FMO DATABASE

FMODB ID: 43YLN

Calculation Name: 3CXJ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3CXJ

Chain ID: A

ChEMBL ID:

UniProt ID: O27461

Base Structure: X-ray

Registration Date: 2023-03-14

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	144
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1392239.602398
FMO2-HF: Nuclear repulsion	1332521.113779
FMO2-HF: Total energy	-59718.48862
FMO2-MP2: Total energy	-59891.313506

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:3:LEU)

Summations of interaction energy for fragment #1(A:3:LEU)

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.
-5.723	-1.029	1.089	-1.538	-4.246	0.006

Interaction energy analysis for fragmet #1(A:3:LEU)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.043 / q_NPA : 0.018

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	5	GLN	0	0.100	0.047	2.499	-6.091	-3.297	0.555	-0.981	-2.368	0.009
4	A	6	GLU	-1	-0.929	-0.950	2.828	-3.259	-1.970	0.523	-0.452	-1.361	-0.003
5	A	7	MET	0	-0.040	-0.016	3.428	-0.049	0.562	0.011	-0.105	-0.517	0.000
6	A	8	ILE	0	0.000	0.009	6.197	0.246	0.246	0.000	0.000	0.000	0.000
7	A	9	LYS	1	0.963	0.989	6.941	0.376	0.376	0.000	0.000	0.000	0.000
8	A	10	LYS	1	0.926	0.970	7.912	0.833	0.833	0.000	0.000	0.000	0.000
9	A	11	TRP	0	-0.031	-0.042	8.049	0.075	0.075	0.000	0.000	0.000	0.000
10	A	12	LEU	0	0.000	0.003	11.597	0.058	0.058	0.000	0.000	0.000	0.000
11	A	13	ASP	-1	-0.826	-0.929	12.990	-0.205	-0.205	0.000	0.000	0.000	0.000
12	A	14	GLU	-1	-0.945	-0.944	12.654	-0.435	-0.435	0.000	0.000	0.000	0.000
13	A	15	GLU	-1	-0.918	-0.965	15.726	-0.148	-0.148	0.000	0.000	0.000	0.000
14	A	16	GLY	0	-0.045	-0.013	17.807	0.025	0.025	0.000	0.000	0.000	0.000
15	A	17	PHE	0	-0.060	-0.036	16.942	0.026	0.026	0.000	0.000	0.000	0.000
16	A	18	LEU	0	-0.037	-0.022	12.036	0.030	0.030	0.000	0.000	0.000	0.000
17	A	19	ARG	1	0.915	0.984	15.978	0.046	0.046	0.000	0.000	0.000	0.000
18	A	20	MET	0	-0.039	-0.025	15.933	-0.016	-0.016	0.000	0.000	0.000	0.000
19	A	21	GLU	-1	-0.922	-0.961	10.030	0.070	0.070	0.000	0.000	0.000	0.000
20	A	22	VAL	0	-0.046	-0.026	13.636	-0.026	-0.026	0.000	0.000	0.000	0.000
21	A	23	PRO	0	-0.009	-0.005	14.415	0.040	0.040	0.000	0.000	0.000	0.000
22	A	24	ASP	-1	-0.795	-0.917	14.911	0.265	0.265	0.000	0.000	0.000	0.000
23	A	25	GLU	-1	-0.933	-0.962	15.704	0.226	0.226	0.000	0.000	0.000	0.000
24	A	26	ASN	0	-0.097	-0.033	17.418	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	27	ALA	0	-0.009	-0.022	13.562	0.022	0.022	0.000	0.000	0.000	0.000
26	A	28	ARG	1	0.825	0.924	8.623	-0.883	-0.883	0.000	0.000	0.000	0.000
27	A	29	PHE	0	-0.002	-0.016	6.717	0.062	0.062	0.000	0.000	0.000	0.000
28	A	30	HIS	0	0.015	-0.012	10.159	-0.034	-0.034	0.000	0.000	0.000	0.000
29	A	31	TYR	0	-0.085	-0.047	6.632	-0.172	-0.172	0.000	0.000	0.000	0.000
