FMO DATABASE

FMODB ID: NNJZQ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-988706.108312
FMO2-HF: Nuclear repulsion	940217.955451
FMO2-HF: Total energy	-48488.152861
FMO2-MP2: Total energy	-48631.818177

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.
-14.954	-13.664	16.281	-8.738	-8.832	-0.05

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 : 0.071 / q_NPA : 0.050

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	-0.890	-0.952	3.418	-8.298	-5.049	0.013	-1.592	-1.670	0.006
4	A	3	SER	0	-0.107	-0.061	5.267	0.426	0.508	-0.001	-0.004	-0.077	0.000
5	A	4	VAL	0	0.057	0.021	8.861	-0.101	-0.101	0.000	0.000	0.000	0.000
6	A	5	LYS	1	0.927	0.961	11.633	0.425	0.425	0.000	0.000	0.000	0.000
7	A	6	ALA	0	-0.001	0.013	15.262	-0.009	-0.009	0.000	0.000	0.000	0.000
8	A	7	MET	0	-0.022	-0.007	18.146	-0.025	-0.025	0.000	0.000	0.000	0.000
9	A	8	TRP	0	0.021	0.011	21.400	0.024	0.024	0.000	0.000	0.000	0.000
10	A	9	GLY	0	0.004	0.002	24.126	-0.024	-0.024	0.000	0.000	0.000	0.000
11	A	10	VAL	0	-0.019	-0.013	24.689	0.002	0.002	0.000	0.000	0.000	0.000
12	A	11	VAL	0	-0.052	-0.016	27.884	0.015	0.015	0.000	0.000	0.000	0.000
13	A	12	THR	0	-0.036	-0.016	30.156	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	13	ASP	-1	-0.898	-0.962	33.428	0.012	0.012	0.000	0.000	0.000	0.000
15	A	14	SER	0	-0.036	0.009	34.348	0.007	0.007	0.000	0.000	0.000	0.000
16	A	15	GLN	0	-0.002	-0.019	28.591	0.003	0.003	0.000	0.000	0.000	0.000
17	A	16	THR	0	0.025	0.013	27.142	-0.009	-0.009	0.000	0.000	0.000	0.000
18	A	17	GLU	-1	-0.814	-0.897	22.574	-0.035	-0.035	0.000	0.000	0.000	0.000
19	A	18	ILE	0	-0.014	-0.004	20.085	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	19	VAL	0	-0.011	-0.005	17.799	0.007	0.007	0.000	0.000	0.000	0.000
21	A	20	ALA	0	-0.002	0.002	14.500	-0.002	-0.002	0.000	0.000	0.000	0.000
22	A	21	LEU	0	-0.017	-0.020	13.523	-0.036	-0.036	0.000	0.000	0.000	0.000
23	A	22	ALA	0	0.037	0.013	8.380	0.035	0.035	0.000	0.000	0.000	0.000
24	A	23	LYS	1	0.903	0.980	7.616	1.602	1.602	0.000	0.000	0.000	0.000
25	A	24	VAL	0	0.042	0.020	3.599	-0.137	0.058	0.001	-0.071	-0.125	0.000
26	A	25	ARG	1	0.956	0.973	2.814	5.155	6.709	0.129	-0.625	-1.058	0.002
27	A	26	ASN	0	-0.036	-0.028	1.897	-3.327	-9.332	12.296	-3.686	-2.605	-0.029
28	A	27	GLU	-1	-0.944	-0.982	2.465	-12.274	-10.071	3.844	-2.757	-3.290	-0.029
29	A	28	ASP	-1	-0.816	-0.882	4.988	1.124	1.136	-0.001	-0.003	-0.007	0.000
