FMO DATABASE

FMODB ID: Z641N

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

Total energy (hartree)

FMO2-HF: Electronic energy	-871802.723431
FMO2-HF: Nuclear repulsion	826196.530896
FMO2-HF: Total energy	-45606.192535
FMO2-MP2: Total energy	-45740.077098

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.
-4.598	-0.563	1.377	-1.998	-3.415	-0.001

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 : -0.034 / q_NPA : -0.034

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

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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	-0.013	-0.010	2.382	0.594	2.124	0.937	-0.701	-1.766	-0.002
4	A	22	LEU	0	-0.014	0.004	4.747	0.090	0.129	-0.001	-0.008	-0.031	0.000
5	A	23	ARG	1	0.793	0.884	2.649	1.288	2.685	0.409	-0.740	-1.067	0.006
6	A	24	PHE	0	0.021	-0.009	9.367	0.027	0.027	0.000	0.000	0.000	0.000
7	A	25	ALA	0	0.003	0.005	13.103	0.044	0.044	0.000	0.000	0.000	0.000
8	A	26	LYS	1	0.818	0.903	15.590	0.207	0.207	0.000	0.000	0.000	0.000
9	A	27	LEU	0	-0.027	-0.016	19.413	0.018	0.018	0.000	0.000	0.000	0.000
10	A	28	THR	0	-0.024	-0.027	21.676	0.018	0.018	0.000	0.000	0.000	0.000
11	A	29	GLU	-1	-0.857	-0.936	23.742	-0.133	-0.133	0.000	0.000	0.000	0.000
12	A	30	ASN	0	-0.054	-0.030	25.837	0.002	0.002	0.000	0.000	0.000	0.000
13	A	31	ALA	0	0.024	0.022	21.545	-0.006	-0.006	0.000	0.000	0.000	0.000
14	A	32	LEU	0	-0.058	-0.022	22.392	0.009	0.009	0.000	0.000	0.000	0.000
15	A	33	GLU	-1	-0.810	-0.906	17.887	-0.257	-0.257	0.000	0.000	0.000	0.000
16	A	34	PRO	0	-0.031	0.011	16.120	0.030	0.030	0.000	0.000	0.000	0.000
17	A	35	VAL	0	-0.028	-0.022	16.831	-0.032	-0.032	0.000	0.000	0.000	0.000
18	A	36	ARG	1	0.881	0.934	17.055	0.299	0.299	0.000	0.000	0.000	0.000
19	A	37	GLY	0	0.048	0.034	19.519	0.028	0.028	0.000	0.000	0.000	0.000
20	A	38	SER	0	-0.015	-0.024	22.443	0.024	0.024	0.000	0.000	0.000	0.000
21	A	39	ALA	0	0.043	0.014	21.901	-0.022	-0.022	0.000	0.000	0.000	0.000
22	A	40	LYS	1	0.940	0.958	21.624	0.115	0.115	0.000	0.000	0.000	0.000
23	A	41	ALA	0	-0.012	0.020	21.118	0.003	0.003	0.000	0.000	0.000	0.000
24	A	42	ALA	0	0.055	0.024	19.496	-0.018	-0.018	0.000	0.000	0.000	0.000
25	A	43	GLY	0	0.055	0.034	17.133	-0.051	-0.051	0.000	0.000	0.000	0.000
26	A	44	VAL	0	-0.083	-0.041	15.521	0.045	0.045	0.000	0.000	0.000	0.000
27	A	45	ASP	-1	-0.819	-0.912	18.358	-0.247	-0.247	0.000	0.000	0.000	0.000
28	A	46	LEU	0	-0.008	0.002	18.198	-0.005	-0.005	0.000	0.000	0.000	0.000
29	A	47	ARG	1	0.895	0.919	21.818	0.228	0.228	0.000	0.000	0.000	0.000
30	A	48	SER	0	-0.010	-0.006	24.480	-0.013	-0.013	0.000	0.000	0.000	0.000
31	A	49	ALA	0	0.036	0.015	25.147	0.006	0.006	0.000	0.000	0.000	0.000
32	A	50	TYR	0	-0.040	-0.026	26.952	0.016	0.016	0.000	0.000	0.000	0.000
33	A	51	ASH	0	-0.078	-0.065	30.738	-0.003	-0.003	0.000	0.000	0.000	0.000
34	A	52	VAL	0	-0.024	-0.016	31.235	0.001	0.001	0.000	0.000	0.000	0.000
35	A	53	VAL	0	0.028	0.019	34.435	-0.002	-0.002	0.000	0.000	0.000	0.000
36	A	54	VAL	0	-0.045	-0.026	34.816	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	55	PRO	0	0.035	0.011	37.609	0.002	0.002	0.000	0.000	0.000	0.000
