FMO DATABASE

FMODB ID: R8VY8

Calculation Name: 3BCI-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3BCI

Chain ID: A

ChEMBL ID:

UniProt ID: Q9EYL5

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	165
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1821926.264299
FMO2-HF: Nuclear repulsion	1754680.904927
FMO2-HF: Total energy	-67245.359371
FMO2-MP2: Total energy	-67443.82848

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:14:GLY)

Summations of interaction energy for fragment #1(A:14: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.
0.117	1.09	-0.014	-0.457	-0.503	0.001

Interaction energy analysis for fragmet #1(A:14:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.007 / q_NPA : -0.019

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	16	PRO	0	0.019	0.002	3.784	1.031	2.004	-0.014	-0.457	-0.503	0.001
4	A	17	LEU	0	0.023	0.025	6.790	0.218	0.218	0.000	0.000	0.000	0.000
5	A	18	VAL	0	-0.012	-0.014	8.238	0.002	0.002	0.000	0.000	0.000	0.000
6	A	19	VAL	0	-0.006	-0.007	11.925	0.062	0.062	0.000	0.000	0.000	0.000
7	A	20	VAL	0	0.012	0.008	14.434	-0.035	-0.035	0.000	0.000	0.000	0.000
8	A	21	TYR	0	0.002	0.005	17.005	0.037	0.037	0.000	0.000	0.000	0.000
9	A	22	GLY	0	0.060	-0.016	20.791	-0.023	-0.023	0.000	0.000	0.000	0.000
10	A	23	ASP	-1	-0.759	-0.880	24.041	0.075	0.075	0.000	0.000	0.000	0.000
11	A	24	TYR	0	0.016	-0.032	23.377	-0.009	-0.009	0.000	0.000	0.000	0.000
12	A	25	LYS	1	0.735	0.870	28.116	-0.048	-0.048	0.000	0.000	0.000	0.000
13	A	26	CYS	0	-0.008	0.028	28.441	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	27	PRO	0	0.106	0.050	29.832	-0.004	-0.004	0.000	0.000	0.000	0.000
15	A	28	TYR	0	0.059	0.019	29.008	-0.004	-0.004	0.000	0.000	0.000	0.000
16	A	29	CYS	0	-0.070	-0.020	25.701	-0.003	-0.003	0.000	0.000	0.000	0.000
17	A	30	LYS	1	0.889	0.953	26.008	0.009	0.009	0.000	0.000	0.000	0.000
18	A	31	GLU	-1	-0.910	-0.958	28.100	-0.034	-0.034	0.000	0.000	0.000	0.000
19	A	32	LEU	0	-0.037	-0.006	20.970	-0.008	-0.008	0.000	0.000	0.000	0.000
20	A	33	ASP	-1	-0.896	-0.965	23.502	-0.042	-0.042	0.000	0.000	0.000	0.000
21	A	34	GLU	-1	-0.867	-0.943	24.575	-0.041	-0.041	0.000	0.000	0.000	0.000
22	A	35	LYS	1	0.905	0.954	26.439	0.046	0.046	0.000	0.000	0.000	0.000
23	A	36	VAL	0	-0.031	-0.002	20.035	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	37	MET	0	-0.009	0.007	17.723	-0.030	-0.030	0.000	0.000	0.000	0.000
25	A	38	PRO	0	-0.028	-0.001	20.738	-0.017	-0.017	0.000	0.000	0.000	0.000
26	A	39	LYS	1	0.960	0.972	21.548	0.141	0.141	0.000	0.000	0.000	0.000
