FMO DATABASE

FMODB ID: Q164Y

Calculation Name: 2QYA-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QYA

Chain ID: A

ChEMBL ID:

UniProt ID: Q8TWR4

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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-854271.846275
FMO2-HF: Nuclear repulsion	809971.974809
FMO2-HF: Total energy	-44299.871466
FMO2-MP2: Total energy	-44428.449011

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:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-8.428	-4.012	0.112	-2.311	-2.217	0

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.036 / q_NPA : 0.021

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	VAL	0	0.040	0.021	3.831	-1.057	1.685	-0.033	-1.565	-1.144	0.004
4	A	5	LEU	0	-0.037	-0.018	7.168	0.040	0.040	0.000	0.000	0.000	0.000
5	A	6	LEU	0	0.002	0.004	10.529	0.095	0.095	0.000	0.000	0.000	0.000
6	A	7	ASN	0	-0.028	-0.015	13.430	0.029	0.029	0.000	0.000	0.000	0.000
7	A	8	ILE	0	0.005	0.010	16.900	0.012	0.012	0.000	0.000	0.000	0.000
8	A	9	HIS	0	0.003	0.011	19.881	0.001	0.001	0.000	0.000	0.000	0.000
9	A	10	GLY	0	0.048	0.030	23.446	0.002	0.002	0.000	0.000	0.000	0.000
10	A	11	THR	0	-0.055	-0.040	26.756	0.009	0.009	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.003	0.004	29.955	0.002	0.002	0.000	0.000	0.000	0.000
12	A	13	ASP	-1	-0.912	-0.957	32.458	-0.131	-0.131	0.000	0.000	0.000	0.000
13	A	14	THR	0	-0.024	-0.004	26.699	-0.001	-0.001	0.000	0.000	0.000	0.000
14	A	15	VAL	0	0.024	0.009	22.945	-0.002	-0.002	0.000	0.000	0.000	0.000
15	A	16	VAL	0	-0.023	-0.006	20.954	0.002	0.002	0.000	0.000	0.000	0.000
16	A	17	LEU	0	-0.004	-0.006	17.824	-0.029	-0.029	0.000	0.000	0.000	0.000
17	A	18	ALA	0	-0.003	-0.007	16.982	0.020	0.020	0.000	0.000	0.000	0.000
18	A	19	LEU	0	-0.005	-0.013	11.094	-0.072	-0.072	0.000	0.000	0.000	0.000
19	A	20	CYS	0	-0.016	-0.014	11.112	0.151	0.151	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.753	-0.861	6.993	-0.902	-0.902	0.000	0.000	0.000	0.000
21	A	22	GLU	-1	-0.850	-0.895	5.647	-1.036	-1.036	0.000	0.000	0.000	0.000
22	A	23	ASP	-1	-0.948	-0.975	6.366	0.728	0.728	0.000	0.000	0.000	0.000
23	A	24	LEU	0	0.006	0.004	7.938	0.076	0.076	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.041	-0.020	10.768	0.004	0.004	0.000	0.000	0.000	0.000
25	A	26	GLY	0	-0.029	-0.013	12.845	0.063	0.063	0.000	0.000	0.000	0.000
26	A	27	VAL	0	-0.011	0.016	14.179	0.039	0.039	0.000	0.000	0.000	0.000
27	A	28	GLU	-1	-0.938	-0.988	16.255	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	29	LEU	0	0.017	0.016	15.464	0.025	0.025	0.000	0.000	0.000	0.000
29	A	30	LYS	1	0.948	0.975	19.647	-0.059	-0.059	0.000	0.000	0.000	0.000
30	A	31	TYR	0	0.073	0.021	22.548	0.006	0.006	0.000	0.000	0.000	0.000
31	A	32	LYS	1	0.963	0.973	24.551	-0.004	-0.004	0.000	0.000	0.000	0.000
32	A	33	GLY	0	-0.004	0.007	28.145	-0.005	-0.005	0.000	0.000	0.000	0.000
33	A	34	ARG	1	0.921	0.973	25.779	0.046	0.046	0.000	0.000	0.000	0.000
34	A	35	THR	0	0.005	-0.015	23.718	0.015	0.015	0.000	0.000	0.000	0.000
