FMO DATABASE

FMODB ID: 98M32

Calculation Name: 2BMX-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2BMX

Chain ID: A

ChEMBL ID:

UniProt ID: P9WQB7

Base Structure: X-ray

Registration Date: 2023-09-22

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	169
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1736635.086347
FMO2-HF: Nuclear repulsion	1671664.403725
FMO2-HF: Total energy	-64970.682622
FMO2-MP2: Total energy	-65163.884482

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:PRO)

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

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.
-2.264	-0.621	0.003	-0.678	-0.967	0.002

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.065 / q_NPA : -0.047

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	LEU	0	-0.012	0.012	3.844	-1.407	-0.092	-0.006	-0.493	-0.816	0.002
4	A	5	THR	0	-0.043	-0.041	6.288	0.686	0.686	0.000	0.000	0.000	0.000
5	A	6	ILE	0	-0.018	-0.016	8.477	-0.034	-0.034	0.000	0.000	0.000	0.000
6	A	7	GLY	0	0.012	0.015	11.930	-0.006	-0.006	0.000	0.000	0.000	0.000
7	A	8	ASP	-1	-0.867	-0.917	7.748	-1.249	-1.249	0.000	0.000	0.000	0.000
8	A	9	GLN	0	-0.047	-0.034	11.008	0.091	0.091	0.000	0.000	0.000	0.000
9	A	10	PHE	0	0.015	0.007	11.183	-0.155	-0.155	0.000	0.000	0.000	0.000
10	A	11	PRO	0	-0.025	-0.012	10.077	0.050	0.050	0.000	0.000	0.000	0.000
11	A	12	ALA	0	0.044	0.021	12.752	0.079	0.079	0.000	0.000	0.000	0.000
12	A	13	TYR	0	-0.034	-0.026	15.207	-0.034	-0.034	0.000	0.000	0.000	0.000
13	A	14	GLN	0	0.021	0.006	17.479	0.019	0.019	0.000	0.000	0.000	0.000
14	A	15	LEU	0	-0.063	-0.013	16.328	-0.005	-0.005	0.000	0.000	0.000	0.000
15	A	16	THR	0	0.002	-0.004	21.016	0.004	0.004	0.000	0.000	0.000	0.000
16	A	17	ALA	0	-0.011	-0.002	22.286	-0.004	-0.004	0.000	0.000	0.000	0.000
17	A	18	LEU	0	-0.053	-0.013	24.346	0.005	0.005	0.000	0.000	0.000	0.000
18	A	19	ILE	0	0.033	0.016	26.253	-0.004	-0.004	0.000	0.000	0.000	0.000
19	A	20	GLY	0	0.024	0.033	28.737	0.006	0.006	0.000	0.000	0.000	0.000
20	A	21	GLY	0	0.027	0.005	29.252	-0.001	-0.001	0.000	0.000	0.000	0.000
21	A	22	ASP	-1	-0.815	-0.906	32.411	0.000	0.000	0.000	0.000	0.000	0.000
22	A	23	LEU	0	0.048	0.024	31.076	-0.003	-0.003	0.000	0.000	0.000	0.000
23	A	24	SER	0	-0.075	-0.034	34.954	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	25	LYS	1	0.785	0.864	37.837	0.007	0.007	0.000	0.000	0.000	0.000
25	A	26	VAL	0	0.025	0.039	34.802	-0.002	-0.002	0.000	0.000	0.000	0.000
26	A	27	ASP	-1	-0.821	-0.899	38.207	-0.024	-0.024	0.000	0.000	0.000	0.000
27	A	28	ALA	0	0.006	0.000	39.253	0.001	0.001	0.000	0.000	0.000	0.000