27	A	40	LEU	0	0.052	0.038	15.258	-0.031	-0.031	0.000	0.000	0.000	0.000
28	A	41	ARG	1	0.804	0.881	16.538	0.031	0.031	0.000	0.000	0.000	0.000
29	A	42	LYS	1	0.943	0.977	17.427	0.147	0.147	0.000	0.000	0.000	0.000
30	A	43	ASN	0	-0.033	-0.025	17.479	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	44	TYR	0	0.024	0.015	11.975	-0.044	-0.044	0.000	0.000	0.000	0.000
32	A	45	ILE	0	0.029	0.027	12.231	-0.058	-0.058	0.000	0.000	0.000	0.000
33	A	46	ASP	-1	-0.795	-0.894	13.467	-0.099	-0.099	0.000	0.000	0.000	0.000
34	A	47	ASN	0	-0.152	-0.076	14.010	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	48	HIS	0	-0.031	-0.029	10.219	-0.046	-0.046	0.000	0.000	0.000	0.000
36	A	49	LYS	1	0.931	0.979	9.115	0.533	0.533	0.000	0.000	0.000	0.000
37	A	50	VAL	0	-0.018	-0.006	7.639	-0.466	-0.466	0.000	0.000	0.000	0.000
38	A	51	GLU	-1	-0.923	-0.951	5.923	0.646	0.646	0.000	0.000	0.000	0.000
39	A	52	TYR	0	-0.024	-0.027	8.723	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	53	GLN	0	-0.011	-0.009	12.293	0.113	0.113	0.000	0.000	0.000	0.000
41	A	54	PHE	0	-0.027	-0.007	14.092	-0.026	-0.026	0.000	0.000	0.000	0.000
42	A	55	VAL	0	-0.022	-0.002	16.913	0.027	0.027	0.000	0.000	0.000	0.000
43	A	56	ASN	0	-0.001	-0.016	19.424	-0.026	-0.026	0.000	0.000	0.000	0.000
44	A	57	LEU	0	0.021	-0.011	23.127	0.012	0.012	0.000	0.000	0.000	0.000
45	A	58	ALA	0	-0.074	-0.045	25.498	0.000	0.000	0.000	0.000	0.000	0.000
46	A	59	PHE	0	-0.017	-0.028	27.956	0.003	0.003	0.000	0.000	0.000	0.000
47	A	60	LEU	0	0.015	0.038	30.887	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	61	GLY	0	0.104	0.056	33.352	-0.005	-0.005	0.000	0.000	0.000	0.000
49	A	62	LYS	1	0.878	0.940	33.815	-0.049	-0.049	0.000	0.000	0.000	0.000
50	A	63	ASP	-1	-0.774	-0.880	34.549	0.050	0.050	0.000	0.000	0.000	0.000
51	A	64	SER	0	0.028	0.024	29.949	0.000	0.000	0.000	0.000	0.000	0.000
52	A	65	ILE	0	-0.017	-0.009	27.498	0.004	0.004	0.000	0.000	0.000	0.000
53	A	66	VAL	0	-0.056	-0.028	28.947	0.008	0.008	0.000	0.000	0.000	0.000
54	A	67	GLY	0	0.072	0.031	29.485	0.002	0.002	0.000	0.000	0.000	0.000
55	A	68	SER	0	-0.015	-0.006	24.664	0.003	0.003	0.000	0.000	0.000	0.000
56	A	69	ARG	1	0.938	0.983	24.829	-0.091	-0.091	0.000	0.000	0.000	0.000
57	A	70	ALA	0	0.032	0.011	25.896	0.007	0.007	0.000	0.000	0.000	0.000
58	A	71	SER	0	0.047	0.051	22.338	-0.005	-0.005	0.000	0.000	0.000	0.000
59	A	72	HIS	0	-0.041	-0.037	18.843	0.007	0.007	0.000	0.000	0.000	0.000
60	A	73	ALA	0	-0.013	-0.010	21.748	0.013	0.013	0.000	0.000	0.000	0.000
61	A	74	VAL	0	0.007	-0.003	22.764	0.004	0.004	0.000	0.000	0.000	0.000
62	A	75	LEU	0	-0.020	0.009	16.044	-0.003	-0.003	0.000	0.000	0.000	0.000