30	A	32	VAL	0	0.059	0.038	13.454	0.010	0.010	0.000	0.000	0.000	0.000
31	A	33	VAL	0	-0.020	-0.018	15.530	-0.035	-0.035	0.000	0.000	0.000	0.000
32	A	34	ASN	0	-0.029	-0.025	17.915	0.004	0.004	0.000	0.000	0.000	0.000
33	A	35	TYR	0	0.038	0.080	21.399	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	36	PRO	0	-0.049	-0.024	23.167	0.012	0.012	0.000	0.000	0.000	0.000
35	A	37	GLU	-1	-0.865	-0.964	25.853	-0.018	-0.018	0.000	0.000	0.000	0.000
36	A	38	ASP	-1	-0.897	-0.946	25.286	-0.018	-0.018	0.000	0.000	0.000	0.000
37	A	39	HIS	0	-0.131	-0.087	24.665	0.015	0.015	0.000	0.000	0.000	0.000
38	A	40	VAL	0	0.021	0.001	21.237	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	41	ILE	0	-0.091	-0.043	19.007	0.005	0.005	0.000	0.000	0.000	0.000
40	A	42	ASP	-1	-0.861	-0.932	17.552	0.120	0.120	0.000	0.000	0.000	0.000
41	A	43	ILE	0	-0.064	-0.035	12.076	0.008	0.008	0.000	0.000	0.000	0.000
42	A	44	ILE	0	0.065	0.028	13.178	0.034	0.034	0.000	0.000	0.000	0.000
43	A	45	GLN	0	-0.025	0.006	8.115	0.244	0.244	0.000	0.000	0.000	0.000
44	A	46	PRO	0	0.016	-0.010	11.952	0.002	0.002	0.000	0.000	0.000	0.000
45	A	47	ALA	0	0.043	0.027	13.235	0.095	0.095	0.000	0.000	0.000	0.000
46	A	48	GLY	0	-0.061	-0.023	13.695	0.087	0.087	0.000	0.000	0.000	0.000
47	A	49	LYS	1	0.921	0.966	13.824	-0.426	-0.426	0.000	0.000	0.000	0.000
48	A	50	ASP	-1	-0.883	-0.940	8.532	1.466	1.466	0.000	0.000	0.000	0.000
49	A	51	ASP	-1	-0.870	-0.931	8.650	1.101	1.101	0.000	0.000	0.000	0.000
50	A	52	MET	0	-0.021	-0.006	10.824	-0.202	-0.202	0.000	0.000	0.000	0.000
51	A	53	ILE	0	-0.014	-0.013	10.224	0.186	0.186	0.000	0.000	0.000	0.000
52	A	54	LEU	0	-0.011	-0.011	12.853	-0.079	-0.079	0.000	0.000	0.000	0.000
53	A	55	ILE	0	-0.019	-0.019	16.067	-0.008	-0.008	0.000	0.000	0.000	0.000
54	A	56	ALA	0	0.037	0.021	17.882	-0.016	-0.016	0.000	0.000	0.000	0.000
55	A	57	CYS	0	-0.015	0.014	20.674	-0.016	-0.016	0.000	0.000	0.000	0.000
56	A	58	ALA	0	0.039	0.028	23.469	-0.002	-0.002	0.000	0.000	0.000	0.000
57	A	59	THR	0	0.011	0.005	26.042	-0.011	-0.011	0.000	0.000	0.000	0.000
58	A	60	SER	0	-0.007	-0.012	29.435	0.003	0.003	0.000	0.000	0.000	0.000
59	A	61	VAL	0	-0.037	-0.029	32.303	-0.005	-0.005	0.000	0.000	0.000	0.000
60	A	62	SER	0	0.067	0.042	35.809	0.000	0.000	0.000	0.000	0.000	0.000
61	A	63	PRO	0	-0.007	-0.005	37.617	0.001	0.001	0.000	0.000	0.000	0.000
62	A	64	GLU	-1	-0.886	-0.970	40.764	0.018	0.018	0.000	0.000	0.000	0.000
63	A	65	HIS	0	0.036	0.017	39.323	0.002	0.002	0.000	0.000	0.000	0.000
64	A	66	GLN	0	-0.141	-0.073	37.605	0.000	0.000	0.000	0.000	0.000	0.000
65	A	67	ALA	0	0.025	0.019	42.156	0.000	0.000	0.000	0.000	0.000	0.000
66	A	68	GLY	0	0.039	0.006	45.282	0.000	0.000	0.000	0.000	0.000	0.000
67	A	69	ILE	0	-0.012	-0.005	40.984	0.000	0.000	0.000	0.000	0.000	0.000
68	A	70	ARG	1	0.954	0.983	42.889	-0.035	-0.035	0.000	0.000	0.000	0.000
69	A	71	ALA	0	0.012	0.026	47.104	0.000	0.000	0.000	0.000	0.000	0.000
