FMO DATABASE

FMODB ID: G69Z1

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

Total energy (hartree)

FMO2-HF: Electronic energy	-984884.794962
FMO2-HF: Nuclear repulsion	934437.86428
FMO2-HF: Total energy	-50446.930682
FMO2-MP2: Total energy	-50593.296479

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.
-1.675	1.327	0.182	-1.415	-1.769	-0.004

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 : -0.010 / q_NPA : -0.025

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	0.017	0.007	2.929	-1.086	0.836	0.084	-0.899	-1.107	0.000
4	A	5	THR	0	-0.058	-0.028	3.010	-0.659	0.417	0.099	-0.512	-0.663	-0.004
5	A	6	ALA	0	0.059	0.044	4.958	0.000	0.004	-0.001	-0.004	0.001	0.000
6	A	7	LYS	1	0.934	0.956	8.659	0.678	0.678	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.072	0.036	11.252	0.004	0.004	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.058	-0.007	14.817	0.018	0.018	0.000	0.000	0.000	0.000
9	A	10	ALA	0	0.037	0.016	17.675	0.006	0.006	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.917	0.947	20.573	0.114	0.114	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.055	0.008	23.932	0.004	0.004	0.000	0.000	0.000	0.000
12	A	13	GLY	0	-0.003	0.015	25.469	0.003	0.003	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.930	0.947	26.212	-0.013	-0.013	0.000	0.000	0.000	0.000
14	A	15	ALA	0	0.020	0.025	28.423	0.002	0.002	0.000	0.000	0.000	0.000
15	A	16	GLY	0	-0.002	0.014	26.474	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	17	HIS	1	0.798	0.874	23.831	0.088	0.088	0.000	0.000	0.000	0.000
17	A	18	ILE	0	-0.040	-0.022	19.669	-0.001	-0.001	0.000	0.000	0.000	0.000
18	A	19	THR	0	0.022	0.008	19.873	0.009	0.009	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.067	-0.048	15.073	0.007	0.007	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.919	-0.966	11.940	-0.459	-0.459	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.856	-0.923	14.668	-0.311	-0.311	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.036	-0.013	16.439	0.015	0.015	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.037	-0.003	17.116	0.027	0.027	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.058	-0.038	16.444	0.027	0.027	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.815	-0.894	19.677	-0.126	-0.126	0.000	0.000	0.000	0.000
26	A	27	PHE	0	-0.017	-0.010	21.509	0.011	0.011	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.826	-0.895	24.556	-0.061	-0.061	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.082	-0.041	22.658	0.003	0.003	0.000	0.000	0.000	0.000
29	A	30	VAL	0	0.002	0.007	26.782	0.001	0.001	0.000	0.000	0.000	0.000
30	A	31	MET	0	-0.033	-0.027	29.870	0.005	0.005	0.000	0.000	0.000	0.000
31	A	32	PRO	0	0.031	-0.007	32.470	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	33	ASN	0	-0.017	-0.002	34.722	0.000	0.000	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.035	0.027	33.540	-0.002	-0.002	0.000	0.000	0.000	0.000
34	A	35	ALA	0	0.047	0.029	35.620	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	36	ALA	0	-0.035	-0.023	38.088	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.027	-0.010	37.690	-0.001	-0.001	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.004	0.011	38.738	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.073	-0.035	33.447	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	40	THR	0	0.009	-0.004	31.343	0.002	0.002	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.005	-0.009	28.053	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	42	THR	0	0.023	0.000	22.849	0.007	0.007	0.000	0.000	0.000	0.000
42	A	43	ASN	0	-0.018	-0.007	24.962	0.005	0.005	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.035	0.007	21.692	-0.002	-0.002	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.803	-0.909	21.754	0.036	0.036	0.000	0.000	0.000	0.000
45	A	46	GLN	0	0.048	0.036	23.502	0.001	0.001	0.000	0.000	0.000	0.000
46	A	47	LEU	0	0.001	0.000	19.027	-0.001	-0.001	0.000	0.000	0.000	0.000
47	A	48	PHE	0	-0.001	0.007	17.557	0.002	0.002	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.003	-0.015	19.945	0.012	0.012	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.004	0.000	20.136	0.006	0.006	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.014	0.008	16.891	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.009	-0.041	17.051	0.016	0.016	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.016	0.009	18.867	0.014	0.014	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.010	0.018	17.427	0.005	0.005	0.000	0.000	0.000	0.000
54	A	55	CYS	0	-0.079	-0.005	14.106	0.089	0.089	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.001	-0.017	16.191	0.025	0.025	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.056	0.021	19.208	0.008	0.008	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.031	0.022	16.411	-0.004	-0.004	0.000	0.000	0.000	0.000
58	A	59	ALA	0	-0.044	-0.025	16.436	0.016	0.016	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.023	-0.019	17.529	0.009	0.009	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.928	-0.961	18.794	0.015	0.015	0.000	0.000	0.000	0.000
61	A	62	HIS	0	-0.010	-0.007	15.619	-0.014	-0.014	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.049	-0.035	18.674	0.008	0.008	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.013	0.016	21.051	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.996	0.992	20.706	-0.038	-0.038	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-1.010	-0.999	19.692	0.189	0.189	0.000	0.000	0.000	0.000
