FMO DATABASE

FMODB ID: QV56Y

Calculation Name: 5HU4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HU4

Chain ID: A

ChEMBL ID:

UniProt ID: Q8Y8H5

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:

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	145
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1363573.392202
FMO2-HF: Nuclear repulsion	1306616.46666
FMO2-HF: Total energy	-56956.925542
FMO2-MP2: Total energy	-57121.363945

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:7:ASP)

Summations of interaction energy for fragment #1(A:7:ASP)

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.
-16.676	-10.746	1.226	-3.122	-4.035	0.018

Interaction energy analysis for fragmet #1(A:7:ASP)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : -1 / q_Mulliken : -0.871 / q_NPA : -0.961

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	9	VAL	0	-0.010	-0.003	2.277	-14.971	-9.910	1.212	-2.708	-3.565	0.015
4	A	10	VAL	0	-0.056	-0.039	4.068	-4.175	-4.172	-0.001	-0.012	0.010	0.000
5	A	11	GLY	0	0.035	0.019	7.096	-3.137	-3.137	0.000	0.000	0.000	0.000
6	A	12	SER	0	-0.011	0.008	8.904	3.902	3.902	0.000	0.000	0.000	0.000
7	A	13	ILE	0	-0.012	-0.014	11.593	-1.771	-1.771	0.000	0.000	0.000	0.000
8	A	14	ALA	0	0.020	0.009	14.955	0.575	0.575	0.000	0.000	0.000	0.000
9	A	15	VAL	0	-0.035	-0.022	17.772	-0.835	-0.835	0.000	0.000	0.000	0.000
10	A	16	PRO	0	0.040	0.021	21.177	-0.146	-0.146	0.000	0.000	0.000	0.000
11	A	17	SER	0	-0.085	-0.043	22.902	-0.151	-0.151	0.000	0.000	0.000	0.000
12	A	18	VAL	0	-0.047	-0.031	22.451	-0.468	-0.468	0.000	0.000	0.000	0.000
13	A	19	ASP	-1	-0.936	-0.966	21.656	15.009	15.009	0.000	0.000	0.000	0.000
14	A	20	VAL	0	-0.017	0.006	17.224	0.673	0.673	0.000	0.000	0.000	0.000
15	A	21	ASN	0	0.007	-0.008	14.619	0.374	0.374	0.000	0.000	0.000	0.000
16	A	22	LEU	0	-0.029	0.001	12.141	0.979	0.979	0.000	0.000	0.000	0.000
17	A	23	LEU	0	0.053	0.027	5.414	-0.507	-0.507	0.000	0.000	0.000	0.000
18	A	24	VAL	0	-0.034	-0.020	8.840	-1.754	-1.754	0.000	0.000	0.000	0.000
19	A	25	PHE	0	0.032	0.007	3.495	1.343	2.209	0.015	-0.402	-0.480	0.003
20	A	26	LYS	1	0.967	0.976	7.407	-30.033	-30.033	0.000	0.000	0.000	0.000
21	A	27	GLY	0	-0.011	-0.006	9.379	1.137	1.137	0.000	0.000	0.000	0.000
22	A	28	THR	0	0.021	0.002	10.950	1.770	1.770	0.000	0.000	0.000	0.000
23	A	29	ASN	0	0.009	-0.001	9.603	-0.893	-0.893	0.000	0.000	0.000	0.000
24	A	30	THR	0	0.015	-0.014	12.727	1.204	1.204	0.000	0.000	0.000	0.000
25	A	31	ALA	0	0.005	0.015	9.492	-0.430	-0.430	0.000	0.000	0.000	0.000
26	A	32	ASN	0	-0.004	-0.006	6.985	4.997	4.997	0.000	0.000	0.000	0.000
27	A	33	LEU	0	-0.026	0.002	9.450	-0.390	-0.390	0.000	0.000	0.000	0.000
28	A	34	LEU	0	-0.010	-0.036	11.933	-1.235	-1.235	0.000	0.000	0.000	0.000
29	A	35	ALA	0	-0.003	0.021	7.036	-0.139	-0.139	0.000	0.000	0.000	0.000
