FMO DATABASE

FMODB ID: QYMLY

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	OptHSide
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	-1622787.332866
FMO2-HF: Nuclear repulsion	1559740.2808
FMO2-HF: Total energy	-63047.052066
FMO2-MP2: Total energy	-63229.472111

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.
-9.154	-2.124	4.329	-5.545	-5.816	-0.019

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 : 0.019

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	0.014	-0.007	3.812	-1.622	0.993	-0.027	-1.473	-1.115	0.008
4	A	288	LEU	0	0.027	0.031	6.149	0.269	0.269	0.000	0.000	0.000	0.000
5	A	289	PRO	0	-0.003	-0.002	8.284	0.023	0.023	0.000	0.000	0.000	0.000
6	A	290	LYS	1	0.861	0.894	12.015	0.390	0.390	0.000	0.000	0.000	0.000
7	A	291	GLU	-1	-0.773	-0.880	14.372	-0.172	-0.172	0.000	0.000	0.000	0.000
8	A	292	MET	0	-0.042	-0.004	10.915	0.030	0.030	0.000	0.000	0.000	0.000
9	A	293	GLU	-1	-0.779	-0.871	8.794	-0.719	-0.719	0.000	0.000	0.000	0.000
10	A	294	ASP	-1	-0.775	-0.865	11.649	-0.302	-0.302	0.000	0.000	0.000	0.000
11	A	295	PHE	0	-0.020	-0.015	14.770	0.034	0.034	0.000	0.000	0.000	0.000
12	A	296	VAL	0	0.037	0.030	9.758	0.046	0.046	0.000	0.000	0.000	0.000
13	A	297	GLN	0	0.001	-0.008	10.919	0.108	0.108	0.000	0.000	0.000	0.000
14	A	298	SER	0	-0.082	-0.043	14.453	0.043	0.043	0.000	0.000	0.000	0.000
15	A	299	SER	0	-0.075	-0.052	14.604	0.032	0.032	0.000	0.000	0.000	0.000
16	A	300	GLY	0	0.016	0.011	17.155	0.025	0.025	0.000	0.000	0.000	0.000
17	A	301	GLU	-1	-0.872	-0.940	16.776	-0.114	-0.114	0.000	0.000	0.000	0.000
18	A	302	ASN	0	-0.027	0.006	18.862	0.029	0.029	0.000	0.000	0.000	0.000
19	A	303	GLY	0	0.019	0.022	14.418	0.028	0.028	0.000	0.000	0.000	0.000
20	A	304	VAL	0	-0.004	-0.019	11.250	-0.010	-0.010	0.000	0.000	0.000	0.000
21	A	305	VAL	0	0.003	0.006	13.583	0.041	0.041	0.000	0.000	0.000	0.000
22	A	306	VAL	0	0.010	0.015	9.927	-0.038	-0.038	0.000	0.000	0.000	0.000
23	A	307	PHE	0	0.052	0.018	13.376	0.037	0.037	0.000	0.000	0.000	0.000
24	A	308	SER	0	0.003	-0.013	15.074	-0.043	-0.043	0.000	0.000	0.000	0.000
25	A	309	LEU	0	0.035	0.012	17.131	0.026	0.026	0.000	0.000	0.000	0.000
26	A	310	GLY	0	0.007	0.020	18.063	-0.001	-0.001	0.000	0.000	0.000	0.000
27	A	311	SER	0	-0.008	-0.026	18.690	-0.018	-0.018	0.000	0.000	0.000	0.000
28	A	312	MET	0	-0.006	0.008	20.519	-0.021	-0.021	0.000	0.000	0.000	0.000
29	A	313	VAL	0	0.023	0.019	22.893	0.008	0.008	0.000	0.000	0.000	0.000
