FMO DATABASE

FMODB ID: KGM23

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:

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1829630.791367
FMO2-HF: Nuclear repulsion	1762384.274621
FMO2-HF: Total energy	-67246.516746
FMO2-MP2: Total energy	-67445.129867

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.
-3.088	-1.649	-0.001	-0.824	-0.614	0.004

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 : 0.024 / q_NPA : 0.010

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	0.027	0.011	3.860	-0.852	0.587	-0.001	-0.824	-0.614	0.004
4	A	17	LEU	0	0.001	0.012	6.573	0.521	0.521	0.000	0.000	0.000	0.000
5	A	18	VAL	0	0.004	0.003	8.248	0.120	0.120	0.000	0.000	0.000	0.000
6	A	19	VAL	0	-0.014	-0.011	12.013	0.109	0.109	0.000	0.000	0.000	0.000
7	A	20	VAL	0	0.015	0.001	14.508	-0.007	-0.007	0.000	0.000	0.000	0.000
8	A	21	TYR	0	0.025	0.024	16.799	0.060	0.060	0.000	0.000	0.000	0.000
9	A	22	GLY	0	0.071	-0.014	20.967	-0.006	-0.006	0.000	0.000	0.000	0.000
10	A	23	ASP	-1	-0.755	-0.868	24.225	-0.069	-0.069	0.000	0.000	0.000	0.000
11	A	24	TYR	0	0.007	-0.016	23.799	-0.010	-0.010	0.000	0.000	0.000	0.000
12	A	25	LYS	1	0.740	0.879	28.439	0.059	0.059	0.000	0.000	0.000	0.000
13	A	26	CYS	0	0.043	0.053	28.758	0.000	0.000	0.000	0.000	0.000	0.000
14	A	27	PRO	0	0.071	0.041	30.080	-0.011	-0.011	0.000	0.000	0.000	0.000
15	A	28	TYR	0	0.027	0.010	29.080	-0.007	-0.007	0.000	0.000	0.000	0.000
16	A	29	CYS	0	-0.070	-0.031	25.870	-0.019	-0.019	0.000	0.000	0.000	0.000
17	A	30	LYS	1	0.844	0.923	26.075	0.117	0.117	0.000	0.000	0.000	0.000
18	A	31	GLU	-1	-0.850	-0.921	28.020	-0.168	-0.168	0.000	0.000	0.000	0.000
19	A	32	LEU	0	-0.021	-0.003	20.949	-0.009	-0.009	0.000	0.000	0.000	0.000
20	A	33	ASP	-1	-0.887	-0.964	23.547	-0.225	-0.225	0.000	0.000	0.000	0.000
21	A	34	GLU	-1	-0.816	-0.909	24.620	-0.158	-0.158	0.000	0.000	0.000	0.000
22	A	35	LYS	1	0.845	0.921	26.434	0.189	0.189	0.000	0.000	0.000	0.000
23	A	36	VAL	0	-0.034	-0.003	20.068	-0.018	-0.018	0.000	0.000	0.000	0.000
24	A	37	MET	0	-0.012	0.012	17.812	-0.045	-0.045	0.000	0.000	0.000	0.000
25	A	38	PRO	0	-0.024	-0.011	21.147	-0.016	-0.016	0.000	0.000	0.000	0.000
26	A	39	LYS	1	0.845	0.928	21.884	0.301	0.301	0.000	0.000	0.000	0.000
27	A	40	LEU	0	0.054	0.012	15.272	-0.024	-0.024	0.000	0.000	0.000	0.000
28	A	41	ARG	1	0.791	0.863	16.874	0.157	0.157	0.000	0.000	0.000	0.000
29	A	42	LYS	1	0.949	0.984	17.487	0.246	0.246	0.000	0.000	0.000	0.000
30	A	43	ASN	0	-0.015	-0.023	17.964	0.027	0.027	0.000	0.000	0.000	0.000
