FMO DATABASE

FMODB ID: 3J8KL

Calculation Name: 3BUT-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3BUT

Chain ID: A

ChEMBL ID:

UniProt ID: O29803

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	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	126
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-992364.246509
FMO2-HF: Nuclear repulsion	943875.157749
FMO2-HF: Total energy	-48489.08876
FMO2-MP2: Total energy	-48632.88745

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:0:SER)

Summations of interaction energy for fragment #1(A:0: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.
-27.917	-23.499	14.165	-9.446	-9.135	-0.081

Interaction energy analysis for fragmet #1(A:0:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.010 / q_NPA : 0.013

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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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	2	GLU	-1	-0.790	-0.873	3.872	-2.365	-0.598	-0.014	-0.743	-1.010	0.002
4	A	3	SER	0	-0.050	-0.028	5.516	-0.580	-0.492	-0.001	-0.003	-0.084	0.000
5	A	4	VAL	0	0.031	0.015	8.723	-0.076	-0.076	0.000	0.000	0.000	0.000
6	A	5	LYS	1	0.888	0.943	11.510	-0.566	-0.566	0.000	0.000	0.000	0.000
7	A	6	ALA	0	0.006	-0.001	15.211	0.032	0.032	0.000	0.000	0.000	0.000
8	A	7	MET	0	-0.029	-0.004	18.106	-0.047	-0.047	0.000	0.000	0.000	0.000
9	A	8	TRP	0	0.036	0.016	21.669	0.027	0.027	0.000	0.000	0.000	0.000
10	A	9	GLY	0	0.001	-0.003	24.225	-0.005	-0.005	0.000	0.000	0.000	0.000
11	A	10	VAL	0	-0.014	-0.010	25.143	-0.016	-0.016	0.000	0.000	0.000	0.000
12	A	11	VAL	0	-0.034	-0.018	28.331	0.018	0.018	0.000	0.000	0.000	0.000
13	A	12	THR	0	-0.001	0.001	30.610	-0.010	-0.010	0.000	0.000	0.000	0.000
14	A	13	ASP	-1	-0.859	-0.911	34.137	0.133	0.133	0.000	0.000	0.000	0.000
15	A	14	SER	0	-0.072	-0.052	35.271	0.004	0.004	0.000	0.000	0.000	0.000
16	A	15	GLN	0	-0.049	-0.037	28.987	0.018	0.018	0.000	0.000	0.000	0.000
17	A	16	THR	0	0.023	0.003	27.617	-0.012	-0.012	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.770	-0.836	22.669	0.279	0.279	0.000	0.000	0.000	0.000
19	A	18	ILE	0	-0.007	0.003	20.312	-0.011	-0.011	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.046	-0.020	18.372	0.021	0.021	0.000	0.000	0.000	0.000
21	A	20	ALA	0	0.005	0.003	14.802	0.018	0.018	0.000	0.000	0.000	0.000
22	A	21	LEU	0	-0.015	-0.015	14.143	-0.037	-0.037	0.000	0.000	0.000	0.000
23	A	22	ALA	0	0.026	0.007	8.976	0.075	0.075	0.000	0.000	0.000	0.000
24	A	23	LYS	1	0.828	0.930	7.577	0.552	0.552	0.000	0.000	0.000	0.000
25	A	24	VAL	0	0.037	0.012	4.138	0.368	0.558	-0.001	-0.060	-0.129	0.000
26	A	25	ARG	1	0.804	0.872	2.404	3.450	5.037	0.509	-0.728	-1.367	0.002
27	A	26	ASN	0	-0.028	-0.023	1.872	-7.527	-10.624	9.110	-3.539	-2.474	-0.033
28	A	27	GLU	-1	-0.915	-0.979	2.442	-21.328	-17.445	4.562	-4.373	-4.071	-0.052
29	A	28	ASP	-1	-0.810	-0.878	5.410	-0.299	-0.299	0.000	0.000	0.000	0.000
30	A	29	VAL	0	-0.039	-0.046	7.956	-0.060	-0.060	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.019	-0.003	10.766	0.149	0.149	0.000	0.000	0.000	0.000
32	A	31	PRO	0	-0.064	-0.035	9.800	-0.189	-0.189	0.000	0.000	0.000	0.000
33	A	32	ILE	0	0.058	0.045	4.940	0.133	0.133	0.000	0.000	0.000	0.000
34	A	33	VAL	0	-0.006	-0.009	9.082	-0.090	-0.090	0.000	0.000	0.000	0.000
35	A	34	VAL	0	-0.009	-0.009	9.380	0.184	0.184	0.000	0.000	0.000	0.000
