FMO DATABASE

FMODB ID: 5J2GZ

Calculation Name: 2QYZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2QYZ

Chain ID: A

ChEMBL ID:

UniProt ID: Q892G2

Base Structure: X-ray

Registration Date: 2023-09-21

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	127
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1111070.249423
FMO2-HF: Nuclear repulsion	1057929.992041
FMO2-HF: Total energy	-53140.257381
FMO2-MP2: Total energy	-53292.18401

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:4:ASN)

Summations of interaction energy for fragment #1(A:4:ASN)

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.
3.869	5.312	0.002	-0.623	-0.822	0.003

Interaction energy analysis for fragmet #1(A:4:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.001 / q_NPA : -0.018

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

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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	6	GLU	-1	-0.824	-0.904	3.899	0.971	2.414	0.002	-0.623	-0.822	0.003
4	A	7	VAL	0	-0.040	-0.022	5.919	0.144	0.144	0.000	0.000	0.000	0.000
5	A	8	LYS	1	0.773	0.858	8.391	-0.447	-0.447	0.000	0.000	0.000	0.000
6	A	9	PHE	0	0.034	-0.002	11.850	0.023	0.023	0.000	0.000	0.000	0.000
7	A	10	ARG	1	0.780	0.877	15.580	-0.382	-0.382	0.000	0.000	0.000	0.000
8	A	11	ALA	0	0.008	-0.012	18.746	0.056	0.056	0.000	0.000	0.000	0.000
9	A	12	TRP	0	0.047	0.025	22.086	-0.046	-0.046	0.000	0.000	0.000	0.000
10	A	13	ASP	-1	-0.751	-0.875	25.671	0.252	0.252	0.000	0.000	0.000	0.000
11	A	14	LYS	1	0.901	0.948	28.091	-0.333	-0.333	0.000	0.000	0.000	0.000
12	A	15	GLU	-1	-0.929	-0.955	31.139	0.208	0.208	0.000	0.000	0.000	0.000
13	A	16	LEU	0	-0.074	-0.047	30.919	-0.021	-0.021	0.000	0.000	0.000	0.000
14	A	17	ASN	0	-0.120	-0.047	31.357	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	18	MET	0	0.044	0.033	27.233	-0.017	-0.017	0.000	0.000	0.000	0.000
16	A	19	MET	0	-0.037	0.014	22.859	0.042	0.042	0.000	0.000	0.000	0.000
17	A	20	VAL	0	-0.038	-0.012	21.525	-0.030	-0.030	0.000	0.000	0.000	0.000
18	A	21	TYR	0	-0.029	-0.024	18.051	0.060	0.060	0.000	0.000	0.000	0.000
19	A	22	THR	0	-0.071	-0.054	16.792	0.023	0.023	0.000	0.000	0.000	0.000
20	A	23	LYS	1	0.931	0.954	19.277	-0.179	-0.179	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.775	-0.865	22.153	0.172	0.172	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.010	-0.017	24.592	0.006	0.006	0.000	0.000	0.000	0.000
23	A	26	THR	0	-0.040	-0.013	24.766	0.013	0.013	0.000	0.000	0.000	0.000
24	A	27	GLY	0	0.032	-0.002	26.090	0.016	0.016	0.000	0.000	0.000	0.000
