FMO DATABASE

FMODB ID: JQ749

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:

Apendix: None

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	126
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-990085.55477
FMO2-HF: Nuclear repulsion	941596.745241
FMO2-HF: Total energy	-48488.80953
FMO2-MP2: Total energy	-48632.526404

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.
-20.732	-22.399	21.229	-10.75	-8.814	-0.072

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 : 0.000 / q_NPA : 0.009

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	2	GLU	-1	-0.818	-0.898	3.799	-3.320	-1.358	-0.005	-0.829	-1.129	0.005
4	A	3	SER	0	-0.061	-0.040	5.687	-0.196	-0.102	-0.001	-0.005	-0.089	0.000
5	A	4	VAL	0	0.056	0.028	9.089	0.041	0.041	0.000	0.000	0.000	0.000
6	A	5	LYS	1	0.909	0.953	11.633	-0.296	-0.296	0.000	0.000	0.000	0.000
7	A	6	ALA	0	0.000	0.011	15.276	0.014	0.014	0.000	0.000	0.000	0.000
8	A	7	MET	0	-0.017	-0.005	18.146	-0.055	-0.055	0.000	0.000	0.000	0.000
9	A	8	TRP	0	0.018	0.009	21.423	0.036	0.036	0.000	0.000	0.000	0.000
10	A	9	GLY	0	-0.001	0.000	24.424	-0.011	-0.011	0.000	0.000	0.000	0.000
11	A	10	VAL	0	-0.023	-0.018	25.168	-0.016	-0.016	0.000	0.000	0.000	0.000
12	A	11	VAL	0	-0.045	-0.014	28.485	0.017	0.017	0.000	0.000	0.000	0.000
13	A	12	THR	0	-0.019	-0.008	30.639	-0.011	-0.011	0.000	0.000	0.000	0.000
14	A	13	ASP	-1	-0.870	-0.941	34.001	0.133	0.133	0.000	0.000	0.000	0.000
15	A	14	SER	0	-0.044	-0.013	35.432	0.005	0.005	0.000	0.000	0.000	0.000
16	A	15	GLN	0	-0.039	-0.032	29.041	0.020	0.020	0.000	0.000	0.000	0.000
17	A	16	THR	0	0.039	0.027	27.650	-0.010	-0.010	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.751	-0.843	23.014	0.281	0.281	0.000	0.000	0.000	0.000
19	A	18	ILE	0	-0.013	-0.006	20.173	-0.015	-0.015	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.020	-0.010	18.375	0.025	0.025	0.000	0.000	0.000	0.000
21	A	20	ALA	0	-0.001	0.001	14.653	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	21	LEU	0	-0.016	-0.016	14.007	-0.005	-0.005	0.000	0.000	0.000	0.000
23	A	22	ALA	0	0.027	0.010	8.732	0.014	0.014	0.000	0.000	0.000	0.000
24	A	23	LYS	1	0.869	0.964	7.489	0.732	0.732	0.000	0.000	0.000	0.000
25	A	24	VAL	0	0.042	0.018	4.111	0.039	0.195	-0.001	-0.059	-0.096	0.000
26	A	25	ARG	1	0.867	0.910	2.705	4.194	5.867	0.186	-0.652	-1.207	0.002
27	A	26	ASN	0	-0.029	-0.023	1.745	-4.219	-13.039	18.015	-6.150	-3.045	-0.045
28	A	27	GLU	-1	-0.928	-0.980	2.646	-18.513	-15.245	3.036	-3.052	-3.252	-0.034
29	A	28	ASP	-1	-0.810	-0.877	4.939	0.150	0.150	-0.001	-0.003	0.004	0.000
30	A	29	VAL	0	-0.055	-0.050	7.740	-0.156	-0.156	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.025	-0.010	10.586	0.098	0.098	0.000	0.000	0.000	0.000
32	A	31	PRO	0	-0.049	-0.029	9.965	-0.094	-0.094	0.000	0.000	0.000	0.000
33	A	32	ILE	0	0.049	0.041	5.389	0.143	0.143	0.000	0.000	0.000	0.000
34	A	33	VAL	0	0.019	0.002	9.583	-0.143	-0.143	0.000	0.000	0.000	0.000
35	A	34	VAL	0	-0.010	0.003	9.723	0.173	0.173	0.000	0.000	0.000	0.000
36	A	35	SER	0	-0.013	-0.035	12.485	-0.083	-0.083	0.000	0.000	0.000	0.000
37	A	36	GLY	0	0.047	0.014	15.470	-0.088	-0.088	0.000	0.000	0.000	0.000
38	A	37	TYR	0	-0.024	0.005	14.901	0.145	0.145	0.000	0.000	0.000	0.000
