FMO DATABASE

FMODB ID: N95JQ

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

Total energy (hartree)

FMO2-HF: Electronic energy	-986365.118769
FMO2-HF: Nuclear repulsion	935916.81308
FMO2-HF: Total energy	-50448.305689
FMO2-MP2: Total energy	-50594.715773

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.
-1.676	1.098	0.076	-1.277	-1.571	-0.003

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 : -0.011 / q_NPA : -0.021

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	0.015	0.015	3.558	-0.993	0.682	-0.002	-0.797	-0.875	0.001
4	A	5	THR	0	-0.053	-0.040	3.013	-1.314	-0.221	0.079	-0.479	-0.693	-0.004
5	A	6	ALA	0	0.045	0.043	5.236	0.100	0.106	-0.001	-0.001	-0.003	0.000
6	A	7	LYS	1	0.824	0.904	8.797	0.687	0.687	0.000	0.000	0.000	0.000
7	A	8	VAL	0	0.038	0.010	11.348	0.029	0.029	0.000	0.000	0.000	0.000
8	A	9	THR	0	-0.050	-0.002	14.966	0.004	0.004	0.000	0.000	0.000	0.000
9	A	10	ALA	0	0.038	0.012	17.792	0.014	0.014	0.000	0.000	0.000	0.000
10	A	11	ARG	1	0.929	0.956	20.618	0.141	0.141	0.000	0.000	0.000	0.000
11	A	12	GLY	0	0.064	0.030	24.192	0.005	0.005	0.000	0.000	0.000	0.000
12	A	13	GLY	0	-0.006	0.005	25.448	0.006	0.006	0.000	0.000	0.000	0.000
13	A	14	ARG	1	0.777	0.835	26.377	0.025	0.025	0.000	0.000	0.000	0.000
14	A	15	ALA	0	0.019	0.014	28.296	0.004	0.004	0.000	0.000	0.000	0.000
15	A	16	GLY	0	0.018	0.030	26.831	-0.001	-0.001	0.000	0.000	0.000	0.000
16	A	17	HIS	1	0.772	0.856	24.031	0.101	0.101	0.000	0.000	0.000	0.000
17	A	18	ILE	0	-0.048	-0.028	19.740	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	19	THR	0	0.023	-0.015	19.691	0.011	0.011	0.000	0.000	0.000	0.000
19	A	20	SER	0	-0.051	-0.043	15.052	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	21	ASP	-1	-0.876	-0.942	12.172	-0.504	-0.504	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.825	-0.885	14.489	-0.275	-0.275	0.000	0.000	0.000	0.000
22	A	23	GLY	0	-0.028	-0.015	16.242	0.024	0.024	0.000	0.000	0.000	0.000
23	A	24	VAL	0	-0.040	-0.013	17.267	0.026	0.026	0.000	0.000	0.000	0.000
24	A	25	LEU	0	-0.043	-0.024	16.321	0.025	0.025	0.000	0.000	0.000	0.000
25	A	26	ASP	-1	-0.824	-0.880	19.819	-0.134	-0.134	0.000	0.000	0.000	0.000
26	A	27	PHE	0	0.005	0.001	21.438	0.012	0.012	0.000	0.000	0.000	0.000
27	A	28	ASP	-1	-0.806	-0.881	24.613	-0.078	-0.078	0.000	0.000	0.000	0.000
28	A	29	ILE	0	-0.065	-0.030	22.676	0.004	0.004	0.000	0.000	0.000	0.000
29	A	30	VAL	0	0.004	0.004	26.793	0.002	0.002	0.000	0.000	0.000	0.000
30	A	31	MET	0	-0.012	-0.009	29.698	0.002	0.002	0.000	0.000	0.000	0.000
31	A	32	PRO	0	0.035	-0.003	32.532	0.000	0.000	0.000	0.000	0.000	0.000
