FMO DATABASE

FMODB ID: G53Y1

Calculation Name: 5ENU-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5ENU

Chain ID: A

ChEMBL ID:

UniProt ID: B1YRI5

Base Structure: X-ray

Registration Date: 2023-09-23

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

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. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	157
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1548450.605989
FMO2-HF: Nuclear repulsion	1487179.181363
FMO2-HF: Total energy	-61271.424626
FMO2-MP2: Total energy	-61450.949471

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:-3:HIS)

Summations of interaction energy for fragment #1(A:-3:HIS)

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.
-6.638	-0.975	4.221	-3.282	-6.604	-0.001

Interaction energy analysis for fragmet #1(A:-3:HIS)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.009 / q_NPA : -0.019

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	-1	HIS	0	-0.008	0.008	2.890	-1.779	1.782	0.051	-1.633	-1.979	0.001
4	A	0	HIS	0	0.010	0.000	3.058	-3.306	-2.177	0.121	-0.577	-0.673	-0.006
5	A	1	MET	0	-0.040	-0.017	2.501	-1.900	-1.038	4.050	-1.069	-3.844	0.004
6	A	2	SER	0	0.053	0.027	5.903	0.384	0.384	0.000	0.000	0.000	0.000
7	A	3	VAL	0	-0.048	-0.018	9.701	0.227	0.227	0.000	0.000	0.000	0.000
8	A	4	GLU	-1	-0.904	-0.961	11.825	-0.227	-0.227	0.000	0.000	0.000	0.000
9	A	5	VAL	0	-0.047	-0.030	13.581	0.111	0.111	0.000	0.000	0.000	0.000
10	A	6	ASP	-1	-0.914	-0.951	15.613	0.253	0.253	0.000	0.000	0.000	0.000
11	A	7	ARG	1	0.856	0.928	10.115	-0.264	-0.264	0.000	0.000	0.000	0.000
12	A	8	GLN	0	-0.032	-0.016	7.943	-0.135	-0.135	0.000	0.000	0.000	0.000
13	A	9	VAL	0	-0.008	-0.003	9.041	-0.004	-0.004	0.000	0.000	0.000	0.000
14	A	10	PRO	0	-0.032	-0.016	5.191	0.274	0.385	-0.001	-0.003	-0.108	0.000
15	A	11	ASP	-1	-0.849	-0.937	6.469	0.307	0.307	0.000	0.000	0.000	0.000
16	A	12	PHE	0	-0.006	-0.007	7.092	-0.272	-0.272	0.000	0.000	0.000	0.000
17	A	13	THR	0	0.046	0.028	9.743	0.128	0.128	0.000	0.000	0.000	0.000
18	A	14	ALA	0	-0.020	0.008	12.695	-0.149	-0.149	0.000	0.000	0.000	0.000
19	A	15	PRO	0	0.041	0.021	15.494	0.064	0.064	0.000	0.000	0.000	0.000
20	A	16	ALA	0	0.041	0.014	19.154	-0.007	-0.007	0.000	0.000	0.000	0.000
21	A	17	THR	0	-0.049	-0.027	21.762	0.000	0.000	0.000	0.000	0.000	0.000
22	A	18	GLY	0	-0.024	-0.018	24.733	0.016	0.016	0.000	0.000	0.000	0.000
23	A	19	GLY	0	0.000	0.007	23.133	0.011	0.011	0.000	0.000	0.000	0.000