25	A	28	HIS	0	-0.087	-0.054	25.973	-0.015	-0.015	0.000	0.000	0.000	0.000
26	A	29	ILE	0	-0.005	0.010	22.167	0.006	0.006	0.000	0.000	0.000	0.000
27	A	30	GLU	-1	-0.919	-0.949	24.819	0.234	0.234	0.000	0.000	0.000	0.000
28	A	31	TYR	0	0.040	0.014	22.699	0.013	0.013	0.000	0.000	0.000	0.000
29	A	32	ASN	0	-0.033	-0.015	24.591	-0.007	-0.007	0.000	0.000	0.000	0.000
30	A	33	THR	0	-0.027	-0.041	21.053	-0.005	-0.005	0.000	0.000	0.000	0.000
31	A	34	ASN	0	-0.023	0.001	17.649	0.076	0.076	0.000	0.000	0.000	0.000
32	A	35	PRO	0	0.065	0.007	14.277	0.009	0.009	0.000	0.000	0.000	0.000
33	A	36	ALA	0	0.007	0.013	14.168	0.048	0.048	0.000	0.000	0.000	0.000
34	A	37	ASP	-1	-0.840	-0.910	15.397	0.631	0.631	0.000	0.000	0.000	0.000
35	A	38	THR	0	-0.001	-0.007	18.120	-0.054	-0.054	0.000	0.000	0.000	0.000
36	A	39	ILE	0	-0.021	-0.003	12.728	-0.013	-0.013	0.000	0.000	0.000	0.000
37	A	40	ASN	0	-0.004	-0.003	16.949	0.046	0.046	0.000	0.000	0.000	0.000
38	A	41	ILE	0	0.005	0.016	18.823	-0.047	-0.047	0.000	0.000	0.000	0.000
39	A	42	ILE	0	-0.002	-0.001	19.385	-0.036	-0.036	0.000	0.000	0.000	0.000
40	A	43	LEU	0	-0.067	-0.033	15.535	-0.014	-0.014	0.000	0.000	0.000	0.000
41	A	44	ASN	0	-0.086	-0.061	20.091	-0.042	-0.042	0.000	0.000	0.000	0.000
42	A	45	GLN	0	-0.044	0.006	23.198	-0.036	-0.036	0.000	0.000	0.000	0.000
43	A	46	ASP	-1	-0.907	-0.961	25.989	0.410	0.410	0.000	0.000	0.000	0.000
44	A	47	ASP	-1	-0.963	-0.992	27.838	0.309	0.309	0.000	0.000	0.000	0.000
45	A	48	TYR	0	-0.021	0.005	26.589	-0.019	-0.019	0.000	0.000	0.000	0.000
46	A	49	GLY	0	0.022	0.009	28.966	-0.016	-0.016	0.000	0.000	0.000	0.000
47	A	50	TYR	0	-0.077	-0.056	22.885	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	51	VAL	0	-0.027	0.001	24.036	0.023	0.023	0.000	0.000	0.000	0.000
49	A	52	PHE	0	0.029	0.005	19.040	0.000	0.000	0.000	0.000	0.000	0.000
50	A	53	MET	0	-0.028	0.015	19.408	-0.019	-0.019	0.000	0.000	0.000	0.000
51	A	54	GLN	0	-0.022	-0.017	11.953	0.314	0.314	0.000	0.000	0.000	0.000
52	A	55	TYR	0	-0.044	-0.016	9.700	-0.113	-0.113	0.000	0.000	0.000	0.000
53	A	56	THR	0	-0.057	-0.070	12.751	0.174	0.174	0.000	0.000	0.000	0.000
54	A	57	GLY	0	-0.027	0.001	10.737	0.168	0.168	0.000	0.000	0.000	0.000
55	A	58	LEU	0	-0.077	-0.028	11.465	-0.268	-0.268	0.000	0.000	0.000	0.000
56	A	59	LYS	1	0.975	0.989	11.871	0.603	0.603	0.000	0.000	0.000	0.000
57	A	60	ASP	-1	-0.785	-0.896	16.666	-0.074	-0.074	0.000	0.000	0.000	0.000
58	A	61	LYS	1	0.873	0.933	20.005	0.076	0.076	0.000	0.000	0.000	0.000
59	A	62	ASN	0	-0.088	-0.045	22.352	-0.046	-0.046	0.000	0.000	0.000	0.000
