FMO DATABASE

FMODB ID: N35MQ

Calculation Name: 3ENU-A-Xray307

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3ENU

Chain ID: A

ChEMBL ID:

UniProt ID: Q2YAE2

Base Structure: X-ray

Registration Date: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

Apendix: None

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. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	113
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-939153.030787
FMO2-HF: Nuclear repulsion	893834.453911
FMO2-HF: Total energy	-45318.576876
FMO2-MP2: Total energy	-45450.935871

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:27:THR )

Summations of interaction energy for fragment #1(A:27: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.
-1.192	0.817	-0.013	-0.811	-1.185	0.001

Interaction energy analysis for fragmet #1(A:27:THR )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.018 / q_NPA : -0.022

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	29	GLU	-1	-0.919	-0.959	3.599	-2.291	-0.406	-0.013	-0.792	-1.081	0.001
4	A	30	VAL	0	-0.014	-0.010	6.073	0.270	0.270	0.000	0.000	0.000	0.000
5	A	31	PRO	0	-0.020	0.001	9.489	-0.085	-0.085	0.000	0.000	0.000	0.000
6	A	32	VAL	0	0.022	0.006	10.747	0.177	0.177	0.000	0.000	0.000	0.000
7	A	33	LEU	0	-0.014	-0.001	13.397	0.019	0.019	0.000	0.000	0.000	0.000
8	A	34	THR	0	-0.028	-0.020	15.392	0.034	0.034	0.000	0.000	0.000	0.000
9	A	35	PHE	0	0.029	0.019	18.255	0.001	0.001	0.000	0.000	0.000	0.000
10	A	36	VAL	0	-0.020	-0.007	17.489	0.006	0.006	0.000	0.000	0.000	0.000
11	A	37	PRO	0	0.025	0.002	20.915	0.016	0.016	0.000	0.000	0.000	0.000
12	A	38	VAL	0	0.076	0.027	22.222	-0.017	-0.017	0.000	0.000	0.000	0.000
13	A	39	GLN	0	0.014	-0.002	23.255	-0.015	-0.015	0.000	0.000	0.000	0.000
14	A	40	VAL	0	0.027	0.019	17.533	-0.001	-0.001	0.000	0.000	0.000	0.000
15	A	41	SER	0	0.049	0.015	18.415	-0.026	-0.026	0.000	0.000	0.000	0.000
16	A	42	ALA	0	-0.014	0.003	19.335	-0.011	-0.011	0.000	0.000	0.000	0.000
17	A	43	GLU	-1	-0.898	-0.939	17.372	-0.197	-0.197	0.000	0.000	0.000	0.000
18	A	44	LEU	0	-0.043	-0.034	13.164	-0.011	-0.011	0.000	0.000	0.000	0.000
19	A	45	GLU	-1	-0.871	-0.920	15.975	-0.246	-0.246	0.000	0.000	0.000	0.000
20	A	46	ASN	0	-0.009	-0.002	18.590	0.027	0.027	0.000	0.000	0.000	0.000
21	A	47	ARG	1	0.934	0.955	11.127	0.399	0.399	0.000	0.000	0.000	0.000
22	A	48	GLY	0	-0.013	-0.004	15.362	0.014	0.014	0.000	0.000	0.000	0.000
23	A	139	CYS	0	-0.061	-0.013	8.099	-0.137	-0.137	0.000	0.000	0.000	0.000
24	A	50	TRP	0	0.027	0.019	12.847	-0.115	-0.115	0.000	0.000	0.000	0.000
25	A	51	VAL	0	0.031	0.008	15.127	0.071	0.071	0.000	0.000	0.000	0.000
26	A	52	LYS	1	0.807	0.898	17.607	0.210	0.210	0.000	0.000	0.000	0.000
27	A	53	PHE	0	0.021	0.003	18.083	0.030	0.030	0.000	0.000	0.000	0.000
28	A	54	PHE	0	0.011	-0.009	22.583	-0.004	-0.004	0.000	0.000	0.000	0.000
29	A	55	ASP	-1	-0.830	-0.905	26.288	-0.148	-0.148	0.000	0.000	0.000	0.000
30	A	56	LYS	1	0.910	0.962	28.850	0.123	0.123	0.000	0.000	0.000	0.000