24	A	20	ASP	-1	-0.990	-0.984	17.523	0.027	0.027	0.000	0.000	0.000	0.000
25	A	21	ILE	0	0.018	0.010	16.913	0.032	0.032	0.000	0.000	0.000	0.000
26	A	22	SER	0	0.018	-0.022	13.114	-0.064	-0.064	0.000	0.000	0.000	0.000
27	A	23	LEU	0	-0.049	-0.011	10.604	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	24	SER	0	-0.014	-0.018	12.436	-0.040	-0.040	0.000	0.000	0.000	0.000
29	A	25	ASP	-1	-0.796	-0.900	14.099	0.285	0.285	0.000	0.000	0.000	0.000
30	A	26	LEU	0	-0.110	-0.068	16.753	-0.060	-0.060	0.000	0.000	0.000	0.000
31	A	27	LYS	1	0.957	0.992	13.457	-0.911	-0.911	0.000	0.000	0.000	0.000
32	A	28	GLY	0	-0.028	-0.010	17.572	-0.052	-0.052	0.000	0.000	0.000	0.000
33	A	29	ARG	1	0.845	0.924	20.221	-0.319	-0.319	0.000	0.000	0.000	0.000
34	A	30	LYS	1	0.865	0.943	20.069	-0.185	-0.185	0.000	0.000	0.000	0.000
35	A	31	LEU	0	0.004	0.002	16.753	-0.028	-0.028	0.000	0.000	0.000	0.000
36	A	32	VAL	0	-0.006	0.004	20.170	0.003	0.003	0.000	0.000	0.000	0.000
37	A	33	LEU	0	0.020	0.015	16.026	-0.017	-0.017	0.000	0.000	0.000	0.000
38	A	34	TYR	0	0.000	-0.012	20.233	-0.015	-0.015	0.000	0.000	0.000	0.000
39	A	35	PHE	0	0.061	0.025	16.056	-0.018	-0.018	0.000	0.000	0.000	0.000
40	A	36	TYR	0	-0.049	-0.059	22.230	0.005	0.005	0.000	0.000	0.000	0.000
41	A	37	PRO	0	-0.046	-0.041	24.972	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	38	LYS	1	0.851	0.892	26.448	0.166	0.166	0.000	0.000	0.000	0.000
43	A	39	ASP	-1	-0.682	-0.804	27.975	-0.094	-0.094	0.000	0.000	0.000	0.000
44	A	40	ASN	0	-0.028	-0.027	30.108	0.003	0.003	0.000	0.000	0.000	0.000
45	A	41	THR	0	-0.005	0.013	31.719	0.004	0.004	0.000	0.000	0.000	0.000
46	A	42	PRO	0	0.073	0.029	34.391	0.006	0.006	0.000	0.000	0.000	0.000
47	A	43	GLY	0	0.025	0.015	33.595	0.007	0.007	0.000	0.000	0.000	0.000
48	A	44	CYS	0	-0.048	0.023	29.721	0.004	0.004	0.000	0.000	0.000	0.000
49	A	45	THR	0	0.010	0.002	31.277	0.007	0.007	0.000	0.000	0.000	0.000
50	A	46	THR	0	-0.020	-0.007	34.010	0.009	0.009	0.000	0.000	0.000	0.000
51	A	47	GLU	-1	-0.806	-0.914	27.742	-0.030	-0.030	0.000	0.000	0.000	0.000
52	A	48	GLY	0	0.014	0.017	30.316	0.011	0.011	0.000	0.000	0.000	0.000
53	A	49	LEU	0	-0.001	-0.017	31.248	0.011	0.011	0.000	0.000	0.000	0.000
54	A	50	GLN	0	0.027	0.009	33.737	0.005	0.005	0.000	0.000	0.000	0.000
55	A	51	PHE	0	0.025	0.010	26.960	0.010	0.010	0.000	0.000	0.000	0.000
56	A	52	ARG	1	0.868	0.942	31.426	0.000	0.000	0.000	0.000	0.000	0.000
57	A	53	GLU	-1	-0.995	-0.984	33.433	0.028	0.028	0.000	0.000	0.000	0.000
