FMO DATABASE

FMODB ID: 2JV8R

Calculation Name: 3ECY-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ECY

Chain ID: A

ChEMBL ID:

UniProt ID: Q9V3I1

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	119
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-869144.23801
FMO2-HF: Nuclear repulsion	823539.34308
FMO2-HF: Total energy	-45604.89493
FMO2-MP2: Total energy	-45738.797099

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:19:THR)

Summations of interaction energy for fragment #1(A:19:THR)

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.
-2.507	-0.565	1.683	-1.059	-2.565	-0.004

Interaction energy analysis for fragmet #1(A:19:THR)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.023 / q_NPA : -0.036

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	21	VAL	0	-0.031	-0.018	2.276	0.707	2.260	1.685	-1.004	-2.234	-0.004
4	A	22	LEU	0	-0.002	0.011	5.073	-0.109	-0.075	-0.001	-0.005	-0.027	0.000
5	A	23	ARG	1	0.931	0.969	3.621	2.638	2.863	0.000	-0.039	-0.186	0.000
6	A	24	PHE	0	0.037	0.004	9.769	0.011	0.011	0.000	0.000	0.000	0.000
7	A	25	ALA	0	-0.015	-0.003	13.503	0.045	0.045	0.000	0.000	0.000	0.000
8	A	26	LYS	1	0.931	0.973	15.868	0.256	0.256	0.000	0.000	0.000	0.000
9	A	27	LEU	0	-0.034	-0.023	19.599	0.009	0.009	0.000	0.000	0.000	0.000
10	A	28	THR	0	-0.016	-0.014	21.878	0.026	0.026	0.000	0.000	0.000	0.000
11	A	29	GLU	-1	-0.898	-0.957	23.821	-0.198	-0.198	0.000	0.000	0.000	0.000
12	A	30	ASN	0	-0.030	-0.013	25.807	0.018	0.018	0.000	0.000	0.000	0.000
13	A	31	ALA	0	-0.011	0.012	21.592	-0.002	-0.002	0.000	0.000	0.000	0.000
14	A	32	LEU	0	-0.057	-0.044	22.633	0.019	0.019	0.000	0.000	0.000	0.000
15	A	33	GLU	-1	-0.915	-0.955	17.755	-0.299	-0.299	0.000	0.000	0.000	0.000
16	A	34	PRO	0	0.004	0.000	16.482	0.045	0.045	0.000	0.000	0.000	0.000
17	A	35	VAL	0	-0.035	0.001	16.767	-0.026	-0.026	0.000	0.000	0.000	0.000
18	A	36	ARG	1	0.916	0.964	16.972	0.218	0.218	0.000	0.000	0.000	0.000
19	A	37	GLY	0	0.046	0.041	19.646	0.029	0.029	0.000	0.000	0.000	0.000
20	A	38	SER	0	-0.041	-0.040	22.308	0.027	0.027	0.000	0.000	0.000	0.000
21	A	39	ALA	0	0.046	0.017	21.299	-0.019	-0.019	0.000	0.000	0.000	0.000
22	A	40	LYS	1	0.942	0.956	21.085	0.072	0.072	0.000	0.000	0.000	0.000
23	A	41	ALA	0	-0.030	0.013	20.983	-0.002	-0.002	0.000	0.000	0.000	0.000
24	A	42	ALA	0	0.050	0.017	19.662	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	43	GLY	0	0.033	0.025	17.269	-0.051	-0.051	0.000	0.000	0.000	0.000
26	A	44	VAL	0	-0.057	-0.018	15.471	0.053	0.053	0.000	0.000	0.000	0.000
27	A	45	ASP	-1	-0.859	-0.961	18.435	-0.269	-0.269	0.000	0.000	0.000	0.000
28	A	46	LEU	0	-0.004	-0.015	18.473	-0.012	-0.012	0.000	0.000	0.000	0.000
29	A	47	ARG	1	0.877	0.919	22.133	0.232	0.232	0.000	0.000	0.000	0.000
30	A	48	SER	0	-0.042	-0.013	24.760	-0.023	-0.023	0.000	0.000	0.000	0.000
31	A	49	ALA	0	0.076	0.041	25.667	0.011	0.011	0.000	0.000	0.000	0.000
32	A	50	TYR	0	-0.045	-0.046	27.397	0.021	0.021	0.000	0.000	0.000	0.000
33	A	51	ASH	0	-0.133	-0.121	31.134	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	52	VAL	0	-0.006	-0.009	32.068	-0.001	-0.001	0.000	0.000	0.000	0.000