38	A	56	ALA	0	0.015	0.008	41.096	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	57	ARG	1	0.780	0.881	42.925	0.072	0.072	0.000	0.000	0.000	0.000
40	A	58	GLY	0	0.042	0.042	40.666	0.001	0.001	0.000	0.000	0.000	0.000
41	A	59	LYS	1	0.919	0.946	35.226	0.102	0.102	0.000	0.000	0.000	0.000
42	A	60	ALA	0	0.021	0.017	34.312	0.005	0.005	0.000	0.000	0.000	0.000
43	A	61	ILE	0	-0.043	-0.013	27.264	-0.007	-0.007	0.000	0.000	0.000	0.000
44	A	62	VAL	0	0.020	0.010	28.204	0.006	0.006	0.000	0.000	0.000	0.000
45	A	63	LYS	1	0.854	0.921	23.716	0.202	0.202	0.000	0.000	0.000	0.000
46	A	64	THR	0	0.049	0.005	21.127	0.000	0.000	0.000	0.000	0.000	0.000
47	A	65	ASP	-1	-0.761	-0.834	22.589	-0.177	-0.177	0.000	0.000	0.000	0.000
48	A	66	LEU	0	-0.019	0.012	17.248	-0.003	-0.003	0.000	0.000	0.000	0.000
49	A	67	GLN	0	-0.038	-0.014	15.522	0.009	0.009	0.000	0.000	0.000	0.000
50	A	68	VAL	0	-0.033	-0.039	11.896	-0.006	-0.006	0.000	0.000	0.000	0.000
51	A	69	GLN	0	-0.029	-0.013	6.178	0.403	0.403	0.000	0.000	0.000	0.000
52	A	70	VAL	0	-0.006	-0.009	8.281	-0.247	-0.247	0.000	0.000	0.000	0.000
53	A	71	PRO	0	-0.003	0.005	5.072	-0.236	-0.236	0.000	0.000	0.000	0.000
54	A	72	GLU	-1	-0.716	-0.800	3.120	-7.684	-6.615	0.032	-0.549	-0.551	-0.005
55	A	73	GLY	0	0.033	0.019	6.276	0.328	0.328	0.000	0.000	0.000	0.000
56	A	74	SER	0	-0.138	-0.096	8.769	0.233	0.233	0.000	0.000	0.000	0.000
57	A	75	TYR	0	0.049	0.017	10.865	0.040	0.040	0.000	0.000	0.000	0.000
58	A	76	GLY	0	0.021	0.004	13.302	-0.085	-0.085	0.000	0.000	0.000	0.000
59	A	77	ARG	1	0.783	0.859	14.985	0.373	0.373	0.000	0.000	0.000	0.000
60	A	78	VAL	0	-0.002	0.000	18.714	-0.017	-0.017	0.000	0.000	0.000	0.000
61	A	79	ALA	0	0.024	0.007	20.906	0.035	0.035	0.000	0.000	0.000	0.000
62	A	80	PRO	0	0.062	0.019	23.473	-0.006	-0.006	0.000	0.000	0.000	0.000
63	A	81	ARG	1	0.889	0.956	25.168	0.153	0.153	0.000	0.000	0.000	0.000
64	A	89	PHE	0	0.033	0.016	36.666	0.001	0.001	0.000	0.000	0.000	0.000
65	A	90	ILE	0	-0.055	-0.032	33.991	0.001	0.001	0.000	0.000	0.000	0.000
66	A	91	ASP	-1	-0.878	-0.927	33.192	-0.134	-0.134	0.000	0.000	0.000	0.000
67	A	92	VAL	0	-0.034	-0.034	27.781	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	93	GLY	0	0.061	0.043	28.876	-0.006	-0.006	0.000	0.000	0.000	0.000
69	A	94	ALA	0	-0.022	-0.019	25.256	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	95	GLY	0	-0.001	-0.007	22.927	0.014	0.014	0.000	0.000	0.000	0.000
71	A	96	VAL	0	-0.052	-0.026	17.664	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	97	VAL	0	-0.028	0.008	14.771	0.034	0.034	0.000	0.000	0.000	0.000
73	A	98	ASP	-1	-0.777	-0.910	13.412	-0.508	-0.508	0.000	0.000	0.000	0.000
74	A	99	GLU	-1	-0.826	-0.912	8.977	-1.101	-1.101	0.000	0.000	0.000	0.000
75	A	100	ASP	-1	-0.869	-0.915	10.762	-0.382	-0.382	0.000	0.000	0.000	0.000
76	A	101	TYR	0	-0.078	-0.036	13.650	0.095	0.095	0.000	0.000	0.000	0.000
77	A	102	ARG	1	0.848	0.905	10.700	0.518	0.518	0.000	0.000	0.000	0.000
78	A	103	GLY	0	0.027	0.027	16.487	0.043	0.043	0.000	0.000	0.000	0.000
