FMO DATABASE

FMODB ID: R9ML8

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

Total energy (hartree)

FMO2-HF: Electronic energy	-1621935.205874
FMO2-HF: Nuclear repulsion	1558888.709383
FMO2-HF: Total energy	-63046.496491
FMO2-MP2: Total energy	-63228.928815

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.
-8.9	-2.123	2.811	-4.618	-4.972	-0.015

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 : 0.023 / q_NPA : 0.022

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	0.010	-0.010	3.812	-1.839	0.894	-0.029	-1.556	-1.148	0.009
4	A	288	LEU	0	0.035	0.033	6.266	0.268	0.268	0.000	0.000	0.000	0.000
5	A	289	PRO	0	-0.009	0.000	8.237	0.029	0.029	0.000	0.000	0.000	0.000
6	A	290	LYS	1	0.952	0.960	11.968	0.407	0.407	0.000	0.000	0.000	0.000
7	A	291	GLU	-1	-0.877	-0.942	14.315	-0.200	-0.200	0.000	0.000	0.000	0.000
8	A	292	MET	0	-0.053	-0.009	10.918	0.029	0.029	0.000	0.000	0.000	0.000
9	A	293	GLU	-1	-0.782	-0.891	9.123	-0.740	-0.740	0.000	0.000	0.000	0.000
10	A	294	ASP	-1	-0.830	-0.919	11.604	-0.321	-0.321	0.000	0.000	0.000	0.000
11	A	295	PHE	0	-0.050	-0.029	14.869	0.040	0.040	0.000	0.000	0.000	0.000
12	A	296	VAL	0	0.031	0.033	9.840	0.050	0.050	0.000	0.000	0.000	0.000
13	A	297	GLN	0	-0.040	-0.027	11.033	0.112	0.112	0.000	0.000	0.000	0.000
14	A	298	SER	0	-0.093	-0.063	14.416	0.044	0.044	0.000	0.000	0.000	0.000
15	A	299	SER	0	-0.062	-0.045	14.612	0.034	0.034	0.000	0.000	0.000	0.000
16	A	300	GLY	0	0.002	0.002	17.164	0.026	0.026	0.000	0.000	0.000	0.000
17	A	301	GLU	-1	-0.878	-0.942	16.761	-0.111	-0.111	0.000	0.000	0.000	0.000
18	A	302	ASN	0	-0.035	0.000	18.860	0.032	0.032	0.000	0.000	0.000	0.000
19	A	303	GLY	0	0.027	0.022	14.421	0.029	0.029	0.000	0.000	0.000	0.000
20	A	304	VAL	0	0.004	-0.016	11.217	-0.009	-0.009	0.000	0.000	0.000	0.000
21	A	305	VAL	0	0.012	0.013	13.617	0.041	0.041	0.000	0.000	0.000	0.000
22	A	306	VAL	0	0.003	0.011	10.004	-0.040	-0.040	0.000	0.000	0.000	0.000
23	A	307	PHE	0	0.057	0.017	13.427	0.042	0.042	0.000	0.000	0.000	0.000
24	A	308	SER	0	0.003	-0.014	15.190	-0.043	-0.043	0.000	0.000	0.000	0.000
25	A	309	LEU	0	0.034	0.016	17.109	0.028	0.028	0.000	0.000	0.000	0.000
26	A	310	GLY	0	-0.001	0.014	18.055	0.001	0.001	0.000	0.000	0.000	0.000
27	A	311	SER	0	0.003	-0.020	18.696	-0.019	-0.019	0.000	0.000	0.000	0.000
28	A	312	MET	0	-0.003	0.010	20.512	-0.021	-0.021	0.000	0.000	0.000	0.000
29	A	313	VAL	0	0.029	0.025	22.996	0.008	0.008	0.000	0.000	0.000	0.000
30	A	314	SER	0	-0.024	-0.008	25.702	-0.009	-0.009	0.000	0.000	0.000	0.000
