FMO DATABASE

FMODB ID: 2J15R

Calculation Name: 3F6A-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3F6A

Chain ID: A

ChEMBL ID:

UniProt ID: A0A0H2

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	150
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1418109.40422
FMO2-HF: Nuclear repulsion	1358783.096905
FMO2-HF: Total energy	-59326.307315
FMO2-MP2: Total energy	-59499.603063

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:1:LEU)

Summations of interaction energy for fragment #1(A:1: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.
-0.425	2.822	0.349	-1.773	-1.824	0.008

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

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.038 / q_NPA : 0.011

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	3	ARG	1	0.948	0.994	3.869	0.069	2.330	-0.025	-1.304	-0.933	0.001
4	A	4	HIS	0	-0.032	-0.025	5.671	-0.501	-0.501	0.000	0.000	0.000	0.000
5	A	5	PHE	0	-0.009	0.000	3.006	-1.443	-0.457	0.374	-0.469	-0.891	0.007
6	A	6	THR	0	-0.034	-0.044	8.497	-0.153	-0.153	0.000	0.000	0.000	0.000
7	A	7	VAL	0	-0.035	-0.012	12.214	0.072	0.072	0.000	0.000	0.000	0.000
8	A	8	SER	0	-0.001	-0.015	15.036	-0.072	-0.072	0.000	0.000	0.000	0.000
9	A	9	VAL	0	-0.016	-0.018	18.628	0.000	0.000	0.000	0.000	0.000	0.000
10	A	10	PHE	0	-0.005	-0.005	21.678	-0.025	-0.025	0.000	0.000	0.000	0.000
11	A	11	ILE	0	-0.001	0.005	24.948	-0.008	-0.008	0.000	0.000	0.000	0.000
12	A	12	VAL	0	0.015	0.002	27.361	-0.008	-0.008	0.000	0.000	0.000	0.000
13	A	13	CYS	0	-0.050	-0.023	30.790	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	14	LYS	1	0.882	0.921	34.122	-0.086	-0.086	0.000	0.000	0.000	0.000
15	A	15	ASP	-1	-0.781	-0.844	36.498	0.085	0.085	0.000	0.000	0.000	0.000
16	A	16	LYS	1	0.796	0.873	34.928	-0.092	-0.092	0.000	0.000	0.000	0.000
17	A	17	VAL	0	0.009	0.009	28.479	0.003	0.003	0.000	0.000	0.000	0.000
18	A	18	LEU	0	-0.032	-0.003	28.298	-0.007	-0.007	0.000	0.000	0.000	0.000
19	A	19	LEU	0	-0.014	-0.010	26.841	0.013	0.013	0.000	0.000	0.000	0.000
20	A	20	HIS	0	0.013	-0.015	23.525	-0.038	-0.038	0.000	0.000	0.000	0.000
21	A	21	LEU	0	-0.034	-0.014	27.446	0.006	0.006	0.000	0.000	0.000	0.000
22	A	22	HIS	0	0.057	0.048	20.771	-0.013	-0.013	0.000	0.000	0.000	0.000
23	A	23	LYS	1	0.811	0.892	25.221	-0.168	-0.168	0.000	0.000	0.000	0.000
24	A	24	LYS	1	0.935	0.949	25.914	-0.100	-0.100	0.000	0.000	0.000	0.000
25	A	25	ALA	0	0.041	0.029	24.961	-0.006	-0.006	0.000	0.000	0.000	0.000
26	A	26	LYS	1	0.914	0.961	26.938	-0.083	-0.083	0.000	0.000	0.000	0.000
27	A	27	LYS	1	0.909	0.939	22.892	-0.194	-0.194	0.000	0.000	0.000	0.000
28	A	28	MET	0	-0.053	-0.001	27.733	0.000	0.000	0.000	0.000	0.000	0.000
29	A	29	LEU	0	-0.006	-0.007	21.519	0.000	0.000	0.000	0.000	0.000	0.000
30	A	30	PRO	0	0.021	0.014	21.508	-0.021	-0.021	0.000	0.000	0.000	0.000
31	A	31	LEU	0	0.000	0.008	23.064	0.000	0.000	0.000	0.000	0.000	0.000
32	A	32	GLY	0	-0.002	-0.021	18.946	0.018	0.018	0.000	0.000	0.000	0.000
