FMO DATABASE

FMODB ID: GN331

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

Total energy (hartree)

FMO2-HF: Electronic energy	-819022.426672
FMO2-HF: Nuclear repulsion	777815.607776
FMO2-HF: Total energy	-41206.818896
FMO2-MP2: Total energy	-41326.670501

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.
-4.026	1	6.652	-5.445	-6.231	-0.045

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 : 0.079 / q_NPA : 0.047

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	-0.025	3.524	0.841	2.323	-0.009	-0.706	-0.767	0.001
4	A	4	VAL	0	0.027	0.027	4.723	-0.351	-0.265	-0.001	-0.010	-0.074	0.000
5	A	5	CYS	0	-0.048	-0.013	7.103	0.217	0.217	0.000	0.000	0.000	0.000
6	A	6	ARG	1	0.880	0.932	10.466	0.371	0.371	0.000	0.000	0.000	0.000
7	A	7	PHE	0	0.034	0.017	13.084	-0.003	-0.003	0.000	0.000	0.000	0.000
8	A	8	TYR	0	-0.038	-0.052	16.468	0.004	0.004	0.000	0.000	0.000	0.000
9	A	9	GLN	0	-0.039	-0.020	20.284	0.019	0.019	0.000	0.000	0.000	0.000
10	A	10	GLY	0	0.018	0.009	21.725	0.000	0.000	0.000	0.000	0.000	0.000
11	A	11	LYS	1	0.822	0.881	22.531	-0.003	-0.003	0.000	0.000	0.000	0.000
12	A	12	HIS	0	0.043	0.039	17.301	0.015	0.015	0.000	0.000	0.000	0.000
13	A	13	ARG	1	0.872	0.951	17.854	0.123	0.123	0.000	0.000	0.000	0.000
14	A	14	GLY	0	-0.062	-0.032	18.164	0.020	0.020	0.000	0.000	0.000	0.000
15	A	15	VAL	0	-0.049	-0.025	13.521	-0.010	-0.010	0.000	0.000	0.000	0.000
16	A	16	GLU	-1	-0.835	-0.909	10.565	-0.480	-0.480	0.000	0.000	0.000	0.000
17	A	17	VAL	0	-0.029	-0.029	8.520	0.128	0.128	0.000	0.000	0.000	0.000
18	A	18	GLU	-1	-0.926	-0.948	2.445	1.871	3.766	2.944	-2.609	-2.230	-0.024
19	A	19	LEU	0	-0.033	-0.032	4.796	0.597	0.698	-0.001	-0.014	-0.086	0.000
20	A	20	PRO	0	0.036	0.024	2.780	-3.203	-1.901	0.199	-0.723	-0.778	-0.009
21	A	21	HIS	0	0.021	-0.014	2.494	-3.508	-3.378	3.521	-1.383	-2.267	-0.013
22	A	22	GLY	0	-0.013	-0.003	5.332	0.248	0.278	-0.001	0.000	-0.029	0.000
23	A	23	ARG	1	0.935	0.956	9.092	-0.256	-0.256	0.000	0.000	0.000	0.000
24	A	24	CYS	0	0.016	0.016	8.406	0.084	0.084	0.000	0.000	0.000	0.000
25	A	25	VAL	0	-0.045	-0.023	10.475	-0.096	-0.096	0.000	0.000	0.000	0.000
26	A	26	PHE	0	0.032	0.008	10.667	0.043	0.043	0.000	0.000	0.000	0.000
27	A	27	GLY	0	0.038	0.005	14.988	-0.011	-0.011	0.000	0.000	0.000	0.000
28	A	28	SER	0	-0.027	-0.009	18.399	0.016	0.016	0.000	0.000	0.000	0.000
29	A	29	ASP	-1	-0.865	-0.910	20.702	0.122	0.122	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.001	-0.003	18.559	0.011	0.011	0.000	0.000	0.000	0.000
31	A	31	LEU	0	-0.069	-0.031	18.565	0.034	0.034	0.000	0.000	0.000	0.000
32	A	32	GLN	0	-0.102	-0.074	18.999	0.007	0.007	0.000	0.000	0.000	0.000
33	A	33	SER	0	-0.041	-0.024	15.764	-0.021	-0.021	0.000	0.000	0.000	0.000
34	A	34	ASP	-1	-0.844	-0.902	10.542	0.402	0.402	0.000	0.000	0.000	0.000
