FMO DATABASE

FMODB ID: K98V3

Calculation Name: 2O6L-A-Xray372

Preferred Name: UDP-glucuronosyltransferase 2B7

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2O6L

Chain ID: A

ChEMBL ID: CHEMBL4370

UniProt ID: P16662

Base Structure: X-ray

Registration Date: 2023-06-22

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	OptAll
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	162
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1626745.675116
FMO2-HF: Nuclear repulsion	1563698.468637
FMO2-HF: Total energy	-63047.206479
FMO2-MP2: Total energy	-63229.640515

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:285:ALA)

Summations of interaction energy for fragment #1(A:285:ALA)

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.
-11.395	-6.507	8.082	-6.359	-6.61	-0.011

Interaction energy analysis for fragmet #1(A:285:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.039 / q_NPA : 0.023

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	287	PRO	0	0.017	-0.004	3.889	-0.807	1.252	-0.017	-1.159	-0.883	0.006
4	A	288	LEU	0	0.032	0.031	6.579	0.174	0.174	0.000	0.000	0.000	0.000
5	A	289	PRO	0	-0.003	-0.001	8.430	-0.001	-0.001	0.000	0.000	0.000	0.000
6	A	290	LYS	1	0.865	0.900	11.922	0.373	0.373	0.000	0.000	0.000	0.000
7	A	291	GLU	-1	-0.789	-0.882	14.374	-0.127	-0.127	0.000	0.000	0.000	0.000
8	A	292	MET	0	-0.036	-0.007	11.130	0.047	0.047	0.000	0.000	0.000	0.000
9	A	293	GLU	-1	-0.789	-0.872	8.844	-0.567	-0.567	0.000	0.000	0.000	0.000
10	A	294	ASP	-1	-0.796	-0.877	11.833	-0.237	-0.237	0.000	0.000	0.000	0.000
11	A	295	PHE	0	-0.010	-0.015	15.183	0.033	0.033	0.000	0.000	0.000	0.000
12	A	296	VAL	0	0.026	0.032	9.899	0.044	0.044	0.000	0.000	0.000	0.000
13	A	297	GLN	0	0.021	0.001	10.691	0.107	0.107	0.000	0.000	0.000	0.000
14	A	298	SER	0	-0.080	-0.045	14.397	0.036	0.036	0.000	0.000	0.000	0.000
15	A	299	SER	0	-0.043	-0.036	14.829	0.023	0.023	0.000	0.000	0.000	0.000
16	A	300	GLY	0	0.032	0.023	17.495	0.018	0.018	0.000	0.000	0.000	0.000
17	A	301	GLU	-1	-0.827	-0.925	16.826	-0.031	-0.031	0.000	0.000	0.000	0.000
18	A	302	ASN	0	-0.014	0.013	18.650	0.030	0.030	0.000	0.000	0.000	0.000
19	A	303	GLY	0	0.032	0.027	14.712	0.031	0.031	0.000	0.000	0.000	0.000
20	A	304	VAL	0	-0.018	-0.017	11.537	-0.021	-0.021	0.000	0.000	0.000	0.000
21	A	305	VAL	0	-0.002	-0.001	13.984	0.054	0.054	0.000	0.000	0.000	0.000
22	A	306	VAL	0	0.023	0.025	10.487	-0.047	-0.047	0.000	0.000	0.000	0.000
23	A	307	PHE	0	0.058	0.015	13.943	0.019	0.019	0.000	0.000	0.000	0.000
24	A	308	SER	0	-0.021	-0.021	14.339	-0.057	-0.057	0.000	0.000	0.000	0.000
