FMO DATABASE

FMODB ID: QVJNY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1824029.770302
FMO2-HF: Nuclear repulsion	1756783.461165
FMO2-HF: Total energy	-67246.309136
FMO2-MP2: Total energy	-67444.915561

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.
-3.31	-1.379	-0.017	-1.103	-0.81	0.006

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 : 0.018 / 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

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	0.013	0.001	3.784	-1.052	0.879	-0.017	-1.103	-0.810	0.006
4	A	17	LEU	0	0.006	0.017	6.790	0.478	0.478	0.000	0.000	0.000	0.000
5	A	18	VAL	0	-0.011	-0.015	8.235	0.135	0.135	0.000	0.000	0.000	0.000
6	A	19	VAL	0	-0.008	-0.009	11.922	0.123	0.123	0.000	0.000	0.000	0.000
7	A	20	VAL	0	0.012	0.006	14.431	-0.003	-0.003	0.000	0.000	0.000	0.000
8	A	21	TYR	0	0.011	0.010	16.442	0.060	0.060	0.000	0.000	0.000	0.000
9	A	22	GLY	0	0.065	-0.015	20.789	-0.007	-0.007	0.000	0.000	0.000	0.000
10	A	23	ASP	-1	-0.753	-0.875	24.039	-0.074	-0.074	0.000	0.000	0.000	0.000
11	A	24	TYR	0	0.014	-0.002	23.392	-0.011	-0.011	0.000	0.000	0.000	0.000
12	A	25	LYS	1	0.734	0.871	28.113	0.062	0.062	0.000	0.000	0.000	0.000
13	A	26	CYS	0	0.023	0.043	28.412	0.000	0.000	0.000	0.000	0.000	0.000
14	A	27	PRO	0	0.093	0.053	29.829	-0.012	-0.012	0.000	0.000	0.000	0.000
15	A	28	TYR	0	0.035	0.013	29.075	-0.006	-0.006	0.000	0.000	0.000	0.000
16	A	29	CYS	0	-0.078	-0.038	25.638	-0.019	-0.019	0.000	0.000	0.000	0.000
17	A	30	LYS	1	0.849	0.925	26.005	0.117	0.117	0.000	0.000	0.000	0.000
18	A	31	GLU	-1	-0.849	-0.915	28.097	-0.171	-0.171	0.000	0.000	0.000	0.000
19	A	32	LEU	0	-0.025	-0.004	20.959	-0.007	-0.007	0.000	0.000	0.000	0.000
20	A	33	ASP	-1	-0.890	-0.961	23.494	-0.227	-0.227	0.000	0.000	0.000	0.000
21	A	34	GLU	-1	-0.830	-0.916	24.571	-0.156	-0.156	0.000	0.000	0.000	0.000
22	A	35	LYS	1	0.840	0.914	26.383	0.191	0.191	0.000	0.000	0.000	0.000
23	A	36	VAL	0	-0.044	-0.012	19.985	-0.016	-0.016	0.000	0.000	0.000	0.000
24	A	37	MET	0	-0.002	0.008	17.673	-0.048	-0.048	0.000	0.000	0.000	0.000
25	A	38	PRO	0	-0.013	0.006	20.735	-0.018	-0.018	0.000	0.000	0.000	0.000
26	A	39	LYS	1	0.908	0.958	21.500	0.309	0.309	0.000	0.000	0.000	0.000
27	A	40	LEU	0	0.046	0.028	15.135	-0.031	-0.031	0.000	0.000	0.000	0.000
28	A	41	ARG	1	0.821	0.879	16.535	0.152	0.152	0.000	0.000	0.000	0.000
29	A	42	LYS	1	0.938	0.976	17.424	0.250	0.250	0.000	0.000	0.000	0.000
30	A	43	ASN	0	-0.024	-0.031	17.479	0.029	0.029	0.000	0.000	0.000	0.000
