FMO DATABASE

FMODB ID: 98R72

Calculation Name: 2Q4Q-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2Q4Q

Chain ID: A

ChEMBL ID:

UniProt ID: Q9H7C9

Base Structure: X-ray

Registration Date: 2023-09-23

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	122
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1020385.566321
FMO2-HF: Nuclear repulsion	973602.05419
FMO2-HF: Total energy	-46783.512131
FMO2-MP2: Total energy	-46919.972917

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:SER)

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

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.
6.254	1.27	10.17	0.802	-5.988	-0.017

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.007 / q_NPA : 0.003

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	3	SER	0	-0.006	0.016	3.805	1.696	3.068	-0.019	-0.697	-0.656	0.002
4	A	4	PRO	0	0.007	0.021	6.307	-0.243	-0.243	0.000	0.000	0.000	0.000
5	A	5	GLU	-1	-0.809	-0.926	8.376	-0.196	-0.196	0.000	0.000	0.000	0.000
6	A	6	ILE	0	-0.048	-0.014	12.133	0.077	0.077	0.000	0.000	0.000	0.000
7	A	7	ALA	0	-0.031	-0.021	14.892	-0.028	-0.028	0.000	0.000	0.000	0.000
8	A	8	SER	0	0.021	0.002	16.916	-0.016	-0.016	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.025	-0.002	19.761	0.025	0.025	0.000	0.000	0.000	0.000
10	A	10	SER	0	0.038	0.034	22.088	-0.013	-0.013	0.000	0.000	0.000	0.000
11	A	11	TRP	0	0.065	0.003	25.027	0.011	0.011	0.000	0.000	0.000	0.000
12	A	12	GLY	0	-0.036	-0.027	25.778	0.001	0.001	0.000	0.000	0.000	0.000
13	A	13	GLN	0	-0.031	-0.015	22.516	0.004	0.004	0.000	0.000	0.000	0.000
14	A	14	MET	0	0.018	0.020	17.573	-0.010	-0.010	0.000	0.000	0.000	0.000
15	A	15	LYS	1	0.927	0.974	16.594	0.003	0.003	0.000	0.000	0.000	0.000
16	A	16	VAL	0	0.037	0.009	10.887	-0.024	-0.024	0.000	0.000	0.000	0.000
17	A	17	LYS	1	0.869	0.934	12.091	0.176	0.176	0.000	0.000	0.000	0.000
18	A	18	GLY	0	0.053	0.016	9.502	0.017	0.017	0.000	0.000	0.000	0.000
19	A	19	SER	0	-0.040	-0.002	10.500	0.069	0.069	0.000	0.000	0.000	0.000
20	A	20	ASN	0	-0.030	-0.011	12.513	-0.089	-0.089	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.028	-0.022	15.335	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	22	THR	0	0.001	-0.004	16.292	0.024	0.024	0.000	0.000	0.000	0.000
23	A	23	TYR	0	0.019	0.010	12.679	-0.021	-0.021	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.977	1.003	19.647	-0.120	-0.120	0.000	0.000	0.000	0.000
25	A	25	ASP	-1	-0.738	-0.844	20.183	0.107	0.107	0.000	0.000	0.000	0.000
26	A	26	CYS	0	-0.082	-0.047	15.008	0.019	0.019	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.905	0.971	12.307	-0.399	-0.399	0.000	0.000	0.000	0.000
28	A	28	VAL	0	-0.006	0.000	9.226	0.123	0.123	0.000	0.000	0.000	0.000
29	A	29	TRP	0	0.034	0.000	4.269	-0.731	-0.602	-0.001	-0.022	-0.106	0.000
30	A	30	PRO	0	-0.020	-0.020	2.868	-0.377	0.486	0.068	-0.317	-0.614	0.000
31	A	31	GLY	0	0.040	0.008	2.206	5.315	3.163	9.628	-3.573	-3.903	-0.021
32	A	32	GLY	0	-0.053	-0.022	3.112	0.670	-4.796	0.493	5.494	-0.521	0.002
33	A	33	SER	0	-0.012	-0.002	6.620	-0.510	-0.510	0.000	0.000	0.000	0.000
34	A	34	ARG	1	0.801	0.879	10.052	-0.366	-0.366	0.000	0.000	0.000	0.000
35	A	35	THR	0	0.009	0.021	13.100	-0.067	-0.067	0.000	0.000	0.000	0.000
