FMO DATABASE

FMODB ID: 6N18Z

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	OptHSide
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	-870376.904709
FMO2-HF: Nuclear repulsion	824771.099541
FMO2-HF: Total energy	-45605.805168
FMO2-MP2: Total energy	-45739.678794

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.
-2.922	0.04	0.671	-1.317	-2.314	-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 : -0.030 / q_NPA : -0.031

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	-0.036	-0.017	2.388	0.707	2.684	0.665	-0.875	-1.766	-0.002
4	A	22	LEU	0	-0.004	0.011	4.830	-0.089	-0.077	-0.001	-0.006	-0.004	0.000
5	A	23	ARG	1	0.910	0.963	3.360	1.221	1.889	0.007	-0.290	-0.385	0.002
6	A	24	PHE	0	0.035	-0.001	9.773	0.002	0.002	0.000	0.000	0.000	0.000
7	A	25	ALA	0	-0.009	0.001	13.522	0.044	0.044	0.000	0.000	0.000	0.000
8	A	26	LYS	1	0.835	0.916	15.928	0.194	0.194	0.000	0.000	0.000	0.000
9	A	27	LEU	0	-0.041	-0.025	19.612	0.013	0.013	0.000	0.000	0.000	0.000
10	A	28	THR	0	-0.015	-0.019	22.034	0.020	0.020	0.000	0.000	0.000	0.000
11	A	29	GLU	-1	-0.879	-0.946	23.784	-0.137	-0.137	0.000	0.000	0.000	0.000
12	A	30	ASN	0	-0.049	-0.029	25.866	0.007	0.007	0.000	0.000	0.000	0.000
13	A	31	ALA	0	0.008	0.019	21.586	-0.005	-0.005	0.000	0.000	0.000	0.000
14	A	32	LEU	0	-0.029	-0.014	22.623	0.013	0.013	0.000	0.000	0.000	0.000
15	A	33	GLU	-1	-0.827	-0.913	17.915	-0.234	-0.234	0.000	0.000	0.000	0.000
16	A	34	PRO	0	-0.032	-0.015	15.970	0.026	0.026	0.000	0.000	0.000	0.000
17	A	35	VAL	0	-0.016	0.006	16.967	-0.025	-0.025	0.000	0.000	0.000	0.000
18	A	36	ARG	1	0.912	0.947	17.248	0.256	0.256	0.000	0.000	0.000	0.000
19	A	37	GLY	0	0.044	0.038	19.969	0.025	0.025	0.000	0.000	0.000	0.000
20	A	38	SER	0	-0.028	-0.032	22.685	0.023	0.023	0.000	0.000	0.000	0.000
21	A	39	ALA	0	0.042	0.017	21.701	-0.019	-0.019	0.000	0.000	0.000	0.000
22	A	40	LYS	1	0.958	0.962	21.195	0.087	0.087	0.000	0.000	0.000	0.000
23	A	41	ALA	0	-0.019	0.023	21.292	-0.001	-0.001	0.000	0.000	0.000	0.000
24	A	42	ALA	0	0.055	0.029	19.660	-0.009	-0.009	0.000	0.000	0.000	0.000
25	A	43	GLY	0	0.043	0.029	17.236	-0.050	-0.050	0.000	0.000	0.000	0.000
26	A	44	VAL	0	-0.074	-0.029	15.668	0.046	0.046	0.000	0.000	0.000	0.000
27	A	45	ASP	-1	-0.840	-0.941	18.466	-0.235	-0.235	0.000	0.000	0.000	0.000
28	A	46	LEU	0	-0.012	-0.010	18.558	-0.010	-0.010	0.000	0.000	0.000	0.000
29	A	47	ARG	1	0.882	0.920	22.058	0.205	0.205	0.000	0.000	0.000	0.000
30	A	48	SER	0	-0.034	-0.008	24.719	-0.015	-0.015	0.000	0.000	0.000	0.000
31	A	49	ALA	0	0.069	0.041	25.608	0.007	0.007	0.000	0.000	0.000	0.000
32	A	50	TYR	0	-0.028	-0.023	27.379	0.017	0.017	0.000	0.000	0.000	0.000
33	A	51	ASH	0	-0.095	-0.073	31.143	-0.004	-0.004	0.000	0.000	0.000	0.000
34	A	52	VAL	0	-0.014	-0.014	32.127	0.001	0.001	0.000	0.000	0.000	0.000
35	A	53	VAL	0	0.031	0.031	35.186	-0.001	-0.001	0.000	0.000	0.000	0.000
36	A	54	VAL	0	-0.038	-0.024	35.492	-0.003	-0.003	0.000	0.000	0.000	0.000
37	A	55	PRO	0	0.038	0.017	38.301	0.003	0.003	0.000	0.000	0.000	0.000