28	A	29	LYS	1	0.753	0.876	39.626	0.031	0.031	0.000	0.000	0.000	0.000
29	A	30	GLN	0	-0.064	-0.027	36.388	-0.001	-0.001	0.000	0.000	0.000	0.000
30	A	31	PRO	0	0.016	-0.013	35.199	0.000	0.000	0.000	0.000	0.000	0.000
31	A	32	GLY	0	0.023	0.007	33.222	0.000	0.000	0.000	0.000	0.000	0.000
32	A	33	ASP	-1	-0.773	-0.887	33.230	-0.036	-0.036	0.000	0.000	0.000	0.000
33	A	34	TYR	0	-0.056	-0.032	32.038	0.001	0.001	0.000	0.000	0.000	0.000
34	A	35	PHE	0	-0.056	-0.032	27.920	0.001	0.001	0.000	0.000	0.000	0.000
35	A	36	THR	0	0.018	0.012	27.032	0.002	0.002	0.000	0.000	0.000	0.000
36	A	37	THR	0	-0.066	-0.030	24.548	-0.004	-0.004	0.000	0.000	0.000	0.000
37	A	38	ILE	0	0.004	0.010	22.135	0.008	0.008	0.000	0.000	0.000	0.000
38	A	39	THR	0	-0.054	-0.057	21.523	-0.017	-0.017	0.000	0.000	0.000	0.000
39	A	40	SER	0	-0.040	-0.046	18.164	0.001	0.001	0.000	0.000	0.000	0.000
40	A	41	ASP	-1	-0.902	-0.927	20.196	-0.218	-0.218	0.000	0.000	0.000	0.000
41	A	42	GLU	-1	-0.865	-0.922	23.393	-0.108	-0.108	0.000	0.000	0.000	0.000
42	A	43	HIS	0	0.024	0.009	24.921	0.013	0.013	0.000	0.000	0.000	0.000
43	A	44	PRO	0	0.000	0.008	25.372	-0.006	-0.006	0.000	0.000	0.000	0.000
44	A	45	GLY	0	-0.022	-0.025	25.837	0.011	0.011	0.000	0.000	0.000	0.000
45	A	46	LYS	1	0.775	0.890	25.488	0.080	0.080	0.000	0.000	0.000	0.000
46	A	47	TRP	0	0.026	0.012	20.275	-0.020	-0.020	0.000	0.000	0.000	0.000
47	A	48	ARG	1	0.851	0.912	18.271	0.226	0.226	0.000	0.000	0.000	0.000
48	A	49	VAL	0	-0.006	0.010	19.059	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	50	VAL	0	0.007	0.008	15.267	0.007	0.007	0.000	0.000	0.000	0.000
50	A	51	PHE	0	-0.018	-0.015	15.580	0.019	0.019	0.000	0.000	0.000	0.000
51	A	52	PHE	0	0.072	0.025	12.164	-0.018	-0.018	0.000	0.000	0.000	0.000
52	A	53	TRP	0	-0.073	-0.038	14.601	0.049	0.049	0.000	0.000	0.000	0.000
53	A	54	PRO	0	0.009	0.005	14.188	-0.033	-0.033	0.000	0.000	0.000	0.000
54	A	55	LYS	1	0.956	0.969	15.366	-0.183	-0.183	0.000	0.000	0.000	0.000
55	A	56	ASP	-1	-0.735	-0.849	18.813	0.030	0.030	0.000	0.000	0.000	0.000
56	A	57	PHE	0	-0.075	-0.040	22.137	0.008	0.008	0.000	0.000	0.000	0.000
57	A	58	THR	0	-0.072	-0.025	20.560	0.011	0.011	0.000	0.000	0.000	0.000
58	A	59	PHE	0	-0.009	-0.016	23.517	-0.007	-0.007	0.000	0.000	0.000	0.000
59	A	60	VAL	0	0.033	0.014	22.531	0.016	0.016	0.000	0.000	0.000	0.000
60	A	61	CYS	0	-0.022	0.003	25.032	-0.006	-0.006	0.000	0.000	0.000	0.000
61	A	62	PRO	0	0.087	0.034	27.654	-0.003	-0.003	0.000	0.000	0.000	0.000
62	A	63	THR	0	-0.019	-0.019	29.352	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	64	GLU	-1	-0.832	-0.908	22.040	0.111	0.111	0.000	0.000	0.000	0.000