31	A	44	TYR	0	-0.045	-0.040	12.328	-0.075	-0.075	0.000	0.000	0.000	0.000
32	A	45	ILE	0	0.032	0.030	12.548	-0.083	-0.083	0.000	0.000	0.000	0.000
33	A	46	ASP	-1	-0.821	-0.901	13.938	-0.226	-0.226	0.000	0.000	0.000	0.000
34	A	47	ASN	0	-0.100	-0.062	14.371	-0.017	-0.017	0.000	0.000	0.000	0.000
35	A	48	HIS	0	-0.031	-0.025	10.415	-0.031	-0.031	0.000	0.000	0.000	0.000
36	A	49	LYS	1	0.888	0.959	9.190	0.614	0.614	0.000	0.000	0.000	0.000
37	A	50	VAL	0	0.007	0.008	7.822	-0.499	-0.499	0.000	0.000	0.000	0.000
38	A	51	GLU	-1	-0.868	-0.914	6.201	0.056	0.056	0.000	0.000	0.000	0.000
39	A	52	TYR	0	-0.025	-0.047	8.974	-0.093	-0.093	0.000	0.000	0.000	0.000
40	A	53	GLN	0	-0.036	-0.010	12.457	0.101	0.101	0.000	0.000	0.000	0.000
41	A	54	PHE	0	-0.003	0.006	14.418	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	55	VAL	0	-0.033	-0.010	17.081	0.036	0.036	0.000	0.000	0.000	0.000
43	A	56	ASN	0	-0.004	-0.016	19.647	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	57	LEU	0	0.010	-0.013	23.048	0.018	0.018	0.000	0.000	0.000	0.000
45	A	58	ALA	0	-0.090	-0.045	25.538	0.013	0.013	0.000	0.000	0.000	0.000
46	A	59	PHE	0	-0.028	-0.021	28.118	0.011	0.011	0.000	0.000	0.000	0.000
47	A	60	LEU	0	0.015	0.033	31.182	0.004	0.004	0.000	0.000	0.000	0.000
48	A	61	GLY	0	0.062	0.030	33.500	0.002	0.002	0.000	0.000	0.000	0.000
49	A	62	LYS	1	0.806	0.873	33.662	0.024	0.024	0.000	0.000	0.000	0.000
50	A	63	ASP	-1	-0.726	-0.861	34.579	-0.046	-0.046	0.000	0.000	0.000	0.000
51	A	64	SER	0	0.041	0.002	29.976	0.002	0.002	0.000	0.000	0.000	0.000
52	A	65	ILE	0	-0.042	-0.014	27.636	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	66	VAL	0	-0.051	-0.023	29.026	0.006	0.006	0.000	0.000	0.000	0.000
54	A	67	GLY	0	0.081	0.028	29.431	0.003	0.003	0.000	0.000	0.000	0.000
55	A	68	SER	0	-0.021	-0.006	24.854	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	69	ARG	1	0.868	0.933	24.935	0.002	0.002	0.000	0.000	0.000	0.000
57	A	70	ALA	0	0.021	0.003	26.028	0.007	0.007	0.000	0.000	0.000	0.000
58	A	71	SER	0	0.033	0.029	22.803	-0.004	-0.004	0.000	0.000	0.000	0.000
59	A	72	HIS	0	-0.012	-0.025	18.793	0.015	0.015	0.000	0.000	0.000	0.000
60	A	73	ALA	0	-0.027	-0.020	21.960	0.016	0.016	0.000	0.000	0.000	0.000
61	A	74	VAL	0	0.006	0.002	22.962	0.010	0.010	0.000	0.000	0.000	0.000
62	A	75	LEU	0	-0.021	0.002	16.179	0.006	0.006	0.000	0.000	0.000	0.000
63	A	76	MET	0	-0.033	-0.005	18.885	0.020	0.020	0.000	0.000	0.000	0.000
64	A	77	TYR	0	-0.075	-0.056	20.260	0.029	0.029	0.000	0.000	0.000	0.000
