FMO DATABASE

FMODB ID: 49J3N

Calculation Name: 5UK3-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5UK3

Chain ID: A

ChEMBL ID:

UniProt ID: T1KZQ3

Base Structure: X-ray

Registration Date: 2023-06-21

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	135
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1088946.556981
FMO2-HF: Nuclear repulsion	1034664.51793
FMO2-HF: Total energy	-54282.03905
FMO2-MP2: Total energy	-54438.681155

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:22:ASN)

Summations of interaction energy for fragment #1(A:22:ASN)

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.
-13.925	-7.436	2.168	-3.472	-5.183	0.018

Interaction energy analysis for fragmet #1(A:22:ASN)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.011 / q_NPA : -0.011

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	24	PHE	0	0.039	0.016	2.927	-1.295	1.371	0.223	-1.194	-1.695	0.006
4	A	25	ILE	0	-0.015	-0.009	2.237	-6.160	-3.299	1.934	-2.040	-2.754	0.011
5	A	26	LYS	1	0.876	0.924	3.398	-3.540	-3.008	0.007	-0.151	-0.388	0.001
6	A	27	ALA	0	0.017	0.005	5.441	-0.191	-0.191	0.000	0.000	0.000	0.000
7	A	28	LYS	1	0.921	0.964	6.975	-3.271	-3.271	0.000	0.000	0.000	0.000
8	A	29	GLU	-1	-0.905	-0.939	6.026	3.627	3.627	0.000	0.000	0.000	0.000
9	A	30	SER	0	-0.013	-0.002	9.557	-0.348	-0.348	0.000	0.000	0.000	0.000
10	A	31	LYS	1	0.930	0.968	11.625	-0.515	-0.515	0.000	0.000	0.000	0.000
11	A	32	GLY	0	0.007	0.026	12.788	-0.083	-0.083	0.000	0.000	0.000	0.000
12	A	33	LEU	0	0.012	0.023	12.122	-0.036	-0.036	0.000	0.000	0.000	0.000
13	A	34	THR	0	-0.016	-0.022	12.101	0.269	0.269	0.000	0.000	0.000	0.000
14	A	35	TYR	0	0.032	-0.008	6.974	-0.178	-0.178	0.000	0.000	0.000	0.000
15	A	36	GLN	0	-0.011	-0.010	12.989	-0.118	-0.118	0.000	0.000	0.000	0.000
16	A	37	GLN	0	0.064	0.029	16.043	-0.013	-0.013	0.000	0.000	0.000	0.000
17	A	38	MET	0	0.035	0.020	10.119	0.050	0.050	0.000	0.000	0.000	0.000
18	A	39	ALA	0	-0.003	0.004	15.095	-0.079	-0.079	0.000	0.000	0.000	0.000
19	A	40	GLN	0	-0.049	-0.028	16.696	-0.115	-0.115	0.000	0.000	0.000	0.000
20	A	41	LEU	0	-0.009	0.001	16.894	-0.058	-0.058	0.000	0.000	0.000	0.000
21	A	42	LEU	0	-0.005	-0.007	14.449	-0.067	-0.067	0.000	0.000	0.000	0.000
22	A	43	SER	0	-0.047	-0.004	18.598	-0.061	-0.061	0.000	0.000	0.000	0.000
23	A	44	VAL	0	-0.001	0.006	15.608	-0.034	-0.034	0.000	0.000	0.000	0.000
24	A	45	ASN	0	0.021	-0.003	17.679	0.078	0.078	0.000	0.000	0.000	0.000
25	A	46	LYS	1	0.973	0.977	14.800	-0.919	-0.919	0.000	0.000	0.000	0.000
26	A	47	VAL	0	-0.003	0.012	13.711	0.206	0.206	0.000	0.000	0.000	0.000
27	A	48	TRP	0	0.059	0.040	12.853	0.183	0.183	0.000	0.000	0.000	0.000