32	A	33	ASN	0	0.007	0.008	35.011	0.001	0.001	0.000	0.000	0.000	0.000
33	A	34	ALA	0	0.005	0.008	33.657	0.000	0.000	0.000	0.000	0.000	0.000
34	A	35	ALA	0	0.055	0.025	35.760	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	36	ALA	0	-0.016	-0.008	38.147	0.000	0.000	0.000	0.000	0.000	0.000
36	A	37	ALA	0	-0.041	-0.013	37.891	0.000	0.000	0.000	0.000	0.000	0.000
37	A	38	GLY	0	0.000	0.014	39.185	-0.002	-0.002	0.000	0.000	0.000	0.000
38	A	39	GLN	0	-0.079	-0.044	33.868	-0.006	-0.006	0.000	0.000	0.000	0.000
39	A	40	THR	0	-0.007	-0.014	32.047	0.004	0.004	0.000	0.000	0.000	0.000
40	A	41	GLY	0	0.012	-0.001	28.302	-0.005	-0.005	0.000	0.000	0.000	0.000
41	A	42	THR	0	0.000	-0.006	23.123	0.006	0.006	0.000	0.000	0.000	0.000
42	A	43	ASN	0	0.011	-0.007	24.975	0.001	0.001	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.032	0.007	21.609	0.000	0.000	0.000	0.000	0.000	0.000
44	A	45	GLU	-1	-0.737	-0.834	21.907	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	46	GLN	0	0.051	0.043	23.870	0.002	0.002	0.000	0.000	0.000	0.000
46	A	47	LEU	0	-0.012	-0.006	19.218	0.002	0.002	0.000	0.000	0.000	0.000
47	A	48	PHE	0	0.005	-0.001	16.977	0.006	0.006	0.000	0.000	0.000	0.000
48	A	49	ALA	0	0.009	0.003	19.843	0.016	0.016	0.000	0.000	0.000	0.000
49	A	50	ALA	0	0.008	0.005	20.569	0.011	0.011	0.000	0.000	0.000	0.000
50	A	51	GLY	0	0.012	0.007	16.781	0.005	0.005	0.000	0.000	0.000	0.000
51	A	52	TYR	0	-0.010	-0.041	16.595	0.021	0.021	0.000	0.000	0.000	0.000
52	A	53	ALA	0	0.027	0.015	18.495	0.021	0.021	0.000	0.000	0.000	0.000
53	A	54	ALA	0	0.014	0.013	16.944	0.011	0.011	0.000	0.000	0.000	0.000
54	A	55	CYS	0	-0.066	0.006	14.052	0.114	0.114	0.000	0.000	0.000	0.000
55	A	56	PHE	0	0.019	-0.015	15.762	0.038	0.038	0.000	0.000	0.000	0.000
56	A	57	GLY	0	0.044	0.028	18.872	0.008	0.008	0.000	0.000	0.000	0.000
57	A	58	GLY	0	0.036	0.015	16.136	0.002	0.002	0.000	0.000	0.000	0.000
58	A	59	ALA	0	-0.062	-0.030	16.166	0.030	0.030	0.000	0.000	0.000	0.000
59	A	60	LEU	0	-0.004	-0.013	17.222	0.010	0.010	0.000	0.000	0.000	0.000
60	A	61	GLU	-1	-0.902	-0.951	19.129	0.121	0.121	0.000	0.000	0.000	0.000
61	A	62	HIS	0	-0.080	-0.048	15.608	0.003	0.003	0.000	0.000	0.000	0.000
62	A	63	VAL	0	-0.026	-0.034	18.480	0.001	0.001	0.000	0.000	0.000	0.000
63	A	64	ALA	0	0.018	0.024	20.867	-0.011	-0.011	0.000	0.000	0.000	0.000
64	A	65	LYS	1	0.852	0.908	20.249	-0.131	-0.131	0.000	0.000	0.000	0.000
65	A	66	GLU	-1	-0.907	-0.939	18.512	0.335	0.335	0.000	0.000	0.000	0.000
66	A	67	GLN	0	-0.065	-0.023	22.441	-0.021	-0.021	0.000	0.000	0.000	0.000