70	A	72	LEU	0	-0.058	-0.015	46.459	-0.001	-0.001	0.000	0.000	0.000	0.000
71	A	73	SER	0	0.060	0.037	50.220	0.001	0.001	0.000	0.000	0.000	0.000
72	A	74	MET	0	0.058	0.026	46.721	0.001	0.001	0.000	0.000	0.000	0.000
73	A	75	GLU	-1	-0.917	-0.960	48.797	0.030	0.030	0.000	0.000	0.000	0.000
74	A	76	LYS	1	0.989	0.974	49.091	-0.022	-0.022	0.000	0.000	0.000	0.000
75	A	77	ARG	1	0.814	0.916	45.152	-0.032	-0.032	0.000	0.000	0.000	0.000
76	A	78	THR	0	0.038	0.012	44.330	0.003	0.003	0.000	0.000	0.000	0.000
77	A	79	GLU	-1	-0.977	-0.977	44.211	0.028	0.028	0.000	0.000	0.000	0.000
78	A	80	PHE	0	-0.017	-0.021	39.583	0.000	0.000	0.000	0.000	0.000	0.000
79	A	81	ILE	0	0.016	0.001	38.926	0.001	0.001	0.000	0.000	0.000	0.000
80	A	82	TRP	0	0.024	-0.003	39.529	0.005	0.005	0.000	0.000	0.000	0.000
81	A	83	LYS	1	0.937	0.970	40.445	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	84	VAL	0	0.025	0.026	35.373	0.001	0.001	0.000	0.000	0.000	0.000
83	A	85	ARG	1	0.924	0.981	35.792	-0.057	-0.057	0.000	0.000	0.000	0.000
84	A	86	PHE	0	-0.037	-0.029	35.783	0.003	0.003	0.000	0.000	0.000	0.000
85	A	87	THR	0	-0.038	-0.028	35.020	-0.001	-0.001	0.000	0.000	0.000	0.000
86	A	88	LEU	0	0.066	0.032	30.158	-0.001	-0.001	0.000	0.000	0.000	0.000
87	A	89	ASN	0	-0.013	0.015	31.375	0.009	0.009	0.000	0.000	0.000	0.000
88	A	90	ARG	1	0.871	0.927	32.752	-0.046	-0.046	0.000	0.000	0.000	0.000
89	A	91	PHE	0	-0.028	-0.020	28.638	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	92	GLY	0	-0.045	-0.005	26.887	0.000	0.000	0.000	0.000	0.000	0.000
91	A	93	VAL	0	-0.013	0.011	24.890	0.005	0.005	0.000	0.000	0.000	0.000
92	A	94	ASP	-1	-0.837	-0.900	24.887	0.138	0.138	0.000	0.000	0.000	0.000
93	A	95	PHE	0	-0.076	-0.065	26.417	-0.004	-0.004	0.000	0.000	0.000	0.000
94	A	96	GLN	0	-0.020	-0.003	28.183	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	97	LEU	0	-0.042	-0.023	30.126	-0.005	-0.005	0.000	0.000	0.000	0.000
96	A	98	ASP	-1	-0.829	-0.906	33.177	0.069	0.069	0.000	0.000	0.000	0.000
97	A	99	HIS	0	-0.029	-0.044	34.961	-0.002	-0.002	0.000	0.000	0.000	0.000
98	A	100	PRO	0	0.040	0.027	38.450	-0.001	-0.001	0.000	0.000	0.000	0.000
99	A	101	GLU	-1	-0.926	-0.961	40.904	0.041	0.041	0.000	0.000	0.000	0.000
100	A	102	ASN	0	-0.044	-0.046	42.116	0.000	0.000	0.000	0.000	0.000	0.000
101	A	103	VAL	0	-0.022	-0.004	41.929	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	104	LEU	0	-0.037	-0.011	35.408	0.003	0.003	0.000	0.000	0.000	0.000
103	A	105	ASN	0	0.017	0.017	35.922	-0.006	-0.006	0.000	0.000	0.000	0.000
104	A	106	SER	0	0.025	0.015	31.195	0.001	0.001	0.000	0.000	0.000	0.000
105	A	107	TYR	0	-0.048	-0.042	30.278	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	108	LEU	0	-0.004	0.012	23.508	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	109	VAL	0	-0.020	-0.016	25.243	0.000	0.000	0.000	0.000	0.000	0.000