28	A	49	LEU	0	0.074	0.063	11.305	0.046	0.046	0.000	0.000	0.000	0.000
29	A	50	THR	0	-0.050	-0.048	9.036	0.261	0.261	0.000	0.000	0.000	0.000
30	A	51	SER	0	-0.036	-0.045	7.948	0.341	0.341	0.000	0.000	0.000	0.000
31	A	52	VAL	0	0.028	0.018	8.438	-0.129	-0.129	0.000	0.000	0.000	0.000
32	A	53	LEU	0	-0.036	-0.013	5.552	-0.107	-0.107	0.000	0.000	0.000	0.000
33	A	54	HIS	0	-0.059	-0.036	3.820	1.241	1.658	0.005	-0.086	-0.336	0.000
34	A	55	GLY	0	0.025	0.029	4.929	-0.847	-0.834	-0.001	-0.001	-0.010	0.000
35	A	56	GLN	0	0.027	0.009	6.781	-0.182	-0.182	0.000	0.000	0.000	0.000
36	A	57	ASN	0	-0.016	0.003	9.791	-0.141	-0.141	0.000	0.000	0.000	0.000
37	A	58	CYS	0	-0.010	0.027	10.410	0.029	0.029	0.000	0.000	0.000	0.000
38	A	59	CYS	0	-0.036	-0.007	12.687	0.095	0.095	0.000	0.000	0.000	0.000
39	A	60	ASP	-1	-0.827	-0.913	14.749	0.145	0.145	0.000	0.000	0.000	0.000
40	A	61	ILE	0	0.080	0.014	15.977	0.044	0.044	0.000	0.000	0.000	0.000
41	A	62	GLN	0	0.002	0.004	16.739	-0.002	-0.002	0.000	0.000	0.000	0.000
42	A	63	LEU	0	-0.029	-0.014	14.668	0.027	0.027	0.000	0.000	0.000	0.000
43	A	64	ALA	0	0.018	0.007	12.560	0.088	0.088	0.000	0.000	0.000	0.000
44	A	65	HIS	0	0.035	0.006	13.022	0.053	0.053	0.000	0.000	0.000	0.000
45	A	66	ARG	1	1.010	1.017	15.338	-0.334	-0.334	0.000	0.000	0.000	0.000
46	A	67	ILE	0	-0.022	-0.001	9.760	0.093	0.093	0.000	0.000	0.000	0.000
47	A	68	CYS	0	-0.082	-0.043	11.259	0.079	0.079	0.000	0.000	0.000	0.000
48	A	69	ASP	-1	-0.922	-0.951	12.310	0.233	0.233	0.000	0.000	0.000	0.000
49	A	70	THR	0	-0.085	-0.038	13.752	0.027	0.027	0.000	0.000	0.000	0.000
50	A	71	LEU	0	-0.075	-0.039	8.073	0.136	0.136	0.000	0.000	0.000	0.000
51	A	72	GLY	0	-0.069	-0.041	11.765	-0.127	-0.127	0.000	0.000	0.000	0.000
52	A	73	ILE	0	-0.028	0.005	8.334	-0.119	-0.119	0.000	0.000	0.000	0.000
53	A	74	SER	0	0.075	0.033	11.909	0.093	0.093	0.000	0.000	0.000	0.000
54	A	75	HIS	0	0.067	0.003	12.474	0.009	0.009	0.000	0.000	0.000	0.000
55	A	76	GLU	-1	-0.938	-0.963	13.900	-0.400	-0.400	0.000	0.000	0.000	0.000
56	A	77	TYR	0	-0.038	-0.019	7.736	-0.226	-0.226	0.000	0.000	0.000	0.000
57	A	78	ALA	0	-0.002	0.000	9.881	-0.009	-0.009	0.000	0.000	0.000	0.000
58	A	79	ASN	0	0.040	0.004	11.866	0.138	0.138	0.000	0.000	0.000	0.000
59	A	80	GLU	-1	-0.877	-0.949	6.236	-2.247	-2.247	0.000	0.000	0.000	0.000
60	A	81	LEU	0	-0.044	-0.021	6.933	0.066	0.066	0.000	0.000	0.000	0.000
61	A	82	THR	0	0.010	0.006	9.705	0.130	0.130	0.000	0.000	0.000	0.000
62	A	83	SER	0	-0.057	-0.007	11.405	-0.001	-0.001	0.000	0.000	0.000	0.000
63	A	84	ILE	0	0.009	-0.003	12.297	0.051	0.051	0.000	0.000	0.000	0.000
64	A	85	PRO	0	-0.027	0.015	10.317	-0.094	-0.094	0.000	0.000	0.000	0.000