35	A	53	VAL	0	0.034	0.032	35.104	0.001	0.001	0.000	0.000	0.000	0.000
36	A	54	VAL	0	-0.038	-0.024	35.256	-0.005	-0.005	0.000	0.000	0.000	0.000
37	A	55	PRO	0	0.036	0.016	38.207	0.006	0.006	0.000	0.000	0.000	0.000
38	A	56	ALA	0	0.060	0.033	41.421	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	57	ARG	1	0.839	0.925	43.314	0.103	0.103	0.000	0.000	0.000	0.000
40	A	58	GLY	0	0.018	0.028	41.105	0.000	0.000	0.000	0.000	0.000	0.000
41	A	59	LYS	1	0.946	0.964	35.857	0.159	0.159	0.000	0.000	0.000	0.000
42	A	60	ALA	0	0.005	0.006	34.677	0.005	0.005	0.000	0.000	0.000	0.000
43	A	61	ILE	0	-0.035	-0.009	27.919	-0.010	-0.010	0.000	0.000	0.000	0.000
44	A	62	VAL	0	0.018	0.008	28.415	0.008	0.008	0.000	0.000	0.000	0.000
45	A	63	LYS	1	0.886	0.941	24.928	0.292	0.292	0.000	0.000	0.000	0.000
46	A	64	THR	0	0.038	0.001	21.616	0.003	0.003	0.000	0.000	0.000	0.000
47	A	65	ASP	-1	-0.738	-0.832	23.174	-0.251	-0.251	0.000	0.000	0.000	0.000
48	A	66	LEU	0	-0.035	0.002	17.718	-0.004	-0.004	0.000	0.000	0.000	0.000
49	A	67	GLN	0	-0.051	-0.030	16.205	0.012	0.012	0.000	0.000	0.000	0.000
50	A	68	VAL	0	-0.014	-0.024	12.622	0.010	0.010	0.000	0.000	0.000	0.000
51	A	69	GLN	0	-0.022	0.002	7.182	0.553	0.553	0.000	0.000	0.000	0.000
52	A	70	VAL	0	-0.026	-0.013	9.148	-0.179	-0.179	0.000	0.000	0.000	0.000
53	A	71	PRO	0	0.013	0.007	5.822	-0.177	-0.177	0.000	0.000	0.000	0.000
54	A	72	GLU	-1	-0.857	-0.911	4.706	-6.262	-6.132	-0.001	-0.011	-0.118	0.000
55	A	73	GLY	0	-0.024	-0.020	7.014	0.140	0.140	0.000	0.000	0.000	0.000
56	A	74	SER	0	-0.145	-0.086	9.397	0.362	0.362	0.000	0.000	0.000	0.000
57	A	75	TYR	0	0.034	0.009	11.082	0.007	0.007	0.000	0.000	0.000	0.000
58	A	76	GLY	0	0.007	0.003	14.336	-0.026	-0.026	0.000	0.000	0.000	0.000
59	A	77	ARG	1	0.910	0.960	15.768	0.456	0.456	0.000	0.000	0.000	0.000
60	A	78	VAL	0	-0.013	-0.002	19.404	0.003	0.003	0.000	0.000	0.000	0.000
61	A	79	ALA	0	-0.001	-0.012	21.592	0.031	0.031	0.000	0.000	0.000	0.000
62	A	80	PRO	0	0.075	0.029	24.116	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	81	ARG	1	0.863	0.941	25.912	0.188	0.188	0.000	0.000	0.000	0.000
64	A	89	PHE	0	0.000	-0.021	37.883	-0.001	-0.001	0.000	0.000	0.000	0.000
65	A	90	ILE	0	-0.018	-0.001	34.258	0.000	0.000	0.000	0.000	0.000	0.000
66	A	91	ASP	-1	-0.911	-0.939	33.791	-0.186	-0.186	0.000	0.000	0.000	0.000
67	A	92	VAL	0	0.002	-0.006	27.768	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	93	GLY	0	0.048	0.025	29.506	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	94	ALA	0	-0.032	-0.027	26.099	-0.003	-0.003	0.000	0.000	0.000	0.000
70	A	95	GLY	0	-0.001	-0.002	23.626	0.012	0.012	0.000	0.000	0.000	0.000
71	A	96	VAL	0	-0.040	-0.019	18.514	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	97	VAL	0	-0.055	-0.015	15.401	0.037	0.037	0.000	0.000	0.000	0.000
73	A	98	ASP	-1	-0.786	-0.914	14.628	-0.832	-0.832	0.000	0.000	0.000	0.000
74	A	99	GLU	-1	-0.807	-0.907	10.319	-1.775	-1.775	0.000	0.000	0.000	0.000
75	A	100	ASP	-1	-0.870	-0.906	12.238	-0.951	-0.951	0.000	0.000	0.000	0.000
76	A	101	TYR	0	-0.069	-0.031	15.068	0.147	0.147	0.000	0.000	0.000	0.000
77	A	102	ARG	1	0.875	0.912	11.790	0.981	0.981	0.000	0.000	0.000	0.000