108	A	110	THR	0	-0.002	-0.028	20.738	0.009	0.009	0.000	0.000	0.000	0.000
109	A	111	ASP	-1	-0.848	-0.931	20.697	0.124	0.124	0.000	0.000	0.000	0.000
110	A	112	GLU	-1	-0.891	-0.937	17.495	0.254	0.254	0.000	0.000	0.000	0.000
111	A	113	ILE	0	-0.071	-0.014	13.383	-0.045	-0.045	0.000	0.000	0.000	0.000
112	A	114	PHE	0	0.026	0.000	13.752	0.075	0.075	0.000	0.000	0.000	0.000
113	A	115	PHE	0	0.026	-0.022	7.355	-0.075	-0.075	0.000	0.000	0.000	0.000
114	A	116	ASP	-1	-0.930	-0.937	10.602	0.218	0.218	0.000	0.000	0.000	0.000
115	A	117	GLY	0	-0.036	-0.028	12.804	-0.064	-0.064	0.000	0.000	0.000	0.000
116	A	118	LEU	0	-0.047	0.001	7.542	-0.041	-0.041	0.000	0.000	0.000	0.000
117	A	119	SER	0	0.001	-0.008	10.644	-0.067	-0.067	0.000	0.000	0.000	0.000
118	A	120	LYS	1	0.881	0.935	11.574	0.313	0.313	0.000	0.000	0.000	0.000
119	A	121	ASP	-1	-0.897	-0.953	12.834	-0.035	-0.035	0.000	0.000	0.000	0.000
120	A	122	ARG	1	0.940	0.990	14.352	-0.092	-0.092	0.000	0.000	0.000	0.000
121	A	123	LEU	0	0.005	-0.002	11.526	0.024	0.024	0.000	0.000	0.000	0.000
122	A	124	ILE	0	0.014	-0.008	14.943	0.023	0.023	0.000	0.000	0.000	0.000
123	A	125	SER	0	-0.043	-0.023	17.603	0.008	0.008	0.000	0.000	0.000	0.000
124	A	126	SER	0	0.017	0.001	17.953	-0.001	-0.001	0.000	0.000	0.000	0.000
125	A	127	ILE	0	0.026	0.033	15.871	0.004	0.004	0.000	0.000	0.000	0.000
126	A	128	LYS	1	0.892	0.925	20.208	0.030	0.030	0.000	0.000	0.000	0.000
127	A	129	ASN	0	-0.063	-0.035	22.821	-0.012	-0.012	0.000	0.000	0.000	0.000
128	A	130	VAL	0	0.081	0.045	21.546	-0.004	-0.004	0.000	0.000	0.000	0.000
129	A	131	PHE	0	-0.014	-0.006	24.308	-0.003	-0.003	0.000	0.000	0.000	0.000
130	A	132	ARG	1	0.961	0.960	25.155	-0.012	-0.012	0.000	0.000	0.000	0.000
131	A	133	ALA	0	0.019	0.024	27.624	-0.002	-0.002	0.000	0.000	0.000	0.000
132	A	134	LYS	1	0.937	0.978	27.469	-0.041	-0.041	0.000	0.000	0.000	0.000
133	A	135	LEU	0	-0.044	-0.007	29.734	-0.004	-0.004	0.000	0.000	0.000	0.000
134	A	136	GLN	0	0.017	0.001	31.591	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	137	VAL	0	0.000	0.002	32.976	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	138	MET	0	0.012	0.016	32.787	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	139	TRP	0	0.010	-0.015	34.986	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	140	MET	0	-0.036	0.001	36.947	-0.002	-0.002	0.000	0.000	0.000	0.000
139	A	141	ILE	0	-0.006	0.006	36.600	-0.001	-0.001	0.000	0.000	0.000	0.000
140	A	142	GLN	0	0.006	-0.009	37.104	0.000	0.000	0.000	0.000	0.000	0.000
141	A	143	GLU	-1	-0.979	-0.979	40.815	0.015	0.015	0.000	0.000	0.000	0.000
142	A	144	ARG	1	0.835	0.925	42.778	-0.026	-0.026	0.000	0.000	0.000	0.000
143	A	145	PHE	0	-0.052	-0.046	42.691	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	146	GLY	0	0.020	0.041	41.706	-0.001	-0.001	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:3:LEU)