30	A	314	SER	0	-0.010	-0.002	25.714	-0.008	-0.008	0.000	0.000	0.000	0.000
31	A	315	ASN	0	0.042	0.007	28.166	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	316	MET	0	-0.008	0.011	24.617	-0.004	-0.004	0.000	0.000	0.000	0.000
33	A	317	THR	0	0.015	0.015	28.725	-0.007	-0.007	0.000	0.000	0.000	0.000
34	A	318	GLU	-1	-0.874	-0.952	30.853	0.028	0.028	0.000	0.000	0.000	0.000
35	A	319	GLU	-1	-0.801	-0.874	32.101	0.058	0.058	0.000	0.000	0.000	0.000
36	A	320	ARG	1	0.771	0.847	29.469	-0.072	-0.072	0.000	0.000	0.000	0.000
37	A	321	ALA	0	0.012	0.000	27.426	0.004	0.004	0.000	0.000	0.000	0.000
38	A	322	ASN	0	0.046	0.005	27.780	-0.002	-0.002	0.000	0.000	0.000	0.000
39	A	323	VAL	0	-0.006	0.028	29.830	-0.002	-0.002	0.000	0.000	0.000	0.000
40	A	324	ILE	0	0.007	0.003	23.888	0.003	0.003	0.000	0.000	0.000	0.000
41	A	325	ALA	0	0.003	-0.002	25.200	0.001	0.001	0.000	0.000	0.000	0.000
42	A	326	SER	0	0.015	-0.011	26.277	-0.007	-0.007	0.000	0.000	0.000	0.000
43	A	327	ALA	0	-0.029	0.004	26.133	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	328	LEU	0	-0.028	-0.017	20.545	0.001	0.001	0.000	0.000	0.000	0.000
45	A	329	ALA	0	-0.016	0.006	23.320	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	330	GLN	0	-0.078	-0.049	25.657	-0.007	-0.007	0.000	0.000	0.000	0.000
47	A	331	ILE	0	-0.044	0.001	19.960	0.003	0.003	0.000	0.000	0.000	0.000
48	A	332	PRO	0	-0.003	-0.007	22.149	-0.007	-0.007	0.000	0.000	0.000	0.000
49	A	333	GLN	0	-0.046	-0.024	17.429	-0.010	-0.010	0.000	0.000	0.000	0.000
50	A	334	LYS	1	0.901	0.963	16.065	0.094	0.094	0.000	0.000	0.000	0.000
51	A	335	VAL	0	0.011	-0.009	16.351	0.018	0.018	0.000	0.000	0.000	0.000
52	A	336	LEU	0	-0.031	-0.009	11.673	-0.029	-0.029	0.000	0.000	0.000	0.000
53	A	337	TRP	0	0.016	-0.004	15.293	0.037	0.037	0.000	0.000	0.000	0.000
54	A	338	ARG	1	0.836	0.911	15.403	-0.187	-0.187	0.000	0.000	0.000	0.000
55	A	339	PHE	0	-0.027	-0.026	17.537	0.018	0.018	0.000	0.000	0.000	0.000
56	A	340	ASP	-1	-0.819	-0.894	21.230	0.017	0.017	0.000	0.000	0.000	0.000
57	A	341	GLY	0	0.038	0.021	23.532	0.008	0.008	0.000	0.000	0.000	0.000
58	A	342	ASN	0	-0.008	0.000	26.967	-0.009	-0.009	0.000	0.000	0.000	0.000
59	A	343	LYS	1	0.937	0.965	26.112	0.029	0.029	0.000	0.000	0.000	0.000
60	A	344	PRO	0	0.021	0.012	25.849	-0.002	-0.002	0.000	0.000	0.000	0.000
61	A	345	ASP	-1	-0.834	-0.902	28.891	0.008	0.008	0.000	0.000	0.000	0.000