25	A	309	LEU	0	0.019	0.013	16.623	0.035	0.035	0.000	0.000	0.000	0.000
26	A	310	GLY	0	0.014	0.023	17.749	-0.012	-0.012	0.000	0.000	0.000	0.000
27	A	311	SER	0	-0.009	-0.024	18.715	-0.013	-0.013	0.000	0.000	0.000	0.000
28	A	312	MET	0	-0.006	0.007	20.497	-0.027	-0.027	0.000	0.000	0.000	0.000
29	A	313	VAL	0	0.029	0.017	22.439	0.012	0.012	0.000	0.000	0.000	0.000
30	A	314	SER	0	0.007	0.005	25.458	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	315	ASN	0	0.034	0.014	27.903	-0.006	-0.006	0.000	0.000	0.000	0.000
32	A	316	MET	0	-0.008	0.009	24.251	-0.003	-0.003	0.000	0.000	0.000	0.000
33	A	317	THR	0	0.023	0.016	28.519	-0.008	-0.008	0.000	0.000	0.000	0.000
34	A	318	GLU	-1	-0.828	-0.919	30.671	0.051	0.051	0.000	0.000	0.000	0.000
35	A	319	GLU	-1	-0.797	-0.869	32.217	0.087	0.087	0.000	0.000	0.000	0.000
36	A	320	ARG	1	0.758	0.844	29.213	-0.104	-0.104	0.000	0.000	0.000	0.000
37	A	321	ALA	0	0.019	0.004	27.294	0.008	0.008	0.000	0.000	0.000	0.000
38	A	322	ASN	0	0.025	-0.008	27.785	0.001	0.001	0.000	0.000	0.000	0.000
39	A	323	VAL	0	-0.028	0.016	30.162	0.000	0.000	0.000	0.000	0.000	0.000
40	A	324	ILE	0	0.010	0.007	23.856	0.005	0.005	0.000	0.000	0.000	0.000
41	A	325	ALA	0	0.010	0.000	25.599	0.004	0.004	0.000	0.000	0.000	0.000
42	A	326	SER	0	0.010	-0.011	26.657	-0.006	-0.006	0.000	0.000	0.000	0.000
43	A	327	ALA	0	-0.023	0.003	26.395	-0.004	-0.004	0.000	0.000	0.000	0.000
44	A	328	LEU	0	-0.027	-0.012	21.195	0.004	0.004	0.000	0.000	0.000	0.000
45	A	329	ALA	0	-0.023	0.003	23.834	-0.004	-0.004	0.000	0.000	0.000	0.000
46	A	330	GLN	0	-0.074	-0.039	26.239	-0.010	-0.010	0.000	0.000	0.000	0.000
47	A	331	ILE	0	-0.022	-0.004	20.344	0.005	0.005	0.000	0.000	0.000	0.000
48	A	332	PRO	0	-0.007	0.000	22.422	-0.006	-0.006	0.000	0.000	0.000	0.000
49	A	333	GLN	0	-0.028	-0.023	17.693	-0.015	-0.015	0.000	0.000	0.000	0.000
50	A	334	LYS	1	0.873	0.947	16.413	0.017	0.017	0.000	0.000	0.000	0.000
51	A	335	VAL	0	0.006	-0.007	16.590	0.033	0.033	0.000	0.000	0.000	0.000
52	A	336	LEU	0	-0.026	-0.013	12.161	-0.040	-0.040	0.000	0.000	0.000	0.000
53	A	337	TRP	0	0.008	-0.005	15.166	0.051	0.051	0.000	0.000	0.000	0.000
54	A	338	ARG	1	0.838	0.899	15.359	-0.242	-0.242	0.000	0.000	0.000	0.000
55	A	339	PHE	0	-0.032	-0.024	17.240	0.014	0.014	0.000	0.000	0.000	0.000
56	A	340	ASP	-1	-0.832	-0.906	20.955	0.044	0.044	0.000	0.000	0.000	0.000
57	A	341	GLY	0	0.030	0.022	23.361	0.006	0.006	0.000	0.000	0.000	0.000
58	A	342	ASN	0	-0.020	-0.015	26.958	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	343	LYS	1	0.937	0.968	26.330	-0.006	-0.006	0.000	0.000	0.000	0.000