36	A	36	TRP	0	-0.058	-0.049	16.592	0.023	0.023	0.000	0.000	0.000	0.000
37	A	37	ASP	-1	-0.865	-0.925	18.063	0.139	0.139	0.000	0.000	0.000	0.000
38	A	38	TRP	0	0.009	-0.010	21.364	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	39	ARG	1	0.990	0.994	23.286	-0.118	-0.118	0.000	0.000	0.000	0.000
40	A	40	GLU	-1	-0.882	-0.907	18.698	0.289	0.289	0.000	0.000	0.000	0.000
41	A	41	THR	0	-0.058	-0.072	20.894	0.005	0.005	0.000	0.000	0.000	0.000
42	A	42	GLY	0	-0.055	-0.016	23.774	-0.012	-0.012	0.000	0.000	0.000	0.000
43	A	43	THR	0	-0.060	-0.024	22.955	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	44	GLU	-1	-0.889	-0.934	25.921	0.070	0.070	0.000	0.000	0.000	0.000
45	A	45	HIS	0	-0.047	-0.075	27.488	0.002	0.002	0.000	0.000	0.000	0.000
46	A	46	SER	0	-0.031	-0.058	29.288	-0.009	-0.009	0.000	0.000	0.000	0.000
47	A	47	PRO	0	0.085	0.037	28.101	0.001	0.001	0.000	0.000	0.000	0.000
48	A	48	GLY	0	-0.021	0.018	26.686	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	49	VAL	0	-0.002	-0.007	20.143	0.007	0.007	0.000	0.000	0.000	0.000
50	A	50	GLN	0	0.069	0.033	22.218	-0.021	-0.021	0.000	0.000	0.000	0.000
51	A	51	PRO	0	0.018	0.009	19.605	0.016	0.016	0.000	0.000	0.000	0.000
52	A	52	ALA	0	0.002	-0.005	18.059	0.015	0.015	0.000	0.000	0.000	0.000
53	A	53	ASP	-1	-0.751	-0.840	17.775	0.180	0.180	0.000	0.000	0.000	0.000
54	A	54	VAL	0	-0.018	-0.024	14.894	0.034	0.034	0.000	0.000	0.000	0.000
55	A	55	LYS	1	0.980	1.007	13.748	-0.179	-0.179	0.000	0.000	0.000	0.000
56	A	56	GLU	-1	-0.793	-0.912	10.753	0.556	0.556	0.000	0.000	0.000	0.000
57	A	57	VAL	0	-0.044	-0.016	9.382	0.106	0.106	0.000	0.000	0.000	0.000
58	A	58	VAL	0	0.016	0.003	8.982	-0.069	-0.069	0.000	0.000	0.000	0.000
59	A	59	GLU	-1	-0.993	-0.995	10.221	0.286	0.286	0.000	0.000	0.000	0.000
60	A	60	LYS	1	0.916	0.969	5.080	-1.404	-1.404	0.000	0.000	0.000	0.000
61	A	61	GLY	0	-0.008	0.011	5.238	-0.461	-0.461	0.000	0.000	0.000	0.000
62	A	62	VAL	0	-0.021	-0.016	6.573	-0.396	-0.396	0.000	0.000	0.000	0.000
63	A	63	GLN	0	0.029	0.013	8.970	-0.040	-0.040	0.000	0.000	0.000	0.000
64	A	64	THR	0	0.013	-0.014	11.896	0.052	0.052	0.000	0.000	0.000	0.000
65	A	65	LEU	0	-0.047	-0.015	12.051	-0.010	-0.010	0.000	0.000	0.000	0.000
66	A	66	VAL	0	-0.018	-0.026	14.000	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	67	ILE	0	-0.003	-0.006	15.989	0.037	0.037	0.000	0.000	0.000	0.000
68	A	68	GLY	0	0.003	-0.004	18.648	-0.018	-0.018	0.000	0.000	0.000	0.000
69	A	69	ARG	1	0.915	0.959	20.591	-0.007	-0.007	0.000	0.000	0.000	0.000
70	A	70	GLY	0	0.062	0.016	23.699	-0.002	-0.002	0.000	0.000	0.000	0.000
71	A	71	MET	0	-0.045	-0.049	25.535	-0.009	-0.009	0.000	0.000	0.000	0.000
72	A	72	SER	0	0.036	-0.022	28.164	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	73	GLU	-1	-0.889	-0.959	27.120	0.007	0.007	0.000	0.000	0.000	0.000
74	A	74	ALA	0	-0.054	-0.010	28.578	0.000	0.000	0.000	0.000	0.000	0.000
75	A	75	LEU	0	-0.066	0.019	23.769	0.001	0.001	0.000	0.000	0.000	0.000
76	A	76	LYS	1	0.933	0.966	27.130	-0.038	-0.038	0.000	0.000	0.000	0.000
77	A	77	VAL	0	0.048	-0.003	23.189	0.008	0.008	0.000	0.000	0.000	0.000
78	A	78	PRO	0	-0.005	0.025	24.607	-0.010	-0.010	0.000	0.000	0.000	0.000
79	A	79	SER	0	0.057	0.020	25.242	0.001	0.001	0.000	0.000	0.000	0.000
