FMO DATABASE

FMODB ID: 82YYY

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	OptAll
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	-819545.49403
FMO2-HF: Nuclear repulsion	778338.569594
FMO2-HF: Total energy	-41206.924436
FMO2-MP2: Total energy	-41326.806369

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.
-11.443	-8.813	13.944	-8.147	-8.426	-0.074

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 : 0.023 / q_NPA : 0.020

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	-0.053	-0.024	3.343	1.414	3.010	-0.003	-0.803	-0.790	0.002
4	A	4	VAL	0	0.012	0.012	4.500	-0.749	-0.678	-0.001	-0.022	-0.048	0.000
5	A	5	CYS	0	-0.060	-0.023	7.213	0.319	0.319	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.837	0.923	10.267	0.472	0.472	0.000	0.000	0.000	0.000
7	A	7	PHE	0	0.051	0.024	12.280	0.005	0.005	0.000	0.000	0.000	0.000
8	A	8	TYR	0	-0.049	-0.044	16.638	0.008	0.008	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.063	-0.039	20.405	0.027	0.027	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.029	0.011	21.418	-0.003	-0.003	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.780	0.870	22.537	0.020	0.020	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.055	0.037	17.402	0.028	0.028	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.821	0.915	18.213	0.173	0.173	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.045	-0.025	18.132	0.022	0.022	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.047	-0.017	14.003	-0.010	-0.010	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.847	-0.923	11.076	-0.617	-0.617	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.029	-0.022	8.115	0.135	0.135	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.898	-0.943	2.446	-2.649	-0.070	2.349	-2.700	-2.229	-0.029
19	A	19	LEU	0	-0.019	-0.016	3.899	0.842	1.131	-0.001	-0.095	-0.193	0.000
20	A	20	PRO	0	0.026	0.016	2.066	-5.460	-5.706	4.243	-2.062	-1.934	-0.026
21	A	21	HIS	0	0.018	0.000	2.261	-4.843	-6.684	7.360	-2.433	-3.086	-0.021
22	A	22	GLY	0	-0.022	-0.005	4.819	0.305	0.359	-0.001	-0.007	-0.046	0.000
23	A	23	ARG	1	0.933	0.953	8.653	-0.422	-0.422	0.000	0.000	0.000	0.000
24	A	24	CYS	0	0.017	0.023	7.720	0.131	0.131	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.070	-0.034	9.813	-0.134	-0.134	0.000	0.000	0.000	0.000
26	A	26	PHE	0	0.036	0.012	10.018	0.038	0.038	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.040	0.006	14.562	-0.007	-0.007	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.020	-0.014	17.967	0.013	0.013	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.847	-0.905	20.307	0.145	0.145	0.000	0.000	0.000	0.000
30	A	30	PRO	0	-0.006	-0.014	17.998	0.016	0.016	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.080	-0.039	18.352	0.045	0.045	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.124	-0.079	18.391	0.011	0.011	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.016	-0.011	15.160	-0.021	-0.021	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.840	-0.909	9.963	0.523	0.523	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.056	-0.025	8.131	0.026	0.026	0.000	0.000	0.000	0.000
36	A	36	VAL	0	0.006	-0.001	12.402	-0.057	-0.057	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.035	-0.008	15.222	-0.026	-0.026	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.003	-0.017	18.283	0.022	0.022	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.841	-0.912	21.614	-0.081	-0.081	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.045	-0.064	23.580	0.009	0.009	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.881	-0.912	25.149	-0.042	-0.042	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.041	0.003	19.264	-0.014	-0.014	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.050	0.027	22.550	0.019	0.019	0.000	0.000	0.000	0.000
44	A	44	PRO	0	-0.008	-0.014	21.260	0.001	0.001	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.026	0.018	17.989	0.019	0.019	0.000	0.000	0.000	0.000
46	A	46	HIS	0	-0.001	-0.011	18.390	0.008	0.008	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.002	-0.002	14.476	-0.019	-0.019	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.032	-0.002	14.197	0.035	0.035	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.012	0.001	10.312	-0.045	-0.045	0.000	0.000	0.000	0.000
50	A	50	MET	0	-0.026	-0.006	10.604	0.170	0.170	0.000	0.000	0.000	0.000
51	A	51	VAL	0	-0.005	0.005	4.473	-0.200	-0.163	-0.001	-0.004	-0.032	0.000