67	A	68	ASN	0	-0.109	-0.057	25.261	-0.021	-0.021	0.000	0.000	0.000	0.000
68	A	69	ILE	0	-0.015	0.002	26.282	-0.014	-0.014	0.000	0.000	0.000	0.000
69	A	70	GLU	-1	-0.848	-0.902	25.558	0.112	0.112	0.000	0.000	0.000	0.000
70	A	71	ILE	0	-0.027	-0.022	23.260	-0.003	-0.003	0.000	0.000	0.000	0.000
71	A	72	ASP	-1	-0.831	-0.900	26.581	0.043	0.043	0.000	0.000	0.000	0.000
72	A	73	SER	0	-0.041	-0.030	24.941	0.007	0.007	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.843	-0.906	26.595	0.034	0.034	0.000	0.000	0.000	0.000
74	A	75	ILE	0	-0.004	-0.006	22.019	0.007	0.007	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.895	-0.930	25.025	0.027	0.027	0.000	0.000	0.000	0.000
76	A	77	GLY	0	0.017	0.004	23.911	0.007	0.007	0.000	0.000	0.000	0.000
77	A	78	GLN	0	-0.045	-0.032	24.846	-0.009	-0.009	0.000	0.000	0.000	0.000
78	A	79	VAL	0	-0.026	-0.001	23.022	0.007	0.007	0.000	0.000	0.000	0.000
79	A	80	SER	0	-0.018	-0.012	26.354	-0.008	-0.008	0.000	0.000	0.000	0.000
80	A	81	LEU	0	-0.014	-0.004	27.478	0.004	0.004	0.000	0.000	0.000	0.000
81	A	82	MET	0	-0.020	-0.010	29.267	0.001	0.001	0.000	0.000	0.000	0.000
82	A	83	LYS	1	0.897	0.933	31.101	-0.016	-0.016	0.000	0.000	0.000	0.000
83	A	84	ASP	-1	-0.798	-0.880	29.805	0.039	0.039	0.000	0.000	0.000	0.000
84	A	85	GLU	-1	-0.880	-0.937	32.587	0.017	0.017	0.000	0.000	0.000	0.000
85	A	86	SER	0	-0.098	-0.058	32.044	0.000	0.000	0.000	0.000	0.000	0.000
86	A	87	ASP	-1	-0.902	-0.944	30.859	0.008	0.008	0.000	0.000	0.000	0.000
87	A	88	GLY	0	-0.028	-0.016	33.207	-0.003	-0.003	0.000	0.000	0.000	0.000
88	A	89	GLY	0	-0.031	-0.004	31.312	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	90	PHE	0	-0.056	-0.044	29.034	0.001	0.001	0.000	0.000	0.000	0.000
90	A	91	LYS	1	0.889	0.946	26.826	-0.044	-0.044	0.000	0.000	0.000	0.000
91	A	92	ILE	0	-0.010	-0.010	23.373	-0.006	-0.006	0.000	0.000	0.000	0.000
92	A	93	GLY	0	0.054	0.032	26.186	0.007	0.007	0.000	0.000	0.000	0.000
93	A	94	VAL	0	-0.052	-0.042	22.856	-0.006	-0.006	0.000	0.000	0.000	0.000
94	A	95	THR	0	0.022	0.014	26.212	0.006	0.006	0.000	0.000	0.000	0.000
95	A	96	LEU	0	-0.031	-0.010	21.798	-0.004	-0.004	0.000	0.000	0.000	0.000
96	A	97	VAL	0	0.020	0.013	26.160	0.005	0.005	0.000	0.000	0.000	0.000
97	A	98	VAL	0	-0.011	-0.001	25.452	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	99	ASN	0	-0.050	-0.053	28.118	0.000	0.000	0.000	0.000	0.000	0.000
99	A	100	THR	0	0.046	0.004	27.629	0.005	0.005	0.000	0.000	0.000	0.000
100	A	101	LYS	1	0.800	0.896	30.083	-0.044	-0.044	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.919	-0.958	33.495	0.049	0.049	0.000	0.000	0.000	0.000