65	A	78	ALA	0	0.017	0.014	22.229	0.005	0.005	0.000	0.000	0.000	0.000
66	A	79	PRO	0	0.074	0.043	17.093	-0.024	-0.024	0.000	0.000	0.000	0.000
67	A	80	LYS	1	0.930	0.951	18.884	0.029	0.029	0.000	0.000	0.000	0.000
68	A	81	SER	0	0.047	0.026	20.375	-0.004	-0.004	0.000	0.000	0.000	0.000
69	A	82	PHE	0	0.018	0.017	17.821	0.003	0.003	0.000	0.000	0.000	0.000
70	A	83	LEU	0	0.036	0.018	16.840	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	84	ASP	-1	-0.842	-0.907	21.313	-0.157	-0.157	0.000	0.000	0.000	0.000
72	A	85	PHE	0	-0.010	-0.005	24.640	0.008	0.008	0.000	0.000	0.000	0.000
73	A	86	GLN	0	0.022	0.017	20.647	-0.023	-0.023	0.000	0.000	0.000	0.000
74	A	87	LYS	1	0.957	0.980	24.674	0.168	0.168	0.000	0.000	0.000	0.000
75	A	88	GLN	0	-0.013	-0.006	26.391	0.013	0.013	0.000	0.000	0.000	0.000
76	A	89	LEU	0	-0.064	-0.027	27.735	0.008	0.008	0.000	0.000	0.000	0.000
77	A	90	PHE	0	0.042	0.008	24.069	0.006	0.006	0.000	0.000	0.000	0.000
78	A	91	ALA	0	-0.017	-0.006	29.517	0.003	0.003	0.000	0.000	0.000	0.000
79	A	92	ALA	0	-0.035	-0.015	32.047	0.005	0.005	0.000	0.000	0.000	0.000
80	A	93	GLN	0	-0.031	-0.023	30.718	0.006	0.006	0.000	0.000	0.000	0.000
81	A	94	GLN	0	-0.074	-0.042	34.080	0.004	0.004	0.000	0.000	0.000	0.000
82	A	95	ASP	-1	-0.786	-0.886	36.426	-0.065	-0.065	0.000	0.000	0.000	0.000
83	A	96	GLU	-1	-0.878	-0.949	35.108	-0.086	-0.086	0.000	0.000	0.000	0.000
84	A	97	ASN	0	-0.046	-0.036	36.905	0.006	0.006	0.000	0.000	0.000	0.000
85	A	98	LYS	1	0.843	0.916	39.622	0.058	0.058	0.000	0.000	0.000	0.000
86	A	99	GLU	-1	-0.874	-0.907	37.909	-0.032	-0.032	0.000	0.000	0.000	0.000
87	A	100	TRP	0	0.035	0.010	31.746	0.005	0.005	0.000	0.000	0.000	0.000
88	A	101	LEU	0	-0.011	0.013	30.839	0.001	0.001	0.000	0.000	0.000	0.000
89	A	102	THR	0	0.042	0.008	34.390	0.006	0.006	0.000	0.000	0.000	0.000
90	A	103	LYS	1	0.922	0.944	34.928	-0.003	-0.003	0.000	0.000	0.000	0.000
91	A	104	GLU	-1	-0.958	-0.951	36.462	-0.024	-0.024	0.000	0.000	0.000	0.000
92	A	105	LEU	0	0.027	0.013	33.851	0.000	0.000	0.000	0.000	0.000	0.000
93	A	106	LEU	0	0.023	0.006	30.212	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	107	ASP	-1	-0.753	-0.859	32.289	-0.008	-0.008	0.000	0.000	0.000	0.000
95	A	108	LYS	1	0.858	0.935	34.233	0.053	0.053	0.000	0.000	0.000	0.000
96	A	109	HIS	0	0.033	0.015	30.658	0.002	0.002	0.000	0.000	0.000	0.000
97	A	110	ILE	0	-0.013	-0.010	28.920	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	111	LYS	1	0.853	0.924	30.751	0.012	0.012	0.000	0.000	0.000	0.000
99	A	112	GLN	0	-0.008	-0.002	32.399	0.005	0.005	0.000	0.000	0.000	0.000