30	A	36	GLY	0	0.009	-0.011	9.177	0.980	0.980	0.000	0.000	0.000	0.000
31	A	37	ALA	0	-0.025	0.014	10.712	-1.789	-1.789	0.000	0.000	0.000	0.000
32	A	38	THR	0	0.005	-0.007	10.009	2.725	2.725	0.000	0.000	0.000	0.000
33	A	39	THR	0	0.007	0.021	11.568	-1.433	-1.433	0.000	0.000	0.000	0.000
34	A	40	MET	0	-0.046	-0.006	13.917	0.114	0.114	0.000	0.000	0.000	0.000
35	A	41	ARG	1	0.774	0.877	16.915	-15.207	-15.207	0.000	0.000	0.000	0.000
36	A	42	SER	0	-0.053	-0.031	15.305	0.736	0.736	0.000	0.000	0.000	0.000
37	A	43	ASP	-1	-0.820	-0.899	15.761	15.173	15.173	0.000	0.000	0.000	0.000
38	A	44	GLN	0	-0.003	0.012	15.677	-0.582	-0.582	0.000	0.000	0.000	0.000
39	A	45	VAL	0	0.006	-0.009	15.991	0.891	0.891	0.000	0.000	0.000	0.000
40	A	46	MET	0	-0.002	0.017	11.829	-0.825	-0.825	0.000	0.000	0.000	0.000
41	A	47	GLY	0	0.046	0.021	17.115	-0.455	-0.455	0.000	0.000	0.000	0.000
42	A	48	LYS	1	0.871	0.931	20.399	-14.597	-14.597	0.000	0.000	0.000	0.000
43	A	49	GLY	0	0.009	0.027	21.477	0.398	0.398	0.000	0.000	0.000	0.000
44	A	50	ASN	0	0.019	0.040	22.842	0.309	0.309	0.000	0.000	0.000	0.000
45	A	51	TYR	0	0.015	-0.001	12.521	0.517	0.517	0.000	0.000	0.000	0.000
46	A	52	PRO	0	0.001	0.003	18.814	0.195	0.195	0.000	0.000	0.000	0.000
47	A	53	LEU	0	-0.018	-0.016	13.793	1.235	1.235	0.000	0.000	0.000	0.000
48	A	54	ALA	0	0.048	0.016	15.587	-1.214	-1.214	0.000	0.000	0.000	0.000
49	A	55	GLY	0	0.069	0.027	14.732	1.773	1.773	0.000	0.000	0.000	0.000
50	A	56	HIS	0	0.031	0.023	15.697	-1.144	-1.144	0.000	0.000	0.000	0.000
51	A	57	HIS	1	0.797	0.878	17.667	-13.239	-13.239	0.000	0.000	0.000	0.000
52	A	58	MET	0	0.043	0.026	17.480	-0.186	-0.186	0.000	0.000	0.000	0.000
53	A	59	ARG	1	0.932	0.948	21.020	-12.194	-12.194	0.000	0.000	0.000	0.000
54	A	60	ASP	-1	-0.811	-0.886	21.227	14.186	14.186	0.000	0.000	0.000	0.000
55	A	61	GLU	-1	-0.841	-0.919	21.752	13.217	13.217	0.000	0.000	0.000	0.000
56	A	62	SER	0	-0.076	-0.051	21.798	0.217	0.217	0.000	0.000	0.000	0.000
57	A	63	MET	0	0.007	0.012	16.134	0.841	0.841	0.000	0.000	0.000	0.000
58	A	64	LEU	0	0.002	-0.001	13.014	-0.689	-0.689	0.000	0.000	0.000	0.000
59	A	65	PHE	0	0.025	0.004	16.350	-0.310	-0.310	0.000	0.000	0.000	0.000
60	A	66	GLY	0	0.005	0.017	18.860	-0.839	-0.839	0.000	0.000	0.000	0.000
61	A	67	PRO	0	-0.008	-0.010	20.465	-0.977	-0.977	0.000	0.000	0.000	0.000
62	A	68	ILE	0	-0.001	0.002	20.619	-0.622	-0.622	0.000	0.000	0.000	0.000
63	A	69	MET	0	-0.015	0.002	23.630	-0.419	-0.419	0.000	0.000	0.000	0.000
64	A	70	LYS	1	0.860	0.955	25.307	-13.001	-13.001	0.000	0.000	0.000	0.000
65	A	71	VAL	0	0.007	0.026	24.699	-0.187	-0.187	0.000	0.000	0.000	0.000
66	A	72	LYS	1	0.915	0.968	27.635	-10.412	-10.412	0.000	0.000	0.000	0.000
67	A	73	LYS	1	0.868	0.976	29.855	-9.602	-9.602	0.000	0.000	0.000	0.000
68	A	74	GLY	0	0.013	-0.021	30.719	-0.347	-0.347	0.000	0.000	0.000	0.000
69	A	75	ASP	-1	-0.837	-0.942	26.906	11.118	11.118	0.000	0.000	0.000	0.000