65	A	86	LEU	0	-0.001	-0.020	12.294	0.106	0.106	0.000	0.000	0.000	0.000
66	A	87	ARG	1	0.839	0.871	12.122	-0.193	-0.193	0.000	0.000	0.000	0.000
67	A	88	GLY	0	-0.010	0.000	13.038	-0.013	-0.013	0.000	0.000	0.000	0.000
68	A	89	ASN	0	-0.007	-0.006	13.098	0.058	0.058	0.000	0.000	0.000	0.000
69	A	90	GLN	0	-0.013	0.015	7.955	-0.025	-0.025	0.000	0.000	0.000	0.000
70	A	91	ASN	0	0.020	-0.004	11.880	0.118	0.118	0.000	0.000	0.000	0.000
71	A	92	ILE	0	0.020	-0.006	10.509	0.028	0.028	0.000	0.000	0.000	0.000
72	A	93	ILE	0	0.008	0.010	14.327	0.059	0.059	0.000	0.000	0.000	0.000
73	A	94	ASN	0	0.009	-0.010	17.535	0.000	0.000	0.000	0.000	0.000	0.000
74	A	95	ASP	-1	-0.877	-0.921	13.912	1.109	1.109	0.000	0.000	0.000	0.000
75	A	96	PRO	0	0.010	-0.004	16.292	-0.035	-0.035	0.000	0.000	0.000	0.000
76	A	97	LEU	0	0.000	0.011	15.254	-0.075	-0.075	0.000	0.000	0.000	0.000
77	A	98	ILE	0	0.023	0.003	14.156	-0.037	-0.037	0.000	0.000	0.000	0.000
78	A	99	TYR	0	-0.005	0.002	17.789	-0.080	-0.080	0.000	0.000	0.000	0.000
79	A	100	ARG	1	0.934	0.959	20.932	-0.526	-0.526	0.000	0.000	0.000	0.000
80	A	101	PHE	0	0.010	0.008	18.273	-0.038	-0.038	0.000	0.000	0.000	0.000
81	A	102	ASN	0	0.037	0.015	19.912	-0.048	-0.048	0.000	0.000	0.000	0.000
82	A	103	GLU	-1	-0.896	-0.940	23.660	0.270	0.270	0.000	0.000	0.000	0.000
83	A	104	LEU	0	0.013	0.002	25.616	-0.030	-0.030	0.000	0.000	0.000	0.000
84	A	105	PHE	0	0.020	-0.002	23.737	-0.024	-0.024	0.000	0.000	0.000	0.000
85	A	106	LYS	1	0.806	0.919	27.946	-0.283	-0.283	0.000	0.000	0.000	0.000
86	A	107	VAL	0	-0.045	-0.022	29.933	-0.020	-0.020	0.000	0.000	0.000	0.000
87	A	108	TYR	0	0.021	0.004	30.651	-0.010	-0.010	0.000	0.000	0.000	0.000
88	A	109	GLY	0	0.031	0.032	30.984	-0.004	-0.004	0.000	0.000	0.000	0.000
89	A	110	SER	0	-0.026	-0.027	31.721	-0.004	-0.004	0.000	0.000	0.000	0.000
90	A	111	SER	0	0.025	0.008	34.998	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	112	LEU	0	0.022	0.008	29.543	-0.003	-0.003	0.000	0.000	0.000	0.000
92	A	113	ARG	1	0.928	0.978	33.591	-0.139	-0.139	0.000	0.000	0.000	0.000
93	A	114	GLY	0	-0.010	-0.011	34.806	-0.007	-0.007	0.000	0.000	0.000	0.000
94	A	115	ILE	0	0.056	0.033	35.953	-0.005	-0.005	0.000	0.000	0.000	0.000
95	A	116	ILE	0	-0.007	0.003	31.389	-0.003	-0.003	0.000	0.000	0.000	0.000
96	A	117	HIS	0	-0.074	-0.053	35.839	-0.010	-0.010	0.000	0.000	0.000	0.000
97	A	118	GLU	-1	-0.973	-0.976	38.584	0.130	0.130	0.000	0.000	0.000	0.000
98	A	119	GLU	-1	-0.951	-0.978	37.968	0.176	0.176	0.000	0.000	0.000	0.000
99	A	120	PHE	0	-0.082	-0.033	34.129	0.003	0.003	0.000	0.000	0.000	0.000
100	A	121	GLY	0	0.000	0.011	38.180	-0.008	-0.008	0.000	0.000	0.000	0.000