64	A	65	ILE	0	0.038	0.017	25.709	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	66	ALA	0	-0.019	-0.008	28.390	-0.009	-0.009	0.000	0.000	0.000	0.000
66	A	67	ALA	0	-0.007	-0.007	27.798	-0.005	-0.005	0.000	0.000	0.000	0.000
67	A	68	PHE	0	0.035	-0.002	22.119	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	69	SER	0	-0.049	-0.033	27.963	-0.008	-0.008	0.000	0.000	0.000	0.000
69	A	70	LYS	1	0.859	0.936	31.576	-0.030	-0.030	0.000	0.000	0.000	0.000
70	A	71	LEU	0	0.012	0.008	27.637	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	72	ASN	0	-0.072	-0.042	29.435	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	73	ASP	-1	-0.821	-0.904	30.386	-0.014	-0.014	0.000	0.000	0.000	0.000
73	A	74	GLU	-1	-0.883	-0.915	30.479	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	75	PHE	0	-0.036	-0.020	23.648	0.000	0.000	0.000	0.000	0.000	0.000
75	A	76	GLU	-1	-0.918	-0.949	28.350	-0.040	-0.040	0.000	0.000	0.000	0.000
76	A	77	ASP	-1	-0.908	-0.954	30.850	-0.026	-0.026	0.000	0.000	0.000	0.000
77	A	78	ARG	1	0.679	0.808	27.355	0.009	0.009	0.000	0.000	0.000	0.000
78	A	79	ASP	-1	-0.792	-0.871	27.502	-0.075	-0.075	0.000	0.000	0.000	0.000
79	A	80	ALA	0	-0.016	-0.011	24.152	-0.014	-0.014	0.000	0.000	0.000	0.000
80	A	81	GLN	0	-0.031	-0.013	24.045	0.010	0.010	0.000	0.000	0.000	0.000
81	A	82	ILE	0	0.019	0.005	22.191	-0.012	-0.012	0.000	0.000	0.000	0.000
82	A	83	LEU	0	-0.011	-0.006	19.468	-0.004	-0.004	0.000	0.000	0.000	0.000
83	A	84	GLY	0	-0.004	0.000	19.151	0.011	0.011	0.000	0.000	0.000	0.000
84	A	85	VAL	0	-0.012	-0.009	14.720	-0.022	-0.022	0.000	0.000	0.000	0.000
85	A	86	SER	0	0.008	-0.020	15.263	0.024	0.024	0.000	0.000	0.000	0.000
86	A	87	ILE	0	0.027	0.009	13.556	-0.027	-0.027	0.000	0.000	0.000	0.000
87	A	88	ASP	-1	-0.829	-0.870	16.562	0.035	0.035	0.000	0.000	0.000	0.000
88	A	89	SER	0	0.010	0.029	20.222	-0.011	-0.011	0.000	0.000	0.000	0.000
89	A	90	GLU	-1	-0.770	-0.890	23.026	-0.054	-0.054	0.000	0.000	0.000	0.000
90	A	91	PHE	0	-0.014	-0.016	24.975	0.008	0.008	0.000	0.000	0.000	0.000
91	A	92	ALA	0	-0.031	-0.001	23.933	0.007	0.007	0.000	0.000	0.000	0.000
92	A	93	HIS	1	0.863	0.890	20.395	0.026	0.026	0.000	0.000	0.000	0.000
93	A	94	PHE	0	-0.010	0.004	25.550	0.005	0.005	0.000	0.000	0.000	0.000
94	A	95	GLN	0	0.010	-0.005	29.201	0.006	0.006	0.000	0.000	0.000	0.000
95	A	96	TRP	0	-0.002	-0.002	22.138	0.003	0.003	0.000	0.000	0.000	0.000
96	A	97	ARG	1	0.827	0.891	27.018	0.012	0.012	0.000	0.000	0.000	0.000
97	A	98	ALA	0	-0.063	-0.021	30.092	-0.001	-0.001	0.000	0.000	0.000	0.000
98	A	99	GLN	0	-0.024	-0.009	32.455	0.001	0.001	0.000	0.000	0.000	0.000
99	A	100	HIS	0	-0.024	-0.013	29.115	0.005	0.005	0.000	0.000	0.000	0.000