63	A	76	MET	0	-0.071	-0.035	18.887	0.009	0.009	0.000	0.000	0.000	0.000
64	A	77	TYR	0	-0.116	-0.089	19.953	0.010	0.010	0.000	0.000	0.000	0.000
65	A	78	ALA	0	0.013	0.011	21.982	-0.008	-0.008	0.000	0.000	0.000	0.000
66	A	79	PRO	0	0.064	0.040	16.938	-0.018	-0.018	0.000	0.000	0.000	0.000
67	A	80	LYS	1	0.928	0.953	18.563	-0.008	-0.008	0.000	0.000	0.000	0.000
68	A	81	SER	0	0.047	0.026	19.999	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	82	PHE	0	-0.016	-0.002	18.019	-0.002	-0.002	0.000	0.000	0.000	0.000
70	A	83	LEU	0	0.068	0.029	17.058	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	84	ASP	-1	-0.888	-0.923	21.113	-0.035	-0.035	0.000	0.000	0.000	0.000
72	A	85	PHE	0	-0.004	-0.006	24.134	0.001	0.001	0.000	0.000	0.000	0.000
73	A	86	GLN	0	0.016	0.014	20.228	-0.011	-0.011	0.000	0.000	0.000	0.000
74	A	87	LYS	1	1.009	1.012	24.387	0.045	0.045	0.000	0.000	0.000	0.000
75	A	88	GLN	0	-0.036	-0.040	26.136	0.004	0.004	0.000	0.000	0.000	0.000
76	A	89	LEU	0	-0.047	-0.013	27.304	0.001	0.001	0.000	0.000	0.000	0.000
77	A	90	PHE	0	0.035	0.008	23.867	0.003	0.003	0.000	0.000	0.000	0.000
78	A	91	ALA	0	-0.025	-0.010	29.218	-0.001	-0.001	0.000	0.000	0.000	0.000
79	A	92	ALA	0	-0.051	-0.019	31.889	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	93	GLN	0	-0.063	-0.055	30.627	0.000	0.000	0.000	0.000	0.000	0.000
81	A	94	GLN	0	-0.057	-0.023	34.026	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	95	ASP	-1	-0.836	-0.935	36.508	0.016	0.016	0.000	0.000	0.000	0.000
83	A	96	GLU	-1	-0.904	-0.964	35.287	0.025	0.025	0.000	0.000	0.000	0.000
84	A	97	ASN	0	-0.034	-0.010	36.775	0.007	0.007	0.000	0.000	0.000	0.000
85	A	98	LYS	1	0.899	0.959	39.320	-0.016	-0.016	0.000	0.000	0.000	0.000
86	A	99	GLU	-1	-0.927	-0.976	37.612	0.045	0.045	0.000	0.000	0.000	0.000
87	A	100	TRP	0	0.019	0.002	31.608	0.001	0.001	0.000	0.000	0.000	0.000
88	A	101	LEU	0	-0.012	0.014	30.910	0.000	0.000	0.000	0.000	0.000	0.000
89	A	102	THR	0	0.040	0.009	34.641	0.006	0.006	0.000	0.000	0.000	0.000
90	A	103	LYS	1	0.976	0.960	35.118	-0.062	-0.062	0.000	0.000	0.000	0.000
91	A	104	GLU	-1	-0.945	-0.944	36.100	0.027	0.027	0.000	0.000	0.000	0.000
92	A	105	LEU	0	0.010	0.009	33.651	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	106	LEU	0	0.028	0.002	30.200	-0.001	-0.001	0.000	0.000	0.000	0.000
94	A	107	ASP	-1	-0.751	-0.853	32.375	0.052	0.052	0.000	0.000	0.000	0.000
95	A	108	LYS	1	0.916	0.973	34.212	-0.018	-0.018	0.000	0.000	0.000	0.000
96	A	109	HIS	0	-0.020	-0.020	30.630	-0.004	-0.004	0.000	0.000	0.000	0.000