58	A	54	LEU	0	0.034	0.008	33.384	0.007	0.007	0.000	0.000	0.000	0.000
59	A	55	TYR	0	-0.033	-0.038	27.543	0.010	0.010	0.000	0.000	0.000	0.000
60	A	56	PRO	0	0.007	-0.012	31.789	0.014	0.014	0.000	0.000	0.000	0.000
61	A	57	LYS	1	0.930	0.963	33.688	-0.058	-0.058	0.000	0.000	0.000	0.000
62	A	58	PHE	0	0.069	0.036	27.676	0.011	0.011	0.000	0.000	0.000	0.000
63	A	59	LYS	1	0.901	0.967	28.126	-0.109	-0.109	0.000	0.000	0.000	0.000
64	A	60	LYS	1	0.922	0.968	30.131	-0.088	-0.088	0.000	0.000	0.000	0.000
65	A	61	ALA	0	-0.020	0.000	29.579	0.006	0.006	0.000	0.000	0.000	0.000
66	A	62	GLY	0	0.022	0.013	27.087	0.016	0.016	0.000	0.000	0.000	0.000
67	A	63	ALA	0	-0.026	-0.010	24.416	0.029	0.029	0.000	0.000	0.000	0.000
68	A	64	GLU	-1	-0.835	-0.890	22.605	0.108	0.108	0.000	0.000	0.000	0.000
69	A	65	ILE	0	-0.038	-0.024	23.544	0.007	0.007	0.000	0.000	0.000	0.000
70	A	66	ILE	0	0.040	0.013	19.180	-0.004	-0.004	0.000	0.000	0.000	0.000
71	A	67	GLY	0	0.012	0.017	22.074	-0.002	-0.002	0.000	0.000	0.000	0.000
72	A	68	VAL	0	-0.002	0.004	18.084	-0.007	-0.007	0.000	0.000	0.000	0.000
73	A	69	SER	0	0.004	-0.021	21.333	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	70	ARG	1	0.883	0.929	20.132	0.333	0.333	0.000	0.000	0.000	0.000
75	A	71	ASP	-1	-0.821	-0.857	22.285	-0.178	-0.178	0.000	0.000	0.000	0.000
76	A	72	SER	0	0.042	0.031	24.028	0.003	0.003	0.000	0.000	0.000	0.000
77	A	73	LEU	0	0.138	0.057	22.681	0.013	0.013	0.000	0.000	0.000	0.000
78	A	74	ARG	1	1.009	1.021	25.954	0.150	0.150	0.000	0.000	0.000	0.000
79	A	75	SER	0	-0.119	-0.084	28.419	0.012	0.012	0.000	0.000	0.000	0.000
80	A	76	HIS	1	0.826	0.885	23.124	0.129	0.129	0.000	0.000	0.000	0.000
81	A	77	ASP	-1	-0.856	-0.922	28.211	-0.051	-0.051	0.000	0.000	0.000	0.000
82	A	78	ASN	0	-0.069	-0.038	30.465	0.015	0.015	0.000	0.000	0.000	0.000
83	A	79	PHE	0	-0.034	-0.015	29.310	0.007	0.007	0.000	0.000	0.000	0.000
84	A	80	LYS	1	0.901	0.928	28.541	-0.007	-0.007	0.000	0.000	0.000	0.000
85	A	81	ALA	0	0.000	0.002	31.602	0.009	0.009	0.000	0.000	0.000	0.000
86	A	82	LYS	1	0.886	0.951	34.959	0.064	0.064	0.000	0.000	0.000	0.000
87	A	83	LEU	0	-0.053	-0.032	32.683	0.002	0.002	0.000	0.000	0.000	0.000
88	A	84	GLU	-1	-0.920	-0.948	35.495	0.008	0.008	0.000	0.000	0.000	0.000
89	A	85	LEU	0	-0.027	-0.007	29.467	0.008	0.008	0.000	0.000	0.000	0.000
90	A	86	PRO	0	-0.033	-0.007	31.297	-0.002	-0.002	0.000	0.000	0.000	0.000
91	A	87	PHE	0	0.011	0.009	26.222	0.012	0.012	0.000	0.000	0.000	0.000