39	A	38	HIS	0	0.013	0.008	16.736	-0.078	-0.078	0.000	0.000	0.000	0.000
40	A	39	TYR	0	-0.053	-0.022	17.491	0.092	0.092	0.000	0.000	0.000	0.000
41	A	40	THR	0	0.022	0.006	19.511	-0.051	-0.051	0.000	0.000	0.000	0.000
42	A	41	ILE	0	-0.039	-0.023	20.807	0.047	0.047	0.000	0.000	0.000	0.000
43	A	42	GLU	-1	-0.814	-0.896	23.321	0.348	0.348	0.000	0.000	0.000	0.000
44	A	43	MET	0	-0.027	-0.017	25.352	0.018	0.018	0.000	0.000	0.000	0.000
45	A	44	ASN	0	-0.001	-0.009	28.145	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	45	GLY	0	0.011	0.011	28.787	-0.014	-0.014	0.000	0.000	0.000	0.000
47	A	46	VAL	0	0.002	0.026	30.027	-0.007	-0.007	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.863	0.907	25.769	-0.331	-0.331	0.000	0.000	0.000	0.000
49	A	48	VAL	0	-0.004	-0.005	26.857	-0.013	-0.013	0.000	0.000	0.000	0.000
50	A	49	ALA	0	-0.027	-0.014	24.392	-0.014	-0.014	0.000	0.000	0.000	0.000
51	A	50	ASP	-1	-0.802	-0.898	24.145	0.418	0.418	0.000	0.000	0.000	0.000
52	A	51	GLY	0	-0.001	0.020	23.135	-0.038	-0.038	0.000	0.000	0.000	0.000
53	A	52	TYR	0	-0.017	-0.010	17.944	0.034	0.034	0.000	0.000	0.000	0.000
54	A	53	GLU	-1	-0.851	-0.902	19.908	0.283	0.283	0.000	0.000	0.000	0.000
55	A	54	ASN	0	-0.007	-0.009	19.749	0.056	0.056	0.000	0.000	0.000	0.000
56	A	55	SER	0	-0.027	-0.025	17.253	-0.043	-0.043	0.000	0.000	0.000	0.000
57	A	56	PRO	0	0.023	0.015	16.438	0.049	0.049	0.000	0.000	0.000	0.000
58	A	57	VAL	0	-0.037	-0.004	12.142	-0.079	-0.079	0.000	0.000	0.000	0.000
59	A	58	THR	0	-0.018	0.002	12.148	0.087	0.087	0.000	0.000	0.000	0.000
60	A	59	VAL	0	-0.037	-0.022	6.169	-0.079	-0.079	0.000	0.000	0.000	0.000
61	A	60	LYS	1	0.977	0.983	9.393	0.456	0.456	0.000	0.000	0.000	0.000
62	A	61	PRO	0	0.075	0.030	8.876	-0.200	-0.200	0.000	0.000	0.000	0.000
63	A	62	ALA	0	0.022	0.019	7.812	0.137	0.137	0.000	0.000	0.000	0.000
64	A	63	SER	0	-0.084	-0.023	8.405	0.021	0.021	0.000	0.000	0.000	0.000
65	A	64	ALA	0	0.026	0.004	6.580	-0.405	-0.405	0.000	0.000	0.000	0.000
66	A	65	THR	0	-0.038	-0.027	7.239	0.210	0.210	0.000	0.000	0.000	0.000
67	A	66	THR	0	-0.038	-0.022	8.403	0.035	0.035	0.000	0.000	0.000	0.000
68	A	67	LEU	0	0.022	0.018	8.549	-0.023	-0.023	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.915	0.954	11.675	-0.266	-0.266	0.000	0.000	0.000	0.000
70	A	69	PHE	0	-0.013	-0.005	10.903	0.024	0.024	0.000	0.000	0.000	0.000
71	A	70	SER	0	-0.081	-0.072	16.561	-0.031	-0.031	0.000	0.000	0.000	0.000
72	A	71	LEU	0	0.010	-0.006	17.468	0.019	0.019	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.856	0.913	21.534	-0.333	-0.333	0.000	0.000	0.000	0.000
74	A	73	LEU	0	0.025	0.001	24.755	0.014	0.014	0.000	0.000	0.000	0.000
75	A	74	ASN	0	0.044	0.019	27.784	-0.027	-0.027	0.000	0.000	0.000	0.000
76	A	75	ASN	0	0.072	0.011	31.198	0.000	0.000	0.000	0.000	0.000	0.000
77	A	76	SER	0	-0.008	0.003	33.627	-0.010	-0.010	0.000	0.000	0.000	0.000
78	A	77	PHE	0	0.040	0.025	31.667	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.012	0.009	29.338	0.004	0.004	0.000	0.000	0.000	0.000
80	A	79	ARG	1	0.888	0.934	32.947	-0.160	-0.160	0.000	0.000	0.000	0.000
81	A	80	GLU	-1	-0.920	-0.956	34.801	0.193	0.193	0.000	0.000	0.000	0.000
82	A	81	TRP	0	-0.009	-0.008	31.722	-0.001	-0.001	0.000	0.000	0.000	0.000
83	A	82	TRP	0	0.035	0.028	34.079	0.000	0.000	0.000	0.000	0.000	0.000