97	A	110	ILE	0	-0.013	-0.011	28.972	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	111	LYS	1	0.924	0.962	30.703	-0.035	-0.035	0.000	0.000	0.000	0.000
99	A	112	GLN	0	-0.065	-0.017	32.237	-0.003	-0.003	0.000	0.000	0.000	0.000
100	A	113	LEU	0	-0.056	-0.020	26.175	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	114	HIS	0	-0.047	-0.011	29.525	-0.001	-0.001	0.000	0.000	0.000	0.000
102	A	115	LEU	0	0.007	0.012	26.276	0.000	0.000	0.000	0.000	0.000	0.000
103	A	116	ASP	-1	-0.786	-0.830	29.384	0.050	0.050	0.000	0.000	0.000	0.000
104	A	117	LYS	1	1.002	0.979	31.566	-0.030	-0.030	0.000	0.000	0.000	0.000
105	A	118	GLU	-1	-0.876	-0.944	32.349	0.057	0.057	0.000	0.000	0.000	0.000
106	A	119	THR	0	-0.116	-0.117	26.503	0.011	0.011	0.000	0.000	0.000	0.000
107	A	120	GLU	-1	-0.883	-0.952	29.132	0.043	0.043	0.000	0.000	0.000	0.000
108	A	121	ASN	0	0.010	-0.012	31.082	0.002	0.002	0.000	0.000	0.000	0.000
109	A	122	LYS	1	0.898	0.970	25.797	-0.098	-0.098	0.000	0.000	0.000	0.000
110	A	123	ILE	0	-0.006	-0.001	25.811	0.009	0.009	0.000	0.000	0.000	0.000
111	A	124	ILE	0	-0.016	-0.010	28.546	0.004	0.004	0.000	0.000	0.000	0.000
112	A	125	LYS	1	0.952	0.984	31.862	-0.093	-0.093	0.000	0.000	0.000	0.000
113	A	126	ASP	-1	-0.811	-0.865	26.681	0.140	0.140	0.000	0.000	0.000	0.000
114	A	127	TYR	0	0.026	0.023	28.367	0.004	0.004	0.000	0.000	0.000	0.000
115	A	128	LYS	1	0.728	0.855	29.408	-0.059	-0.059	0.000	0.000	0.000	0.000
116	A	129	THR	0	-0.066	-0.049	31.457	-0.005	-0.005	0.000	0.000	0.000	0.000
117	A	130	LYS	1	0.974	0.974	31.129	-0.092	-0.092	0.000	0.000	0.000	0.000
118	A	131	ASP	-1	-0.935	-0.968	29.344	0.130	0.130	0.000	0.000	0.000	0.000
119	A	132	SER	0	-0.003	-0.008	28.102	0.012	0.012	0.000	0.000	0.000	0.000
120	A	133	LYS	1	0.982	0.966	21.943	-0.188	-0.188	0.000	0.000	0.000	0.000
121	A	134	SER	0	0.016	-0.003	23.310	0.011	0.011	0.000	0.000	0.000	0.000
122	A	135	TRP	0	-0.019	0.002	24.516	-0.006	-0.006	0.000	0.000	0.000	0.000
123	A	136	LYS	1	0.930	0.952	24.131	-0.180	-0.180	0.000	0.000	0.000	0.000
124	A	137	ALA	0	-0.007	0.014	20.573	0.009	0.009	0.000	0.000	0.000	0.000
125	A	138	ALA	0	0.032	0.018	21.998	0.003	0.003	0.000	0.000	0.000	0.000
126	A	139	GLU	-1	-0.942	-0.977	24.374	0.123	0.123	0.000	0.000	0.000	0.000
127	A	140	LYS	1	0.912	0.953	16.752	-0.407	-0.407	0.000	0.000	0.000	0.000
128	A	141	ASP	-1	-0.750	-0.860	19.609	0.215	0.215	0.000	0.000	0.000	0.000
129	A	142	LYS	1	0.954	0.976	21.495	-0.114	-0.114	0.000	0.000	0.000	0.000
130	A	143	LYS	1	0.812	0.896	21.379	-0.272	-0.272	0.000	0.000	0.000	0.000
131	A	144	ILE	0	-0.010	0.001	16.709	0.011	0.011	0.000	0.000	0.000	0.000