30	A	29	VAL	0	-0.071	-0.053	8.034	-0.438	-0.438	0.000	0.000	0.000	0.000
31	A	30	VAL	0	-0.013	-0.005	10.707	-0.076	-0.076	0.000	0.000	0.000	0.000
32	A	31	PRO	0	-0.045	-0.031	9.945	-0.067	-0.067	0.000	0.000	0.000	0.000
33	A	32	ILE	0	0.051	0.045	4.990	0.054	0.054	0.000	0.000	0.000	0.000
34	A	33	VAL	0	0.020	-0.001	9.142	-0.235	-0.235	0.000	0.000	0.000	0.000
35	A	34	VAL	0	-0.014	0.000	8.928	0.147	0.147	0.000	0.000	0.000	0.000
36	A	35	SER	0	0.021	0.007	11.615	-0.070	-0.070	0.000	0.000	0.000	0.000
37	A	36	GLY	0	0.074	0.031	14.541	-0.042	-0.042	0.000	0.000	0.000	0.000
38	A	37	TYR	0	-0.051	-0.008	13.987	0.070	0.070	0.000	0.000	0.000	0.000
39	A	38	HIS	0	0.008	0.010	15.832	-0.042	-0.042	0.000	0.000	0.000	0.000
40	A	39	TYR	0	-0.040	-0.017	17.189	0.043	0.043	0.000	0.000	0.000	0.000
41	A	40	THR	0	-0.020	-0.006	19.302	-0.020	-0.020	0.000	0.000	0.000	0.000
42	A	41	ILE	0	-0.004	-0.013	20.805	0.022	0.022	0.000	0.000	0.000	0.000
43	A	42	GLU	-1	-0.900	-0.953	23.316	0.238	0.238	0.000	0.000	0.000	0.000
44	A	43	MET	0	-0.018	-0.018	25.343	0.007	0.007	0.000	0.000	0.000	0.000
45	A	44	ASN	0	-0.007	-0.021	28.142	0.003	0.003	0.000	0.000	0.000	0.000
46	A	45	GLY	0	0.022	0.012	28.841	-0.005	-0.005	0.000	0.000	0.000	0.000
47	A	46	VAL	0	0.009	0.037	30.020	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	47	LYS	1	0.964	0.975	25.811	-0.209	-0.209	0.000	0.000	0.000	0.000
49	A	48	VAL	0	-0.001	-0.006	26.869	-0.011	-0.011	0.000	0.000	0.000	0.000
50	A	49	ALA	0	-0.030	-0.020	24.379	-0.018	-0.018	0.000	0.000	0.000	0.000
51	A	50	ASP	-1	-0.883	-0.959	24.014	0.244	0.244	0.000	0.000	0.000	0.000
52	A	51	GLY	0	-0.001	0.021	22.788	-0.021	-0.021	0.000	0.000	0.000	0.000
53	A	52	TYR	0	-0.021	-0.011	17.576	0.013	0.013	0.000	0.000	0.000	0.000
54	A	53	GLU	-1	-0.923	-0.965	18.894	-0.042	-0.042	0.000	0.000	0.000	0.000
55	A	54	ASN	0	-0.006	-0.005	18.780	0.028	0.028	0.000	0.000	0.000	0.000
56	A	55	SER	0	-0.022	-0.032	16.412	-0.022	-0.022	0.000	0.000	0.000	0.000
57	A	56	PRO	0	0.020	0.029	15.679	-0.015	-0.015	0.000	0.000	0.000	0.000
58	A	57	VAL	0	-0.029	-0.001	11.363	-0.060	-0.060	0.000	0.000	0.000	0.000
59	A	58	THR	0	-0.016	-0.003	11.716	0.019	0.019	0.000	0.000	0.000	0.000
60	A	59	VAL	0	-0.024	-0.006	6.281	-0.107	-0.107	0.000	0.000	0.000	0.000
61	A	60	LYS	1	0.970	0.973	9.331	0.778	0.778	0.000	0.000	0.000	0.000