100	A	113	LEU	0	-0.063	-0.023	26.332	-0.007	-0.007	0.000	0.000	0.000	0.000
101	A	114	HIS	0	-0.040	-0.014	29.607	0.004	0.004	0.000	0.000	0.000	0.000
102	A	115	LEU	0	-0.001	0.010	26.291	0.004	0.004	0.000	0.000	0.000	0.000
103	A	116	ASP	-1	-0.775	-0.857	29.552	0.029	0.029	0.000	0.000	0.000	0.000
104	A	117	LYS	1	0.871	0.921	31.765	-0.005	-0.005	0.000	0.000	0.000	0.000
105	A	118	GLU	-1	-0.785	-0.886	32.722	0.029	0.029	0.000	0.000	0.000	0.000
106	A	119	THR	0	-0.061	-0.061	26.583	0.014	0.014	0.000	0.000	0.000	0.000
107	A	120	GLU	-1	-0.826	-0.902	29.334	-0.003	-0.003	0.000	0.000	0.000	0.000
108	A	121	ASN	0	-0.002	-0.024	31.581	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	122	LYS	1	0.820	0.910	26.259	-0.052	-0.052	0.000	0.000	0.000	0.000
110	A	123	ILE	0	-0.003	-0.003	26.063	0.005	0.005	0.000	0.000	0.000	0.000
111	A	124	ILE	0	-0.025	-0.019	28.547	-0.001	-0.001	0.000	0.000	0.000	0.000
112	A	125	LYS	1	0.908	0.949	31.967	-0.049	-0.049	0.000	0.000	0.000	0.000
113	A	126	ASP	-1	-0.756	-0.828	26.676	0.066	0.066	0.000	0.000	0.000	0.000
114	A	127	TYR	0	0.047	0.018	28.571	0.000	0.000	0.000	0.000	0.000	0.000
115	A	128	LYS	1	0.786	0.900	29.657	-0.002	-0.002	0.000	0.000	0.000	0.000
116	A	129	THR	0	-0.054	-0.022	31.621	0.001	0.001	0.000	0.000	0.000	0.000
117	A	130	LYS	1	0.998	0.988	31.424	-0.038	-0.038	0.000	0.000	0.000	0.000
118	A	131	ASP	-1	-0.859	-0.925	29.639	0.065	0.065	0.000	0.000	0.000	0.000
119	A	132	SER	0	0.004	0.010	28.320	0.013	0.013	0.000	0.000	0.000	0.000
120	A	133	LYS	1	0.865	0.911	22.482	-0.100	-0.100	0.000	0.000	0.000	0.000
121	A	134	SER	0	0.011	-0.021	23.491	-0.004	-0.004	0.000	0.000	0.000	0.000
122	A	135	TRP	0	-0.017	-0.008	24.739	-0.014	-0.014	0.000	0.000	0.000	0.000
123	A	136	LYS	1	0.826	0.873	24.133	-0.094	-0.094	0.000	0.000	0.000	0.000
124	A	137	ALA	0	-0.011	0.003	20.637	0.000	0.000	0.000	0.000	0.000	0.000
125	A	138	ALA	0	0.029	0.016	22.018	-0.014	-0.014	0.000	0.000	0.000	0.000
126	A	139	GLU	-1	-0.813	-0.908	24.446	-0.013	-0.013	0.000	0.000	0.000	0.000
127	A	140	LYS	1	0.922	0.969	16.338	-0.135	-0.135	0.000	0.000	0.000	0.000
128	A	141	ASP	-1	-0.741	-0.866	19.210	-0.084	-0.084	0.000	0.000	0.000	0.000
129	A	142	LYS	1	0.877	0.946	21.254	0.005	0.005	0.000	0.000	0.000	0.000
130	A	143	LYS	1	0.767	0.872	22.255	-0.042	-0.042	0.000	0.000	0.000	0.000
131	A	144	ILE	0	0.021	0.016	16.495	0.005	0.005	0.000	0.000	0.000	0.000
132	A	145	ALA	0	0.063	0.031	19.806	-0.020	-0.020	0.000	0.000	0.000	0.000
