FMO DATABASE

FMODB ID: R8N18

Calculation Name: 1U5G-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1U5G

Chain ID: A

ChEMBL ID:

UniProt ID: Q3UND0

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	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	115
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1021596.882848
FMO2-HF: Nuclear repulsion	973832.179012
FMO2-HF: Total energy	-47764.703836
FMO2-MP2: Total energy	-47903.578963

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:105:GLN)

Summations of interaction energy for fragment #1(A:105:GLN)

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.
-3.29	2.084	4.847	-4.251	-5.969	-0.009

Interaction energy analysis for fragmet #1(A:105:GLN)

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 : -0.030

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	107	PRO	0	-0.010	0.008	3.775	-1.569	0.333	0.007	-0.822	-1.088	-0.002
4	A	108	PRO	0	-0.041	-0.021	6.688	-0.513	-0.513	0.000	0.000	0.000	0.000
5	A	109	ILE	0	0.049	0.043	6.551	0.350	0.350	0.000	0.000	0.000	0.000
6	A	110	ALA	0	0.008	0.012	9.620	-0.203	-0.203	0.000	0.000	0.000	0.000
7	A	111	ALA	0	-0.010	-0.002	11.813	-0.013	-0.013	0.000	0.000	0.000	0.000
8	A	112	GLN	0	-0.012	-0.030	13.124	-0.022	-0.022	0.000	0.000	0.000	0.000
9	A	113	ASP	-1	-0.922	-0.955	12.677	-0.080	-0.080	0.000	0.000	0.000	0.000
10	A	114	LEU	0	-0.051	0.002	7.574	0.064	0.064	0.000	0.000	0.000	0.000
11	A	115	PRO	0	0.012	0.007	8.502	0.118	0.118	0.000	0.000	0.000	0.000
12	A	116	PHE	0	-0.046	-0.021	10.469	-0.087	-0.087	0.000	0.000	0.000	0.000
13	A	117	VAL	0	0.011	0.011	12.186	-0.038	-0.038	0.000	0.000	0.000	0.000
14	A	118	ILE	0	0.022	0.031	12.594	0.045	0.045	0.000	0.000	0.000	0.000
15	A	119	LYS	1	0.896	0.947	13.963	0.413	0.413	0.000	0.000	0.000	0.000
16	A	120	ALA	0	0.038	0.016	14.101	-0.105	-0.105	0.000	0.000	0.000	0.000
17	A	121	GLY	0	-0.001	0.010	15.931	0.085	0.085	0.000	0.000	0.000	0.000
18	A	122	TYR	0	-0.044	-0.018	16.922	-0.092	-0.092	0.000	0.000	0.000	0.000
19	A	123	LEU	0	0.015	0.020	15.330	0.033	0.033	0.000	0.000	0.000	0.000
20	A	124	GLU	-1	-0.942	-0.986	18.362	-0.533	-0.533	0.000	0.000	0.000	0.000
21	A	125	LYS	1	0.933	0.979	12.737	1.398	1.398	0.000	0.000	0.000	0.000
22	A	126	ARG	1	0.856	0.933	17.037	0.733	0.733	0.000	0.000	0.000	0.000
23	A	127	ARG	1	0.895	0.941	16.513	0.623	0.623	0.000	0.000	0.000	0.000
24	A	128	LYS	1	0.935	0.965	12.379	1.488	1.488	0.000	0.000	0.000	0.000
25	A	129	ASP	-1	-0.912	-0.962	16.454	-0.770	-0.770	0.000	0.000	0.000	0.000
26	A	130	HIS	0	0.073	0.022	19.842	-0.025	-0.025	0.000	0.000	0.000	0.000
27	A	131	SER	0	-0.002	0.011	23.684	0.054	0.054	0.000	0.000	0.000	0.000
28	A	132	PHE	0	-0.039	-0.017	22.007	-0.017	-0.017	0.000	0.000	0.000	0.000
29	A	133	LEU	0	0.028	0.002	24.958	0.011	0.011	0.000	0.000	0.000	0.000
30	A	134	GLY	0	0.004	0.016	27.040	-0.011	-0.011	0.000	0.000	0.000	0.000
31	A	135	PHE	0	-0.055	-0.037	22.229	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	136	GLU	-1	-0.835	-0.901	21.948	-0.647	-0.647	0.000	0.000	0.000	0.000