33	A	33	GLY	0	0.010	0.025	16.777	-0.043	-0.043	0.000	0.000	0.000	0.000
34	A	34	HIS	0	-0.021	-0.015	12.313	0.092	0.092	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.004	0.006	9.528	-0.050	-0.050	0.000	0.000	0.000	0.000
36	A	36	GLU	-1	-0.890	-0.943	10.672	0.410	0.410	0.000	0.000	0.000	0.000
37	A	37	VAL	0	-0.054	-0.039	7.404	0.138	0.138	0.000	0.000	0.000	0.000
38	A	38	ASN	0	-0.113	-0.072	8.948	-0.160	-0.160	0.000	0.000	0.000	0.000
39	A	39	GLU	-1	-0.803	-0.882	10.735	0.383	0.383	0.000	0.000	0.000	0.000
40	A	40	LEU	0	-0.012	-0.014	10.952	0.174	0.174	0.000	0.000	0.000	0.000
41	A	41	PRO	0	0.022	-0.004	10.726	-0.028	-0.028	0.000	0.000	0.000	0.000
42	A	42	GLU	-1	-0.820	-0.918	13.403	0.263	0.263	0.000	0.000	0.000	0.000
43	A	43	GLU	-1	-0.849	-0.928	15.610	0.292	0.292	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.039	0.026	14.344	-0.039	-0.039	0.000	0.000	0.000	0.000
45	A	45	CYS	0	-0.082	-0.043	16.476	-0.046	-0.046	0.000	0.000	0.000	0.000
46	A	46	ILE	0	-0.034	-0.019	18.900	-0.043	-0.043	0.000	0.000	0.000	0.000
47	A	47	ARG	1	0.718	0.837	16.216	-0.396	-0.396	0.000	0.000	0.000	0.000
48	A	48	GLU	-1	-0.788	-0.879	17.354	0.355	0.355	0.000	0.000	0.000	0.000
49	A	49	ALA	0	-0.026	-0.022	20.953	-0.031	-0.031	0.000	0.000	0.000	0.000
50	A	50	LYS	1	0.804	0.905	23.918	-0.160	-0.160	0.000	0.000	0.000	0.000
51	A	51	GLU	-1	-0.754	-0.856	21.183	0.230	0.230	0.000	0.000	0.000	0.000
52	A	52	GLU	-1	-0.775	-0.897	22.660	0.234	0.234	0.000	0.000	0.000	0.000
53	A	53	ALA	0	-0.036	-0.041	25.848	-0.013	-0.013	0.000	0.000	0.000	0.000
54	A	54	GLY	0	0.043	0.039	28.483	-0.012	-0.012	0.000	0.000	0.000	0.000
55	A	55	LEU	0	-0.044	-0.004	28.122	-0.009	-0.009	0.000	0.000	0.000	0.000
56	A	56	ASN	0	0.021	0.023	27.985	0.011	0.011	0.000	0.000	0.000	0.000
57	A	57	VAL	0	0.023	0.014	24.274	-0.006	-0.006	0.000	0.000	0.000	0.000
58	A	58	THR	0	-0.046	-0.022	26.287	-0.006	-0.006	0.000	0.000	0.000	0.000
59	A	59	LEU	0	0.026	0.019	19.817	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	60	TYR	0	0.014	0.001	23.950	-0.014	-0.014	0.000	0.000	0.000	0.000
61	A	61	ASN	0	0.033	-0.002	22.293	0.019	0.019	0.000	0.000	0.000	0.000
62	A	62	PRO	0	-0.007	0.010	22.740	-0.016	-0.016	0.000	0.000	0.000	0.000
63	A	63	ILE	0	-0.008	-0.012	23.280	0.001	0.001	0.000	0.000	0.000	0.000
64	A	64	ASP	-1	-0.737	-0.858	23.448	0.079	0.079	0.000	0.000	0.000	0.000
65	A	65	ILE	0	-0.032	-0.028	24.796	0.000	0.000	0.000	0.000	0.000	0.000
66	A	66	ASN	0	-0.070	-0.041	26.733	-0.011	-0.011	0.000	0.000	0.000	0.000
67	A	67	LEU	0	0.059	0.042	18.985	-0.006	-0.006	0.000	0.000	0.000	0.000
68	A	68	LYS	1	0.868	0.927	22.480	-0.108	-0.108	0.000	0.000	0.000	0.000
69	A	69	LYS	1	0.936	0.959	23.514	-0.059	-0.059	0.000	0.000	0.000	0.000
70	A	70	SER	0	-0.017	-0.021	24.266	-0.005	-0.005	0.000	0.000	0.000	0.000
71	A	71	CYS	0	-0.007	0.018	19.829	-0.006	-0.006	0.000	0.000	0.000	0.000
72	A	72	ASP	-1	-0.796	-0.890	21.461	0.088	0.088	0.000	0.000	0.000	0.000