60	A	344	PRO	0	0.005	0.000	26.299	-0.003	-0.003	0.000	0.000	0.000	0.000
61	A	345	ASP	-1	-0.834	-0.900	29.178	0.035	0.035	0.000	0.000	0.000	0.000
62	A	346	THR	0	-0.065	-0.042	30.668	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	347	LEU	0	-0.063	-0.027	23.538	0.005	0.005	0.000	0.000	0.000	0.000
64	A	348	GLY	0	0.058	0.032	26.365	-0.009	-0.009	0.000	0.000	0.000	0.000
65	A	349	LEU	0	0.003	-0.016	24.748	0.001	0.001	0.000	0.000	0.000	0.000
66	A	350	ASN	0	-0.043	-0.013	21.549	-0.019	-0.019	0.000	0.000	0.000	0.000
67	A	351	THR	0	-0.010	-0.009	20.098	0.014	0.014	0.000	0.000	0.000	0.000
68	A	352	ARG	1	0.794	0.888	18.178	0.060	0.060	0.000	0.000	0.000	0.000
69	A	353	LEU	0	-0.004	0.011	18.879	0.025	0.025	0.000	0.000	0.000	0.000
70	A	354	TYR	0	-0.001	-0.002	15.898	-0.041	-0.041	0.000	0.000	0.000	0.000
71	A	355	LYS	1	0.903	0.932	17.874	-0.013	-0.013	0.000	0.000	0.000	0.000
72	A	356	TRP	0	-0.050	-0.026	10.430	0.033	0.033	0.000	0.000	0.000	0.000
73	A	357	ILE	0	0.048	0.020	11.223	-0.051	-0.051	0.000	0.000	0.000	0.000
74	A	358	PRO	0	0.001	0.007	6.579	0.097	0.097	0.000	0.000	0.000	0.000
75	A	359	GLN	0	-0.031	-0.030	6.806	-0.072	-0.072	0.000	0.000	0.000	0.000
76	A	360	ASN	0	0.058	0.030	2.206	-4.892	-5.016	4.678	-2.211	-2.342	0.008
77	A	361	ASP	-1	-0.829	-0.910	2.401	-2.597	-0.835	3.117	-2.584	-2.295	-0.025
78	A	362	LEU	0	-0.004	-0.010	3.511	-0.477	-0.387	0.008	0.057	-0.154	0.000
79	A	363	LEU	0	-0.054	-0.013	6.675	-0.190	-0.190	0.000	0.000	0.000	0.000
80	A	364	GLY	0	0.049	0.022	2.988	-0.394	-0.123	0.078	-0.120	-0.230	0.000
81	A	365	HIS	0	-0.052	-0.036	4.067	-0.715	-0.563	0.000	-0.017	-0.135	0.000
82	A	366	PRO	0	0.007	-0.006	5.549	0.125	0.125	0.000	0.000	0.000	0.000
83	A	367	LYS	1	0.810	0.908	8.493	0.091	0.091	0.000	0.000	0.000	0.000
84	A	368	THR	0	-0.038	-0.034	8.672	-0.079	-0.079	0.000	0.000	0.000	0.000
85	A	369	ARG	1	0.831	0.921	11.002	-0.110	-0.110	0.000	0.000	0.000	0.000
86	A	370	ALA	0	0.019	0.009	14.153	0.012	0.012	0.000	0.000	0.000	0.000
87	A	371	PHE	0	-0.021	-0.012	12.673	0.021	0.021	0.000	0.000	0.000	0.000
88	A	372	ILE	0	0.006	0.012	14.685	-0.022	-0.022	0.000	0.000	0.000	0.000
89	A	373	THR	0	0.015	0.001	16.284	0.012	0.012	0.000	0.000	0.000	0.000
90	A	374	HIS	0	0.060	0.030	17.827	-0.004	-0.004	0.000	0.000	0.000	0.000
91	A	375	GLY	0	0.054	0.019	19.035	-0.022	-0.022	0.000	0.000	0.000	0.000
92	A	376	GLY	0	-0.018	-0.017	18.402	-0.018	-0.018	0.000	0.000	0.000	0.000
93	A	377	ALA	0	0.039	0.016	16.836	0.067	0.067	0.000	0.000	0.000	0.000