70	A	76	LYS	1	0.892	0.956	25.077	-10.789	-10.789	0.000	0.000	0.000	0.000
71	A	77	ILE	0	-0.020	-0.012	19.830	0.313	0.313	0.000	0.000	0.000	0.000
72	A	78	TYR	0	-0.003	0.002	19.222	-0.363	-0.363	0.000	0.000	0.000	0.000
73	A	79	LEU	0	0.024	0.004	14.193	0.928	0.928	0.000	0.000	0.000	0.000
74	A	80	THR	0	-0.008	-0.001	12.624	-0.833	-0.833	0.000	0.000	0.000	0.000
75	A	81	ASP	-1	-0.724	-0.892	11.209	20.516	20.516	0.000	0.000	0.000	0.000
76	A	82	LEU	0	-0.056	-0.038	9.336	0.952	0.952	0.000	0.000	0.000	0.000
77	A	83	GLU	-1	-0.961	-0.946	12.712	17.714	17.714	0.000	0.000	0.000	0.000
78	A	84	ASN	0	-0.084	-0.055	15.553	-1.738	-1.738	0.000	0.000	0.000	0.000
79	A	85	LEU	0	-0.032	-0.010	16.657	1.153	1.153	0.000	0.000	0.000	0.000
80	A	86	TYR	0	-0.052	-0.043	16.051	-1.390	-1.390	0.000	0.000	0.000	0.000
81	A	87	GLU	-1	-0.839	-0.926	20.169	12.466	12.466	0.000	0.000	0.000	0.000
82	A	88	TYR	0	-0.009	-0.010	19.535	-0.257	-0.257	0.000	0.000	0.000	0.000
83	A	89	THR	0	-0.002	-0.012	24.261	0.068	0.068	0.000	0.000	0.000	0.000
84	A	90	VAL	0	-0.060	-0.026	25.960	-0.219	-0.219	0.000	0.000	0.000	0.000
85	A	91	THR	0	-0.021	-0.033	27.998	-0.476	-0.476	0.000	0.000	0.000	0.000
86	A	92	GLU	-1	-0.881	-0.948	29.552	9.907	9.907	0.000	0.000	0.000	0.000
87	A	93	THR	0	-0.003	0.011	28.426	0.338	0.338	0.000	0.000	0.000	0.000
88	A	94	LYS	1	0.847	0.931	29.166	-11.099	-11.099	0.000	0.000	0.000	0.000
89	A	95	THR	0	0.028	0.014	29.110	0.494	0.494	0.000	0.000	0.000	0.000
90	A	96	ILE	0	-0.025	-0.008	26.910	-0.413	-0.413	0.000	0.000	0.000	0.000
91	A	97	ASP	-1	-0.794	-0.875	29.596	10.365	10.365	0.000	0.000	0.000	0.000
92	A	98	GLU	-1	-0.891	-0.963	26.052	12.077	12.077	0.000	0.000	0.000	0.000
93	A	99	THR	0	-0.066	-0.074	26.911	0.231	0.231	0.000	0.000	0.000	0.000
94	A	100	GLU	-1	-0.968	-0.976	29.507	9.769	9.769	0.000	0.000	0.000	0.000
95	A	101	VAL	0	0.003	-0.010	24.617	0.356	0.356	0.000	0.000	0.000	0.000
96	A	102	SER	0	0.041	0.026	26.167	0.452	0.452	0.000	0.000	0.000	0.000
97	A	103	VAL	0	-0.048	-0.012	24.630	0.057	0.057	0.000	0.000	0.000	0.000
98	A	104	ILE	0	0.006	-0.014	21.179	0.544	0.544	0.000	0.000	0.000	0.000
99	A	105	ASP	-1	-0.866	-0.925	23.001	12.161	12.161	0.000	0.000	0.000	0.000
100	A	106	ASN	0	-0.022	-0.019	23.352	0.504	0.504	0.000	0.000	0.000	0.000
101	A	107	THR	0	0.014	0.006	24.977	-0.305	-0.305	0.000	0.000	0.000	0.000
102	A	108	LYS	1	0.901	0.938	26.961	-10.155	-10.155	0.000	0.000	0.000	0.000
103	A	109	ASP	-1	-0.799	-0.865	28.754	10.841	10.841	0.000	0.000	0.000	0.000
104	A	110	ALA	0	0.022	0.011	24.391	0.299	0.299	0.000	0.000	0.000	0.000
105	A	111	ARG	1	0.857	0.914	24.094	-11.494	-11.494	0.000	0.000	0.000	0.000
106	A	112	ILE	0	0.002	0.016	17.970	0.543	0.543	0.000	0.000	0.000	0.000
107	A	113	THR	0	-0.021	-0.047	20.842	-0.878	-0.878	0.000	0.000	0.000	0.000