33	A	137	TRP	0	0.027	0.018	19.556	-0.089	-0.089	0.000	0.000	0.000	0.000
34	A	138	GLN	0	-0.038	-0.031	18.229	-0.024	-0.024	0.000	0.000	0.000	0.000
35	A	139	LYS	1	0.978	0.998	18.542	0.422	0.422	0.000	0.000	0.000	0.000
36	A	140	ARG	1	0.899	0.942	14.241	0.885	0.885	0.000	0.000	0.000	0.000
37	A	141	TRP	0	0.063	0.049	12.859	0.017	0.017	0.000	0.000	0.000	0.000
38	A	142	CYS	0	-0.031	-0.005	12.259	-0.194	-0.194	0.000	0.000	0.000	0.000
39	A	143	ALA	0	0.043	0.006	10.888	0.171	0.171	0.000	0.000	0.000	0.000
40	A	144	LEU	0	-0.005	0.008	8.915	-0.296	-0.296	0.000	0.000	0.000	0.000
41	A	145	SER	0	-0.042	-0.034	6.661	0.255	0.255	0.000	0.000	0.000	0.000
42	A	146	LYS	1	1.004	0.985	7.238	-0.782	-0.782	0.000	0.000	0.000	0.000
43	A	147	THR	0	0.047	0.032	6.575	-0.087	-0.087	0.000	0.000	0.000	0.000
44	A	148	VAL	0	0.019	0.013	2.553	-1.587	-0.459	0.834	-0.606	-1.355	0.003
45	A	149	PHE	0	-0.006	0.012	5.301	0.444	0.488	-0.001	-0.004	-0.038	0.000
46	A	150	TYR	0	0.070	0.012	3.601	-1.009	-0.532	0.005	-0.200	-0.282	-0.001
47	A	151	TYR	0	-0.026	-0.020	7.729	0.595	0.595	0.000	0.000	0.000	0.000
48	A	152	TYR	0	0.002	-0.008	9.829	-0.159	-0.159	0.000	0.000	0.000	0.000
49	A	153	GLY	0	-0.067	-0.029	12.988	0.041	0.041	0.000	0.000	0.000	0.000
50	A	154	SER	0	-0.010	0.002	16.517	0.065	0.065	0.000	0.000	0.000	0.000
51	A	155	ASP	-1	-0.889	-0.958	16.269	-0.460	-0.460	0.000	0.000	0.000	0.000
52	A	156	LYS	1	0.902	0.952	17.352	0.309	0.309	0.000	0.000	0.000	0.000
53	A	157	ASP	-1	-0.866	-0.940	14.882	-0.610	-0.610	0.000	0.000	0.000	0.000
54	A	158	LYS	1	0.958	0.962	15.145	0.280	0.280	0.000	0.000	0.000	0.000
55	A	159	GLN	0	0.034	0.010	11.408	0.136	0.136	0.000	0.000	0.000	0.000
56	A	160	GLN	0	-0.019	0.016	5.515	0.837	0.837	0.000	0.000	0.000	0.000
57	A	161	LYS	1	0.862	0.906	9.815	0.961	0.961	0.000	0.000	0.000	0.000
58	A	162	GLY	0	0.019	0.011	7.103	0.024	0.024	0.000	0.000	0.000	0.000
59	A	163	GLU	-1	-0.915	-0.958	2.112	-5.793	-5.561	3.801	-2.168	-1.865	-0.008
60	A	164	PHE	0	-0.059	-0.025	3.121	-1.313	-0.815	0.048	-0.150	-0.396	0.000
61	A	165	ALA	0	0.048	0.033	2.810	-0.100	0.912	0.153	-0.282	-0.883	-0.001
62	A	166	ILE	0	-0.020	-0.032	4.280	-0.436	-0.355	0.000	-0.019	-0.062	0.000
63	A	167	ASP	-1	-0.839	-0.918	6.424	1.432	1.432	0.000	0.000	0.000	0.000
64	A	168	GLY	0	-0.017	-0.014	8.370	-0.523	-0.523	0.000	0.000	0.000	0.000
65	A	169	TYR	0	-0.143	-0.064	6.601	-0.380	-0.380	0.000	0.000	0.000	0.000
66	A	170	ASP	-1	-0.799	-0.899	11.750	-0.326	-0.326	0.000	0.000	0.000	0.000
67	A	171	VAL	0	-0.082	-0.053	14.541	-0.174	-0.174	0.000	0.000	0.000	0.000
68	A	172	ARG	1	0.844	0.926	16.964	0.693	0.693	0.000	0.000	0.000	0.000
69	A	173	MET	0	0.070	0.036	20.127	-0.080	-0.080	0.000	0.000	0.000	0.000
70	A	174	ASN	0	-0.011	-0.008	21.124	0.051	0.051	0.000	0.000	0.000	0.000
71	A	175	ASN	0	0.005	0.013	23.610	-0.028	-0.028	0.000	0.000	0.000	0.000
72	A	176	THR	0	0.000	-0.025	24.692	0.017	0.017	0.000	0.000	0.000	0.000
73	A	177	LEU	0	-0.094	-0.045	20.117	-0.006	-0.006	0.000	0.000	0.000	0.000
74	A	178	ARG	1	0.859	0.911	24.223	0.464	0.464	0.000	0.000	0.000	0.000