36	A	35	SER	0	-0.010	-0.028	12.200	-0.052	-0.052	0.000	0.000	0.000	0.000
37	A	36	GLY	0	0.041	0.011	15.317	-0.063	-0.063	0.000	0.000	0.000	0.000
38	A	37	TYR	0	-0.061	-0.025	14.715	0.130	0.130	0.000	0.000	0.000	0.000
39	A	38	HIS	0	0.019	0.010	16.505	-0.068	-0.068	0.000	0.000	0.000	0.000
40	A	39	TYR	0	-0.086	-0.046	17.256	0.099	0.099	0.000	0.000	0.000	0.000
41	A	40	THR	0	0.020	0.004	19.268	-0.050	-0.050	0.000	0.000	0.000	0.000
42	A	41	ILE	0	-0.043	-0.027	20.662	0.050	0.050	0.000	0.000	0.000	0.000
43	A	42	GLU	-1	-0.803	-0.870	23.230	0.341	0.341	0.000	0.000	0.000	0.000
44	A	43	MET	0	-0.025	-0.018	25.319	0.020	0.020	0.000	0.000	0.000	0.000
45	A	44	ASN	0	-0.021	-0.027	28.136	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	45	GLY	0	0.017	0.020	28.904	-0.012	-0.012	0.000	0.000	0.000	0.000
47	A	46	VAL	0	0.000	0.015	30.016	-0.004	-0.004	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.865	0.917	25.457	-0.315	-0.315	0.000	0.000	0.000	0.000
49	A	48	VAL	0	-0.005	-0.010	26.713	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	49	ALA	0	-0.016	-0.009	24.278	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	50	ASP	-1	-0.799	-0.896	24.089	0.392	0.392	0.000	0.000	0.000	0.000
52	A	51	GLY	0	0.015	0.026	23.241	-0.038	-0.038	0.000	0.000	0.000	0.000
53	A	52	TYR	0	-0.031	-0.022	17.646	0.030	0.030	0.000	0.000	0.000	0.000
54	A	53	GLU	-1	-0.789	-0.874	19.397	0.248	0.248	0.000	0.000	0.000	0.000
55	A	54	ASN	0	-0.027	-0.014	19.316	0.044	0.044	0.000	0.000	0.000	0.000
56	A	55	SER	0	-0.004	-0.006	16.787	-0.033	-0.033	0.000	0.000	0.000	0.000
57	A	56	PRO	0	0.018	0.010	16.182	0.033	0.033	0.000	0.000	0.000	0.000
58	A	57	VAL	0	-0.041	-0.002	11.904	-0.061	-0.061	0.000	0.000	0.000	0.000
59	A	58	THR	0	-0.002	0.005	11.541	0.060	0.060	0.000	0.000	0.000	0.000
60	A	59	VAL	0	-0.039	-0.028	5.953	-0.026	-0.026	0.000	0.000	0.000	0.000
61	A	60	LYS	1	0.983	0.992	8.869	0.553	0.553	0.000	0.000	0.000	0.000
62	A	61	PRO	0	0.099	0.044	8.872	-0.278	-0.278	0.000	0.000	0.000	0.000
63	A	62	ALA	0	0.018	0.022	8.015	0.210	0.210	0.000	0.000	0.000	0.000
64	A	63	SER	0	-0.083	-0.027	8.392	0.024	0.024	0.000	0.000	0.000	0.000
65	A	64	ALA	0	0.037	0.009	6.651	-0.574	-0.574	0.000	0.000	0.000	0.000
66	A	65	THR	0	-0.026	0.004	7.467	0.262	0.262	0.000	0.000	0.000	0.000
67	A	66	THR	0	-0.022	-0.014	8.595	0.057	0.057	0.000	0.000	0.000	0.000
68	A	67	LEU	0	0.032	0.027	8.428	-0.039	-0.039	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.872	0.918	11.673	-0.251	-0.251	0.000	0.000	0.000	0.000
70	A	69	PHE	0	-0.004	0.006	10.897	0.034	0.034	0.000	0.000	0.000	0.000
71	A	70	SER	0	-0.048	-0.061	16.594	-0.030	-0.030	0.000	0.000	0.000	0.000
72	A	71	LEU	0	0.020	0.004	17.354	0.001	0.001	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.846	0.914	21.379	-0.296	-0.296	0.000	0.000	0.000	0.000
74	A	73	LEU	0	0.032	0.013	24.726	0.012	0.012	0.000	0.000	0.000	0.000
75	A	74	ASN	0	0.036	0.018	27.433	-0.028	-0.028	0.000	0.000	0.000	0.000
76	A	75	ASN	0	0.080	0.033	30.927	0.010	0.010	0.000	0.000	0.000	0.000
77	A	76	SER	0	-0.013	0.005	33.475	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	77	PHE	0	0.056	0.026	31.680	-0.004	-0.004	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.011	0.003	29.514	0.003	0.003	0.000	0.000	0.000	0.000
80	A	79	ARG	1	0.897	0.947	33.159	-0.159	-0.159	0.000	0.000	0.000	0.000
81	A	80	GLU	-1	-0.902	-0.954	34.997	0.185	0.185	0.000	0.000	0.000	0.000