73	A	73	LEU	0	-0.102	-0.056	23.446	-0.008	-0.008	0.000	0.000	0.000	0.000
74	A	74	SER	0	-0.034	-0.020	20.610	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	75	GLY	0	-0.050	-0.012	20.401	-0.011	-0.011	0.000	0.000	0.000	0.000
76	A	76	GLU	-1	-0.958	-0.963	15.284	0.058	0.058	0.000	0.000	0.000	0.000
77	A	77	LYS	1	0.889	0.917	17.337	-0.109	-0.109	0.000	0.000	0.000	0.000
78	A	78	LEU	0	-0.015	-0.004	17.151	0.019	0.019	0.000	0.000	0.000	0.000
79	A	79	LEU	0	0.015	0.019	13.023	-0.009	-0.009	0.000	0.000	0.000	0.000
80	A	80	ILE	0	-0.063	-0.012	17.032	-0.017	-0.017	0.000	0.000	0.000	0.000
81	A	81	ASN	0	-0.012	-0.015	15.480	0.066	0.066	0.000	0.000	0.000	0.000
82	A	82	PRO	0	-0.018	0.008	13.783	-0.030	-0.030	0.000	0.000	0.000	0.000
83	A	83	ILE	0	-0.007	0.003	16.939	-0.034	-0.034	0.000	0.000	0.000	0.000
84	A	84	HIS	1	0.751	0.844	18.421	-0.264	-0.264	0.000	0.000	0.000	0.000
85	A	85	THR	0	0.050	0.026	11.862	0.036	0.036	0.000	0.000	0.000	0.000
86	A	86	ILE	0	-0.041	-0.014	14.367	-0.074	-0.074	0.000	0.000	0.000	0.000
87	A	87	LEU	0	-0.008	0.011	11.093	0.098	0.098	0.000	0.000	0.000	0.000
88	A	88	GLY	0	0.010	0.007	13.557	-0.078	-0.078	0.000	0.000	0.000	0.000
89	A	89	ASP	-1	-0.858	-0.927	13.861	0.263	0.263	0.000	0.000	0.000	0.000
90	A	90	VAL	0	-0.064	-0.045	16.005	-0.036	-0.036	0.000	0.000	0.000	0.000
91	A	91	SER	0	-0.054	-0.016	18.648	0.005	0.005	0.000	0.000	0.000	0.000
92	A	92	PRO	0	0.099	0.060	14.178	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	93	ASN	0	-0.033	-0.030	16.192	0.021	0.021	0.000	0.000	0.000	0.000
94	A	94	HIS	0	0.002	-0.012	10.591	-0.106	-0.106	0.000	0.000	0.000	0.000
95	A	95	SER	0	-0.006	-0.006	10.918	0.037	0.037	0.000	0.000	0.000	0.000
96	A	96	HIS	0	-0.096	-0.039	9.604	0.073	0.073	0.000	0.000	0.000	0.000
97	A	97	ILE	0	-0.002	0.000	6.746	-0.198	-0.198	0.000	0.000	0.000	0.000
98	A	98	ASP	-1	-0.759	-0.828	10.191	0.727	0.727	0.000	0.000	0.000	0.000
99	A	99	PHE	0	-0.023	-0.019	8.056	-0.100	-0.100	0.000	0.000	0.000	0.000
100	A	100	VAL	0	0.020	0.005	14.025	-0.037	-0.037	0.000	0.000	0.000	0.000
101	A	101	TYR	0	0.029	-0.009	15.048	-0.006	-0.006	0.000	0.000	0.000	0.000
102	A	102	TYR	0	-0.045	-0.050	20.095	-0.008	-0.008	0.000	0.000	0.000	0.000
103	A	103	ALA	0	0.022	0.008	23.924	0.004	0.004	0.000	0.000	0.000	0.000
104	A	104	THR	0	0.039	0.032	25.893	-0.009	-0.009	0.000	0.000	0.000	0.000
105	A	105	THR	0	-0.024	-0.039	29.037	0.003	0.003	0.000	0.000	0.000	0.000
106	A	106	THR	0	0.016	0.011	31.490	-0.004	-0.004	0.000	0.000	0.000	0.000
107	A	107	SER	0	-0.018	-0.020	34.457	-0.008	-0.008	0.000	0.000	0.000	0.000
108	A	108	PHE	0	0.018	-0.006	34.463	0.004	0.004	0.000	0.000	0.000	0.000
109	A	109	GLU	-1	-0.976	-0.971	35.557	0.084	0.084	0.000	0.000	0.000	0.000
110	A	110	THR	0	-0.026	-0.018	31.695	0.006	0.006	0.000	0.000	0.000	0.000
111	A	111	SER	0	-0.042	-0.030	32.301	-0.010	-0.010	0.000	0.000	0.000	0.000
112	A	112	PRO	0	-0.006	0.011	29.157	0.002	0.002	0.000	0.000	0.000	0.000