31	A	44	TYR	0	-0.016	-0.017	12.204	-0.091	-0.091	0.000	0.000	0.000	0.000
32	A	45	ILE	0	0.037	0.029	12.228	-0.084	-0.084	0.000	0.000	0.000	0.000
33	A	46	ASP	-1	-0.808	-0.892	13.464	-0.231	-0.231	0.000	0.000	0.000	0.000
34	A	47	ASN	0	-0.143	-0.076	14.004	-0.012	-0.012	0.000	0.000	0.000	0.000
35	A	48	HIS	0	-0.037	-0.030	10.184	-0.017	-0.017	0.000	0.000	0.000	0.000
36	A	49	LYS	1	0.898	0.966	9.120	0.665	0.665	0.000	0.000	0.000	0.000
37	A	50	VAL	0	-0.015	-0.010	7.636	-0.542	-0.542	0.000	0.000	0.000	0.000
38	A	51	GLU	-1	-0.865	-0.917	5.914	0.138	0.138	0.000	0.000	0.000	0.000
39	A	52	TYR	0	-0.027	-0.041	8.720	-0.094	-0.094	0.000	0.000	0.000	0.000
40	A	53	GLN	0	-0.010	-0.010	12.290	0.092	0.092	0.000	0.000	0.000	0.000
41	A	54	PHE	0	-0.015	0.001	14.089	-0.025	-0.025	0.000	0.000	0.000	0.000
42	A	55	VAL	0	-0.027	-0.006	16.811	0.040	0.040	0.000	0.000	0.000	0.000
43	A	56	ASN	0	0.004	-0.018	19.422	-0.011	-0.011	0.000	0.000	0.000	0.000
44	A	57	LEU	0	0.014	-0.012	23.035	0.017	0.017	0.000	0.000	0.000	0.000
45	A	58	ALA	0	-0.088	-0.050	25.496	0.014	0.014	0.000	0.000	0.000	0.000
46	A	59	PHE	0	-0.018	-0.023	28.004	0.011	0.011	0.000	0.000	0.000	0.000
47	A	60	LEU	0	0.009	0.038	30.885	0.003	0.003	0.000	0.000	0.000	0.000
48	A	61	GLY	0	0.094	0.049	33.349	0.002	0.002	0.000	0.000	0.000	0.000
49	A	62	LYS	1	0.807	0.876	33.813	0.024	0.024	0.000	0.000	0.000	0.000
50	A	63	ASP	-1	-0.770	-0.878	34.547	-0.047	-0.047	0.000	0.000	0.000	0.000
51	A	64	SER	0	0.030	0.016	29.866	0.001	0.001	0.000	0.000	0.000	0.000
52	A	65	ILE	0	-0.032	-0.015	27.410	-0.003	-0.003	0.000	0.000	0.000	0.000
53	A	66	VAL	0	-0.047	-0.021	28.945	0.007	0.007	0.000	0.000	0.000	0.000
54	A	67	GLY	0	0.073	0.031	29.482	0.004	0.004	0.000	0.000	0.000	0.000
55	A	68	SER	0	-0.020	-0.010	24.655	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	69	ARG	1	0.887	0.946	24.827	0.003	0.003	0.000	0.000	0.000	0.000
57	A	70	ALA	0	0.019	0.006	25.895	0.008	0.008	0.000	0.000	0.000	0.000
58	A	71	SER	0	0.043	0.028	22.385	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	72	HIS	0	-0.037	-0.036	18.722	0.016	0.016	0.000	0.000	0.000	0.000
60	A	73	ALA	0	-0.027	-0.017	21.746	0.017	0.017	0.000	0.000	0.000	0.000
61	A	74	VAL	0	0.010	-0.002	22.854	0.012	0.012	0.000	0.000	0.000	0.000
62	A	75	LEU	0	-0.025	0.010	16.011	0.008	0.008	0.000	0.000	0.000	0.000
63	A	76	MET	0	-0.038	-0.016	18.886	0.023	0.023	0.000	0.000	0.000	0.000
64	A	77	TYR	0	-0.088	-0.070	19.952	0.031	0.031	0.000	0.000	0.000	0.000
65	A	78	ALA	0	0.008	0.007	21.978	0.007	0.007	0.000	0.000	0.000	0.000