31	A	315	ASN	0	0.050	0.012	28.050	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	316	MET	0	-0.015	0.009	24.727	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	317	THR	0	0.027	0.021	28.728	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	318	GLU	-1	-0.889	-0.956	30.875	0.024	0.024	0.000	0.000	0.000	0.000
35	A	319	GLU	-1	-0.827	-0.896	32.145	0.054	0.054	0.000	0.000	0.000	0.000
36	A	320	ARG	1	0.792	0.868	29.482	-0.069	-0.069	0.000	0.000	0.000	0.000
37	A	321	ALA	0	0.024	0.005	27.480	0.004	0.004	0.000	0.000	0.000	0.000
38	A	322	ASN	0	0.056	0.021	27.823	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	323	VAL	0	0.003	0.025	29.748	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	324	ILE	0	0.005	0.004	23.857	0.003	0.003	0.000	0.000	0.000	0.000
41	A	325	ALA	0	-0.004	-0.009	25.236	0.000	0.000	0.000	0.000	0.000	0.000
42	A	326	SER	0	0.028	0.009	26.315	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	327	ALA	0	-0.024	-0.001	26.165	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	328	LEU	0	-0.029	-0.018	20.627	0.001	0.001	0.000	0.000	0.000	0.000
45	A	329	ALA	0	-0.022	0.001	23.351	-0.007	-0.007	0.000	0.000	0.000	0.000
46	A	330	GLN	0	-0.073	-0.039	25.684	-0.008	-0.008	0.000	0.000	0.000	0.000
47	A	331	ILE	0	-0.048	0.001	20.007	0.003	0.003	0.000	0.000	0.000	0.000
48	A	332	PRO	0	-0.014	-0.013	22.019	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	333	GLN	0	-0.035	-0.016	17.408	-0.008	-0.008	0.000	0.000	0.000	0.000
50	A	334	LYS	1	0.922	0.983	16.064	0.089	0.089	0.000	0.000	0.000	0.000
51	A	335	VAL	0	0.019	-0.003	16.372	0.016	0.016	0.000	0.000	0.000	0.000
52	A	336	LEU	0	-0.023	-0.010	11.601	-0.028	-0.028	0.000	0.000	0.000	0.000
53	A	337	TRP	0	0.022	-0.002	15.332	0.036	0.036	0.000	0.000	0.000	0.000
54	A	338	ARG	1	0.847	0.921	15.616	-0.193	-0.193	0.000	0.000	0.000	0.000
55	A	339	PHE	0	-0.034	-0.037	17.512	0.019	0.019	0.000	0.000	0.000	0.000
56	A	340	ASP	-1	-0.922	-0.968	21.205	0.016	0.016	0.000	0.000	0.000	0.000
57	A	341	GLY	0	0.037	0.021	23.511	0.009	0.009	0.000	0.000	0.000	0.000
58	A	342	ASN	0	-0.014	-0.005	26.942	-0.011	-0.011	0.000	0.000	0.000	0.000
59	A	343	LYS	1	0.941	0.967	26.036	0.041	0.041	0.000	0.000	0.000	0.000
60	A	344	PRO	0	0.013	0.006	25.927	-0.001	-0.001	0.000	0.000	0.000	0.000
61	A	345	ASP	-1	-0.868	-0.929	28.920	0.001	0.001	0.000	0.000	0.000	0.000
62	A	346	THR	0	-0.063	-0.030	30.189	-0.002	-0.002	0.000	0.000	0.000	0.000
