FMO DATABASE

FMODB ID: 8534Y

Calculation Name: 2BJO-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2BJO

Chain ID: A

ChEMBL ID:

UniProt ID: P80242

Base Structure: X-ray

Registration Date: 2023-09-20

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	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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-986051.032914
FMO2-HF: Nuclear repulsion	935603.107824
FMO2-HF: Total energy	-50447.92509
FMO2-MP2: Total energy	-50594.330454

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:2:ALA)

Summations of interaction energy for fragment #1(A:2:ALA)

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.
-1.665	1.14	0.092	-1.29	-1.608	-0.002

Interaction energy analysis for fragmet #1(A:2:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.035 / q_NPA : -0.031

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	4	PHE	0	0.008	0.002	3.089	-1.096	0.758	0.039	-0.848	-1.045	0.001
4	A	5	THR	0	-0.029	-0.013	3.347	-0.845	0.107	0.054	-0.440	-0.567	-0.003
5	A	6	ALA	0	0.031	0.032	4.997	0.036	0.035	-0.001	-0.002	0.004	0.000
6	A	7	LYS	1	0.892	0.942	8.715	0.639	0.639	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.061	0.029	11.260	0.013	0.013	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.046	0.000	14.828	0.008	0.008	0.000	0.000	0.000	0.000
9	A	10	ALA	0	0.029	0.012	17.659	0.009	0.009	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.920	0.948	20.560	0.124	0.124	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.060	0.010	23.908	0.004	0.004	0.000	0.000	0.000	0.000
12	A	13	GLY	0	-0.006	0.014	25.439	0.004	0.004	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.822	0.867	26.205	0.014	0.014	0.000	0.000	0.000	0.000
14	A	15	ALA	0	0.011	0.020	28.419	0.002	0.002	0.000	0.000	0.000	0.000
15	A	16	GLY	0	-0.001	0.016	26.469	-0.002	-0.002	0.000	0.000	0.000	0.000
16	A	17	HIS	1	0.792	0.858	23.770	0.097	0.097	0.000	0.000	0.000	0.000
17	A	18	ILE	0	-0.052	-0.030	19.706	-0.004	-0.004	0.000	0.000	0.000	0.000
18	A	19	THR	0	0.022	-0.011	19.895	0.009	0.009	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.072	-0.058	15.129	0.002	0.002	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.910	-0.982	12.017	-0.450	-0.450	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.844	-0.897	14.688	-0.275	-0.275	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.023	-0.005	16.496	0.016	0.016	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.038	-0.006	17.204	0.025	0.025	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.057	-0.037	16.370	0.024	0.024	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.796	-0.865	19.748	-0.127	-0.127	0.000	0.000	0.000	0.000
26	A	27	PHE	0	-0.030	-0.018	21.475	0.010	0.010	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.800	-0.868	24.590	-0.072	-0.072	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.073	-0.034	22.696	0.002	0.002	0.000	0.000	0.000	0.000
29	A	30	VAL	0	-0.001	0.000	26.810	0.002	0.002	0.000	0.000	0.000	0.000
30	A	31	MET	0	-0.030	-0.018	29.902	0.003	0.003	0.000	0.000	0.000	0.000
31	A	32	PRO	0	0.044	-0.002	32.496	-0.001	-0.001	0.000	0.000	0.000	0.000
32	A	33	ASN	0	-0.013	0.000	34.758	0.000	0.000	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.024	0.020	33.579	-0.001	-0.001	0.000	0.000	0.000	0.000
34	A	35	ALA	0	0.049	0.029	35.664	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	ALA	0	-0.029	-0.021	38.145	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.024	-0.005	37.729	0.000	0.000	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.006	0.020	38.787	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.087	-0.049	33.563	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	40	THR	0	0.012	-0.003	31.556	0.003	0.003	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.006	-0.010	28.112	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	42	THR	0	0.007	-0.006	22.955	0.005	0.005	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.004	-0.003	25.032	0.002	0.002	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.034	0.006	21.695	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.726	-0.844	21.800	-0.003	-0.003	0.000	0.000	0.000	0.000
45	A	46	GLN	0	0.063	0.044	23.567	0.000	0.000	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.000	0.003	19.097	0.000	0.000	0.000	0.000	0.000	0.000
47	A	48	PHE	0	-0.001	0.002	17.263	0.001	0.001	0.000	0.000	0.000	0.000
48	A	49	ALA	0	-0.005	-0.016	20.028	0.011	0.011	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.004	0.000	20.346	0.007	0.007	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.018	0.015	16.979	-0.003	-0.003	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.007	-0.036	17.099	0.012	0.012	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.033	0.020	18.876	0.014	0.014	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.010	0.014	17.564	0.008	0.008	0.000	0.000	0.000	0.000
54	A	55	CYS	0	-0.065	-0.001	14.109	0.081	0.081	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.000	-0.020	16.201	0.026	0.026	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.053	0.025	19.217	0.010	0.010	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.036	0.025	16.422	0.000	0.000	0.000	0.000	0.000	0.000
58	A	59	ALA	0	-0.051	-0.025	16.468	0.019	0.019	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.014	-0.018	17.538	0.011	0.011	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.932	-0.968	19.100	0.037	0.037	0.000	0.000	0.000	0.000
61	A	62	HIS	0	-0.060	-0.039	15.658	-0.005	-0.005	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.046	-0.037	18.683	0.009	0.009	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.006	0.014	21.057	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.841	0.897	20.592	-0.058	-0.058	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.919	-0.945	18.661	0.232	0.232	0.000	0.000	0.000	0.000