38	A	56	ALA	0	0.039	0.016	41.435	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	57	ARG	1	0.789	0.895	43.262	0.078	0.078	0.000	0.000	0.000	0.000
40	A	58	GLY	0	0.025	0.033	41.009	0.000	0.000	0.000	0.000	0.000	0.000
41	A	59	LYS	1	0.938	0.959	35.656	0.117	0.117	0.000	0.000	0.000	0.000
42	A	60	ALA	0	0.007	0.010	34.724	0.005	0.005	0.000	0.000	0.000	0.000
43	A	61	ILE	0	-0.028	-0.007	27.493	-0.008	-0.008	0.000	0.000	0.000	0.000
44	A	62	VAL	0	0.012	0.005	28.650	0.007	0.007	0.000	0.000	0.000	0.000
45	A	63	LYS	1	0.853	0.916	24.451	0.216	0.216	0.000	0.000	0.000	0.000
46	A	64	THR	0	0.033	-0.006	21.796	0.001	0.001	0.000	0.000	0.000	0.000
47	A	65	ASP	-1	-0.753	-0.841	23.221	-0.181	-0.181	0.000	0.000	0.000	0.000
48	A	66	LEU	0	-0.025	0.009	17.768	-0.001	-0.001	0.000	0.000	0.000	0.000
49	A	67	GLN	0	-0.045	-0.017	16.011	0.009	0.009	0.000	0.000	0.000	0.000
50	A	68	VAL	0	-0.021	-0.028	12.534	0.003	0.003	0.000	0.000	0.000	0.000
51	A	69	GLN	0	-0.039	-0.013	6.526	0.416	0.416	0.000	0.000	0.000	0.000
52	A	70	VAL	0	-0.027	-0.018	9.102	-0.190	-0.190	0.000	0.000	0.000	0.000
53	A	71	PRO	0	0.006	0.003	5.528	-0.071	-0.071	0.000	0.000	0.000	0.000
54	A	72	GLU	-1	-0.820	-0.890	3.770	-5.893	-5.588	0.000	-0.146	-0.159	-0.001
55	A	73	GLY	0	0.014	0.017	6.909	0.065	0.065	0.000	0.000	0.000	0.000
56	A	74	SER	0	-0.139	-0.086	9.306	0.292	0.292	0.000	0.000	0.000	0.000
57	A	75	TYR	0	0.035	0.008	11.180	0.023	0.023	0.000	0.000	0.000	0.000
58	A	76	GLY	0	0.000	0.005	14.230	-0.043	-0.043	0.000	0.000	0.000	0.000
59	A	77	ARG	1	0.819	0.883	15.492	0.404	0.404	0.000	0.000	0.000	0.000
60	A	78	VAL	0	-0.010	-0.003	19.166	-0.004	-0.004	0.000	0.000	0.000	0.000
61	A	79	ALA	0	0.009	-0.005	21.495	0.029	0.029	0.000	0.000	0.000	0.000
62	A	80	PRO	0	0.069	0.029	24.090	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	81	ARG	1	0.864	0.945	25.748	0.158	0.158	0.000	0.000	0.000	0.000
64	A	89	PHE	0	0.018	0.004	37.290	0.001	0.001	0.000	0.000	0.000	0.000
65	A	90	ILE	0	-0.033	-0.025	34.366	0.001	0.001	0.000	0.000	0.000	0.000
66	A	91	ASP	-1	-0.929	-0.947	33.531	-0.148	-0.148	0.000	0.000	0.000	0.000
67	A	92	VAL	0	0.011	-0.003	27.816	-0.002	-0.002	0.000	0.000	0.000	0.000
68	A	93	GLY	0	0.048	0.032	29.284	-0.002	-0.002	0.000	0.000	0.000	0.000
69	A	94	ALA	0	-0.029	-0.026	25.848	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	95	GLY	0	-0.001	-0.005	23.263	0.013	0.013	0.000	0.000	0.000	0.000
71	A	96	VAL	0	-0.042	-0.020	18.256	-0.010	-0.010	0.000	0.000	0.000	0.000
72	A	97	VAL	0	-0.046	-0.009	15.273	0.035	0.035	0.000	0.000	0.000	0.000
73	A	98	ASP	-1	-0.788	-0.916	14.069	-0.598	-0.598	0.000	0.000	0.000	0.000
74	A	99	GLU	-1	-0.815	-0.915	9.402	-1.342	-1.342	0.000	0.000	0.000	0.000
75	A	100	ASP	-1	-0.867	-0.914	11.458	-0.545	-0.545	0.000	0.000	0.000	0.000
76	A	101	TYR	0	-0.066	-0.021	14.243	0.124	0.124	0.000	0.000	0.000	0.000
77	A	102	ARG	1	0.852	0.896	11.390	0.626	0.626	0.000	0.000	0.000	0.000
78	A	103	GLY	0	0.012	0.024	17.321	0.045	0.045	0.000	0.000	0.000	0.000
