FMO DATABASE

FMODB ID: 1411Z

Calculation Name: 4A0E-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 4A0E

Chain ID: A

ChEMBL ID:

UniProt ID: Q56975

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	108
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-818615.354345
FMO2-HF: Nuclear repulsion	777408.791197
FMO2-HF: Total energy	-41206.563148
FMO2-MP2: Total energy	-41326.421344

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:GLY)

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

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.
-2.004	-3.487	17.409	-7.848	-8.077	-0.062

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.065 / q_NPA : 0.036

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	TRP	0	-0.043	-0.018	3.671	1.156	2.568	-0.006	-0.676	-0.730	0.001
4	A	4	VAL	0	0.032	0.030	4.708	-0.405	-0.322	-0.001	-0.010	-0.071	0.000
5	A	5	CYS	0	-0.012	-0.007	7.090	0.210	0.210	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.870	0.946	10.453	0.411	0.411	0.000	0.000	0.000	0.000
7	A	7	PHE	0	0.027	0.017	13.305	0.001	0.001	0.000	0.000	0.000	0.000
8	A	8	TYR	0	-0.026	-0.059	16.547	0.006	0.006	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.036	-0.020	20.273	0.023	0.023	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.010	0.010	21.716	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.833	0.893	22.444	0.026	0.026	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.051	0.051	17.286	0.019	0.019	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.950	1.001	17.847	0.129	0.129	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.063	-0.033	18.156	0.023	0.023	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.038	-0.014	13.469	-0.009	-0.009	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.861	-0.937	10.493	-0.541	-0.541	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.029	-0.027	8.433	0.135	0.135	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.930	-0.949	2.403	2.623	4.369	3.651	-2.908	-2.488	-0.025
19	A	19	LEU	0	-0.034	-0.032	4.787	0.574	0.677	-0.001	-0.013	-0.089	0.000
20	A	20	PRO	0	0.040	0.026	2.768	-3.658	-2.302	0.212	-0.767	-0.802	-0.010
21	A	21	HIS	0	0.044	0.000	2.038	-1.964	-8.178	13.555	-3.474	-3.867	-0.028
22	A	22	GLY	0	-0.010	-0.003	5.359	0.262	0.293	-0.001	0.000	-0.030	0.000
23	A	23	ARG	1	0.927	0.952	9.125	-0.221	-0.221	0.000	0.000	0.000	0.000
24	A	24	CYS	0	0.022	0.024	8.469	0.060	0.060	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.040	-0.014	10.472	-0.077	-0.077	0.000	0.000	0.000	0.000
26	A	26	PHE	0	0.021	0.007	10.826	0.029	0.029	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.051	0.001	14.961	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.025	0.007	18.331	0.012	0.012	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.859	-0.915	20.656	0.084	0.084	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.008	-0.009	18.448	0.007	0.007	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.067	-0.034	18.447	0.031	0.031	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.106	-0.070	18.920	0.010	0.010	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.043	-0.009	15.694	-0.023	-0.023	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.843	-0.910	10.458	0.284	0.284	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.049	-0.024	8.840	0.024	0.024	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.001	-0.009	12.890	-0.030	-0.030	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.029	-0.013	15.704	-0.012	-0.012	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.008	-0.024	18.747	0.019	0.019	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.867	-0.928	21.946	-0.086	-0.086	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.058	-0.030	24.310	0.005	0.005	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.893	-0.960	25.625	-0.063	-0.063	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.049	-0.005	19.924	-0.011	-0.011	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.025	0.005	23.010	0.016	0.016	0.000	0.000	0.000	0.000
44	A	44	PRO	0	-0.010	-0.018	21.755	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.026	0.012	18.536	0.009	0.009	0.000	0.000	0.000	0.000
46	A	46	HIS	0	-0.008	-0.014	18.908	0.009	0.009	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.001	-0.001	14.796	-0.014	-0.014	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.035	-0.003	14.755	0.016	0.016	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.013	-0.004	10.659	-0.032	-0.032	0.000	0.000	0.000	0.000