94	A	378	ASN	0	0.023	0.003	13.234	0.014	0.014	0.000	0.000	0.000	0.000
95	A	379	GLY	0	0.033	0.030	12.211	0.166	0.166	0.000	0.000	0.000	0.000
96	A	380	ILE	0	0.011	-0.001	12.396	0.096	0.096	0.000	0.000	0.000	0.000
97	A	381	TYR	0	-0.013	-0.010	12.920	0.014	0.014	0.000	0.000	0.000	0.000
98	A	382	GLU	-1	-0.828	-0.913	8.177	1.744	1.744	0.000	0.000	0.000	0.000
99	A	383	ALA	0	-0.010	-0.005	8.449	0.243	0.243	0.000	0.000	0.000	0.000
100	A	384	ILE	0	0.018	-0.002	10.745	-0.061	-0.061	0.000	0.000	0.000	0.000
101	A	385	TYR	0	-0.028	-0.004	4.696	-0.481	-0.421	-0.001	-0.004	-0.055	0.000
102	A	386	HIS	0	-0.018	-0.016	2.576	-2.077	-1.459	0.219	-0.321	-0.516	0.000
103	A	387	GLY	0	0.048	0.034	7.326	-0.285	-0.285	0.000	0.000	0.000	0.000
104	A	388	ILE	0	-0.066	-0.031	8.995	-0.185	-0.185	0.000	0.000	0.000	0.000
105	A	389	PRO	0	0.001	0.016	11.871	0.010	0.010	0.000	0.000	0.000	0.000
106	A	390	MET	0	-0.009	-0.017	14.663	0.004	0.004	0.000	0.000	0.000	0.000
107	A	391	VAL	0	-0.008	-0.005	17.415	-0.046	-0.046	0.000	0.000	0.000	0.000
108	A	392	GLY	0	0.019	-0.005	20.117	0.016	0.016	0.000	0.000	0.000	0.000
109	A	393	ILE	0	-0.023	-0.030	21.841	-0.032	-0.032	0.000	0.000	0.000	0.000
110	A	394	PRO	0	-0.026	0.000	24.132	0.002	0.002	0.000	0.000	0.000	0.000
111	A	395	LEU	0	-0.051	-0.025	23.968	-0.021	-0.021	0.000	0.000	0.000	0.000
112	A	396	PHE	0	-0.008	-0.019	23.792	-0.014	-0.014	0.000	0.000	0.000	0.000
113	A	397	ALA	0	0.010	-0.001	26.024	0.019	0.019	0.000	0.000	0.000	0.000
114	A	398	ASP	-1	-0.827	-0.915	24.381	0.243	0.243	0.000	0.000	0.000	0.000
115	A	399	GLN	0	-0.011	0.014	22.305	0.007	0.007	0.000	0.000	0.000	0.000
116	A	400	PRO	0	-0.008	-0.016	24.197	0.014	0.014	0.000	0.000	0.000	0.000
117	A	401	ASP	-1	-0.857	-0.927	26.349	0.215	0.215	0.000	0.000	0.000	0.000
118	A	402	ASN	0	-0.023	-0.010	20.905	0.012	0.012	0.000	0.000	0.000	0.000
119	A	403	ILE	0	-0.004	0.002	20.351	0.025	0.025	0.000	0.000	0.000	0.000
120	A	404	ALA	0	-0.032	-0.011	22.783	-0.002	-0.002	0.000	0.000	0.000	0.000
121	A	405	HIS	0	-0.001	-0.001	21.399	0.003	0.003	0.000	0.000	0.000	0.000
122	A	406	MET	0	0.047	0.030	18.139	0.020	0.020	0.000	0.000	0.000	0.000
123	A	407	LYS	1	0.932	0.968	21.246	-0.216	-0.216	0.000	0.000	0.000	0.000
124	A	408	ALA	0	-0.040	-0.016	24.321	-0.013	-0.013	0.000	0.000	0.000	0.000
125	A	409	ARG	1	0.885	0.943	21.152	-0.324	-0.324	0.000	0.000	0.000	0.000
126	A	410	GLY	0	0.023	0.018	22.055	0.012	0.012	0.000	0.000	0.000	0.000
127	A	411	ALA	0	0.036	0.023	17.780	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	412	ALA	0	-0.028	-0.017	18.429	0.037	0.037	0.000	0.000	0.000	0.000