52	A	52	ASP	-1	-0.877	-0.945	6.447	-0.092	-0.092	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.877	-0.947	5.981	-1.248	-1.248	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.959	-0.978	7.075	-0.647	-0.647	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.061	-0.035	9.103	-0.004	-0.004	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.023	0.022	7.146	-0.058	-0.058	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.909	0.960	10.259	0.387	0.387	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.045	0.033	13.200	0.018	0.018	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.107	-0.051	14.631	0.037	0.037	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.899	-0.967	16.887	0.005	0.005	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.029	-0.040	17.899	-0.026	-0.026	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.031	0.007	20.239	0.007	0.007	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.919	-0.961	22.786	-0.092	-0.092	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.020	-0.014	22.593	-0.011	-0.011	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.052	0.043	16.765	-0.006	-0.006	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.037	-0.011	20.823	0.005	0.005	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.059	0.015	17.718	-0.073	-0.073	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.851	-0.925	21.095	-0.324	-0.324	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.052	0.031	23.604	0.019	0.019	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.071	-0.032	24.708	0.022	0.022	0.000	0.000	0.000	0.000
71	A	71	PRO	0	-0.002	0.001	23.720	-0.017	-0.017	0.000	0.000	0.000	0.000
72	A	72	VAL	0	0.001	0.000	18.499	-0.002	-0.002	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.013	-0.006	21.944	0.017	0.017	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.041	0.026	19.897	-0.025	-0.025	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.011	0.002	17.578	0.010	0.010	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.088	-0.062	17.321	-0.020	-0.020	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.027	-0.015	12.628	0.003	0.003	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.017	-0.003	12.642	0.044	0.044	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.857	0.917	14.255	0.291	0.291	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.046	0.038	12.453	0.017	0.017	0.000	0.000	0.000	0.000
81	A	81	GLY	0	-0.022	-0.017	14.003	0.082	0.082	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.076	-0.040	16.409	0.074	0.074	0.000	0.000	0.000	0.000
83	A	83	CYS	0	-0.049	-0.001	17.695	-0.029	-0.029	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.008	0.005	14.578	0.018	0.018	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.837	-0.931	18.487	-0.205	-0.205	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.004	0.001	18.313	0.005	0.005	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.091	0.067	21.118	0.014	0.014	0.000	0.000	0.000	0.000
88	A	88	PHE	0	-0.031	-0.018	22.390	-0.012	-0.012	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.006	0.005	15.832	-0.008	-0.008	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.011	0.011	19.317	-0.021	-0.021	0.000	0.000	0.000	0.000
91	A	91	TRP	0	-0.015	-0.036	11.000	-0.023	-0.023	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.019	-0.011	14.696	-0.016	-0.016	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.006	-0.007	9.034	-0.031	-0.031	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.013	-0.003	10.083	0.183	0.183	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.058	0.029	8.134	-0.348	-0.348	0.000	0.000	0.000	0.000
96	A	96	VAL	0	0.008	-0.001	5.038	0.564	0.655	-0.001	-0.021	-0.068	0.000
97	A	97	GLY	0	-0.008	0.001	7.193	0.353	0.353	0.000	0.000	0.000	0.000
98	A	98	GLN	0	-0.079	-0.041	10.538	0.300	0.300	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.007	-0.014	12.405	-0.034	-0.034	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.046	0.044	10.726	-0.014	-0.014	0.000	0.000	0.000	0.000
101	A	101	PRO	0	-0.016	0.005	14.985	0.071	0.071	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.803	-0.899	18.515	-0.234	-0.234	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.016	-0.018	20.720	0.012	0.012	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.036	0.016	18.313	-0.026	-0.026	0.000	0.000	0.000	0.000
105	A	105	GLN	0	-0.062	-0.038	22.663	0.026	0.026	0.000	0.000	0.000	0.000
106	A	106	VAL	0	0.063	0.029	24.252	-0.009	-0.009	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.041	-0.007	25.090	0.017	0.017	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.030	-0.007	28.319	0.009	0.009	0.000	0.000	0.000	0.000

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