133	A	146	LYS	1	0.928	0.970	21.713	0.013	0.013	0.000	0.000	0.000	0.000
134	A	147	ASP	-1	-0.824	-0.899	20.169	0.013	0.013	0.000	0.000	0.000	0.000
135	A	148	ASN	0	-0.067	-0.041	16.643	-0.035	-0.035	0.000	0.000	0.000	0.000
136	A	149	HIS	0	-0.033	-0.009	19.929	-0.023	-0.023	0.000	0.000	0.000	0.000
137	A	150	ILE	0	-0.003	-0.001	19.556	-0.008	-0.008	0.000	0.000	0.000	0.000
138	A	151	LYS	1	0.923	0.959	23.609	0.130	0.130	0.000	0.000	0.000	0.000
139	A	152	THR	0	-0.018	0.004	25.722	0.011	0.011	0.000	0.000	0.000	0.000
140	A	153	THR	0	-0.034	0.002	24.344	-0.014	-0.014	0.000	0.000	0.000	0.000
141	A	154	PRO	0	0.051	0.016	23.999	0.014	0.014	0.000	0.000	0.000	0.000
142	A	155	THR	0	-0.058	-0.040	21.563	-0.003	-0.003	0.000	0.000	0.000	0.000
143	A	156	ALA	0	-0.006	0.008	18.142	0.006	0.006	0.000	0.000	0.000	0.000
144	A	157	PHE	0	0.007	-0.004	14.847	0.033	0.033	0.000	0.000	0.000	0.000
145	A	158	ILE	0	0.023	0.005	10.623	-0.016	-0.016	0.000	0.000	0.000	0.000
146	A	159	ASN	0	0.001	-0.007	7.445	-0.287	-0.287	0.000	0.000	0.000	0.000
147	A	160	GLY	0	0.010	0.013	9.455	0.101	0.101	0.000	0.000	0.000	0.000
148	A	161	GLU	-1	-0.883	-0.925	12.803	-0.458	-0.458	0.000	0.000	0.000	0.000
149	A	162	LYS	1	0.780	0.872	14.878	0.310	0.310	0.000	0.000	0.000	0.000
150	A	163	VAL	0	0.014	0.005	16.899	-0.013	-0.013	0.000	0.000	0.000	0.000
151	A	164	GLU	-1	-0.844	-0.885	18.828	-0.357	-0.357	0.000	0.000	0.000	0.000
152	A	165	ASP	-1	-0.796	-0.903	22.084	-0.230	-0.230	0.000	0.000	0.000	0.000
153	A	166	PRO	0	-0.040	-0.016	21.658	-0.026	-0.026	0.000	0.000	0.000	0.000
154	A	167	TYR	0	-0.006	-0.012	22.690	-0.001	-0.001	0.000	0.000	0.000	0.000
155	A	168	ASP	-1	-0.773	-0.889	24.052	-0.331	-0.331	0.000	0.000	0.000	0.000
156	A	169	TYR	0	-0.042	-0.040	18.329	-0.023	-0.023	0.000	0.000	0.000	0.000
157	A	170	GLU	-1	-0.869	-0.929	19.977	-0.381	-0.381	0.000	0.000	0.000	0.000
158	A	171	SER	0	0.028	0.010	20.476	-0.027	-0.027	0.000	0.000	0.000	0.000
159	A	172	TYR	0	-0.072	-0.056	16.239	-0.046	-0.046	0.000	0.000	0.000	0.000
160	A	173	GLU	-1	-0.788	-0.850	16.028	-0.648	-0.648	0.000	0.000	0.000	0.000
161	A	174	LYS	1	0.827	0.886	16.589	0.354	0.354	0.000	0.000	0.000	0.000
162	A	175	LEU	0	-0.003	0.009	13.905	-0.010	-0.010	0.000	0.000	0.000	0.000
163	A	176	LEU	0	-0.066	-0.038	10.832	-0.207	-0.207	0.000	0.000	0.000	0.000
164	A	177	LYS	1	0.841	0.932	12.607	0.499	0.499	0.000	0.000	0.000	0.000
165	A	178	ASP	-1	-0.971	-0.979	10.846	-1.107	-1.107	0.000	0.000	0.000	0.000

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