60	A	63	GLU	-1	-0.901	-0.946	16.082	-0.515	-0.515	0.000	0.000	0.000	0.000
61	A	64	LYS	1	0.907	0.969	17.790	-0.118	-0.118	0.000	0.000	0.000	0.000
62	A	65	GLU	-1	-0.861	-0.901	13.088	0.051	0.051	0.000	0.000	0.000	0.000
63	A	66	ILE	0	-0.022	-0.017	16.227	0.024	0.024	0.000	0.000	0.000	0.000
64	A	67	TYR	0	-0.020	-0.007	14.937	0.133	0.133	0.000	0.000	0.000	0.000
65	A	68	GLU	-1	-0.814	-0.908	18.113	0.633	0.633	0.000	0.000	0.000	0.000
66	A	69	GLY	0	0.066	0.025	20.097	-0.015	-0.015	0.000	0.000	0.000	0.000
67	A	70	ASP	-1	-0.775	-0.875	20.843	0.187	0.187	0.000	0.000	0.000	0.000
68	A	71	ILE	0	0.020	0.018	23.621	0.010	0.010	0.000	0.000	0.000	0.000
69	A	72	ILE	0	-0.030	-0.012	23.029	-0.025	-0.025	0.000	0.000	0.000	0.000
70	A	73	LYS	1	0.878	0.951	26.430	0.018	0.018	0.000	0.000	0.000	0.000
71	A	74	LYS	1	0.908	0.950	25.583	-0.049	-0.049	0.000	0.000	0.000	0.000
72	A	75	SER	0	-0.018	-0.010	27.828	0.006	0.006	0.000	0.000	0.000	0.000
73	A	76	ASN	0	-0.061	-0.047	29.676	-0.024	-0.024	0.000	0.000	0.000	0.000
74	A	77	ARG	1	0.965	0.988	32.137	0.032	0.032	0.000	0.000	0.000	0.000
75	A	78	SER	0	-0.040	-0.019	32.841	0.005	0.005	0.000	0.000	0.000	0.000
76	A	79	SER	0	0.048	0.007	34.662	-0.002	-0.002	0.000	0.000	0.000	0.000
77	A	80	ASN	0	-0.049	-0.010	32.427	0.006	0.006	0.000	0.000	0.000	0.000
78	A	81	LEU	0	0.032	0.023	30.710	-0.011	-0.011	0.000	0.000	0.000	0.000
79	A	82	TYR	0	-0.027	-0.025	26.719	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	83	GLU	-1	-0.787	-0.901	25.922	0.257	0.257	0.000	0.000	0.000	0.000
81	A	84	ILE	0	-0.065	-0.027	19.617	0.008	0.008	0.000	0.000	0.000	0.000
82	A	85	ILE	0	0.060	0.038	22.585	0.012	0.012	0.000	0.000	0.000	0.000
83	A	86	TYR	0	0.061	0.023	15.787	0.064	0.064	0.000	0.000	0.000	0.000
84	A	87	GLN	0	-0.004	-0.008	20.204	-0.070	-0.070	0.000	0.000	0.000	0.000
85	A	88	ASP	-1	-0.787	-0.909	20.178	0.729	0.729	0.000	0.000	0.000	0.000
86	A	89	SER	0	-0.038	-0.013	20.845	0.026	0.026	0.000	0.000	0.000	0.000
87	A	90	ILE	0	-0.075	-0.037	20.888	-0.043	-0.043	0.000	0.000	0.000	0.000
88	A	91	ALA	0	-0.016	0.002	16.513	0.021	0.021	0.000	0.000	0.000	0.000
89	A	92	CYS	0	-0.040	-0.018	16.107	0.076	0.076	0.000	0.000	0.000	0.000
90	A	93	PHE	0	0.060	0.041	13.348	-0.064	-0.064	0.000	0.000	0.000	0.000
91	A	94	ARG	1	0.839	0.910	18.199	-0.370	-0.370	0.000	0.000	0.000	0.000
92	A	95	CYS	0	-0.018	0.003	21.324	0.006	0.006	0.000	0.000	0.000	0.000
93	A	96	LYS	1	0.912	0.967	24.327	-0.227	-0.227	0.000	0.000	0.000	0.000
94	A	97	VAL	0	-0.041	-0.023	27.530	-0.010	-0.010	0.000	0.000	0.000	0.000