62	A	61	PRO	0	0.068	0.029	8.953	-0.325	-0.325	0.000	0.000	0.000	0.000
63	A	62	ALA	0	0.025	0.028	7.654	0.031	0.031	0.000	0.000	0.000	0.000
64	A	63	SER	0	-0.067	-0.029	8.467	-0.129	-0.129	0.000	0.000	0.000	0.000
65	A	64	ALA	0	-0.011	-0.013	6.750	-0.603	-0.603	0.000	0.000	0.000	0.000
66	A	65	THR	0	-0.019	-0.012	7.484	0.502	0.502	0.000	0.000	0.000	0.000
67	A	66	THR	0	-0.052	-0.029	8.343	-0.286	-0.286	0.000	0.000	0.000	0.000
68	A	67	LEU	0	0.022	0.014	7.668	0.121	0.121	0.000	0.000	0.000	0.000
69	A	68	LYS	1	0.971	0.984	11.167	0.173	0.173	0.000	0.000	0.000	0.000
70	A	69	PHE	0	-0.004	0.001	10.020	0.038	0.038	0.000	0.000	0.000	0.000
71	A	70	SER	0	-0.092	-0.070	15.739	0.001	0.001	0.000	0.000	0.000	0.000
72	A	71	LEU	0	0.012	-0.002	17.152	0.031	0.031	0.000	0.000	0.000	0.000
73	A	72	ARG	1	0.927	0.974	21.065	-0.031	-0.031	0.000	0.000	0.000	0.000
74	A	73	LEU	0	0.031	0.003	24.796	0.019	0.019	0.000	0.000	0.000	0.000
75	A	74	ASN	0	0.037	0.013	27.539	-0.010	-0.010	0.000	0.000	0.000	0.000
76	A	75	ASN	0	0.080	0.013	30.876	0.003	0.003	0.000	0.000	0.000	0.000
77	A	76	SER	0	-0.054	-0.024	33.469	-0.001	-0.001	0.000	0.000	0.000	0.000
78	A	77	PHE	0	0.065	0.045	31.540	0.001	0.001	0.000	0.000	0.000	0.000
79	A	78	LEU	0	0.007	0.006	29.835	0.006	0.006	0.000	0.000	0.000	0.000
80	A	79	ARG	1	0.910	0.948	32.941	-0.061	-0.061	0.000	0.000	0.000	0.000
81	A	80	GLU	-1	-0.903	-0.945	34.800	0.106	0.106	0.000	0.000	0.000	0.000
82	A	81	TRP	0	-0.006	-0.010	31.615	0.000	0.000	0.000	0.000	0.000	0.000
83	A	82	TRP	0	0.023	0.026	34.070	0.003	0.003	0.000	0.000	0.000	0.000
84	A	83	VAL	0	0.036	0.015	36.533	-0.001	-0.001	0.000	0.000	0.000	0.000
85	A	84	THR	0	-0.003	-0.032	34.107	0.003	0.003	0.000	0.000	0.000	0.000
86	A	85	HIS	0	-0.002	0.037	33.274	0.012	0.012	0.000	0.000	0.000	0.000
87	A	86	ILE	0	0.032	0.005	35.371	0.000	0.000	0.000	0.000	0.000	0.000
88	A	87	ALA	0	-0.024	0.000	38.528	-0.001	-0.001	0.000	0.000	0.000	0.000
89	A	88	ASN	0	-0.072	-0.025	35.171	0.003	0.003	0.000	0.000	0.000	0.000
90	A	89	GLY	0	-0.034	-0.022	36.714	0.003	0.003	0.000	0.000	0.000	0.000
91	A	90	GLU	-1	-0.835	-0.909	36.626	0.059	0.059	0.000	0.000	0.000	0.000
92	A	91	LYS	1	0.930	0.975	32.639	-0.112	-0.112	0.000	0.000	0.000	0.000
93	A	92	THR	0	0.007	-0.016	28.444	0.004	0.004	0.000	0.000	0.000	0.000
94	A	93	LYS	1	0.941	0.981	24.500	-0.253	-0.253	0.000	0.000	0.000	0.000
95	A	94	ILE	0	0.011	0.004	22.769	-0.002	-0.002	0.000	0.000	0.000	0.000
