0.058	-0.057	4.414	-0.307	0.056	-0.001	-0.110	-0.252	0.000
49	A	49	ASP	-1	-0.946	-0.961	2.167	-7.421	-6.388	6.310	-3.980	-3.363	-0.032
50	A	50	GLY	0	0.011	0.001	3.504	-0.418	-0.269	0.022	-0.012	-0.160	-0.001
51	A	51	GLU	-1	-0.939	-0.980	6.402	0.063	0.063	0.000	0.000	0.000	0.000
52	A	52	LYS	1	0.950	0.987	7.535	0.209	0.209	0.000	0.000	0.000	0.000
53	A	53	PRO	0	0.018	0.024	6.542	-0.178	-0.178	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.025	-0.041	3.079	-0.392	0.031	0.037	-0.090	-0.371	-0.001
55	A	55	GLY	0	-0.006	-0.021	6.427	0.416	0.416	0.000	0.000	0.000	0.000
56	A	56	ALA	0	0.021	0.020	7.819	-0.144	-0.144	0.000	0.000	0.000	0.000
57	A	57	GLY	0	0.023	0.019	10.977	0.067	0.067	0.000	0.000	0.000	0.000
58	A	58	ARG	1	0.737	0.843	13.505	-0.176	-0.176	0.000	0.000	0.000	0.000
59	A	59	TRP	0	-0.060	-0.043	16.207	0.017	0.017	0.000	0.000	0.000	0.000
60	A	60	ARG	1	0.979	0.997	18.650	-0.142	-0.142	0.000	0.000	0.000	0.000
61	A	61	MET	0	0.002	0.032	22.183	0.009	0.009	0.000	0.000	0.000	0.000
62	A	62	LYS	1	0.892	0.941	24.893	-0.106	-0.106	0.000	0.000	0.000	0.000
63	A	63	ASP	-1	-0.890	-0.949	27.475	0.089	0.089	0.000	0.000	0.000	0.000
64	A	64	GLY	0	-0.003	0.002	28.733	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	65	TYR	0	0.031	0.024	25.024	0.002	0.002	0.000	0.000	0.000	0.000
66	A	66	GLY	0	0.055	0.021	21.413	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	67	LYS	1	0.781	0.895	21.634	-0.136	-0.136	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.001	0.000	15.444	0.007	0.007	0.000	0.000	0.000	0.000
69	A	69	GLU	-1	-0.783	-0.918	17.869	0.143	0.143	0.000	0.000	0.000	0.000
70	A	70	ARG	1	0.941	0.965	16.914	-0.116	-0.116	0.000	0.000	0.000	0.000
71	A	71	ILE	0	-0.023	0.006	11.955	0.023	0.023	0.000	0.000	0.000	0.000
72	A	72	CYS	0	-0.039	-0.005	12.707	-0.034	-0.034	0.000	0.000	0.000	0.000
73	A	73	VAL	0	-0.010	-0.021	8.080	0.114	0.114	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.063	0.053	9.138	-0.057	-0.057	0.000	0.000	0.000	0.000
75	A	75	LYS	1	0.880	0.903	10.775	0.005	0.005	0.000	0.000	0.000	0.000
76	A	76	SER	0	-0.042	-0.044	9.600	0.004	0.004	0.000	0.000	0.000	0.000
77	A	77	HIS	0	0.047	0.044	4.774	-0.102	0.011	-0.001	-0.004	-0.107	0.000
78	A	78	ARG	1	0.959	0.990	7.039	0.275	0.275	0.000	0.000	0.000	0.000
79	A	79	SER	0	-0.062	-0.025	7.977	0.118	0.118	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.030	0.017	2.799	-0.731	-0.224	0.125	-0.133	-0.500	0.000
81	A	81	GLY	0	-0.006	-0.003	2.374	-3.174	-2.871	3.051	-1.256	-2.100	-0.019
82	A	82	VAL	0	0.051	0.015	3.274	0.620	1.633	0.766	-0.350	-1.429	0.001
83	A	83	GLY	0	0.029	0.017	4.648	-0.990	-1.003	0.006	0.015	-0.008	0.000
84	A	84	GLY	0	0.013	-0.002	7.607	-0.233	-0.233	0.000	0.000	0.000	0.000
85	A	85	ILE	0	-0.050	-0.023	2.562	-0.804	-1.527	3.726	-0.611	-2.392	0.004
86	A	86	ILE	0	0.032	0.023	6.275	-0.500	-0.500	0.000	0.000	0.000	0.000
87	A	87	MET	0	0.004	0.018	8.335	-0.220	-0.220	0.000	0.000	0.000	0.000
88	A	88	LYS	1	0.966	0.991	7.766	-0.901	-0.901	0.000	0.000	0.000	0.000
89	A	89	ALA	0	-0.036	-0.012	8.421	-0.118	-0.118	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.036	0.006	10.486	-0.081	-0.081	0.000	0.000	0.000	0.000
91	A	91	GLU	-1	-0.882	-0.937	13.425	0.307	0.307	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.896	0.953	12.710	-0.244	-0.244	0.000	0.000	0.000	0.000
93	A	93	ALA	0	0.030	0.018	14.485	-0.028	-0.028	0.000	0.000	0.000	0.000
94	A	94	ALA	0	0.026	0.010	16.140	-0.024	-0.024	0.000	0.000	0.000	0.000
95	A	95	ALA	0	-0.033	-0.025	18.395	-0.020	-0.020	0.000	0.000	0.000	0.000