92	A	88	PRO	0	0.021	0.015	23.025	-0.021	-0.021	0.000	0.000	0.000	0.000
93	A	89	LEU	0	-0.018	-0.011	23.740	0.002	0.002	0.000	0.000	0.000	0.000
94	A	90	ILE	0	0.098	0.039	16.824	-0.008	-0.008	0.000	0.000	0.000	0.000
95	A	91	SER	0	-0.122	-0.071	20.577	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	92	ASP	-1	-0.680	-0.850	15.819	-0.429	-0.429	0.000	0.000	0.000	0.000
97	A	93	ALA	0	-0.055	-0.030	18.573	-0.039	-0.039	0.000	0.000	0.000	0.000
98	A	94	ASP	-1	-0.921	-0.962	15.397	-0.612	-0.612	0.000	0.000	0.000	0.000
99	A	95	GLU	-1	-0.834	-0.911	15.973	-0.621	-0.621	0.000	0.000	0.000	0.000
100	A	96	ALA	0	0.057	0.050	11.208	-0.069	-0.069	0.000	0.000	0.000	0.000
101	A	97	LEU	0	-0.008	-0.021	11.947	-0.026	-0.026	0.000	0.000	0.000	0.000
102	A	98	CYS	0	-0.102	-0.076	13.683	0.061	0.061	0.000	0.000	0.000	0.000
103	A	99	ALA	0	-0.013	-0.001	12.439	0.025	0.025	0.000	0.000	0.000	0.000
104	A	100	LEU	0	-0.014	0.008	8.152	-0.050	-0.050	0.000	0.000	0.000	0.000
105	A	101	PHE	0	-0.008	-0.024	11.315	0.121	0.121	0.000	0.000	0.000	0.000
106	A	102	ASP	-1	-0.896	-0.930	14.477	-0.436	-0.436	0.000	0.000	0.000	0.000
107	A	103	VAL	0	-0.009	0.001	16.152	0.056	0.056	0.000	0.000	0.000	0.000
108	A	104	ILE	0	-0.035	-0.011	18.261	0.039	0.039	0.000	0.000	0.000	0.000
109	A	105	LYS	1	0.959	0.977	20.590	0.217	0.217	0.000	0.000	0.000	0.000
110	A	106	MET	0	-0.018	-0.001	23.814	0.005	0.005	0.000	0.000	0.000	0.000
111	A	107	LYS	1	0.901	0.950	26.119	0.236	0.236	0.000	0.000	0.000	0.000
112	A	108	LYS	1	0.954	0.982	29.810	0.238	0.238	0.000	0.000	0.000	0.000
113	A	109	MET	0	-0.021	-0.014	32.233	0.016	0.016	0.000	0.000	0.000	0.000
114	A	110	TYR	0	0.041	0.013	35.525	-0.005	-0.005	0.000	0.000	0.000	0.000
115	A	111	GLY	0	0.024	0.018	36.390	0.000	0.000	0.000	0.000	0.000	0.000
116	A	112	LYS	1	0.925	0.973	30.384	0.244	0.244	0.000	0.000	0.000	0.000
117	A	113	GLU	-1	-0.882	-0.941	27.931	-0.300	-0.300	0.000	0.000	0.000	0.000
118	A	114	VAL	0	-0.052	-0.041	28.836	-0.012	-0.012	0.000	0.000	0.000	0.000
119	A	115	ARG	1	0.949	0.961	18.573	0.577	0.577	0.000	0.000	0.000	0.000
120	A	116	GLY	0	-0.049	-0.030	25.322	0.015	0.015	0.000	0.000	0.000	0.000
121	A	117	ILE	0	0.062	0.049	21.408	-0.030	-0.030	0.000	0.000	0.000	0.000
122	A	118	GLU	-1	-0.987	-0.987	22.974	-0.159	-0.159	0.000	0.000	0.000	0.000
123	A	119	ARG	1	0.864	0.913	23.407	0.078	0.078	0.000	0.000	0.000	0.000
124	A	120	SER	0	0.023	0.008	21.445	0.000	0.000	0.000	0.000	0.000	0.000