96	A	95	ARG	1	0.843	0.920	21.227	-0.241	-0.241	0.000	0.000	0.000	0.000
97	A	96	VAL	0	0.004	0.009	17.550	-0.028	-0.028	0.000	0.000	0.000	0.000
98	A	97	ALA	0	0.013	0.006	16.531	0.068	0.068	0.000	0.000	0.000	0.000
99	A	98	ILE	0	-0.007	0.002	13.132	-0.076	-0.076	0.000	0.000	0.000	0.000
100	A	99	LYS	1	0.951	0.971	13.556	-0.379	-0.379	0.000	0.000	0.000	0.000
101	A	100	PRO	0	-0.005	-0.002	9.850	-0.113	-0.113	0.000	0.000	0.000	0.000
102	A	101	THR	0	-0.001	-0.003	12.601	0.116	0.116	0.000	0.000	0.000	0.000
103	A	102	ILE	0	-0.009	0.001	7.428	-0.128	-0.128	0.000	0.000	0.000	0.000
104	A	103	GLU	-1	-0.906	-0.975	11.253	0.247	0.247	0.000	0.000	0.000	0.000
105	A	104	ILE	0	0.013	0.002	8.736	-0.096	-0.096	0.000	0.000	0.000	0.000
106	A	105	GLY	0	0.077	0.040	13.309	0.033	0.033	0.000	0.000	0.000	0.000
107	A	106	GLY	0	-0.035	-0.015	16.703	-0.036	-0.036	0.000	0.000	0.000	0.000
108	A	107	ARG	1	0.878	0.925	18.684	-0.195	-0.195	0.000	0.000	0.000	0.000
109	A	108	ASP	-1	-0.909	-0.934	17.543	0.344	0.344	0.000	0.000	0.000	0.000
110	A	109	VAL	0	-0.052	-0.032	14.648	0.000	0.000	0.000	0.000	0.000	0.000
111	A	110	GLU	-1	-0.898	-0.940	9.920	1.735	1.735	0.000	0.000	0.000	0.000
112	A	111	VAL	0	-0.070	-0.047	12.431	-0.061	-0.061	0.000	0.000	0.000	0.000
113	A	112	PRO	0	0.016	0.029	8.982	-0.070	-0.070	0.000	0.000	0.000	0.000
114	A	113	VAL	0	0.013	-0.018	11.844	-0.157	-0.157	0.000	0.000	0.000	0.000
115	A	114	PHE	0	-0.015	0.000	6.955	0.037	0.037	0.000	0.000	0.000	0.000
116	A	115	LEU	0	0.031	0.005	12.285	-0.161	-0.161	0.000	0.000	0.000	0.000
117	A	116	ARG	1	0.954	0.978	14.624	-0.232	-0.232	0.000	0.000	0.000	0.000
118	A	117	GLU	-1	-0.935	-0.966	16.762	0.355	0.355	0.000	0.000	0.000	0.000
119	A	118	SER	0	-0.091	-0.048	20.254	-0.014	-0.014	0.000	0.000	0.000	0.000
120	A	119	GLU	-1	-0.947	-0.986	22.751	0.176	0.176	0.000	0.000	0.000	0.000
121	A	120	PHE	0	-0.024	-0.003	26.505	-0.012	-0.012	0.000	0.000	0.000	0.000
122	A	121	THR	0	0.011	0.003	29.208	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	122	THR	0	-0.054	-0.030	32.930	-0.004	-0.004	0.000	0.000	0.000	0.000
124	A	123	LYS	1	0.950	0.960	35.331	-0.062	-0.062	0.000	0.000	0.000	0.000
125	A	124	LEU	0	-0.018	0.001	37.993	-0.006	-0.006	0.000	0.000	0.000	0.000
126	A	125	LEU	0	0.007	0.023	41.200	-0.006	-0.006	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:0:SER)