96	A	96	ASP	-1	-0.938	-0.967	17.548	0.145	0.145	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.049	-0.018	20.365	-0.013	-0.013	0.000	0.000	0.000	0.000
98	A	98	GLY	0	-0.048	-0.028	22.189	-0.010	-0.010	0.000	0.000	0.000	0.000
99	A	99	ALA	0	-0.044	-0.026	21.858	-0.006	-0.006	0.000	0.000	0.000	0.000
100	A	100	SER	0	-0.038	-0.015	23.924	-0.001	-0.001	0.000	0.000	0.000	0.000
101	A	101	GLY	0	0.012	0.019	23.893	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	102	PHE	0	-0.024	-0.033	19.084	0.011	0.011	0.000	0.000	0.000	0.000
103	A	103	ILE	0	0.006	0.010	22.027	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	104	LEU	0	-0.016	-0.015	17.213	0.011	0.011	0.000	0.000	0.000	0.000
105	A	105	ASN	0	0.006	0.016	20.613	-0.022	-0.022	0.000	0.000	0.000	0.000
106	A	106	ALA	0	-0.002	-0.007	19.061	0.026	0.026	0.000	0.000	0.000	0.000
107	A	107	GLN	0	0.063	0.044	15.592	-0.056	-0.056	0.000	0.000	0.000	0.000
108	A	108	THR	0	0.049	0.009	20.144	0.015	0.015	0.000	0.000	0.000	0.000
109	A	109	GLN	0	0.036	0.000	19.323	0.020	0.020	0.000	0.000	0.000	0.000
110	A	110	ALA	0	-0.013	0.004	15.966	0.003	0.003	0.000	0.000	0.000	0.000
111	A	111	VAL	0	0.023	0.011	17.430	0.028	0.028	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.011	-0.021	18.419	0.007	0.007	0.000	0.000	0.000	0.000
113	A	113	PHE	0	0.020	0.010	10.476	-0.006	-0.006	0.000	0.000	0.000	0.000
114	A	114	TYR	0	0.092	0.023	14.174	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	115	LYS	1	0.947	0.996	17.187	-0.126	-0.126	0.000	0.000	0.000	0.000
116	A	116	LYS	1	0.880	0.959	13.320	-0.238	-0.238	0.000	0.000	0.000	0.000
117	A	117	HIS	0	-0.097	-0.063	12.244	0.087	0.087	0.000	0.000	0.000	0.000
118	A	118	GLY	0	0.009	0.011	16.701	0.003	0.003	0.000	0.000	0.000	0.000
119	A	119	TYR	0	-0.037	-0.007	16.840	-0.026	-0.026	0.000	0.000	0.000	0.000
120	A	120	ARG	1	0.938	0.953	21.295	-0.121	-0.121	0.000	0.000	0.000	0.000
121	A	121	VAL	0	-0.010	-0.007	24.689	0.006	0.006	0.000	0.000	0.000	0.000
122	A	122	LEU	0	0.000	0.008	26.230	-0.007	-0.007	0.000	0.000	0.000	0.000
123	A	123	SER	0	0.013	-0.010	28.583	-0.011	-0.011	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.932	-0.966	29.120	0.071	0.071	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.845	0.925	31.107	-0.070	-0.070	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.904	-0.956	27.642	0.088	0.088	0.000	0.000	0.000	0.000
127	A	127	PHE	0	-0.063	-0.029	25.366	-0.008	-0.008	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.002	-0.001	27.271	0.007	0.007	0.000	0.000	0.000	0.000
129	A	129	ASP	-1	-0.899	-0.936	23.226	0.144	0.144	0.000	0.000	0.000	0.000
130	A	130	ALA	0	0.084	0.032	23.018	-0.005	-0.005	0.000	0.000	0.000	0.000
131	A	131	GLY	0	0.033	0.014	24.913	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	132	ILE	0	-0.001	-0.001	21.847	-0.005	-0.005	0.000	0.000	0.000	0.000
133	A	133	PRO	0	-0.026	-0.001	24.938	0.007	0.007	0.000	0.000	0.000	0.000
134	A	134	HIS	0	-0.035	-0.033	21.156	0.031	0.031	0.000	0.000	0.000	0.000
135	A	135	LEU	0	0.028	0.016	23.502	-0.014	-0.014	0.000	0.000	0.000	0.000
136	A	136	GLN	0	-0.021	-0.001	23.556	0.010	0.010	0.000	0.000	0.000	0.000
137	A	137	MET	0	-0.084	-0.039	21.130	-0.004	-0.004	0.000	0.000	0.000	0.000
138	A	138	MET	0	0.012	0.018	23.729	0.004	0.004	0.000	0.000	0.000	0.000
139	A	139	LYS	1	0.912	0.968	17.818	-0.239	-0.239	0.000	0.000	0.000	0.000
140	A	140	ASP	-1	-0.902	-0.946	22.862	0.125	0.125	0.000	0.000	0.000	0.000

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