31	A	57	LYS	1	0.959	0.978	30.238	0.077	0.077	0.000	0.000	0.000	0.000
32	A	58	ASN	0	-0.058	-0.047	31.579	0.001	0.001	0.000	0.000	0.000	0.000
33	A	59	PHE	0	0.013	-0.002	26.544	0.007	0.007	0.000	0.000	0.000	0.000
34	A	60	GLN	0	-0.060	-0.004	29.334	0.003	0.003	0.000	0.000	0.000	0.000
35	A	61	GLY	0	0.000	-0.013	30.391	-0.006	-0.006	0.000	0.000	0.000	0.000
36	A	62	ASP	-1	-0.905	-0.941	27.974	-0.185	-0.185	0.000	0.000	0.000	0.000
37	A	63	SER	0	0.009	-0.022	23.878	-0.003	-0.003	0.000	0.000	0.000	0.000
38	A	64	LEU	0	-0.011	0.020	19.099	-0.003	-0.003	0.000	0.000	0.000	0.000
39	A	65	PHE	0	-0.010	-0.019	16.342	0.003	0.003	0.000	0.000	0.000	0.000
40	A	66	LEU	0	-0.006	-0.002	14.019	-0.042	-0.042	0.000	0.000	0.000	0.000
41	A	67	SER	0	0.023	0.002	11.588	0.127	0.127	0.000	0.000	0.000	0.000
42	A	68	GLY	0	-0.028	0.009	9.191	-0.113	-0.113	0.000	0.000	0.000	0.000
43	A	69	PRO	0	-0.001	-0.024	4.401	0.168	0.292	0.000	-0.019	-0.104	0.000
44	A	70	ALA	0	0.003	-0.009	6.759	-0.522	-0.522	0.000	0.000	0.000	0.000
45	A	71	THR	0	0.022	0.029	8.014	0.529	0.529	0.000	0.000	0.000	0.000
46	A	72	LEU	0	0.016	-0.003	10.171	-0.069	-0.069	0.000	0.000	0.000	0.000
47	A	73	PRO	0	-0.014	0.009	12.785	0.129	0.129	0.000	0.000	0.000	0.000
48	A	74	ARG	1	1.031	0.986	15.338	0.331	0.331	0.000	0.000	0.000	0.000
49	A	75	LEU	0	0.010	0.033	17.788	-0.064	-0.064	0.000	0.000	0.000	0.000
50	A	76	ILE	0	0.017	0.012	18.986	0.038	0.038	0.000	0.000	0.000	0.000
51	A	77	GLY	0	-0.012	-0.019	18.739	-0.063	-0.063	0.000	0.000	0.000	0.000
52	A	78	PRO	0	-0.010	-0.009	18.569	0.037	0.037	0.000	0.000	0.000	0.000
53	A	79	PHE	0	-0.028	-0.037	21.428	0.012	0.012	0.000	0.000	0.000	0.000
54	A	80	GLY	0	0.015	0.013	24.677	0.015	0.015	0.000	0.000	0.000	0.000
55	A	81	TYR	0	-0.036	0.015	20.969	0.022	0.022	0.000	0.000	0.000	0.000
56	A	82	ASP	-1	-0.856	-0.938	23.247	-0.238	-0.238	0.000	0.000	0.000	0.000
57	A	83	TRP	0	-0.055	-0.035	17.737	0.017	0.017	0.000	0.000	0.000	0.000
58	A	84	GLU	-1	-0.774	-0.875	23.633	-0.200	-0.200	0.000	0.000	0.000	0.000
59	A	85	ASN	0	-0.067	-0.053	25.404	0.018	0.018	0.000	0.000	0.000	0.000
60	A	86	LYS	1	0.892	0.954	26.149	0.174	0.174	0.000	0.000	0.000	0.000
61	A	87	VAL	0	0.002	0.014	22.708	0.008	0.008	0.000	0.000	0.000	0.000
62	A	88	ARG	1	0.880	0.938	26.136	0.147	0.147	0.000	0.000	0.000	0.000
63	A	89	SER	0	-0.076	-0.030	27.113	0.013	0.013	0.000	0.000	0.000	0.000
64	A	90	VAL	0	0.028	0.017	20.881	-0.020	-0.020	0.000	0.000	0.000	0.000
65	A	91	LYS	1	0.851	0.922	22.415	0.173	0.173	0.000	0.000	0.000	0.000
66	A	92	VAL	0	0.026	0.015	16.804	-0.048	-0.048	0.000	0.000	0.000	0.000
67	A	93	GLY	0	0.002	0.010	17.456	0.033	0.033	0.000	0.000	0.000	0.000
68	A	94	PRO	0	-0.036	-0.033	17.704	0.021	0.021	0.000	0.000	0.000	0.000
69	A	95	ARG	1	0.925	0.959	13.691	0.195	0.195	0.000	0.000	0.000	0.000
70	A	96	ALA	0	0.037	0.023	12.700	-0.070	-0.070	0.000	0.000	0.000	0.000
71	A	97	ASN	0	-0.041	-0.007	12.755	0.138	0.138	0.000	0.000	0.000	0.000
72	A	98	LEU	0	-0.004	-0.008	13.177	-0.094	-0.094	0.000	0.000	0.000	0.000