102	A	103	LEU	0	-0.067	-0.007	28.977	0.002	0.002	0.000	0.000	0.000	0.000
103	A	104	ASP	-1	-0.864	-0.931	33.155	0.074	0.074	0.000	0.000	0.000	0.000
104	A	105	ARG	1	0.893	0.942	33.228	-0.067	-0.067	0.000	0.000	0.000	0.000
105	A	106	GLU	-1	-0.913	-0.971	32.934	0.082	0.082	0.000	0.000	0.000	0.000
106	A	107	LYS	1	0.820	0.887	29.311	-0.123	-0.123	0.000	0.000	0.000	0.000
107	A	108	ALA	0	0.058	0.023	28.892	0.011	0.011	0.000	0.000	0.000	0.000
108	A	109	GLN	0	-0.005	-0.012	28.178	0.000	0.000	0.000	0.000	0.000	0.000
109	A	110	GLU	-1	-0.860	-0.903	27.382	0.153	0.153	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.022	0.015	24.436	0.015	0.015	0.000	0.000	0.000	0.000
111	A	112	VAL	0	0.021	0.004	23.580	0.016	0.016	0.000	0.000	0.000	0.000
112	A	113	ASN	0	-0.025	-0.018	23.608	0.007	0.007	0.000	0.000	0.000	0.000
113	A	114	ALA	0	0.009	-0.001	22.097	0.017	0.017	0.000	0.000	0.000	0.000
114	A	115	ALA	0	0.023	0.015	19.469	0.035	0.035	0.000	0.000	0.000	0.000
115	A	116	HIS	0	0.049	0.044	18.599	0.030	0.030	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.825	-0.884	18.861	0.255	0.255	0.000	0.000	0.000	0.000
117	A	118	PHE	0	-0.027	0.002	13.653	0.068	0.068	0.000	0.000	0.000	0.000
118	A	120	PRO	0	0.015	-0.008	10.198	-0.018	-0.018	0.000	0.000	0.000	0.000
119	A	121	TYR	0	0.038	0.005	12.515	-0.026	-0.026	0.000	0.000	0.000	0.000
120	A	122	SER	0	0.040	0.033	15.267	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	123	LYS	1	0.799	0.920	13.195	-0.554	-0.554	0.000	0.000	0.000	0.000
122	A	124	ALA	0	-0.007	-0.013	13.441	-0.019	-0.019	0.000	0.000	0.000	0.000
123	A	125	THR	0	-0.005	-0.019	15.294	-0.029	-0.029	0.000	0.000	0.000	0.000
124	A	126	ARG	1	0.786	0.863	18.392	-0.253	-0.253	0.000	0.000	0.000	0.000
125	A	127	GLY	0	-0.016	-0.012	20.279	-0.003	-0.003	0.000	0.000	0.000	0.000
126	A	128	ASN	0	-0.077	-0.036	21.096	-0.025	-0.025	0.000	0.000	0.000	0.000
127	A	129	VAL	0	-0.006	-0.003	22.264	-0.014	-0.014	0.000	0.000	0.000	0.000
128	A	130	ASP	-1	-0.871	-0.920	24.478	0.079	0.079	0.000	0.000	0.000	0.000
129	A	131	VAL	0	-0.039	-0.027	22.024	-0.008	-0.008	0.000	0.000	0.000	0.000
130	A	132	LYS	1	0.817	0.928	25.492	-0.061	-0.061	0.000	0.000	0.000	0.000
131	A	133	LEU	0	-0.011	-0.010	23.743	0.001	0.001	0.000	0.000	0.000	0.000
132	A	134	GLU	-1	-0.891	-0.945	27.752	0.058	0.058	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.011	0.008	29.274	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	136	LYS	1	0.892	0.960	31.572	-0.047	-0.047	0.000	0.000	0.000	0.000

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