66	A	67	GLN	0	-0.066	-0.017	22.678	-0.012	-0.012	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.100	-0.054	25.541	-0.009	-0.009	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.009	0.007	26.363	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.827	-0.889	25.800	0.048	0.048	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.027	-0.018	23.338	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.832	-0.902	26.481	0.009	0.009	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.050	-0.047	24.999	0.006	0.006	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.876	-0.931	26.753	0.005	0.005	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.017	-0.016	22.523	0.006	0.006	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.894	-0.924	25.500	0.010	0.010	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.004	0.003	24.343	0.008	0.008	0.000	0.000	0.000	0.000
77	A	78	GLN	0	-0.053	-0.043	25.332	-0.007	-0.007	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.026	-0.003	23.179	0.007	0.007	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.024	-0.011	26.558	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.026	-0.013	27.500	0.004	0.004	0.000	0.000	0.000	0.000
81	A	82	MET	0	-0.027	-0.018	29.612	0.000	0.000	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.904	0.937	31.388	-0.022	-0.022	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.816	-0.893	29.764	0.049	0.049	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.880	-0.949	32.608	0.025	0.025	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.123	-0.075	31.970	0.000	0.000	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.904	-0.959	30.580	0.026	0.026	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.050	-0.005	33.330	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.008	0.019	31.140	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.072	-0.057	28.961	-0.001	-0.001	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.943	0.982	26.931	-0.053	-0.053	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.001	-0.004	23.492	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.037	0.036	26.446	0.007	0.007	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.019	-0.028	22.753	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	95	THR	0	0.045	0.028	26.100	0.008	0.008	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.037	-0.009	21.953	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.023	0.020	26.461	0.004	0.004	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.014	-0.026	25.735	-0.004	-0.004	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.064	-0.055	28.435	0.003	0.003	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.031	0.001	27.604	0.000	0.000	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.817	0.917	30.247	-0.012	-0.012	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.912	-0.951	33.495	0.024	0.024	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.078	-0.016	28.941	0.003	0.003	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.871	-0.926	33.135	0.049	0.049	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.979	0.980	33.273	-0.049	-0.049	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.925	-0.972	33.244	0.060	0.060	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.825	0.890	29.336	-0.089	-0.089	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.033	0.011	29.244	0.008	0.008	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.030	-0.028	28.461	0.000	0.000	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.849	-0.900	27.542	0.117	0.117	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.026	0.002	24.613	0.013	0.013	0.000	0.000	0.000	0.000
111	A	112	VAL	0	0.049	0.029	23.660	0.011	0.011	0.000	0.000	0.000	0.000
112	A	113	ASN	0	-0.023	-0.016	23.670	0.007	0.007	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.024	0.013	22.144	0.016	0.016	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.017	0.011	19.611	0.030	0.030	0.000	0.000	0.000	0.000
115	A	116	HIS	0	0.033	0.032	18.830	0.021	0.021	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.868	-0.906	19.306	0.224	0.224	0.000	0.000	0.000	0.000
117	A	118	PHE	0	-0.030	-0.008	13.712	0.062	0.062	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.019	-0.003	10.486	0.003	0.003	0.000	0.000	0.000	0.000
119	A	121	TYR	0	0.046	0.002	12.649	0.000	0.000	0.000	0.000	0.000	0.000
120	A	122	SER	0	0.047	0.032	15.327	-0.017	-0.017	0.000	0.000	0.000	0.000
121	A	123	LYS	1	0.808	0.917	12.306	-0.521	-0.521	0.000	0.000	0.000	0.000
122	A	124	ALA	0	-0.037	-0.018	13.534	-0.004	-0.004	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.003	-0.015	15.265	-0.021	-0.021	0.000	0.000	0.000	0.000
124	A	126	ARG	1	0.835	0.897	18.526	-0.240	-0.240	0.000	0.000	0.000	0.000
125	A	127	GLY	0	-0.019	-0.015	20.498	0.004	0.004	0.000	0.000	0.000	0.000
126	A	128	ASN	0	-0.075	-0.025	20.752	-0.020	-0.020	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.008	-0.005	22.702	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.865	-0.917	24.486	0.079	0.079	0.000	0.000	0.000	0.000
129	A	131	VAL	0	-0.038	-0.032	22.077	-0.010	-0.010	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.822	0.930	25.552	-0.057	-0.057	0.000	0.000	0.000	0.000
131	A	133	LEU	0	-0.005	0.000	23.999	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	134	GLU	-1	-0.918	-0.958	28.059	0.045	0.045	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.014	0.011	29.701	-0.001	-0.001	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.927	0.975	31.915	-0.026	-0.026	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:2:ALA)