35	A	35	ILE	0	-0.055	-0.028	8.801	0.035	0.035	0.000	0.000	0.000	0.000
36	A	36	VAL	0	-0.001	-0.009	12.976	-0.044	-0.044	0.000	0.000	0.000	0.000
37	A	37	LEU	0	-0.039	-0.014	15.780	-0.013	-0.013	0.000	0.000	0.000	0.000
38	A	38	SER	0	0.025	-0.010	18.818	0.015	0.015	0.000	0.000	0.000	0.000
39	A	39	ASP	-1	-0.866	-0.921	22.235	-0.046	-0.046	0.000	0.000	0.000	0.000
40	A	40	SER	0	-0.038	-0.046	24.366	0.006	0.006	0.000	0.000	0.000	0.000
41	A	41	GLU	-1	-0.902	-0.935	25.630	-0.030	-0.030	0.000	0.000	0.000	0.000
42	A	42	ILE	0	-0.046	-0.002	19.875	-0.010	-0.010	0.000	0.000	0.000	0.000
43	A	43	ALA	0	0.040	0.020	23.033	0.015	0.015	0.000	0.000	0.000	0.000
44	A	44	PRO	0	0.000	-0.012	21.793	0.002	0.002	0.000	0.000	0.000	0.000
45	A	45	VAL	0	0.018	0.008	18.598	0.013	0.013	0.000	0.000	0.000	0.000
46	A	46	HIS	0	0.004	-0.005	18.912	0.005	0.005	0.000	0.000	0.000	0.000
47	A	47	LEU	0	-0.004	0.000	14.946	-0.019	-0.019	0.000	0.000	0.000	0.000
48	A	48	VAL	0	-0.034	-0.003	14.733	0.025	0.025	0.000	0.000	0.000	0.000
49	A	49	LEU	0	0.009	-0.004	10.871	-0.042	-0.042	0.000	0.000	0.000	0.000
50	A	50	MET	0	-0.021	0.004	11.170	0.119	0.119	0.000	0.000	0.000	0.000
51	A	51	VAL	0	0.000	0.002	5.143	-0.117	-0.117	0.000	0.000	0.000	0.000
52	A	52	ASP	-1	-0.891	-0.950	6.370	-0.307	-0.307	0.000	0.000	0.000	0.000
53	A	53	GLU	-1	-0.923	-0.968	5.907	-1.272	-1.272	0.000	0.000	0.000	0.000
54	A	54	GLU	-1	-0.948	-0.964	6.802	-0.685	-0.685	0.000	0.000	0.000	0.000
55	A	55	GLY	0	-0.068	-0.035	9.211	0.040	0.040	0.000	0.000	0.000	0.000
56	A	56	ILE	0	0.006	0.011	7.959	0.014	0.014	0.000	0.000	0.000	0.000
57	A	57	ARG	1	0.925	0.961	10.790	0.393	0.393	0.000	0.000	0.000	0.000
58	A	58	LEU	0	0.027	0.024	13.864	0.021	0.021	0.000	0.000	0.000	0.000
59	A	59	THR	0	-0.098	-0.051	15.091	0.031	0.031	0.000	0.000	0.000	0.000
60	A	60	ASP	-1	-0.890	-0.961	17.350	-0.025	-0.025	0.000	0.000	0.000	0.000
61	A	61	SER	0	-0.059	-0.046	18.366	-0.024	-0.024	0.000	0.000	0.000	0.000
62	A	62	ALA	0	-0.003	0.016	20.671	0.009	0.009	0.000	0.000	0.000	0.000
63	A	63	GLU	-1	-0.938	-0.973	23.222	-0.078	-0.078	0.000	0.000	0.000	0.000
64	A	64	PRO	0	-0.019	-0.004	23.180	-0.012	-0.012	0.000	0.000	0.000	0.000
65	A	65	LEU	0	0.063	0.042	17.522	-0.003	-0.003	0.000	0.000	0.000	0.000
66	A	66	LEU	0	-0.034	-0.014	21.606	0.003	0.003	0.000	0.000	0.000	0.000
67	A	67	GLN	0	0.057	0.024	18.305	-0.057	-0.057	0.000	0.000	0.000	0.000
68	A	68	GLU	-1	-0.900	-0.964	21.650	-0.269	-0.269	0.000	0.000	0.000	0.000
69	A	69	GLY	0	0.032	0.022	24.064	0.015	0.015	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.080	-0.037	25.224	0.019	0.019	0.000	0.000	0.000	0.000
71	A	71	PRO	0	0.014	0.010	24.276	-0.016	-0.016	0.000	0.000	0.000	0.000