84	A	83	VAL	0	0.037	0.012	36.544	-0.005	-0.005	0.000	0.000	0.000	0.000
85	A	84	THR	0	-0.004	-0.021	34.099	0.000	0.000	0.000	0.000	0.000	0.000
86	A	85	HIS	0	-0.005	0.037	33.348	0.012	0.012	0.000	0.000	0.000	0.000
87	A	86	ILE	0	0.035	0.005	35.386	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	87	ALA	0	-0.020	0.003	38.556	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	88	ASN	0	-0.056	-0.018	35.206	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	89	GLY	0	-0.018	-0.004	36.732	0.004	0.004	0.000	0.000	0.000	0.000
91	A	90	GLU	-1	-0.825	-0.882	36.656	0.138	0.138	0.000	0.000	0.000	0.000
92	A	91	LYS	1	0.881	0.931	32.656	-0.174	-0.174	0.000	0.000	0.000	0.000
93	A	92	THR	0	0.003	-0.018	28.490	0.001	0.001	0.000	0.000	0.000	0.000
94	A	93	LYS	1	0.857	0.935	24.198	-0.376	-0.376	0.000	0.000	0.000	0.000
95	A	94	ILE	0	-0.003	-0.005	22.900	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	95	ARG	1	0.823	0.902	21.241	-0.375	-0.375	0.000	0.000	0.000	0.000
97	A	96	VAL	0	-0.001	0.004	17.564	-0.031	-0.031	0.000	0.000	0.000	0.000
98	A	97	ALA	0	0.006	0.001	16.535	0.082	0.082	0.000	0.000	0.000	0.000
99	A	98	ILE	0	-0.002	0.003	13.535	-0.089	-0.089	0.000	0.000	0.000	0.000
100	A	99	LYS	1	0.944	0.969	13.551	-0.585	-0.585	0.000	0.000	0.000	0.000
101	A	100	PRO	0	-0.009	-0.002	10.328	-0.149	-0.149	0.000	0.000	0.000	0.000
102	A	101	THR	0	0.015	0.002	13.325	0.082	0.082	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.017	-0.002	8.038	-0.016	-0.016	0.000	0.000	0.000	0.000
104	A	103	GLU	-1	-0.859	-0.926	12.004	0.349	0.349	0.000	0.000	0.000	0.000
105	A	104	ILE	0	0.014	0.001	8.892	-0.039	-0.039	0.000	0.000	0.000	0.000
106	A	105	GLY	0	0.087	0.045	13.601	-0.022	-0.022	0.000	0.000	0.000	0.000
107	A	106	GLY	0	-0.018	0.000	17.206	-0.035	-0.035	0.000	0.000	0.000	0.000
108	A	107	ARG	1	0.849	0.904	19.268	-0.270	-0.270	0.000	0.000	0.000	0.000
109	A	108	ASP	-1	-0.895	-0.927	17.730	0.297	0.297	0.000	0.000	0.000	0.000
110	A	109	VAL	0	-0.063	-0.040	15.173	0.025	0.025	0.000	0.000	0.000	0.000
111	A	110	GLU	-1	-0.893	-0.932	9.887	1.393	1.393	0.000	0.000	0.000	0.000
112	A	111	VAL	0	-0.079	-0.057	13.032	0.046	0.046	0.000	0.000	0.000	0.000
113	A	112	PRO	0	0.028	0.032	8.942	-0.124	-0.124	0.000	0.000	0.000	0.000
114	A	113	VAL	0	0.010	-0.018	11.829	-0.068	-0.068	0.000	0.000	0.000	0.000
115	A	114	PHE	0	-0.018	0.000	6.777	0.014	0.014	0.000	0.000	0.000	0.000
116	A	115	LEU	0	0.026	0.008	12.288	-0.164	-0.164	0.000	0.000	0.000	0.000
117	A	116	ARG	1	0.951	0.974	14.638	-0.501	-0.501	0.000	0.000	0.000	0.000
118	A	117	GLU	-1	-0.839	-0.915	16.777	0.416	0.416	0.000	0.000	0.000	0.000
119	A	118	SER	0	-0.108	-0.065	20.274	0.000	0.000	0.000	0.000	0.000	0.000
120	A	119	GLU	-1	-0.913	-0.970	22.771	0.268	0.268	0.000	0.000	0.000	0.000
121	A	120	PHE	0	-0.022	-0.001	26.525	-0.006	-0.006	0.000	0.000	0.000	0.000
122	A	121	THR	0	0.025	0.013	29.229	-0.010	-0.010	0.000	0.000	0.000	0.000
123	A	122	THR	0	-0.066	-0.049	32.952	0.003	0.003	0.000	0.000	0.000	0.000
124	A	123	LYS	1	0.925	0.938	34.830	-0.153	-0.153	0.000	0.000	0.000	0.000
125	A	124	LEU	0	-0.015	0.001	38.179	-0.006	-0.006	0.000	0.000	0.000	0.000
126	A	125	LEU	0	0.000	0.019	41.220	-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:0:SER)