35	A	36	LEU	0	-0.064	-0.008	18.740	-0.009	-0.009	0.000	0.000	0.000	0.000
36	A	37	HIS	0	0.021	0.004	20.397	0.012	0.012	0.000	0.000	0.000	0.000
37	A	38	ILE	0	0.000	0.013	14.134	-0.026	-0.026	0.000	0.000	0.000	0.000
38	A	39	SER	0	-0.030	-0.018	16.721	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	40	GLU	-1	-0.858	-0.942	17.334	-0.200	-0.200	0.000	0.000	0.000	0.000
40	A	41	PRO	0	-0.045	-0.019	18.377	-0.025	-0.025	0.000	0.000	0.000	0.000
41	A	42	PHE	0	-0.022	-0.011	20.158	-0.012	-0.012	0.000	0.000	0.000	0.000
42	A	43	TYR	0	-0.029	-0.012	14.711	-0.028	-0.028	0.000	0.000	0.000	0.000
43	A	44	SER	0	0.066	-0.027	14.735	0.021	0.021	0.000	0.000	0.000	0.000
44	A	45	GLY	0	-0.004	0.051	13.579	0.034	0.034	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.919	0.954	12.325	0.756	0.756	0.000	0.000	0.000	0.000
46	A	47	SER	0	-0.026	-0.057	7.024	-0.294	-0.294	0.000	0.000	0.000	0.000
47	A	48	MET	0	-0.155	-0.085	8.185	0.301	0.301	0.000	0.000	0.000	0.000
48	A	49	GLU	-1	-0.857	-0.928	3.608	-8.249	-7.389	0.020	-0.543	-0.337	-0.003
49	A	50	PRO	0	0.082	0.039	3.762	0.771	1.030	0.002	-0.044	-0.217	0.000
50	A	51	ASP	-1	-0.803	-0.888	6.837	-0.723	-0.723	0.000	0.000	0.000	0.000
51	A	52	ARG	1	0.837	0.908	8.985	1.151	1.151	0.000	0.000	0.000	0.000
52	A	53	ALA	0	-0.019	-0.018	9.652	0.212	0.212	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.119	0.058	10.922	0.178	0.178	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.825	0.914	12.859	0.664	0.664	0.000	0.000	0.000	0.000
55	A	56	LYS	1	0.915	0.945	14.560	0.736	0.736	0.000	0.000	0.000	0.000
56	A	57	ILE	0	0.021	0.023	14.035	0.063	0.063	0.000	0.000	0.000	0.000
57	A	58	ARG	1	0.922	0.959	15.146	0.565	0.565	0.000	0.000	0.000	0.000
58	A	59	GLU	-1	-0.916	-0.962	18.946	-0.438	-0.438	0.000	0.000	0.000	0.000
59	A	60	ALA	0	0.028	0.023	20.027	0.032	0.032	0.000	0.000	0.000	0.000
60	A	61	VAL	0	-0.019	-0.020	20.605	0.031	0.031	0.000	0.000	0.000	0.000
61	A	62	GLN	0	-0.024	-0.012	22.884	0.011	0.011	0.000	0.000	0.000	0.000
62	A	63	GLU	-1	-0.999	-0.991	24.492	-0.273	-0.273	0.000	0.000	0.000	0.000
63	A	64	TYR	0	0.002	-0.015	24.452	0.023	0.023	0.000	0.000	0.000	0.000
64	A	65	GLU	-1	-0.900	-0.933	27.583	-0.186	-0.186	0.000	0.000	0.000	0.000
65	A	66	ASP	-1	-0.809	-0.879	28.891	-0.144	-0.144	0.000	0.000	0.000	0.000
66	A	67	GLU	-1	-0.991	-1.009	31.038	-0.162	-0.162	0.000	0.000	0.000	0.000
67	A	68	LYS	1	0.795	0.902	28.565	0.169	0.169	0.000	0.000	0.000	0.000
68	A	69	THR	0	0.013	0.012	27.711	0.000	0.000	0.000	0.000	0.000	0.000
69	A	70	VAL	0	0.004	0.004	22.351	-0.009	-0.009	0.000	0.000	0.000	0.000
70	A	71	ALA	0	-0.028	-0.013	23.627	0.010	0.010	0.000	0.000	0.000	0.000
71	A	72	ILE	0	0.012	-0.002	17.296	-0.028	-0.028	0.000	0.000	0.000	0.000
72	A	73	ASN	0	0.003	-0.010	18.419	0.058	0.058	0.000	0.000	0.000	0.000
73	A	74	ALA	0	-0.013	0.003	13.193	-0.056	-0.056	0.000	0.000	0.000	0.000
74	A	75	LEU	0	-0.003	0.000	13.572	0.069	0.069	0.000	0.000	0.000	0.000
75	A	76	GLY	0	0.051	0.004	10.374	-0.066	-0.066	0.000	0.000	0.000	0.000