72	A	72	VAL	0	-0.010	-0.003	19.241	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.021	-0.006	22.650	0.013	0.013	0.000	0.000	0.000	0.000
74	A	74	LEU	0	0.059	0.031	20.628	-0.024	-0.024	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.011	0.001	18.409	0.009	0.009	0.000	0.000	0.000	0.000
76	A	76	THR	0	-0.091	-0.062	18.217	-0.021	-0.021	0.000	0.000	0.000	0.000
77	A	77	LEU	0	-0.028	-0.013	13.163	0.000	0.000	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.007	0.005	13.507	0.040	0.040	0.000	0.000	0.000	0.000
79	A	79	ARG	1	0.914	0.954	14.786	0.264	0.264	0.000	0.000	0.000	0.000
80	A	80	ALA	0	0.043	0.032	12.926	0.022	0.022	0.000	0.000	0.000	0.000
81	A	81	GLY	0	-0.032	-0.023	14.379	0.070	0.070	0.000	0.000	0.000	0.000
82	A	82	SER	0	-0.081	-0.045	16.435	0.069	0.069	0.000	0.000	0.000	0.000
83	A	83	CYS	0	0.004	0.026	17.954	-0.023	-0.023	0.000	0.000	0.000	0.000
84	A	84	LEU	0	-0.018	0.001	15.225	0.017	0.017	0.000	0.000	0.000	0.000
85	A	85	GLU	-1	-0.883	-0.957	19.099	-0.164	-0.164	0.000	0.000	0.000	0.000
86	A	86	VAL	0	0.011	0.002	18.916	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	87	GLY	0	0.081	0.069	21.744	0.013	0.013	0.000	0.000	0.000	0.000
88	A	88	PHE	0	-0.027	-0.030	23.131	-0.009	-0.009	0.000	0.000	0.000	0.000
89	A	89	LEU	0	-0.021	0.008	16.362	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	90	LEU	0	-0.003	0.012	20.290	-0.015	-0.015	0.000	0.000	0.000	0.000
91	A	91	TRP	0	-0.001	-0.030	11.692	-0.016	-0.016	0.000	0.000	0.000	0.000
92	A	92	THR	0	0.019	-0.010	14.764	-0.019	-0.019	0.000	0.000	0.000	0.000
93	A	93	PHE	0	-0.001	-0.003	9.552	-0.016	-0.016	0.000	0.000	0.000	0.000
94	A	94	VAL	0	-0.011	0.001	10.184	0.126	0.126	0.000	0.000	0.000	0.000
95	A	95	ALA	0	0.048	0.021	8.273	-0.268	-0.268	0.000	0.000	0.000	0.000
96	A	96	VAL	0	0.020	0.004	4.973	0.583	0.583	0.000	0.000	0.000	0.000
97	A	97	GLY	0	-0.009	-0.003	7.106	0.254	0.254	0.000	0.000	0.000	0.000
98	A	98	GLN	0	-0.081	-0.038	10.366	0.252	0.252	0.000	0.000	0.000	0.000
99	A	99	PRO	0	-0.003	-0.006	12.261	-0.009	-0.009	0.000	0.000	0.000	0.000
100	A	100	LEU	0	0.031	0.028	10.783	-0.016	-0.016	0.000	0.000	0.000	0.000
101	A	101	PRO	0	-0.004	0.011	15.062	0.056	0.056	0.000	0.000	0.000	0.000
102	A	102	GLU	-1	-0.854	-0.929	18.336	-0.174	-0.174	0.000	0.000	0.000	0.000
103	A	103	THR	0	-0.062	-0.031	20.721	0.016	0.016	0.000	0.000	0.000	0.000
104	A	104	LEU	0	0.041	0.026	18.400	-0.020	-0.020	0.000	0.000	0.000	0.000
105	A	105	GLN	0	-0.045	-0.026	22.505	0.022	0.022	0.000	0.000	0.000	0.000
106	A	106	VAL	0	0.042	0.018	24.639	-0.012	-0.012	0.000	0.000	0.000	0.000
107	A	107	PRO	0	-0.027	-0.004	25.506	0.015	0.015	0.000	0.000	0.000	0.000
108	A	108	THR	0	-0.017	-0.004	28.700	0.007	0.007	0.000	0.000	0.000	0.000

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