95	A	98	ILE	0	0.034	0.022	29.942	0.009	0.009	0.000	0.000	0.000	0.000
96	A	99	LYS	1	0.958	0.985	32.500	-0.075	-0.075	0.000	0.000	0.000	0.000
97	A	100	GLY	0	0.030	0.003	34.114	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	101	ASP	-1	-0.922	-0.973	36.692	0.073	0.073	0.000	0.000	0.000	0.000
99	A	102	ILE	0	0.042	0.022	33.914	-0.001	-0.001	0.000	0.000	0.000	0.000
100	A	103	LYS	1	0.848	0.936	33.489	-0.051	-0.051	0.000	0.000	0.000	0.000
101	A	104	SER	0	-0.047	-0.003	29.397	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	105	PHE	0	0.083	0.018	22.496	-0.005	-0.005	0.000	0.000	0.000	0.000
103	A	106	PRO	0	-0.045	-0.037	24.195	0.019	0.019	0.000	0.000	0.000	0.000
104	A	107	CYS	0	0.062	0.039	19.631	0.008	0.008	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.054	0.055	17.921	-0.066	-0.066	0.000	0.000	0.000	0.000
106	A	109	ASN	0	-0.004	-0.005	15.998	0.004	0.004	0.000	0.000	0.000	0.000
107	A	110	ILE	0	0.141	0.058	12.359	-0.012	-0.012	0.000	0.000	0.000	0.000
108	A	111	GLY	0	0.006	0.006	15.765	-0.045	-0.045	0.000	0.000	0.000	0.000
109	A	112	THR	0	-0.124	-0.094	19.058	-0.014	-0.014	0.000	0.000	0.000	0.000
110	A	113	VAL	0	0.071	0.021	17.668	0.014	0.014	0.000	0.000	0.000	0.000
111	A	114	ARG	1	0.970	1.009	19.910	0.152	0.152	0.000	0.000	0.000	0.000
112	A	115	ASN	0	-0.065	-0.044	21.022	-0.025	-0.025	0.000	0.000	0.000	0.000
113	A	116	CYS	0	-0.050	0.001	22.982	0.024	0.024	0.000	0.000	0.000	0.000
114	A	117	GLU	-1	-0.795	-0.902	23.818	-0.061	-0.061	0.000	0.000	0.000	0.000
115	A	118	VAL	0	-0.017	-0.025	21.291	0.022	0.022	0.000	0.000	0.000	0.000
116	A	119	ILE	0	-0.091	-0.053	24.630	-0.024	-0.024	0.000	0.000	0.000	0.000
117	A	120	GLY	0	0.091	0.051	26.753	-0.010	-0.010	0.000	0.000	0.000	0.000
118	A	121	ASN	0	-0.081	-0.056	24.859	0.027	0.027	0.000	0.000	0.000	0.000
119	A	122	ILE	0	-0.020	-0.023	26.616	-0.017	-0.017	0.000	0.000	0.000	0.000
120	A	123	TYR	0	0.008	0.004	25.607	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	124	GLU	-1	-0.849	-0.913	26.103	0.156	0.156	0.000	0.000	0.000	0.000
122	A	125	ASN	0	-0.072	-0.037	29.719	-0.010	-0.010	0.000	0.000	0.000	0.000
123	A	126	PRO	0	0.070	0.039	32.029	0.002	0.002	0.000	0.000	0.000	0.000
124	A	127	GLU	-1	-0.860	-0.933	34.606	0.097	0.097	0.000	0.000	0.000	0.000
125	A	128	LEU	0	-0.103	-0.055	30.782	-0.008	-0.008	0.000	0.000	0.000	0.000
126	A	129	LEU	0	-0.096	-0.036	31.229	0.006	0.006	0.000	0.000	0.000	0.000
127	A	130	GLU	-1	-0.989	-0.980	34.800	0.101	0.101	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ASN)