79	A	104	ASN	0	-0.005	-0.015	19.203	-0.043	-0.043	0.000	0.000	0.000	0.000
80	A	105	LEU	0	0.018	0.013	17.020	0.020	0.020	0.000	0.000	0.000	0.000
81	A	106	GLY	0	0.042	0.016	21.155	0.023	0.023	0.000	0.000	0.000	0.000
82	A	107	VAL	0	-0.035	0.001	24.394	-0.017	-0.017	0.000	0.000	0.000	0.000
83	A	108	VAL	0	-0.018	-0.001	27.092	0.012	0.012	0.000	0.000	0.000	0.000
84	A	109	LEU	0	-0.014	0.005	30.448	-0.003	-0.003	0.000	0.000	0.000	0.000
85	A	110	PHE	0	0.004	-0.023	32.447	0.007	0.007	0.000	0.000	0.000	0.000
86	A	111	ASN	0	-0.016	-0.011	36.443	0.000	0.000	0.000	0.000	0.000	0.000
87	A	112	HIS	0	-0.021	-0.010	37.763	0.008	0.008	0.000	0.000	0.000	0.000
88	A	113	SER	0	-0.037	-0.022	42.042	0.006	0.006	0.000	0.000	0.000	0.000
89	A	114	ASP	-1	-0.846	-0.943	44.344	-0.070	-0.070	0.000	0.000	0.000	0.000
90	A	115	VAL	0	-0.019	-0.002	44.830	0.003	0.003	0.000	0.000	0.000	0.000
91	A	116	ASP	-1	-0.849	-0.908	42.363	-0.084	-0.084	0.000	0.000	0.000	0.000
92	A	117	PHE	0	-0.021	-0.017	34.849	0.001	0.001	0.000	0.000	0.000	0.000
93	A	118	GLU	-1	-0.812	-0.870	37.601	-0.096	-0.096	0.000	0.000	0.000	0.000
94	A	119	VAL	0	-0.026	-0.010	31.147	-0.003	-0.003	0.000	0.000	0.000	0.000
95	A	120	LYS	1	0.880	0.929	33.616	0.098	0.098	0.000	0.000	0.000	0.000
96	A	121	HIS	0	-0.029	-0.017	27.769	-0.007	-0.007	0.000	0.000	0.000	0.000
97	A	122	GLY	0	0.036	0.001	27.569	0.007	0.007	0.000	0.000	0.000	0.000
98	A	123	ASP	-1	-0.865	-0.910	28.093	-0.134	-0.134	0.000	0.000	0.000	0.000
99	A	124	ARG	1	0.818	0.896	25.366	0.163	0.163	0.000	0.000	0.000	0.000
100	A	125	ILE	0	0.010	-0.002	25.511	0.015	0.015	0.000	0.000	0.000	0.000
101	A	126	ALA	0	-0.001	0.004	23.842	0.005	0.005	0.000	0.000	0.000	0.000
102	A	127	GLN	0	-0.045	-0.024	21.064	-0.016	-0.016	0.000	0.000	0.000	0.000
103	A	128	PHE	0	0.035	0.023	13.619	0.012	0.012	0.000	0.000	0.000	0.000
104	A	129	ILE	0	-0.017	-0.017	17.197	-0.024	-0.024	0.000	0.000	0.000	0.000
105	A	130	CYS	0	0.008	0.012	12.207	-0.053	-0.053	0.000	0.000	0.000	0.000
106	A	131	GLU	-1	-0.826	-0.879	14.226	-0.295	-0.295	0.000	0.000	0.000	0.000
107	A	132	ARG	1	0.806	0.855	6.140	1.752	1.752	0.000	0.000	0.000	0.000
108	A	133	ILE	0	0.020	0.023	13.707	0.077	0.077	0.000	0.000	0.000	0.000
109	A	134	PHE	0	-0.016	-0.011	14.771	0.005	0.005	0.000	0.000	0.000	0.000
110	A	135	TYR	0	0.014	-0.005	15.529	-0.010	-0.010	0.000	0.000	0.000	0.000
111	A	136	PRO	0	-0.022	0.006	19.417	0.028	0.028	0.000	0.000	0.000	0.000
112	A	137	GLN	0	0.010	0.000	21.615	-0.004	-0.004	0.000	0.000	0.000	0.000
113	A	138	LEU	0	0.002	0.000	24.577	-0.008	-0.008	0.000	0.000	0.000	0.000
114	A	139	VAL	0	-0.004	-0.006	27.529	0.007	0.007	0.000	0.000	0.000	0.000
115	A	140	MET	0	0.001	0.010	31.151	-0.008	-0.008	0.000	0.000	0.000	0.000
116	A	141	VAL	0	-0.008	-0.012	33.769	0.005	0.005	0.000	0.000	0.000	0.000
117	A	142	ASP	-1	-0.841	-0.905	36.466	-0.021	-0.021	0.000	0.000	0.000	0.000
118	A	143	LYS	1	0.855	0.906	39.174	0.017	0.017	0.000	0.000	0.000	0.000
119	A	144	LEU	0	-0.004	0.012	33.604	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)