63	A	347	LEU	0	-0.050	-0.018	23.190	0.002	0.002	0.000	0.000	0.000	0.000
64	A	348	GLY	0	0.080	0.040	25.329	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	349	LEU	0	0.002	-0.014	24.468	-0.005	-0.005	0.000	0.000	0.000	0.000
66	A	350	ASN	0	-0.064	-0.027	21.286	-0.017	-0.017	0.000	0.000	0.000	0.000
67	A	351	THR	0	-0.003	0.003	19.857	0.004	0.004	0.000	0.000	0.000	0.000
68	A	352	ARG	1	0.920	0.971	17.788	0.133	0.133	0.000	0.000	0.000	0.000
69	A	353	LEU	0	0.001	0.005	18.585	0.015	0.015	0.000	0.000	0.000	0.000
70	A	354	TYR	0	-0.004	0.002	15.665	-0.038	-0.038	0.000	0.000	0.000	0.000
71	A	355	LYS	1	0.999	1.008	18.045	0.016	0.016	0.000	0.000	0.000	0.000
72	A	356	TRP	0	-0.050	-0.035	10.683	0.038	0.038	0.000	0.000	0.000	0.000
73	A	357	ILE	0	0.040	0.014	11.407	-0.050	-0.050	0.000	0.000	0.000	0.000
74	A	358	PRO	0	-0.006	0.016	6.737	0.131	0.131	0.000	0.000	0.000	0.000
75	A	359	GLN	0	-0.044	-0.046	7.008	-0.147	-0.147	0.000	0.000	0.000	0.000
76	A	360	ASN	0	0.089	0.053	3.136	-2.021	-1.125	0.100	-0.402	-0.594	0.000
77	A	361	ASP	-1	-0.833	-0.903	2.441	-3.744	-1.696	2.565	-2.294	-2.319	-0.022
78	A	362	LEU	0	-0.030	-0.016	3.719	-0.788	-0.506	0.009	-0.060	-0.231	-0.001
79	A	363	LEU	0	-0.048	-0.009	6.374	-0.139	-0.139	0.000	0.000	0.000	0.000
80	A	364	GLY	0	0.049	0.028	2.935	-0.264	0.015	0.109	-0.140	-0.249	0.000
81	A	365	HIS	0	-0.060	-0.017	4.005	-0.619	-0.487	0.000	-0.007	-0.125	0.000
82	A	366	PRO	0	0.024	-0.004	5.571	0.214	0.214	0.000	0.000	0.000	0.000
83	A	367	LYS	1	0.855	0.917	8.673	0.295	0.295	0.000	0.000	0.000	0.000
84	A	368	THR	0	-0.050	-0.033	8.002	-0.026	-0.026	0.000	0.000	0.000	0.000
85	A	369	ARG	1	0.891	0.945	10.729	0.024	0.024	0.000	0.000	0.000	0.000
86	A	370	ALA	0	0.010	0.001	13.792	0.021	0.021	0.000	0.000	0.000	0.000
87	A	371	PHE	0	-0.006	0.000	12.462	-0.002	-0.002	0.000	0.000	0.000	0.000
88	A	372	ILE	0	0.000	0.009	14.425	-0.003	-0.003	0.000	0.000	0.000	0.000
89	A	373	THR	0	0.033	0.017	15.900	0.004	0.004	0.000	0.000	0.000	0.000
90	A	374	HIS	0	0.061	0.017	17.465	-0.016	-0.016	0.000	0.000	0.000	0.000
91	A	375	GLY	0	0.022	-0.001	18.849	-0.018	-0.018	0.000	0.000	0.000	0.000
92	A	376	GLY	0	-0.012	-0.002	18.363	-0.007	-0.007	0.000	0.000	0.000	0.000
93	A	377	ALA	0	0.066	0.018	17.061	0.041	0.041	0.000	0.000	0.000	0.000
94	A	378	ASN	0	0.024	0.002	13.278	0.062	0.062	0.000	0.000	0.000	0.000
95	A	379	GLY	0	0.011	0.014	12.189	0.128	0.128	0.000	0.000	0.000	0.000
96	A	380	ILE	0	0.025	0.012	12.129	0.081	0.081	0.000	0.000	0.000	0.000