100	A	101	ASN	0	-0.027	-0.032	32.178	-0.004	-0.004	0.000	0.000	0.000	0.000
101	A	102	ASP	-1	-0.854	-0.924	31.330	0.038	0.038	0.000	0.000	0.000	0.000
102	A	103	LEU	0	0.011	0.012	26.433	-0.002	-0.002	0.000	0.000	0.000	0.000
103	A	104	LYS	1	0.842	0.952	30.246	-0.012	-0.012	0.000	0.000	0.000	0.000
104	A	105	THR	0	0.006	-0.029	33.173	-0.004	-0.004	0.000	0.000	0.000	0.000
105	A	106	LEU	0	-0.005	0.015	24.922	0.000	0.000	0.000	0.000	0.000	0.000
106	A	107	PRO	0	0.051	0.032	28.541	-0.005	-0.005	0.000	0.000	0.000	0.000
107	A	108	PHE	0	-0.007	0.005	22.203	-0.004	-0.004	0.000	0.000	0.000	0.000
108	A	109	PRO	0	0.009	-0.002	24.075	0.006	0.006	0.000	0.000	0.000	0.000
109	A	110	MET	0	-0.060	-0.018	21.891	0.002	0.002	0.000	0.000	0.000	0.000
110	A	111	LEU	0	0.078	0.027	18.504	0.001	0.001	0.000	0.000	0.000	0.000
111	A	112	SER	0	-0.055	-0.041	19.460	0.014	0.014	0.000	0.000	0.000	0.000
112	A	113	ASP	-1	-0.706	-0.844	12.953	-0.288	-0.288	0.000	0.000	0.000	0.000
113	A	114	ILE	0	-0.010	-0.007	15.765	-0.002	-0.002	0.000	0.000	0.000	0.000
114	A	115	LYS	1	0.762	0.863	16.382	0.234	0.234	0.000	0.000	0.000	0.000
115	A	116	ARG	1	0.836	0.923	11.702	0.056	0.056	0.000	0.000	0.000	0.000
116	A	117	GLU	-1	-0.796	-0.881	11.198	-0.344	-0.344	0.000	0.000	0.000	0.000
117	A	118	LEU	0	0.006	0.008	10.897	-0.122	-0.122	0.000	0.000	0.000	0.000
118	A	119	SER	0	-0.008	-0.049	9.439	-0.089	-0.089	0.000	0.000	0.000	0.000
119	A	120	GLN	0	-0.065	-0.034	6.690	-0.061	-0.061	0.000	0.000	0.000	0.000
120	A	121	ALA	0	-0.028	-0.008	5.990	-0.523	-0.523	0.000	0.000	0.000	0.000
121	A	122	ALA	0	0.051	0.020	7.564	-0.251	-0.251	0.000	0.000	0.000	0.000
122	A	123	GLY	0	0.007	0.009	3.620	-0.478	-0.276	0.008	-0.099	-0.111	0.000
123	A	124	VAL	0	-0.029	-0.022	3.986	1.368	1.494	0.001	-0.086	-0.040	0.000
124	A	125	LEU	0	-0.066	-0.021	6.104	0.229	0.229	0.000	0.000	0.000	0.000
125	A	126	ASN	0	0.005	-0.011	6.024	0.054	0.054	0.000	0.000	0.000	0.000
126	A	127	ALA	0	-0.013	-0.019	8.263	-0.165	-0.165	0.000	0.000	0.000	0.000
127	A	128	ASP	-1	-0.954	-0.960	10.086	0.275	0.275	0.000	0.000	0.000	0.000
128	A	129	GLY	0	-0.071	-0.025	11.453	-0.064	-0.064	0.000	0.000	0.000	0.000
129	A	130	VAL	0	0.002	-0.013	11.678	-0.089	-0.089	0.000	0.000	0.000	0.000
130	A	131	ALA	0	0.057	0.040	9.943	0.054	0.054	0.000	0.000	0.000	0.000
131	A	132	ASP	-1	-0.820	-0.909	8.646	0.989	0.989	0.000	0.000	0.000	0.000
132	A	133	ARG	1	0.852	0.920	10.990	-0.342	-0.342	0.000	0.000	0.000	0.000
133	A	134	VAL	0	-0.009	-0.001	8.840	0.080	0.080	0.000	0.000	0.000	0.000
134	A	135	THR	0	-0.009	-0.011	12.278	-0.076	-0.076	0.000	0.000	0.000	0.000