108	A	114	LEU	0	-0.024	0.000	18.668	0.825	0.825	0.000	0.000	0.000	0.000
109	A	115	ILE	0	0.033	0.006	19.778	-0.903	-0.903	0.000	0.000	0.000	0.000
110	A	116	THR	0	0.017	-0.007	19.600	0.786	0.786	0.000	0.000	0.000	0.000
111	A	117	CYS	0	-0.005	0.006	21.532	-0.597	-0.597	0.000	0.000	0.000	0.000
112	A	118	ASP	-1	-0.768	-0.895	23.934	11.194	11.194	0.000	0.000	0.000	0.000
113	A	119	LYS	1	0.865	0.930	26.456	-10.663	-10.663	0.000	0.000	0.000	0.000
114	A	120	PRO	0	-0.008	0.016	23.994	0.309	0.309	0.000	0.000	0.000	0.000
115	A	121	THR	0	-0.046	-0.023	24.566	0.190	0.190	0.000	0.000	0.000	0.000
116	A	122	GLU	-1	-0.890	-0.960	24.946	12.820	12.820	0.000	0.000	0.000	0.000
117	A	123	THR	0	-0.086	-0.043	26.322	-0.626	-0.626	0.000	0.000	0.000	0.000
118	A	124	THR	0	0.084	0.067	27.079	0.343	0.343	0.000	0.000	0.000	0.000
119	A	125	LYS	1	0.855	0.946	29.005	-9.773	-9.773	0.000	0.000	0.000	0.000
120	A	126	ARG	1	0.857	0.911	23.148	-12.477	-12.477	0.000	0.000	0.000	0.000
121	A	127	PHE	0	0.012	0.007	25.167	-0.582	-0.582	0.000	0.000	0.000	0.000
122	A	128	VAL	0	-0.012	-0.017	24.564	0.583	0.583	0.000	0.000	0.000	0.000
123	A	129	ALA	0	0.006	0.002	24.169	-0.597	-0.597	0.000	0.000	0.000	0.000
124	A	130	VAL	0	0.027	0.019	24.341	0.601	0.601	0.000	0.000	0.000	0.000
125	A	131	GLY	0	0.019	0.006	24.939	-0.454	-0.454	0.000	0.000	0.000	0.000
126	A	132	GLH	0	-0.058	-0.035	25.102	0.311	0.311	0.000	0.000	0.000	0.000
127	A	133	LEU	0	-0.025	-0.013	22.514	0.105	0.105	0.000	0.000	0.000	0.000
128	A	134	GLU	-1	-0.895	-0.941	25.733	10.313	10.313	0.000	0.000	0.000	0.000
129	A	135	LYS	1	0.901	0.952	25.493	-11.479	-11.479	0.000	0.000	0.000	0.000
130	A	136	THR	0	-0.007	-0.013	21.348	0.678	0.678	0.000	0.000	0.000	0.000
131	A	137	GLU	-1	-0.933	-0.956	22.217	11.654	11.654	0.000	0.000	0.000	0.000
132	A	138	LYS	1	1.006	1.005	20.270	-13.322	-13.322	0.000	0.000	0.000	0.000
133	A	139	LEU	0	0.008	0.027	14.924	-0.493	-0.493	0.000	0.000	0.000	0.000
134	A	140	THR	0	-0.011	-0.013	18.857	0.177	0.177	0.000	0.000	0.000	0.000
135	A	141	LYS	1	1.009	0.981	18.816	-14.880	-14.880	0.000	0.000	0.000	0.000
136	A	142	GLU	-1	-0.918	-0.958	19.864	12.455	12.455	0.000	0.000	0.000	0.000
137	A	143	LEU	0	0.011	0.007	20.653	0.142	0.142	0.000	0.000	0.000	0.000
138	A	144	GLU	-1	-0.940	-0.970	13.576	21.282	21.282	0.000	0.000	0.000	0.000
139	A	145	ASN	0	-0.030	-0.027	17.237	0.534	0.534	0.000	0.000	0.000	0.000
140	A	146	LYS	1	0.893	0.971	18.879	-12.713	-12.713	0.000	0.000	0.000	0.000
141	A	147	TYR	0	-0.040	-0.031	19.464	-0.509	-0.509	0.000	0.000	0.000	0.000
142	A	148	PHE	0	-0.042	-0.012	14.207	0.249	0.249	0.000	0.000	0.000	0.000
143	A	149	PRO	0	0.024	0.039	15.244	0.895	0.895	0.000	0.000	0.000	0.000
144	A	150	SER	0	-0.015	-0.039	14.042	1.404	1.404	0.000	0.000	0.000	0.000
145	A	151	LYS	1	0.985	1.012	12.991	-22.380	-22.380	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:ASP)