101	A	122	ASP	-1	-0.940	-0.979	37.867	0.111	0.111	0.000	0.000	0.000	0.000
102	A	123	GLY	0	0.009	-0.020	35.065	-0.007	-0.007	0.000	0.000	0.000	0.000
103	A	124	ILE	0	-0.059	-0.008	28.371	0.004	0.004	0.000	0.000	0.000	0.000
104	A	125	MET	0	0.032	0.024	24.841	0.001	0.001	0.000	0.000	0.000	0.000
105	A	126	SER	0	-0.019	-0.018	25.626	0.007	0.007	0.000	0.000	0.000	0.000
106	A	127	ALA	0	0.036	0.009	20.984	0.023	0.023	0.000	0.000	0.000	0.000
107	A	128	ILE	0	-0.059	-0.024	20.429	0.026	0.026	0.000	0.000	0.000	0.000
108	A	129	ASP	-1	-0.908	-0.957	21.187	0.264	0.264	0.000	0.000	0.000	0.000
109	A	130	CYS	0	-0.009	-0.019	20.887	0.002	0.002	0.000	0.000	0.000	0.000
110	A	131	LYS	1	0.943	0.987	20.445	-0.292	-0.292	0.000	0.000	0.000	0.000
111	A	132	ILE	0	0.002	-0.001	17.739	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	133	ASP	-1	-0.848	-0.907	19.502	0.599	0.599	0.000	0.000	0.000	0.000
113	A	134	VAL	0	-0.034	-0.035	17.090	-0.012	-0.012	0.000	0.000	0.000	0.000
114	A	135	THR	0	-0.030	-0.021	20.110	0.065	0.065	0.000	0.000	0.000	0.000
115	A	136	LYS	1	0.950	0.990	22.326	-0.633	-0.633	0.000	0.000	0.000	0.000
116	A	137	ASN	0	0.058	0.042	23.880	0.013	0.013	0.000	0.000	0.000	0.000
117	A	138	GLU	-1	-0.846	-0.929	27.584	0.385	0.385	0.000	0.000	0.000	0.000
118	A	139	GLN	0	0.012	-0.014	30.303	0.001	0.001	0.000	0.000	0.000	0.000
119	A	140	SER	0	-0.113	-0.060	25.906	0.009	0.009	0.000	0.000	0.000	0.000
120	A	141	ARG	1	0.976	1.002	26.322	-0.358	-0.358	0.000	0.000	0.000	0.000
121	A	142	VAL	0	-0.018	-0.012	21.199	0.023	0.023	0.000	0.000	0.000	0.000
122	A	143	ILE	0	-0.004	-0.006	23.929	-0.035	-0.035	0.000	0.000	0.000	0.000
123	A	144	LEU	0	-0.013	-0.012	19.803	0.047	0.047	0.000	0.000	0.000	0.000
124	A	145	ARG	1	0.958	0.981	22.814	-0.412	-0.412	0.000	0.000	0.000	0.000
125	A	146	ILE	0	0.006	-0.011	21.894	0.041	0.041	0.000	0.000	0.000	0.000
126	A	147	ASP	-1	-0.933	-0.953	23.882	0.287	0.287	0.000	0.000	0.000	0.000
127	A	148	GLY	0	0.061	0.021	24.955	0.012	0.012	0.000	0.000	0.000	0.000
128	A	149	LYS	1	0.899	0.969	26.407	-0.203	-0.203	0.000	0.000	0.000	0.000
129	A	150	PHE	0	0.053	0.032	28.964	0.003	0.003	0.000	0.000	0.000	0.000
130	A	151	LEU	0	-0.056	-0.035	28.918	-0.008	-0.008	0.000	0.000	0.000	0.000
131	A	152	PRO	0	-0.012	-0.001	32.713	0.000	0.000	0.000	0.000	0.000	0.000
132	A	153	TYR	0	0.035	0.014	33.856	-0.008	-0.008	0.000	0.000	0.000	0.000
133	A	154	TYR	0	-0.048	-0.029	37.142	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	155	LYS	1	0.969	0.975	39.330	-0.088	-0.088	0.000	0.000	0.000	0.000
135	A	156	GLY	0	-0.001	0.024	42.942	-0.003	-0.003	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:ASN)