66	A	79	PRO	0	0.074	0.045	16.918	-0.025	-0.025	0.000	0.000	0.000	0.000
67	A	80	LYS	1	0.925	0.955	18.490	0.013	0.013	0.000	0.000	0.000	0.000
68	A	81	SER	0	0.032	0.015	19.997	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	82	PHE	0	-0.003	0.002	17.617	0.001	0.001	0.000	0.000	0.000	0.000
70	A	83	LEU	0	0.071	0.031	16.905	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	84	ASP	-1	-0.838	-0.897	21.111	-0.147	-0.147	0.000	0.000	0.000	0.000
72	A	85	PHE	0	0.010	0.004	24.213	0.006	0.006	0.000	0.000	0.000	0.000
73	A	86	GLN	0	0.014	0.019	20.396	-0.022	-0.022	0.000	0.000	0.000	0.000
74	A	87	LYS	1	0.951	0.976	24.385	0.162	0.162	0.000	0.000	0.000	0.000
75	A	88	GLN	0	-0.027	-0.029	26.133	0.013	0.013	0.000	0.000	0.000	0.000
76	A	89	LEU	0	-0.060	-0.021	27.364	0.009	0.009	0.000	0.000	0.000	0.000
77	A	90	PHE	0	0.044	0.010	23.779	0.007	0.007	0.000	0.000	0.000	0.000
78	A	91	ALA	0	-0.022	-0.006	29.215	0.004	0.004	0.000	0.000	0.000	0.000
79	A	92	ALA	0	-0.038	-0.013	31.886	0.006	0.006	0.000	0.000	0.000	0.000
80	A	93	GLN	0	-0.040	-0.038	30.622	0.006	0.006	0.000	0.000	0.000	0.000
81	A	94	GLN	0	-0.080	-0.040	34.023	0.005	0.005	0.000	0.000	0.000	0.000
82	A	95	ASP	-1	-0.826	-0.911	36.505	-0.070	-0.070	0.000	0.000	0.000	0.000
83	A	96	GLU	-1	-0.874	-0.954	35.247	-0.089	-0.089	0.000	0.000	0.000	0.000
84	A	97	ASN	0	-0.071	-0.044	36.772	0.005	0.005	0.000	0.000	0.000	0.000
85	A	98	LYS	1	0.904	0.962	39.317	0.056	0.056	0.000	0.000	0.000	0.000
86	A	99	GLU	-1	-0.860	-0.910	37.601	-0.033	-0.033	0.000	0.000	0.000	0.000
87	A	100	TRP	0	0.027	0.001	31.499	0.006	0.006	0.000	0.000	0.000	0.000
88	A	101	LEU	0	-0.014	0.017	30.875	0.001	0.001	0.000	0.000	0.000	0.000
89	A	102	THR	0	0.038	0.009	34.639	0.006	0.006	0.000	0.000	0.000	0.000
90	A	103	LYS	1	0.976	0.963	35.013	-0.001	-0.001	0.000	0.000	0.000	0.000
91	A	104	GLU	-1	-0.956	-0.951	36.098	-0.026	-0.026	0.000	0.000	0.000	0.000
92	A	105	LEU	0	0.031	0.017	33.763	0.000	0.000	0.000	0.000	0.000	0.000
93	A	106	LEU	0	0.034	0.006	30.112	-0.003	-0.003	0.000	0.000	0.000	0.000
94	A	107	ASP	-1	-0.799	-0.872	32.372	-0.008	-0.008	0.000	0.000	0.000	0.000
95	A	108	LYS	1	0.858	0.936	34.210	0.052	0.052	0.000	0.000	0.000	0.000
96	A	109	HIS	0	0.029	0.008	30.631	0.002	0.002	0.000	0.000	0.000	0.000
97	A	110	ILE	0	-0.012	-0.011	28.825	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	111	LYS	1	0.911	0.952	30.701	0.012	0.012	0.000	0.000	0.000	0.000
99	A	112	GLN	0	-0.015	0.009	32.249	0.005	0.005	0.000	0.000	0.000	0.000