135	A	136	PHE	0	0.025	0.016	8.524	0.071	0.071	0.000	0.000	0.000	0.000
136	A	137	ILE	0	-0.007	0.000	14.401	0.021	0.021	0.000	0.000	0.000	0.000
137	A	138	VAL	0	-0.006	0.001	15.160	-0.031	-0.031	0.000	0.000	0.000	0.000
138	A	139	ASP	-1	-0.710	-0.836	17.659	-0.169	-0.169	0.000	0.000	0.000	0.000
139	A	140	PRO	0	-0.008	-0.013	20.448	-0.020	-0.020	0.000	0.000	0.000	0.000
140	A	141	ASN	0	-0.093	-0.047	19.903	0.011	0.011	0.000	0.000	0.000	0.000
141	A	142	ASN	0	-0.050	-0.016	15.599	0.002	0.002	0.000	0.000	0.000	0.000
142	A	143	GLU	-1	-0.888	-0.928	15.131	-0.325	-0.325	0.000	0.000	0.000	0.000
143	A	144	ILE	0	-0.034	-0.018	10.451	0.058	0.058	0.000	0.000	0.000	0.000
144	A	145	GLN	0	-0.026	-0.033	14.196	0.014	0.014	0.000	0.000	0.000	0.000
145	A	146	PHE	0	-0.020	-0.021	14.432	0.053	0.053	0.000	0.000	0.000	0.000
146	A	147	VAL	0	0.001	0.010	9.121	-0.030	-0.030	0.000	0.000	0.000	0.000
147	A	148	SER	0	-0.060	-0.011	12.265	0.076	0.076	0.000	0.000	0.000	0.000
148	A	149	ALA	0	0.046	0.015	9.889	-0.035	-0.035	0.000	0.000	0.000	0.000
149	A	150	THR	0	-0.042	-0.018	11.778	0.039	0.039	0.000	0.000	0.000	0.000
150	A	151	ALA	0	0.067	0.037	13.134	0.022	0.022	0.000	0.000	0.000	0.000
151	A	152	GLY	0	-0.006	-0.006	14.286	-0.078	-0.078	0.000	0.000	0.000	0.000
152	A	153	SER	0	-0.018	-0.023	17.116	-0.010	-0.010	0.000	0.000	0.000	0.000
153	A	154	VAL	0	-0.014	0.011	18.358	-0.032	-0.032	0.000	0.000	0.000	0.000
154	A	155	GLY	0	-0.012	0.000	19.588	0.000	0.000	0.000	0.000	0.000	0.000
155	A	156	ARG	1	0.822	0.906	16.013	-0.103	-0.103	0.000	0.000	0.000	0.000
156	A	157	ASN	0	-0.001	0.000	21.230	-0.029	-0.029	0.000	0.000	0.000	0.000
157	A	158	VAL	0	0.013	-0.008	22.554	-0.001	-0.001	0.000	0.000	0.000	0.000
158	A	159	ASP	-1	-0.883	-0.935	24.229	0.037	0.037	0.000	0.000	0.000	0.000
159	A	160	GLU	-1	-0.839	-0.911	20.944	0.087	0.087	0.000	0.000	0.000	0.000
160	A	161	VAL	0	-0.021	-0.018	19.080	-0.006	-0.006	0.000	0.000	0.000	0.000
161	A	162	LEU	0	0.035	0.033	21.488	-0.016	-0.016	0.000	0.000	0.000	0.000
162	A	163	ARG	1	0.868	0.923	22.186	-0.068	-0.068	0.000	0.000	0.000	0.000
163	A	164	VAL	0	-0.070	-0.038	18.604	-0.004	-0.004	0.000	0.000	0.000	0.000
164	A	165	LEU	0	0.008	0.005	22.067	-0.012	-0.012	0.000	0.000	0.000	0.000
165	A	166	ASP	-1	-0.839	-0.905	22.967	-0.010	-0.010	0.000	0.000	0.000	0.000
166	A	167	ALA	0	-0.027	-0.019	23.339	-0.004	-0.004	0.000	0.000	0.000	0.000
167	A	168	LEU	0	-0.075	-0.039	18.522	-0.006	-0.006	0.000	0.000	0.000	0.000
168	A	169	GLN	0	-0.018	-0.011	22.936	-0.005	-0.005	0.000	0.000	0.000	0.000
169	A	170	SER	0	-0.128	-0.051	26.285	0.006	0.006	0.000	0.000	0.000	0.000

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