66	A	67	GLN	0	-0.096	-0.039	22.673	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.092	-0.053	25.542	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.032	-0.007	26.351	-0.010	-0.010	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.935	-0.959	25.790	0.021	0.021	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.046	-0.035	23.407	0.002	0.002	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.871	-0.926	26.468	0.001	0.001	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.061	-0.051	24.931	0.008	0.008	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.955	-0.973	26.740	0.000	0.000	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.011	-0.006	22.714	0.008	0.008	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.879	-0.910	25.488	0.021	0.021	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.000	-0.002	24.325	0.010	0.010	0.000	0.000	0.000	0.000
77	A	78	GLN	0	-0.066	-0.059	25.322	-0.006	-0.006	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.022	0.001	23.113	0.010	0.010	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.031	-0.018	26.490	-0.010	-0.010	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.017	-0.005	27.481	0.006	0.006	0.000	0.000	0.000	0.000
81	A	82	MET	0	-0.036	-0.021	29.580	-0.002	-0.002	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.979	0.988	31.377	-0.040	-0.040	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.818	-0.881	29.679	0.086	0.086	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.977	-1.015	32.579	0.049	0.049	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.129	-0.083	31.804	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.930	-0.963	29.806	0.066	0.066	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.047	-0.004	33.320	-0.005	-0.005	0.000	0.000	0.000	0.000
88	A	89	GLY	0	0.001	0.008	31.117	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.058	-0.047	28.790	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.975	0.992	26.886	-0.091	-0.091	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.001	-0.001	23.176	-0.009	-0.009	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.043	0.035	26.418	0.009	0.009	0.000	0.000	0.000	0.000
93	A	94	VAL	0	0.003	-0.015	22.742	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	95	THR	0	-0.007	0.000	26.094	0.007	0.007	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.004	0.003	22.024	-0.006	-0.006	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.016	0.019	26.453	0.003	0.003	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.011	-0.024	25.889	-0.005	-0.005	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.022	-0.024	28.426	0.002	0.002	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.038	0.007	27.652	0.000	0.000	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.890	0.947	30.237	-0.010	-0.010	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.903	-0.942	33.484	0.022	0.022	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.089	-0.019	29.034	0.002	0.002	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.875	-0.924	33.125	0.048	0.048	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.989	0.976	33.266	-0.056	-0.056	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.891	-0.953	33.238	0.066	0.066	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.903	0.965	28.653	-0.084	-0.084	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.034	0.013	29.232	0.009	0.009	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.056	-0.033	28.455	0.000	0.000	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.890	-0.951	27.412	0.127	0.127	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.020	0.001	24.700	0.016	0.016	0.000	0.000	0.000	0.000
111	A	112	VAL	0	0.025	0.016	23.654	0.013	0.013	0.000	0.000	0.000	0.000
112	A	113	ASN	0	-0.006	-0.009	23.666	0.011	0.011	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.033	0.019	22.140	0.020	0.020	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.012	0.010	19.607	0.035	0.035	0.000	0.000	0.000	0.000
115	A	116	HIS	0	0.031	0.019	18.825	0.032	0.032	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.928	-0.964	19.309	0.261	0.261	0.000	0.000	0.000	0.000
117	A	118	PHE	0	-0.059	-0.030	13.256	0.075	0.075	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.007	-0.008	10.410	0.014	0.014	0.000	0.000	0.000	0.000
119	A	121	TYR	0	0.040	-0.002	12.645	0.010	0.010	0.000	0.000	0.000	0.000
120	A	122	SER	0	0.036	0.032	15.322	-0.016	-0.016	0.000	0.000	0.000	0.000
121	A	123	LYS	1	0.888	0.961	11.980	-0.717	-0.717	0.000	0.000	0.000	0.000
122	A	124	ALA	0	-0.037	-0.017	13.568	0.000	0.000	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.024	-0.014	15.266	-0.027	-0.027	0.000	0.000	0.000	0.000
124	A	126	ARG	1	0.907	0.952	18.322	-0.319	-0.319	0.000	0.000	0.000	0.000
125	A	127	GLY	0	-0.035	-0.017	20.500	0.008	0.008	0.000	0.000	0.000	0.000
126	A	128	ASN	0	-0.045	-0.007	19.972	-0.025	-0.025	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.024	-0.016	22.782	-0.018	-0.018	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.935	-0.957	24.486	0.121	0.121	0.000	0.000	0.000	0.000
129	A	131	VAL	0	-0.062	-0.039	22.087	-0.013	-0.013	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.925	0.982	25.549	-0.075	-0.075	0.000	0.000	0.000	0.000
131	A	133	LEU	0	0.006	0.005	23.984	-0.004	-0.004	0.000	0.000	0.000	0.000
132	A	134	GLU	-1	-0.926	-0.959	28.054	0.060	0.060	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.001	0.014	30.069	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.925	0.970	31.907	-0.033	-0.033	0.000	0.000	0.000	0.000

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