113	A	113	GLU	-1	-0.873	-0.921	27.371	0.126	0.126	0.000	0.000	0.000	0.000
114	A	114	ILE	0	-0.019	-0.015	27.940	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	115	GLY	0	-0.023	-0.004	27.448	0.008	0.008	0.000	0.000	0.000	0.000
116	A	116	GLU	-1	-0.750	-0.859	24.061	0.189	0.189	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.055	-0.039	27.087	-0.020	-0.020	0.000	0.000	0.000	0.000
118	A	118	LYS	1	0.805	0.883	29.029	-0.116	-0.116	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.061	-0.021	31.620	-0.008	-0.008	0.000	0.000	0.000	0.000
120	A	120	LEU	0	0.071	0.045	29.459	0.007	0.007	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.853	0.914	31.797	-0.109	-0.109	0.000	0.000	0.000	0.000
122	A	122	TRP	0	0.035	0.025	31.418	0.009	0.009	0.000	0.000	0.000	0.000
123	A	123	TYR	0	-0.024	-0.021	32.293	-0.012	-0.012	0.000	0.000	0.000	0.000
124	A	124	SER	0	0.032	-0.016	34.167	0.003	0.003	0.000	0.000	0.000	0.000
125	A	125	LYS	1	0.873	0.895	34.634	-0.097	-0.097	0.000	0.000	0.000	0.000
126	A	126	GLU	-1	-0.932	-0.956	36.375	0.069	0.069	0.000	0.000	0.000	0.000
127	A	127	ASP	-1	-0.887	-0.909	36.485	0.086	0.086	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.012	0.026	32.963	0.000	0.000	0.000	0.000	0.000	0.000
129	A	129	LYS	1	0.947	0.965	34.669	-0.069	-0.069	0.000	0.000	0.000	0.000
130	A	130	ASN	0	-0.011	-0.003	36.970	-0.007	-0.007	0.000	0.000	0.000	0.000
131	A	131	ALA	0	-0.026	-0.004	34.363	-0.003	-0.003	0.000	0.000	0.000	0.000
132	A	132	HIS	0	0.030	0.011	35.334	0.002	0.002	0.000	0.000	0.000	0.000
133	A	133	ASN	0	-0.075	-0.049	32.042	-0.004	-0.004	0.000	0.000	0.000	0.000
134	A	134	ILE	0	0.021	0.011	28.610	0.008	0.008	0.000	0.000	0.000	0.000
135	A	135	GLN	0	0.049	0.040	22.530	-0.008	-0.008	0.000	0.000	0.000	0.000
136	A	136	GLU	-1	-0.824	-0.921	27.645	0.121	0.121	0.000	0.000	0.000	0.000
137	A	137	ASN	0	0.041	0.016	21.463	-0.014	-0.014	0.000	0.000	0.000	0.000
138	A	138	ILE	0	-0.017	0.003	22.185	0.010	0.010	0.000	0.000	0.000	0.000
139	A	139	LEU	0	0.025	0.010	25.525	0.000	0.000	0.000	0.000	0.000	0.000
140	A	140	VAL	0	-0.003	0.013	26.565	-0.005	-0.005	0.000	0.000	0.000	0.000
141	A	141	MET	0	0.000	0.015	20.884	0.006	0.006	0.000	0.000	0.000	0.000
142	A	142	ALA	0	0.011	0.008	25.761	0.000	0.000	0.000	0.000	0.000	0.000
143	A	143	THR	0	-0.044	-0.038	28.326	-0.010	-0.010	0.000	0.000	0.000	0.000
144	A	144	GLU	-1	-0.782	-0.863	25.255	0.181	0.181	0.000	0.000	0.000	0.000
145	A	145	ALA	0	-0.008	0.003	26.631	-0.004	-0.004	0.000	0.000	0.000	0.000
146	A	146	LEU	0	0.011	-0.003	28.310	-0.007	-0.007	0.000	0.000	0.000	0.000
147	A	147	ASP	-1	-0.893	-0.917	31.454	0.094	0.094	0.000	0.000	0.000	0.000
148	A	148	LEU	0	-0.086	-0.030	26.487	-0.005	-0.005	0.000	0.000	0.000	0.000
149	A	149	LEU	0	-0.093	-0.053	27.279	0.000	0.000	0.000	0.000	0.000	0.000
150	A	150	GLU	-1	-0.987	-0.997	31.827	0.086	0.086	0.000	0.000	0.000	0.000

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