78	A	103	GLY	0	-0.010	0.015	17.728	0.057	0.057	0.000	0.000	0.000	0.000
79	A	104	ASN	0	-0.014	-0.008	19.375	-0.051	-0.051	0.000	0.000	0.000	0.000
80	A	105	LEU	0	0.048	0.018	17.221	0.028	0.028	0.000	0.000	0.000	0.000
81	A	106	GLY	0	0.025	0.002	21.199	0.031	0.031	0.000	0.000	0.000	0.000
82	A	107	VAL	0	-0.034	0.005	24.498	-0.021	-0.021	0.000	0.000	0.000	0.000
83	A	108	VAL	0	-0.019	-0.009	27.159	0.013	0.013	0.000	0.000	0.000	0.000
84	A	109	LEU	0	-0.014	0.006	30.420	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	110	PHE	0	-0.006	-0.022	32.640	0.007	0.007	0.000	0.000	0.000	0.000
86	A	111	ASN	0	-0.019	-0.013	36.533	0.003	0.003	0.000	0.000	0.000	0.000
87	A	112	HIS	0	-0.006	-0.002	38.262	0.009	0.009	0.000	0.000	0.000	0.000
88	A	113	SER	0	-0.047	-0.025	42.090	0.008	0.008	0.000	0.000	0.000	0.000
89	A	114	ASP	-1	-0.876	-0.962	44.295	-0.089	-0.089	0.000	0.000	0.000	0.000
90	A	115	VAL	0	-0.030	-0.009	44.685	0.003	0.003	0.000	0.000	0.000	0.000
91	A	116	ASP	-1	-0.859	-0.922	42.229	-0.108	-0.108	0.000	0.000	0.000	0.000
92	A	117	PHE	0	-0.034	-0.025	34.955	0.002	0.002	0.000	0.000	0.000	0.000
93	A	118	GLU	-1	-0.805	-0.842	37.301	-0.120	-0.120	0.000	0.000	0.000	0.000
94	A	119	VAL	0	-0.034	-0.013	31.124	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	120	LYS	1	0.905	0.954	33.726	0.118	0.118	0.000	0.000	0.000	0.000
96	A	121	HIS	0	-0.015	-0.005	27.853	-0.005	-0.005	0.000	0.000	0.000	0.000
97	A	122	GLY	0	0.032	-0.002	27.578	0.010	0.010	0.000	0.000	0.000	0.000
98	A	123	ASP	-1	-0.861	-0.917	28.060	-0.156	-0.156	0.000	0.000	0.000	0.000
99	A	124	ARG	1	0.858	0.928	25.264	0.167	0.167	0.000	0.000	0.000	0.000
100	A	125	ILE	0	0.010	0.006	25.381	0.018	0.018	0.000	0.000	0.000	0.000
101	A	126	ALA	0	0.000	0.000	23.728	0.005	0.005	0.000	0.000	0.000	0.000
102	A	127	GLN	0	-0.012	-0.009	20.961	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	128	PHE	0	0.005	0.017	13.759	0.008	0.008	0.000	0.000	0.000	0.000
104	A	129	ILE	0	-0.024	-0.021	17.217	-0.016	-0.016	0.000	0.000	0.000	0.000
105	A	130	CYS	0	0.002	0.008	12.211	-0.090	-0.090	0.000	0.000	0.000	0.000
106	A	131	GLU	-1	-0.898	-0.949	14.125	-0.331	-0.331	0.000	0.000	0.000	0.000
107	A	132	ARG	1	0.895	0.932	6.002	1.649	1.649	0.000	0.000	0.000	0.000
108	A	133	ILE	0	0.016	0.026	13.571	0.094	0.094	0.000	0.000	0.000	0.000
109	A	134	PHE	0	-0.023	-0.021	14.634	0.000	0.000	0.000	0.000	0.000	0.000
110	A	135	TYR	0	0.022	0.003	15.547	-0.015	-0.015	0.000	0.000	0.000	0.000
111	A	136	PRO	0	-0.028	0.005	19.279	0.036	0.036	0.000	0.000	0.000	0.000
112	A	137	GLN	0	0.013	-0.003	21.466	-0.007	-0.007	0.000	0.000	0.000	0.000
113	A	138	LEU	0	0.001	0.002	24.433	-0.008	-0.008	0.000	0.000	0.000	0.000
114	A	139	VAL	0	0.002	0.000	27.387	0.008	0.008	0.000	0.000	0.000	0.000
115	A	140	MET	0	-0.005	0.002	31.005	-0.009	-0.009	0.000	0.000	0.000	0.000
116	A	141	VAL	0	-0.011	-0.015	33.626	0.007	0.007	0.000	0.000	0.000	0.000
117	A	142	ASP	-1	-0.841	-0.903	36.312	-0.024	-0.024	0.000	0.000	0.000	0.000
118	A	143	LYS	1	0.862	0.915	39.003	0.015	0.015	0.000	0.000	0.000	0.000
119	A	144	LEU	0	-0.008	0.005	33.482	0.004	0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:19:THR)