62	A	346	THR	0	-0.075	-0.041	30.328	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	347	LEU	0	-0.057	-0.020	23.180	0.002	0.002	0.000	0.000	0.000	0.000
64	A	348	GLY	0	0.076	0.038	25.304	-0.005	-0.005	0.000	0.000	0.000	0.000
65	A	349	LEU	0	-0.006	-0.019	24.456	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	350	ASN	0	-0.041	-0.008	21.335	-0.015	-0.015	0.000	0.000	0.000	0.000
67	A	351	THR	0	-0.017	-0.012	19.845	0.006	0.006	0.000	0.000	0.000	0.000
68	A	352	ARG	1	0.820	0.907	17.663	0.126	0.126	0.000	0.000	0.000	0.000
69	A	353	LEU	0	-0.013	0.002	18.565	0.016	0.016	0.000	0.000	0.000	0.000
70	A	354	TYR	0	-0.004	-0.003	15.495	-0.036	-0.036	0.000	0.000	0.000	0.000
71	A	355	LYS	1	0.892	0.929	18.072	0.003	0.003	0.000	0.000	0.000	0.000
72	A	356	TRP	0	-0.044	-0.030	10.490	0.037	0.037	0.000	0.000	0.000	0.000
73	A	357	ILE	0	0.046	0.019	11.469	-0.049	-0.049	0.000	0.000	0.000	0.000
74	A	358	PRO	0	0.005	0.020	6.729	0.117	0.117	0.000	0.000	0.000	0.000
75	A	359	GLN	0	-0.047	-0.058	7.033	-0.121	-0.121	0.000	0.000	0.000	0.000
76	A	360	ASN	0	0.063	0.043	2.517	-2.639	-1.334	0.732	-0.938	-1.099	0.001
77	A	361	ASP	-1	-0.827	-0.921	2.349	-2.939	-0.997	3.388	-2.723	-2.607	-0.026
78	A	362	LEU	0	-0.024	-0.013	3.683	-0.855	-0.548	0.009	-0.067	-0.249	-0.001
79	A	363	LEU	0	-0.046	-0.010	6.335	-0.143	-0.143	0.000	0.000	0.000	0.000
80	A	364	GLY	0	0.048	0.025	2.945	-0.277	0.007	0.115	-0.145	-0.255	0.000
81	A	365	HIS	0	-0.071	-0.046	4.019	-0.602	-0.467	0.001	-0.007	-0.129	0.000
82	A	366	PRO	0	0.015	-0.007	5.564	0.193	0.193	0.000	0.000	0.000	0.000
83	A	367	LYS	1	0.862	0.926	8.677	0.260	0.260	0.000	0.000	0.000	0.000
84	A	368	THR	0	-0.042	-0.023	8.074	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	369	ARG	1	0.878	0.935	10.696	0.015	0.015	0.000	0.000	0.000	0.000
86	A	370	ALA	0	0.009	0.002	13.741	0.018	0.018	0.000	0.000	0.000	0.000
87	A	371	PHE	0	-0.007	-0.003	12.408	0.002	0.002	0.000	0.000	0.000	0.000
88	A	372	ILE	0	-0.009	0.006	14.400	-0.005	-0.005	0.000	0.000	0.000	0.000
89	A	373	THR	0	0.037	0.012	15.851	0.007	0.007	0.000	0.000	0.000	0.000
90	A	374	HIS	0	0.058	0.020	17.715	-0.009	-0.009	0.000	0.000	0.000	0.000
91	A	375	GLY	0	0.030	0.002	18.784	-0.018	-0.018	0.000	0.000	0.000	0.000
92	A	376	GLY	0	-0.013	-0.002	18.365	-0.008	-0.008	0.000	0.000	0.000	0.000
93	A	377	ALA	0	0.059	0.014	16.983	0.041	0.041	0.000	0.000	0.000	0.000
94	A	378	ASN	0	0.015	-0.002	13.278	0.031	0.031	0.000	0.000	0.000	0.000
95	A	379	GLY	0	0.019	0.022	12.117	0.124	0.124	0.000	0.000	0.000	0.000