97	A	381	TYR	0	-0.003	-0.009	13.158	0.011	0.011	0.000	0.000	0.000	0.000
98	A	382	GLU	-1	-0.836	-0.920	7.913	1.651	1.651	0.000	0.000	0.000	0.000
99	A	383	ALA	0	-0.004	-0.005	8.541	0.177	0.177	0.000	0.000	0.000	0.000
100	A	384	ILE	0	-0.003	-0.007	10.654	-0.045	-0.045	0.000	0.000	0.000	0.000
101	A	385	TYR	0	-0.041	-0.013	5.285	0.088	0.088	0.000	0.000	0.000	0.000
102	A	386	HIS	0	-0.012	-0.012	2.963	-1.321	-0.914	0.057	-0.159	-0.306	-0.001
103	A	387	GLY	0	0.026	0.023	7.747	-0.236	-0.236	0.000	0.000	0.000	0.000
104	A	388	ILE	0	-0.078	-0.038	9.028	-0.154	-0.154	0.000	0.000	0.000	0.000
105	A	389	PRO	0	0.023	0.020	12.070	0.022	0.022	0.000	0.000	0.000	0.000
106	A	390	MET	0	0.001	-0.013	14.759	0.007	0.007	0.000	0.000	0.000	0.000
107	A	391	VAL	0	0.013	0.018	17.358	-0.032	-0.032	0.000	0.000	0.000	0.000
108	A	392	GLY	0	-0.016	-0.025	19.725	0.018	0.018	0.000	0.000	0.000	0.000
109	A	393	ILE	0	-0.014	-0.023	21.573	-0.024	-0.024	0.000	0.000	0.000	0.000
110	A	394	PRO	0	-0.045	-0.016	23.893	0.003	0.003	0.000	0.000	0.000	0.000
111	A	395	LEU	0	-0.022	-0.012	24.107	-0.018	-0.018	0.000	0.000	0.000	0.000
112	A	396	PHE	0	-0.011	-0.023	24.465	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	397	ALA	0	0.010	-0.001	25.690	0.017	0.017	0.000	0.000	0.000	0.000
114	A	398	ASP	-1	-0.821	-0.909	24.452	0.218	0.218	0.000	0.000	0.000	0.000
115	A	399	GLN	0	-0.032	0.009	22.177	0.001	0.001	0.000	0.000	0.000	0.000
116	A	400	PRO	0	-0.015	-0.024	23.946	0.010	0.010	0.000	0.000	0.000	0.000
117	A	401	ASP	-1	-0.853	-0.921	26.190	0.189	0.189	0.000	0.000	0.000	0.000
118	A	402	ASN	0	-0.034	-0.014	20.640	0.008	0.008	0.000	0.000	0.000	0.000
119	A	403	ILE	0	-0.012	-0.007	20.373	0.016	0.016	0.000	0.000	0.000	0.000
120	A	404	ALA	0	-0.027	-0.012	22.764	-0.004	-0.004	0.000	0.000	0.000	0.000
121	A	405	HIS	0	0.018	0.010	21.598	0.008	0.008	0.000	0.000	0.000	0.000
122	A	406	MET	0	0.021	0.008	18.175	0.017	0.017	0.000	0.000	0.000	0.000
123	A	407	LYS	1	0.900	0.955	21.247	-0.174	-0.174	0.000	0.000	0.000	0.000
124	A	408	ALA	0	-0.027	0.000	24.226	-0.011	-0.011	0.000	0.000	0.000	0.000
125	A	409	ARG	1	0.903	0.955	20.838	-0.300	-0.300	0.000	0.000	0.000	0.000
126	A	410	GLY	0	0.008	0.009	22.399	0.005	0.005	0.000	0.000	0.000	0.000
127	A	411	ALA	0	0.029	0.014	17.861	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	412	ALA	0	-0.017	-0.013	18.679	0.021	0.021	0.000	0.000	0.000	0.000
129	A	413	VAL	0	-0.008	0.009	20.987	-0.023	-0.023	0.000	0.000	0.000	0.000
130	A	414	ARG	1	0.894	0.953	23.071	-0.139	-0.139	0.000	0.000	0.000	0.000