125	A	121	THR	0	-0.058	-0.010	22.175	-0.002	-0.002	0.000	0.000	0.000	0.000
126	A	122	PHE	0	0.037	0.032	17.697	-0.008	-0.008	0.000	0.000	0.000	0.000
127	A	123	LEU	0	-0.002	0.015	19.829	0.003	0.003	0.000	0.000	0.000	0.000
128	A	124	ILE	0	0.020	0.011	14.698	0.009	0.009	0.000	0.000	0.000	0.000
129	A	125	ASP	-1	-0.765	-0.888	17.278	0.477	0.477	0.000	0.000	0.000	0.000
130	A	126	ALA	0	0.006	0.006	17.709	0.042	0.042	0.000	0.000	0.000	0.000
131	A	127	ASP	-1	-0.900	-0.939	15.903	0.577	0.577	0.000	0.000	0.000	0.000
132	A	128	GLY	0	-0.040	-0.020	13.335	0.156	0.156	0.000	0.000	0.000	0.000
133	A	129	VAL	0	0.002	0.002	12.614	0.128	0.128	0.000	0.000	0.000	0.000
134	A	130	LEU	0	-0.029	-0.009	13.791	-0.104	-0.104	0.000	0.000	0.000	0.000
135	A	131	ARG	1	0.856	0.922	15.638	-0.357	-0.357	0.000	0.000	0.000	0.000
136	A	132	GLN	0	0.027	0.010	19.093	-0.017	-0.017	0.000	0.000	0.000	0.000
137	A	133	ALA	0	0.009	0.009	19.179	0.010	0.010	0.000	0.000	0.000	0.000
138	A	134	TRP	0	0.000	0.000	21.152	-0.007	-0.007	0.000	0.000	0.000	0.000
139	A	135	ARG	1	0.925	0.945	16.552	0.160	0.160	0.000	0.000	0.000	0.000
140	A	136	GLY	0	0.028	0.016	24.074	0.001	0.001	0.000	0.000	0.000	0.000
141	A	137	ILE	0	-0.033	0.006	26.680	0.005	0.005	0.000	0.000	0.000	0.000
142	A	138	LYS	1	0.922	0.952	29.143	0.017	0.017	0.000	0.000	0.000	0.000
143	A	139	VAL	0	0.020	-0.001	31.311	0.006	0.006	0.000	0.000	0.000	0.000
144	A	140	PRO	0	-0.043	-0.040	32.960	0.008	0.008	0.000	0.000	0.000	0.000
145	A	141	GLY	0	0.077	0.038	35.043	-0.003	-0.003	0.000	0.000	0.000	0.000
146	A	142	HIS	0	0.023	0.016	26.258	0.008	0.008	0.000	0.000	0.000	0.000
147	A	143	VAL	0	0.002	-0.007	30.243	0.011	0.011	0.000	0.000	0.000	0.000
148	A	144	ASP	-1	-0.887	-0.940	31.233	0.045	0.045	0.000	0.000	0.000	0.000
149	A	145	ASP	-1	-0.917	-0.955	30.321	0.042	0.042	0.000	0.000	0.000	0.000
150	A	146	VAL	0	-0.053	-0.030	25.609	0.016	0.016	0.000	0.000	0.000	0.000
151	A	147	LEU	0	-0.032	-0.015	27.946	0.020	0.020	0.000	0.000	0.000	0.000
152	A	148	SER	0	-0.002	-0.007	30.313	0.012	0.012	0.000	0.000	0.000	0.000
153	A	149	ALA	0	-0.003	0.002	26.028	0.011	0.011	0.000	0.000	0.000	0.000
154	A	150	VAL	0	-0.022	-0.022	25.114	0.021	0.021	0.000	0.000	0.000	0.000
155	A	151	GLN	0	-0.063	-0.050	27.049	0.013	0.013	0.000	0.000	0.000	0.000
156	A	152	ALA	0	-0.008	0.018	28.872	0.003	0.003	0.000	0.000	0.000	0.000
157	A	153	LEU	0	-0.067	-0.018	22.446	0.012	0.012	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:-3:HIS)