79	A	104	ASN	0	0.003	-0.025	18.675	-0.049	-0.049	0.000	0.000	0.000	0.000
80	A	105	LEU	0	0.035	0.023	16.160	0.019	0.019	0.000	0.000	0.000	0.000
81	A	106	GLY	0	-0.010	-0.007	20.442	0.024	0.024	0.000	0.000	0.000	0.000
82	A	107	VAL	0	-0.018	0.011	23.620	-0.016	-0.016	0.000	0.000	0.000	0.000
83	A	108	VAL	0	-0.037	-0.019	26.447	0.011	0.011	0.000	0.000	0.000	0.000
84	A	109	LEU	0	0.003	0.014	29.988	-0.002	-0.002	0.000	0.000	0.000	0.000
85	A	110	PHE	0	0.006	-0.027	31.812	0.008	0.008	0.000	0.000	0.000	0.000
86	A	111	ASN	0	-0.001	-0.001	35.913	0.000	0.000	0.000	0.000	0.000	0.000
87	A	112	HIS	0	-0.032	-0.015	36.926	0.009	0.009	0.000	0.000	0.000	0.000
88	A	113	SER	0	-0.054	-0.032	41.197	0.005	0.005	0.000	0.000	0.000	0.000
89	A	114	ASP	-1	-0.849	-0.927	43.715	-0.066	-0.066	0.000	0.000	0.000	0.000
90	A	115	VAL	0	-0.015	-0.010	44.781	0.003	0.003	0.000	0.000	0.000	0.000
91	A	116	ASP	-1	-0.832	-0.896	42.147	-0.081	-0.081	0.000	0.000	0.000	0.000
92	A	117	PHE	0	-0.002	0.000	34.430	0.000	0.000	0.000	0.000	0.000	0.000
93	A	118	GLU	-1	-0.800	-0.864	37.450	-0.098	-0.098	0.000	0.000	0.000	0.000
94	A	119	VAL	0	-0.018	0.010	30.793	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	120	LYS	1	0.861	0.908	33.219	0.104	0.104	0.000	0.000	0.000	0.000
96	A	121	HIS	0	-0.020	-0.013	27.518	-0.008	-0.008	0.000	0.000	0.000	0.000
97	A	122	GLY	0	0.042	0.014	27.218	0.006	0.006	0.000	0.000	0.000	0.000
98	A	123	ASP	-1	-0.879	-0.928	27.785	-0.143	-0.143	0.000	0.000	0.000	0.000
99	A	124	ARG	1	0.817	0.909	25.191	0.178	0.178	0.000	0.000	0.000	0.000
100	A	125	ILE	0	-0.007	-0.005	25.083	0.015	0.015	0.000	0.000	0.000	0.000
101	A	126	ALA	0	-0.005	0.002	23.343	0.009	0.009	0.000	0.000	0.000	0.000
102	A	127	GLN	0	-0.055	-0.032	21.095	-0.024	-0.024	0.000	0.000	0.000	0.000
103	A	128	PHE	0	0.022	0.011	12.963	0.020	0.020	0.000	0.000	0.000	0.000
104	A	129	ILE	0	0.003	-0.003	16.875	-0.036	-0.036	0.000	0.000	0.000	0.000
105	A	130	CYS	0	-0.012	0.006	11.747	-0.056	-0.056	0.000	0.000	0.000	0.000
106	A	131	GLU	-1	-0.826	-0.868	13.673	-0.268	-0.268	0.000	0.000	0.000	0.000
107	A	132	ARG	1	0.745	0.789	6.024	1.395	1.395	0.000	0.000	0.000	0.000
108	A	133	ILE	0	0.013	0.016	13.537	0.067	0.067	0.000	0.000	0.000	0.000
109	A	134	PHE	0	-0.023	-0.011	14.676	0.024	0.024	0.000	0.000	0.000	0.000
110	A	135	TYR	0	0.020	-0.002	15.442	-0.014	-0.014	0.000	0.000	0.000	0.000
111	A	136	PRO	0	-0.012	0.010	19.599	0.026	0.026	0.000	0.000	0.000	0.000
112	A	137	GLN	0	-0.004	-0.009	21.980	-0.005	-0.005	0.000	0.000	0.000	0.000
113	A	138	LEU	0	-0.003	0.009	25.109	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	139	VAL	0	0.005	-0.005	27.844	0.006	0.006	0.000	0.000	0.000	0.000
115	A	140	MET	0	-0.002	0.001	31.471	-0.007	-0.007	0.000	0.000	0.000	0.000
116	A	141	VAL	0	-0.010	-0.013	34.465	0.004	0.004	0.000	0.000	0.000	0.000
117	A	142	ASP	-1	-0.829	-0.892	37.173	-0.013	-0.013	0.000	0.000	0.000	0.000
118	A	143	LYS	1	0.842	0.897	39.470	0.011	0.011	0.000	0.000	0.000	0.000
119	A	144	LEU	0	0.000	0.016	33.974	0.002	0.002	0.000	0.000	0.000	0.000

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