82	A	81	TRP	0	0.007	-0.006	31.760	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	82	TRP	0	0.029	0.029	33.971	0.002	0.002	0.000	0.000	0.000	0.000
84	A	83	VAL	0	0.025	0.009	36.297	-0.004	-0.004	0.000	0.000	0.000	0.000
85	A	84	THR	0	-0.014	-0.026	33.965	0.002	0.002	0.000	0.000	0.000	0.000
86	A	85	HIS	0	-0.007	0.041	33.105	0.012	0.012	0.000	0.000	0.000	0.000
87	A	86	ILE	0	0.009	-0.008	35.408	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	87	ALA	0	0.009	0.015	38.593	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	88	ASN	0	-0.052	-0.022	34.887	-0.003	-0.003	0.000	0.000	0.000	0.000
90	A	89	GLY	0	-0.005	0.003	37.110	0.002	0.002	0.000	0.000	0.000	0.000
91	A	90	GLU	-1	-0.795	-0.857	36.909	0.155	0.155	0.000	0.000	0.000	0.000
92	A	91	LYS	1	0.837	0.907	32.595	-0.182	-0.182	0.000	0.000	0.000	0.000
93	A	92	THR	0	0.020	-0.014	28.456	-0.005	-0.005	0.000	0.000	0.000	0.000
94	A	93	LYS	1	0.861	0.935	23.996	-0.392	-0.392	0.000	0.000	0.000	0.000
95	A	94	ILE	0	-0.026	-0.014	22.864	-0.010	-0.010	0.000	0.000	0.000	0.000
96	A	95	ARG	1	0.792	0.872	21.329	-0.375	-0.375	0.000	0.000	0.000	0.000
97	A	96	VAL	0	0.011	0.012	17.504	-0.029	-0.029	0.000	0.000	0.000	0.000
98	A	97	ALA	0	-0.002	-0.003	16.484	0.067	0.067	0.000	0.000	0.000	0.000
99	A	98	ILE	0	0.002	0.003	13.414	-0.088	-0.088	0.000	0.000	0.000	0.000
100	A	99	LYS	1	0.913	0.969	13.557	-0.518	-0.518	0.000	0.000	0.000	0.000
101	A	100	PRO	0	0.008	0.007	10.214	-0.147	-0.147	0.000	0.000	0.000	0.000
102	A	101	THR	0	0.015	0.010	13.185	0.066	0.066	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.004	-0.001	7.719	-0.035	-0.035	0.000	0.000	0.000	0.000
104	A	103	GLU	-1	-0.847	-0.905	11.676	0.216	0.216	0.000	0.000	0.000	0.000
105	A	104	ILE	0	-0.009	-0.018	8.626	-0.071	-0.071	0.000	0.000	0.000	0.000
106	A	105	GLY	0	0.046	0.026	13.309	-0.019	-0.019	0.000	0.000	0.000	0.000
107	A	106	GLY	0	0.002	0.017	17.006	-0.035	-0.035	0.000	0.000	0.000	0.000
108	A	107	ARG	1	0.818	0.893	18.969	-0.172	-0.172	0.000	0.000	0.000	0.000
109	A	108	ASP	-1	-0.859	-0.915	16.953	0.169	0.169	0.000	0.000	0.000	0.000
110	A	109	VAL	0	-0.054	-0.041	14.441	0.003	0.003	0.000	0.000	0.000	0.000
111	A	110	GLU	-1	-0.906	-0.934	8.935	1.263	1.263	0.000	0.000	0.000	0.000
112	A	111	VAL	0	-0.060	-0.050	12.620	0.005	0.005	0.000	0.000	0.000	0.000
113	A	112	PRO	0	0.035	0.028	8.896	-0.116	-0.116	0.000	0.000	0.000	0.000
114	A	113	VAL	0	0.013	-0.021	11.751	-0.091	-0.091	0.000	0.000	0.000	0.000
115	A	114	PHE	0	0.002	0.004	6.664	-0.030	-0.030	0.000	0.000	0.000	0.000
116	A	115	LEU	0	0.017	0.007	12.072	-0.165	-0.165	0.000	0.000	0.000	0.000
117	A	116	ARG	1	0.916	0.956	14.367	-0.519	-0.519	0.000	0.000	0.000	0.000
118	A	117	GLU	-1	-0.802	-0.898	16.740	0.409	0.409	0.000	0.000	0.000	0.000
119	A	118	SER	0	-0.069	-0.042	19.783	0.020	0.020	0.000	0.000	0.000	0.000
120	A	119	GLU	-1	-0.910	-0.960	22.518	0.284	0.284	0.000	0.000	0.000	0.000
121	A	120	PHE	0	-0.013	0.006	26.317	0.002	0.002	0.000	0.000	0.000	0.000
122	A	121	THR	0	0.014	0.000	29.006	-0.012	-0.012	0.000	0.000	0.000	0.000
123	A	122	THR	0	-0.076	-0.057	32.819	0.004	0.004	0.000	0.000	0.000	0.000
124	A	123	LYS	1	0.923	0.942	35.191	-0.177	-0.177	0.000	0.000	0.000	0.000
125	A	124	LEU	0	-0.005	-0.003	38.111	-0.006	-0.006	0.000	0.000	0.000	0.000
126	A	125	LEU	0	-0.020	0.014	41.225	-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:0:SER)