100	A	113	LEU	0	-0.069	-0.027	26.196	-0.006	-0.006	0.000	0.000	0.000	0.000
101	A	114	HIS	0	-0.050	-0.013	29.523	0.004	0.004	0.000	0.000	0.000	0.000
102	A	115	LEU	0	-0.003	0.010	26.380	0.003	0.003	0.000	0.000	0.000	0.000
103	A	116	ASP	-1	-0.796	-0.869	29.338	0.030	0.030	0.000	0.000	0.000	0.000
104	A	117	LYS	1	0.889	0.913	31.565	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	118	GLU	-1	-0.792	-0.898	32.513	0.031	0.031	0.000	0.000	0.000	0.000
106	A	119	THR	0	-0.097	-0.083	26.400	0.010	0.010	0.000	0.000	0.000	0.000
107	A	120	GLU	-1	-0.818	-0.904	29.131	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	121	ASN	0	-0.013	-0.023	31.081	-0.007	-0.007	0.000	0.000	0.000	0.000
109	A	122	LYS	1	0.883	0.959	25.941	-0.058	-0.058	0.000	0.000	0.000	0.000
110	A	123	ILE	0	-0.013	-0.002	25.842	0.004	0.004	0.000	0.000	0.000	0.000
111	A	124	ILE	0	-0.026	-0.017	28.545	-0.002	-0.002	0.000	0.000	0.000	0.000
112	A	125	LYS	1	0.924	0.961	31.860	-0.052	-0.052	0.000	0.000	0.000	0.000
113	A	126	ASP	-1	-0.796	-0.848	26.638	0.064	0.064	0.000	0.000	0.000	0.000
114	A	127	TYR	0	0.033	0.019	28.359	0.001	0.001	0.000	0.000	0.000	0.000
115	A	128	LYS	1	0.747	0.871	29.407	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	129	THR	0	-0.049	-0.025	31.383	0.002	0.002	0.000	0.000	0.000	0.000
117	A	130	LYS	1	0.975	0.982	31.128	-0.035	-0.035	0.000	0.000	0.000	0.000
118	A	131	ASP	-1	-0.885	-0.953	29.321	0.064	0.064	0.000	0.000	0.000	0.000
119	A	132	SER	0	0.030	0.024	28.089	0.014	0.014	0.000	0.000	0.000	0.000
120	A	133	LYS	1	0.927	0.931	22.139	-0.117	-0.117	0.000	0.000	0.000	0.000
121	A	134	SER	0	0.011	-0.018	23.309	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	135	TRP	0	-0.014	-0.003	24.515	-0.015	-0.015	0.000	0.000	0.000	0.000
123	A	136	LYS	1	0.848	0.904	24.097	-0.099	-0.099	0.000	0.000	0.000	0.000
124	A	137	ALA	0	-0.006	0.014	20.573	-0.002	-0.002	0.000	0.000	0.000	0.000
125	A	138	ALA	0	0.036	0.018	21.997	-0.015	-0.015	0.000	0.000	0.000	0.000
126	A	139	GLU	-1	-0.826	-0.909	24.372	-0.014	-0.014	0.000	0.000	0.000	0.000
127	A	140	LYS	1	0.932	0.963	16.502	-0.134	-0.134	0.000	0.000	0.000	0.000
128	A	141	ASP	-1	-0.749	-0.861	19.406	-0.087	-0.087	0.000	0.000	0.000	0.000
129	A	142	LYS	1	0.887	0.943	21.494	0.004	0.004	0.000	0.000	0.000	0.000
130	A	143	LYS	1	0.764	0.869	21.984	-0.039	-0.039	0.000	0.000	0.000	0.000
131	A	144	ILE	0	0.009	0.012	16.785	0.005	0.005	0.000	0.000	0.000	0.000
132	A	145	ALA	0	0.068	0.037	19.845	-0.019	-0.019	0.000	0.000	0.000	0.000