132	A	145	ALA	0	0.060	0.035	20.069	0.004	0.004	0.000	0.000	0.000	0.000
133	A	146	LYS	1	0.932	0.975	21.898	-0.146	-0.146	0.000	0.000	0.000	0.000
134	A	147	ASP	-1	-0.847	-0.916	20.755	0.230	0.230	0.000	0.000	0.000	0.000
135	A	148	ASN	0	-0.092	-0.045	16.952	0.021	0.021	0.000	0.000	0.000	0.000
136	A	149	HIS	0	-0.031	-0.010	20.412	-0.031	-0.031	0.000	0.000	0.000	0.000
137	A	150	ILE	0	-0.018	0.000	19.708	-0.019	-0.019	0.000	0.000	0.000	0.000
138	A	151	LYS	1	0.924	0.962	23.644	-0.050	-0.050	0.000	0.000	0.000	0.000
139	A	152	THR	0	-0.001	-0.006	26.501	0.001	0.001	0.000	0.000	0.000	0.000
140	A	153	THR	0	-0.025	0.020	24.459	0.007	0.007	0.000	0.000	0.000	0.000
141	A	154	PRO	0	0.040	-0.012	23.654	0.000	0.000	0.000	0.000	0.000	0.000
142	A	155	THR	0	-0.039	-0.025	21.605	-0.004	-0.004	0.000	0.000	0.000	0.000
143	A	156	ALA	0	0.016	0.008	17.526	0.016	0.016	0.000	0.000	0.000	0.000
144	A	157	PHE	0	-0.012	-0.009	14.952	-0.004	-0.004	0.000	0.000	0.000	0.000
145	A	158	ILE	0	0.029	0.013	10.534	0.014	0.014	0.000	0.000	0.000	0.000
146	A	159	ASN	0	0.016	0.008	6.437	0.257	0.257	0.000	0.000	0.000	0.000
147	A	160	GLY	0	-0.015	-0.011	9.810	0.036	0.036	0.000	0.000	0.000	0.000
148	A	161	GLU	-1	-0.883	-0.918	12.969	-0.106	-0.106	0.000	0.000	0.000	0.000
149	A	162	LYS	1	0.865	0.929	14.871	0.026	0.026	0.000	0.000	0.000	0.000
150	A	163	VAL	0	0.006	0.007	16.799	-0.027	-0.027	0.000	0.000	0.000	0.000
151	A	164	GLU	-1	-0.946	-0.986	18.910	-0.120	-0.120	0.000	0.000	0.000	0.000
152	A	165	ASP	-1	-0.810	-0.912	22.204	-0.063	-0.063	0.000	0.000	0.000	0.000
153	A	166	PRO	0	-0.060	-0.026	21.437	-0.014	-0.014	0.000	0.000	0.000	0.000
154	A	167	TYR	0	0.013	0.001	22.456	0.005	0.005	0.000	0.000	0.000	0.000
155	A	168	ASP	-1	-0.826	-0.915	24.000	-0.145	-0.145	0.000	0.000	0.000	0.000
156	A	169	TYR	0	-0.024	-0.024	18.130	-0.020	-0.020	0.000	0.000	0.000	0.000
157	A	170	GLU	-1	-0.915	-0.963	20.036	-0.209	-0.209	0.000	0.000	0.000	0.000
158	A	171	SER	0	0.026	0.017	20.284	-0.016	-0.016	0.000	0.000	0.000	0.000
159	A	172	TYR	0	-0.109	-0.084	16.133	-0.007	-0.007	0.000	0.000	0.000	0.000
160	A	173	GLU	-1	-0.917	-0.973	15.769	-0.381	-0.381	0.000	0.000	0.000	0.000
161	A	174	LYS	1	0.899	0.951	16.252	0.135	0.135	0.000	0.000	0.000	0.000
162	A	175	LEU	0	0.020	0.008	13.557	-0.027	-0.027	0.000	0.000	0.000	0.000
163	A	176	LEU	0	-0.065	-0.029	10.819	-0.104	-0.104	0.000	0.000	0.000	0.000
164	A	177	LYS	1	0.811	0.937	11.937	0.289	0.289	0.000	0.000	0.000	0.000
165	A	178	ASP	-1	-0.924	-0.954	9.604	-0.657	-0.657	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:14:GLY)