131	A	415	VAL	0	-0.014	0.005	24.908	-0.013	-0.013	0.000	0.000	0.000	0.000
132	A	416	ASP	-1	-0.875	-0.945	27.129	0.130	0.130	0.000	0.000	0.000	0.000
133	A	417	PHE	0	0.037	-0.011	26.634	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	418	ASN	0	0.008	-0.012	29.155	-0.005	-0.005	0.000	0.000	0.000	0.000
135	A	419	THR	0	0.014	0.019	32.877	-0.005	-0.005	0.000	0.000	0.000	0.000
136	A	420	MET	0	-0.059	0.013	26.551	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	421	SER	0	0.048	0.026	31.812	-0.005	-0.005	0.000	0.000	0.000	0.000
138	A	422	SER	0	0.027	-0.031	29.785	0.004	0.004	0.000	0.000	0.000	0.000
139	A	423	THR	0	0.004	-0.007	29.408	0.002	0.002	0.000	0.000	0.000	0.000
140	A	424	ASP	-1	-0.843	-0.903	30.418	0.079	0.079	0.000	0.000	0.000	0.000
141	A	425	LEU	0	-0.007	-0.003	23.542	0.009	0.009	0.000	0.000	0.000	0.000
142	A	426	LEU	0	0.017	0.006	25.561	0.008	0.008	0.000	0.000	0.000	0.000
143	A	427	ASN	0	-0.016	-0.020	26.308	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	428	ALA	0	-0.036	-0.017	24.540	0.004	0.004	0.000	0.000	0.000	0.000
145	A	429	LEU	0	0.024	0.006	20.426	0.012	0.012	0.000	0.000	0.000	0.000
146	A	430	LYS	1	0.964	0.981	22.187	-0.045	-0.045	0.000	0.000	0.000	0.000
147	A	431	ARG	1	0.905	0.964	24.102	-0.122	-0.122	0.000	0.000	0.000	0.000
148	A	432	VAL	0	-0.005	-0.007	18.433	0.002	0.002	0.000	0.000	0.000	0.000
149	A	433	ILE	0	-0.049	-0.017	18.305	0.013	0.013	0.000	0.000	0.000	0.000
150	A	434	ASN	0	-0.041	-0.035	20.079	-0.010	-0.010	0.000	0.000	0.000	0.000
151	A	435	ASP	-1	-0.882	-0.902	23.030	0.107	0.107	0.000	0.000	0.000	0.000
152	A	436	PRO	0	0.025	-0.012	21.242	0.017	0.017	0.000	0.000	0.000	0.000
153	A	437	SER	0	0.015	0.010	21.013	0.024	0.024	0.000	0.000	0.000	0.000
154	A	438	TYR	0	-0.007	0.003	19.702	0.015	0.015	0.000	0.000	0.000	0.000
155	A	439	LYS	1	0.921	0.955	12.056	-0.301	-0.301	0.000	0.000	0.000	0.000
156	A	440	GLU	-1	-0.924	-0.970	16.876	0.182	0.182	0.000	0.000	0.000	0.000
157	A	441	ASN	0	-0.035	-0.033	19.042	0.016	0.016	0.000	0.000	0.000	0.000
158	A	442	VAL	0	-0.030	-0.010	14.053	0.018	0.018	0.000	0.000	0.000	0.000
159	A	443	MET	0	-0.033	-0.013	12.673	0.081	0.081	0.000	0.000	0.000	0.000
160	A	444	LYS	1	0.883	0.960	15.588	-0.198	-0.198	0.000	0.000	0.000	0.000
161	A	445	LEU	0	-0.080	-0.028	16.323	-0.010	-0.010	0.000	0.000	0.000	0.000
162	A	446	SER	0	-0.045	0.002	11.109	-0.007	-0.007	0.000	0.000	0.000	0.000

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