50	A	50	MET	0	-0.030	-0.002	11.262	0.111	0.111	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.008	0.002	5.284	-0.091	-0.091	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.880	-0.941	6.228	-0.314	-0.314	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.925	-0.974	5.539	-1.105	-1.105	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.955	-0.968	6.702	-0.679	-0.679	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.070	-0.037	9.044	0.032	0.032	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.014	0.017	8.239	0.015	0.015	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.892	0.938	10.950	0.412	0.412	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.024	0.025	13.978	0.012	0.012	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.089	-0.044	15.260	0.038	0.038	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.892	-0.965	17.436	-0.054	-0.054	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.073	-0.064	18.421	-0.029	-0.029	0.000	0.000	0.000	0.000
62	A	62	ALA	0	0.001	0.016	20.719	0.013	0.013	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.952	-0.980	23.264	-0.101	-0.101	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.023	0.010	23.243	-0.014	-0.014	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.070	0.045	17.773	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.040	-0.014	21.698	0.006	0.006	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.055	0.018	18.597	-0.061	-0.061	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.902	-0.959	21.776	-0.281	-0.281	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.035	0.025	24.191	0.017	0.017	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.081	-0.039	25.363	0.020	0.020	0.000	0.000	0.000	0.000
71	A	71	PRO	0	0.019	0.014	24.405	-0.017	-0.017	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.016	-0.009	19.457	-0.003	-0.003	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.017	0.000	22.782	0.013	0.013	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.061	0.047	20.744	-0.026	-0.026	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.006	0.004	18.539	0.012	0.012	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.083	-0.074	18.259	-0.017	-0.017	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.007	-0.010	13.682	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.016	0.002	13.790	0.043	0.043	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.926	0.961	14.926	0.282	0.282	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.045	0.027	13.064	0.019	0.019	0.000	0.000	0.000	0.000
81	A	81	GLY	0	-0.036	-0.026	14.538	0.077	0.077	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.091	-0.042	16.419	0.071	0.071	0.000	0.000	0.000	0.000
83	A	83	CYS	0	0.021	0.020	18.067	-0.027	-0.027	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.043	-0.003	15.229	0.019	0.019	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.882	-0.963	19.195	-0.186	-0.186	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.023	0.013	19.002	0.000	0.000	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.081	0.066	21.797	0.012	0.012	0.000	0.000	0.000	0.000
88	A	88	PHE	0	-0.022	-0.022	23.261	-0.010	-0.010	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.025	0.005	16.275	-0.005	-0.005	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.005	0.017	20.331	-0.015	-0.015	0.000	0.000	0.000	0.000
91	A	91	TRP	0	0.003	-0.032	11.701	-0.023	-0.023	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.025	-0.005	14.708	-0.014	-0.014	0.000	0.000	0.000	0.000
93	A	93	PHE	0	0.003	0.000	9.796	-0.026	-0.026	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.005	0.004	10.160	0.141	0.141	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.044	0.015	8.268	-0.284	-0.284	0.000	0.000	0.000	0.000
96	A	96	VAL	0	0.020	0.003	4.971	0.572	0.572	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.023	-0.012	7.096	0.271	0.271	0.000	0.000	0.000	0.000
98	A	98	GLN	0	-0.060	-0.028	10.359	0.259	0.259	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.006	-0.004	12.251	-0.014	-0.014	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.025	0.023	10.944	-0.018	-0.018	0.000	0.000	0.000	0.000
101	A	101	PRO	0	-0.009	0.008	15.050	0.060	0.060	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.931	-0.961	18.325	-0.201	-0.201	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.064	-0.030	20.710	0.013	0.013	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.038	0.017	18.669	-0.021	-0.021	0.000	0.000	0.000	0.000
105	A	105	GLN	0	-0.052	-0.029	22.491	0.026	0.026	0.000	0.000	0.000	0.000
106	A	106	VAL	0	0.038	0.019	24.759	-0.013	-0.013	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.018	0.003	25.555	0.017	0.017	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.020	-0.008	28.806	0.008	0.008	0.000	0.000	0.000	0.000

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