76	A	77	GLU	-1	-0.921	-0.953	8.050	0.122	0.122	0.000	0.000	0.000	0.000
77	A	78	LEU	0	-0.017	-0.002	3.063	-0.816	-0.261	0.123	-0.159	-0.519	-0.001
78	A	79	ALA	0	0.009	-0.009	6.716	-0.109	-0.109	0.000	0.000	0.000	0.000
79	A	80	CYS	0	-0.036	-0.016	9.592	0.045	0.045	0.000	0.000	0.000	0.000
80	A	81	SER	0	-0.021	-0.008	7.929	0.003	0.003	0.000	0.000	0.000	0.000
81	A	82	VAL	0	0.006	0.004	8.099	-0.027	-0.027	0.000	0.000	0.000	0.000
82	A	83	VAL	0	-0.024	-0.015	10.624	0.061	0.061	0.000	0.000	0.000	0.000
83	A	84	VAL	0	-0.005	0.003	13.442	0.039	0.039	0.000	0.000	0.000	0.000
84	A	85	ASP	-1	-0.930	-0.963	11.570	-0.532	-0.532	0.000	0.000	0.000	0.000
85	A	86	ALA	0	-0.074	-0.038	13.682	0.012	0.012	0.000	0.000	0.000	0.000
86	A	87	GLY	0	-0.058	-0.024	15.858	0.038	0.038	0.000	0.000	0.000	0.000
87	A	88	LEU	0	-0.062	-0.032	17.672	0.030	0.030	0.000	0.000	0.000	0.000
88	A	89	ALA	0	0.015	0.008	17.719	0.026	0.026	0.000	0.000	0.000	0.000
89	A	90	ARG	1	0.860	0.912	18.222	0.112	0.112	0.000	0.000	0.000	0.000
90	A	91	GLU	-1	-0.901	-0.964	15.382	-0.165	-0.165	0.000	0.000	0.000	0.000
91	A	92	ASP	-1	-0.918	-0.953	17.641	-0.102	-0.102	0.000	0.000	0.000	0.000
92	A	93	GLU	-1	-0.921	-0.956	20.222	-0.154	-0.154	0.000	0.000	0.000	0.000
93	A	94	ILE	0	-0.087	-0.021	14.970	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	95	GLY	0	0.012	0.011	18.292	0.028	0.028	0.000	0.000	0.000	0.000
95	A	96	GLU	-1	-0.880	-0.965	17.888	0.005	0.005	0.000	0.000	0.000	0.000
96	A	97	LEU	0	-0.062	-0.042	18.231	0.005	0.005	0.000	0.000	0.000	0.000
97	A	98	GLY	0	-0.039	-0.026	18.505	0.001	0.001	0.000	0.000	0.000	0.000
98	A	99	GLY	0	-0.053	-0.020	18.449	0.022	0.022	0.000	0.000	0.000	0.000
99	A	100	VAL	0	-0.025	0.003	12.896	0.026	0.026	0.000	0.000	0.000	0.000
100	A	101	PRO	0	0.038	0.030	12.382	-0.022	-0.022	0.000	0.000	0.000	0.000
101	A	102	HIS	0	-0.004	-0.013	14.564	-0.025	-0.025	0.000	0.000	0.000	0.000
102	A	103	VAL	0	0.056	0.032	16.120	0.019	0.019	0.000	0.000	0.000	0.000
103	A	104	GLN	0	-0.008	-0.002	18.285	-0.013	-0.013	0.000	0.000	0.000	0.000
104	A	105	MET	0	-0.026	-0.002	19.950	0.007	0.007	0.000	0.000	0.000	0.000
105	A	106	TYR	0	-0.026	-0.016	22.738	-0.009	-0.009	0.000	0.000	0.000	0.000
106	A	107	ILE	0	0.007	0.008	22.098	0.010	0.010	0.000	0.000	0.000	0.000
107	A	108	LEU	0	-0.030	-0.018	26.418	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.026	0.015	29.916	-0.004	-0.004	0.000	0.000	0.000	0.000
109	A	110	ARG	1	0.808	0.891	31.158	0.167	0.167	0.000	0.000	0.000	0.000
110	A	111	GLU	-1	-0.947	-0.976	33.536	-0.097	-0.097	0.000	0.000	0.000	0.000
111	A	112	PRO	0	-0.010	-0.001	37.222	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	113	PHE	0	-0.047	-0.014	35.549	0.007	0.007	0.000	0.000	0.000	0.000
113	A	114	LEU	0	-0.043	-0.021	40.774	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	115	GLU	-1	-0.897	-0.952	38.733	-0.117	-0.117	0.000	0.000	0.000	0.000
115	A	116	GLY	0	-0.062	-0.028	43.136	0.003	0.003	0.000	0.000	0.000	0.000

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