80	A	80	SER	0	0.012	0.002	25.820	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	81	THR	0	0.006	-0.016	20.864	0.003	0.003	0.000	0.000	0.000	0.000
82	A	82	VAL	0	0.009	0.002	20.981	0.001	0.001	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.906	-0.958	21.344	-0.014	-0.014	0.000	0.000	0.000	0.000
84	A	84	TYR	0	-0.044	-0.012	17.188	0.000	0.000	0.000	0.000	0.000	0.000
85	A	85	LEU	0	0.018	0.011	15.649	0.000	0.000	0.000	0.000	0.000	0.000
86	A	86	LYS	1	1.022	1.016	17.907	0.021	0.021	0.000	0.000	0.000	0.000
87	A	87	LYS	1	0.889	0.964	20.245	-0.028	-0.028	0.000	0.000	0.000	0.000
88	A	88	HIS	0	-0.114	-0.080	15.688	0.024	0.024	0.000	0.000	0.000	0.000
89	A	89	GLY	0	0.006	0.007	15.931	-0.016	-0.016	0.000	0.000	0.000	0.000
90	A	90	ILE	0	-0.035	-0.004	13.167	-0.023	-0.023	0.000	0.000	0.000	0.000
91	A	91	ASP	-1	-0.848	-0.896	15.717	-0.097	-0.097	0.000	0.000	0.000	0.000
92	A	92	VAL	0	-0.013	-0.019	16.385	0.003	0.003	0.000	0.000	0.000	0.000
93	A	93	ARG	1	0.853	0.927	18.122	0.121	0.121	0.000	0.000	0.000	0.000
94	A	94	VAL	0	0.001	0.003	19.549	0.015	0.015	0.000	0.000	0.000	0.000
95	A	95	LEU	0	0.015	0.010	20.873	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	96	GLN	0	0.084	0.069	23.373	0.009	0.009	0.000	0.000	0.000	0.000
97	A	97	THR	0	-0.016	-0.076	21.171	-0.006	-0.006	0.000	0.000	0.000	0.000
98	A	98	GLU	-1	-0.902	-0.963	22.145	0.007	0.007	0.000	0.000	0.000	0.000
99	A	99	GLN	0	-0.046	-0.023	23.534	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	100	ALA	0	-0.008	0.009	19.789	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	101	VAL	0	0.006	-0.009	17.664	-0.009	-0.009	0.000	0.000	0.000	0.000
102	A	102	LYS	1	0.938	0.970	18.266	0.033	0.033	0.000	0.000	0.000	0.000
103	A	103	GLU	-1	-0.848	-0.925	18.717	-0.142	-0.142	0.000	0.000	0.000	0.000
104	A	104	TYR	0	0.021	0.002	10.205	-0.006	-0.006	0.000	0.000	0.000	0.000
105	A	105	ASN	0	0.072	0.020	14.513	-0.045	-0.045	0.000	0.000	0.000	0.000
106	A	106	ALA	0	0.021	0.032	15.620	-0.045	-0.045	0.000	0.000	0.000	0.000
107	A	107	LEU	0	-0.011	-0.020	13.940	-0.037	-0.037	0.000	0.000	0.000	0.000
108	A	108	VAL	0	-0.054	-0.026	10.628	-0.076	-0.076	0.000	0.000	0.000	0.000
109	A	109	ALA	0	-0.036	-0.008	12.399	-0.089	-0.089	0.000	0.000	0.000	0.000
110	A	110	GLN	0	-0.096	-0.038	15.056	-0.026	-0.026	0.000	0.000	0.000	0.000
111	A	111	GLY	0	0.011	0.006	11.064	-0.014	-0.014	0.000	0.000	0.000	0.000
112	A	112	VAL	0	0.000	0.017	11.128	-0.088	-0.088	0.000	0.000	0.000	0.000
113	A	113	ARG	1	0.819	0.904	3.455	2.621	2.891	0.001	-0.083	-0.188	0.000
114	A	114	VAL	0	-0.004	0.010	8.467	0.166	0.166	0.000	0.000	0.000	0.000
115	A	115	GLY	0	0.047	0.003	8.498	0.054	0.054	0.000	0.000	0.000	0.000
116	A	116	GLY	0	-0.004	-0.004	10.078	-0.071	-0.071	0.000	0.000	0.000	0.000
117	A	117	VAL	0	-0.016	0.017	13.017	0.087	0.087	0.000	0.000	0.000	0.000
118	A	118	PHE	0	-0.010	-0.002	13.887	-0.047	-0.047	0.000	0.000	0.000	0.000
119	A	119	HIS	1	0.800	0.879	18.594	-0.072	-0.072	0.000	0.000	0.000	0.000
120	A	120	SER	0	0.013	0.020	22.170	-0.022	-0.022	0.000	0.000	0.000	0.000
121	A	121	THR	0	-0.023	0.005	23.539	-0.011	-0.011	0.000	0.000	0.000	0.000
122	A	122	CYS	0	0.038	0.107	26.642	0.004	0.004	0.000	0.000	0.000	0.000

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