129	A	413	VAL	0	-0.035	-0.006	20.774	-0.034	-0.034	0.000	0.000	0.000	0.000
130	A	414	ARG	1	0.810	0.886	22.867	-0.172	-0.172	0.000	0.000	0.000	0.000
131	A	415	VAL	0	-0.013	0.001	25.286	-0.016	-0.016	0.000	0.000	0.000	0.000
132	A	416	ASP	-1	-0.780	-0.874	27.076	0.178	0.178	0.000	0.000	0.000	0.000
133	A	417	PHE	0	0.060	0.012	26.024	-0.011	-0.011	0.000	0.000	0.000	0.000
134	A	418	ASN	0	-0.004	-0.006	29.100	-0.001	-0.001	0.000	0.000	0.000	0.000
135	A	419	THR	0	-0.019	-0.008	32.537	-0.006	-0.006	0.000	0.000	0.000	0.000
136	A	420	MET	0	-0.060	0.004	26.504	0.000	0.000	0.000	0.000	0.000	0.000
137	A	421	SER	0	0.056	-0.007	31.766	-0.006	-0.006	0.000	0.000	0.000	0.000
138	A	422	SER	0	0.014	-0.037	29.838	0.006	0.006	0.000	0.000	0.000	0.000
139	A	423	THR	0	0.010	0.000	29.521	0.005	0.005	0.000	0.000	0.000	0.000
140	A	424	ASP	-1	-0.829	-0.868	30.457	0.115	0.115	0.000	0.000	0.000	0.000
141	A	425	LEU	0	0.015	0.012	23.437	0.012	0.012	0.000	0.000	0.000	0.000
142	A	426	LEU	0	0.012	0.013	25.473	0.013	0.013	0.000	0.000	0.000	0.000
143	A	427	ASN	0	0.012	-0.003	26.427	0.000	0.000	0.000	0.000	0.000	0.000
144	A	428	ALA	0	-0.016	-0.009	24.547	0.005	0.005	0.000	0.000	0.000	0.000
145	A	429	LEU	0	0.007	0.003	20.613	0.018	0.018	0.000	0.000	0.000	0.000
146	A	430	LYS	1	0.910	0.955	22.378	-0.094	-0.094	0.000	0.000	0.000	0.000
147	A	431	ARG	1	0.903	0.959	24.405	-0.177	-0.177	0.000	0.000	0.000	0.000
148	A	432	VAL	0	0.007	-0.012	18.209	0.000	0.000	0.000	0.000	0.000	0.000
149	A	433	ILE	0	-0.044	-0.011	18.468	0.027	0.027	0.000	0.000	0.000	0.000
150	A	434	ASN	0	-0.071	-0.041	19.857	-0.013	-0.013	0.000	0.000	0.000	0.000
151	A	435	ASP	-1	-0.838	-0.879	22.590	0.168	0.168	0.000	0.000	0.000	0.000
152	A	436	PRO	0	0.026	-0.005	21.033	0.022	0.022	0.000	0.000	0.000	0.000
153	A	437	SER	0	-0.015	-0.014	20.620	0.031	0.031	0.000	0.000	0.000	0.000
154	A	438	TYR	0	0.012	0.011	19.710	0.017	0.017	0.000	0.000	0.000	0.000
155	A	439	LYS	1	0.925	0.949	11.433	-0.505	-0.505	0.000	0.000	0.000	0.000
156	A	440	GLU	-1	-0.852	-0.924	16.393	0.248	0.248	0.000	0.000	0.000	0.000
157	A	441	ASN	0	-0.047	-0.029	18.446	0.010	0.010	0.000	0.000	0.000	0.000
158	A	442	VAL	0	-0.006	-0.003	13.677	0.013	0.013	0.000	0.000	0.000	0.000
159	A	443	MET	0	-0.031	-0.003	11.916	0.092	0.092	0.000	0.000	0.000	0.000
160	A	444	LYS	1	0.782	0.885	15.179	-0.249	-0.249	0.000	0.000	0.000	0.000
161	A	445	LEU	0	-0.081	-0.027	16.114	-0.026	-0.026	0.000	0.000	0.000	0.000
162	A	446	SER	0	-0.067	-0.014	10.556	-0.033	-0.033	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:285:ALA)