75	A	179	LYS	1	0.961	0.956	27.012	0.355	0.355	0.000	0.000	0.000	0.000
76	A	180	ASP	-1	-0.805	-0.868	29.089	-0.378	-0.378	0.000	0.000	0.000	0.000
77	A	181	GLY	0	0.027	-0.008	31.292	-0.004	-0.004	0.000	0.000	0.000	0.000
78	A	182	LYS	1	0.947	0.975	25.825	0.437	0.437	0.000	0.000	0.000	0.000
79	A	183	LYS	1	0.953	1.004	26.942	0.292	0.292	0.000	0.000	0.000	0.000
80	A	184	ASP	-1	-0.924	-0.970	26.707	-0.341	-0.341	0.000	0.000	0.000	0.000
81	A	185	CYS	0	-0.034	-0.002	24.918	0.009	0.009	0.000	0.000	0.000	0.000
82	A	186	CYS	0	-0.066	-0.016	22.408	-0.029	-0.029	0.000	0.000	0.000	0.000
83	A	187	PHE	0	0.033	0.010	16.080	0.031	0.031	0.000	0.000	0.000	0.000
84	A	188	GLU	-1	-0.794	-0.883	16.602	-0.823	-0.823	0.000	0.000	0.000	0.000
85	A	189	ILE	0	-0.002	0.014	11.219	0.069	0.069	0.000	0.000	0.000	0.000
86	A	190	CYS	0	-0.070	-0.054	13.000	-0.158	-0.158	0.000	0.000	0.000	0.000
87	A	191	ALA	0	0.103	0.042	11.345	0.065	0.065	0.000	0.000	0.000	0.000
88	A	192	PRO	0	-0.022	-0.009	13.436	-0.098	-0.098	0.000	0.000	0.000	0.000
89	A	193	ASP	-1	-0.862	-0.922	11.479	-1.206	-1.206	0.000	0.000	0.000	0.000
90	A	194	LYS	1	0.844	0.936	7.061	1.716	1.716	0.000	0.000	0.000	0.000
91	A	195	ARG	1	0.897	0.957	8.667	2.603	2.603	0.000	0.000	0.000	0.000
92	A	196	ILE	0	0.042	0.046	10.143	-0.216	-0.216	0.000	0.000	0.000	0.000
93	A	197	TYR	0	-0.039	-0.016	6.908	0.182	0.182	0.000	0.000	0.000	0.000
94	A	198	GLN	0	0.041	-0.004	13.074	0.146	0.146	0.000	0.000	0.000	0.000
95	A	199	PHE	0	0.034	-0.002	12.336	-0.039	-0.039	0.000	0.000	0.000	0.000
96	A	200	THR	0	-0.037	-0.009	18.338	0.075	0.075	0.000	0.000	0.000	0.000
97	A	201	ALA	0	-0.002	0.005	21.145	-0.027	-0.027	0.000	0.000	0.000	0.000
98	A	202	ALA	0	-0.065	-0.033	22.324	0.021	0.021	0.000	0.000	0.000	0.000
99	A	203	SER	0	0.024	-0.002	25.329	0.034	0.034	0.000	0.000	0.000	0.000
100	A	204	PRO	0	0.111	0.040	25.919	-0.026	-0.026	0.000	0.000	0.000	0.000
101	A	205	LYS	1	1.006	1.017	26.423	0.212	0.212	0.000	0.000	0.000	0.000
102	A	206	ASP	-1	-0.864	-0.953	22.289	-0.450	-0.450	0.000	0.000	0.000	0.000
103	A	207	ALA	0	0.001	0.007	21.653	-0.032	-0.032	0.000	0.000	0.000	0.000
104	A	208	GLU	-1	-0.875	-0.960	21.655	-0.374	-0.374	0.000	0.000	0.000	0.000
105	A	209	GLU	-1	-0.958	-0.966	21.778	-0.272	-0.272	0.000	0.000	0.000	0.000
106	A	210	TRP	0	-0.013	-0.024	13.953	-0.025	-0.025	0.000	0.000	0.000	0.000
107	A	211	VAL	0	-0.032	-0.001	17.513	-0.038	-0.038	0.000	0.000	0.000	0.000
108	A	212	GLN	0	0.013	0.006	18.878	0.005	0.005	0.000	0.000	0.000	0.000
109	A	213	GLN	0	-0.025	-0.027	16.056	0.055	0.055	0.000	0.000	0.000	0.000
110	A	214	LEU	0	-0.015	-0.026	12.472	0.004	0.004	0.000	0.000	0.000	0.000
111	A	215	LYS	1	0.989	0.986	15.037	0.365	0.365	0.000	0.000	0.000	0.000
112	A	216	PHE	0	-0.085	-0.015	17.778	0.060	0.060	0.000	0.000	0.000	0.000
113	A	217	ILE	0	0.004	-0.011	11.947	0.059	0.059	0.000	0.000	0.000	0.000
114	A	218	LEU	0	-0.062	-0.020	12.002	0.062	0.062	0.000	0.000	0.000	0.000
115	A	219	GLN	0	-0.046	0.007	15.071	0.058	0.058	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:105:GLN)