133	A	146	LYS	1	0.942	0.979	21.637	0.016	0.016	0.000	0.000	0.000	0.000
134	A	147	ASP	-1	-0.829	-0.903	20.094	0.007	0.007	0.000	0.000	0.000	0.000
135	A	148	ASN	0	-0.087	-0.048	16.316	-0.031	-0.031	0.000	0.000	0.000	0.000
136	A	149	HIS	0	-0.038	-0.012	19.610	-0.025	-0.025	0.000	0.000	0.000	0.000
137	A	150	ILE	0	-0.015	0.001	18.936	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	151	LYS	1	0.925	0.964	23.011	0.142	0.142	0.000	0.000	0.000	0.000
139	A	152	THR	0	0.014	0.009	25.515	0.011	0.011	0.000	0.000	0.000	0.000
140	A	153	THR	0	-0.042	0.012	24.276	-0.013	-0.013	0.000	0.000	0.000	0.000
141	A	154	PRO	0	0.048	-0.002	23.630	0.016	0.016	0.000	0.000	0.000	0.000
142	A	155	THR	0	-0.054	-0.042	21.035	-0.005	-0.005	0.000	0.000	0.000	0.000
143	A	156	ALA	0	0.010	0.008	17.471	0.008	0.008	0.000	0.000	0.000	0.000
144	A	157	PHE	0	-0.005	-0.008	14.321	0.037	0.037	0.000	0.000	0.000	0.000
145	A	158	ILE	0	0.025	0.010	10.332	-0.031	-0.031	0.000	0.000	0.000	0.000
146	A	159	ASN	0	0.021	0.012	6.852	-0.262	-0.262	0.000	0.000	0.000	0.000
147	A	160	GLY	0	-0.010	-0.008	9.211	0.103	0.103	0.000	0.000	0.000	0.000
148	A	161	GLU	-1	-0.873	-0.914	12.497	-0.492	-0.492	0.000	0.000	0.000	0.000
149	A	162	LYS	1	0.798	0.890	14.459	0.318	0.318	0.000	0.000	0.000	0.000
150	A	163	VAL	0	0.019	0.015	16.543	-0.016	-0.016	0.000	0.000	0.000	0.000
151	A	164	GLU	-1	-0.858	-0.903	18.597	-0.361	-0.361	0.000	0.000	0.000	0.000
152	A	165	ASP	-1	-0.783	-0.900	21.985	-0.239	-0.239	0.000	0.000	0.000	0.000
153	A	166	PRO	0	-0.051	-0.021	21.257	-0.021	-0.021	0.000	0.000	0.000	0.000
154	A	167	TYR	0	0.001	-0.003	22.266	-0.002	-0.002	0.000	0.000	0.000	0.000
155	A	168	ASP	-1	-0.793	-0.905	23.872	-0.330	-0.330	0.000	0.000	0.000	0.000
156	A	169	TYR	0	-0.048	-0.042	18.474	-0.032	-0.032	0.000	0.000	0.000	0.000
157	A	170	GLU	-1	-0.907	-0.976	20.036	-0.381	-0.381	0.000	0.000	0.000	0.000
158	A	171	SER	0	0.041	0.029	20.148	-0.022	-0.022	0.000	0.000	0.000	0.000
159	A	172	TYR	0	-0.087	-0.070	16.061	-0.058	-0.058	0.000	0.000	0.000	0.000
160	A	173	GLU	-1	-0.806	-0.867	15.862	-0.646	-0.646	0.000	0.000	0.000	0.000
161	A	174	LYS	1	0.833	0.893	16.512	0.369	0.369	0.000	0.000	0.000	0.000
162	A	175	LEU	0	0.017	0.004	13.657	-0.028	-0.028	0.000	0.000	0.000	0.000
163	A	176	LEU	0	-0.068	-0.030	10.800	-0.170	-0.170	0.000	0.000	0.000	0.000
164	A	177	LYS	1	0.806	0.922	12.197	0.479	0.479	0.000	0.000	0.000	0.000
165	A	178	ASP	-1	-0.968	-0.976	10.722	-1.123	-1.123	0.000	0.000	0.000	0.000

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