73	A	99	THR	0	0.014	0.019	14.730	0.083	0.083	0.000	0.000	0.000	0.000
74	A	100	ILE	0	-0.064	-0.025	15.980	-0.066	-0.066	0.000	0.000	0.000	0.000
75	A	101	PHE	0	0.051	0.000	14.358	0.029	0.029	0.000	0.000	0.000	0.000
76	A	102	ASP	-1	-0.879	-0.945	19.727	-0.119	-0.119	0.000	0.000	0.000	0.000
77	A	103	ASN	0	0.005	0.031	21.944	-0.028	-0.028	0.000	0.000	0.000	0.000
78	A	104	HIS	0	-0.064	-0.043	19.643	-0.005	-0.005	0.000	0.000	0.000	0.000
79	A	105	ASN	0	-0.134	-0.100	16.209	0.054	0.054	0.000	0.000	0.000	0.000
80	A	106	TYR	0	0.021	-0.006	11.454	0.028	0.028	0.000	0.000	0.000	0.000
81	A	107	ARG	1	0.893	0.966	16.374	0.146	0.146	0.000	0.000	0.000	0.000
82	A	108	ASP	-1	-0.873	-0.952	19.742	-0.071	-0.071	0.000	0.000	0.000	0.000
83	A	109	GLU	-1	-0.912	-0.948	21.337	-0.027	-0.027	0.000	0.000	0.000	0.000
84	A	110	ASP	-1	-0.913	-0.960	18.994	-0.016	-0.016	0.000	0.000	0.000	0.000
85	A	111	LYS	1	0.875	0.949	20.289	0.051	0.051	0.000	0.000	0.000	0.000
86	A	112	PHE	0	0.017	0.015	15.264	-0.030	-0.030	0.000	0.000	0.000	0.000
87	A	113	LEU	0	-0.064	-0.036	18.522	0.004	0.004	0.000	0.000	0.000	0.000
88	A	114	ASP	-1	-0.772	-0.889	17.898	-0.006	-0.006	0.000	0.000	0.000	0.000
89	A	115	ALA	0	0.005	-0.007	16.999	-0.034	-0.034	0.000	0.000	0.000	0.000
90	A	116	GLY	0	-0.074	-0.036	18.431	0.022	0.022	0.000	0.000	0.000	0.000
91	A	117	ALA	0	-0.041	-0.002	20.857	0.006	0.006	0.000	0.000	0.000	0.000
92	A	118	ASN	0	0.035	0.024	22.630	-0.037	-0.037	0.000	0.000	0.000	0.000
93	A	119	VAL	0	0.023	0.027	24.313	0.016	0.016	0.000	0.000	0.000	0.000
94	A	120	ALA	0	0.007	-0.010	26.728	-0.012	-0.012	0.000	0.000	0.000	0.000
95	A	121	ASN	0	0.014	-0.006	29.882	-0.008	-0.008	0.000	0.000	0.000	0.000
96	A	122	LEU	0	0.007	0.014	24.061	0.008	0.008	0.000	0.000	0.000	0.000
97	A	123	SER	0	0.044	0.016	28.218	-0.003	-0.003	0.000	0.000	0.000	0.000
98	A	124	LYS	1	1.001	1.000	30.192	0.061	0.061	0.000	0.000	0.000	0.000
99	A	125	GLU	-1	-1.001	-0.995	31.090	-0.050	-0.050	0.000	0.000	0.000	0.000
100	A	126	MET	0	-0.074	-0.032	31.116	0.007	0.007	0.000	0.000	0.000	0.000
101	A	127	GLY	0	0.010	0.014	30.085	0.002	0.002	0.000	0.000	0.000	0.000
102	A	128	PHE	0	-0.060	-0.047	24.230	0.000	0.000	0.000	0.000	0.000	0.000
103	A	129	PHE	0	0.042	0.018	22.125	0.005	0.005	0.000	0.000	0.000	0.000
104	A	130	ASP	-1	-0.861	-0.938	27.245	-0.090	-0.090	0.000	0.000	0.000	0.000
105	A	131	ASN	0	-0.046	-0.038	26.354	-0.018	-0.018	0.000	0.000	0.000	0.000
106	A	132	PHE	0	-0.007	0.028	19.141	0.004	0.004	0.000	0.000	0.000	0.000
107	A	133	ARG	1	0.907	0.951	21.454	0.153	0.153	0.000	0.000	0.000	0.000
108	A	134	SER	0	-0.076	-0.034	16.137	-0.024	-0.024	0.000	0.000	0.000	0.000
109	A	135	MET	0	-0.015	-0.001	13.889	0.060	0.060	0.000	0.000	0.000	0.000
110	A	136	VAL	0	0.034	0.020	9.465	-0.128	-0.128	0.000	0.000	0.000	0.000
111	A	137	LEU	0	-0.025	-0.004	10.844	0.150	0.150	0.000	0.000	0.000	0.000
112	A	138	ASN	0	0.021	-0.006	8.185	-0.298	-0.298	0.000	0.000	0.000	0.000
113	A	140	ILE	-1	-0.930	-0.948	9.204	0.200	0.200	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:27:THR )