96	A	380	ILE	0	0.015	0.008	12.057	0.080	0.080	0.000	0.000	0.000	0.000
97	A	381	TYR	0	-0.004	-0.010	13.078	0.014	0.014	0.000	0.000	0.000	0.000
98	A	382	GLU	-1	-0.826	-0.906	8.142	1.442	1.442	0.000	0.000	0.000	0.000
99	A	383	ALA	0	-0.006	-0.009	8.476	0.176	0.176	0.000	0.000	0.000	0.000
100	A	384	ILE	0	0.001	-0.005	10.599	-0.044	-0.044	0.000	0.000	0.000	0.000
101	A	385	TYR	0	-0.036	-0.011	5.032	-0.340	-0.340	0.000	0.000	0.000	0.000
102	A	386	HIS	0	-0.009	-0.004	2.759	-1.219	-0.777	0.111	-0.192	-0.362	-0.001
103	A	387	GLY	0	0.035	0.028	7.717	-0.229	-0.229	0.000	0.000	0.000	0.000
104	A	388	ILE	0	-0.080	-0.035	9.042	-0.153	-0.153	0.000	0.000	0.000	0.000
105	A	389	PRO	0	0.021	0.020	12.052	0.020	0.020	0.000	0.000	0.000	0.000
106	A	390	MET	0	0.001	-0.011	14.700	0.009	0.009	0.000	0.000	0.000	0.000
107	A	391	VAL	0	0.003	0.010	17.322	-0.032	-0.032	0.000	0.000	0.000	0.000
108	A	392	GLY	0	-0.010	-0.019	19.685	0.018	0.018	0.000	0.000	0.000	0.000
109	A	393	ILE	0	-0.019	-0.025	21.527	-0.024	-0.024	0.000	0.000	0.000	0.000
110	A	394	PRO	0	-0.028	-0.006	23.839	0.004	0.004	0.000	0.000	0.000	0.000
111	A	395	LEU	0	-0.034	-0.016	24.238	-0.018	-0.018	0.000	0.000	0.000	0.000
112	A	396	PHE	0	-0.014	-0.019	24.328	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	397	ALA	0	0.008	-0.006	25.805	0.017	0.017	0.000	0.000	0.000	0.000
114	A	398	ASP	-1	-0.822	-0.909	24.281	0.216	0.216	0.000	0.000	0.000	0.000
115	A	399	GLN	0	-0.026	0.008	22.104	0.004	0.004	0.000	0.000	0.000	0.000
116	A	400	PRO	0	-0.006	-0.017	23.877	0.010	0.010	0.000	0.000	0.000	0.000
117	A	401	ASP	-1	-0.862	-0.928	26.124	0.187	0.187	0.000	0.000	0.000	0.000
118	A	402	ASN	0	-0.028	-0.011	20.574	0.012	0.012	0.000	0.000	0.000	0.000
119	A	403	ILE	0	-0.007	-0.006	20.191	0.016	0.016	0.000	0.000	0.000	0.000
120	A	404	ALA	0	-0.032	-0.011	22.702	-0.003	-0.003	0.000	0.000	0.000	0.000
121	A	405	HIS	0	0.025	0.011	21.539	0.002	0.002	0.000	0.000	0.000	0.000
122	A	406	MET	0	0.034	0.021	18.128	0.018	0.018	0.000	0.000	0.000	0.000
123	A	407	LYS	1	0.911	0.962	21.196	-0.172	-0.172	0.000	0.000	0.000	0.000
124	A	408	ALA	0	-0.033	-0.004	24.179	-0.012	-0.012	0.000	0.000	0.000	0.000
125	A	409	ARG	1	0.894	0.948	20.928	-0.291	-0.291	0.000	0.000	0.000	0.000
126	A	410	GLY	0	0.012	0.012	22.362	0.005	0.005	0.000	0.000	0.000	0.000
127	A	411	ALA	0	0.024	0.012	17.880	-0.005	-0.005	0.000	0.000	0.000	0.000
128	A	412	ALA	0	-0.016	-0.012	18.645	0.022	0.022	0.000	0.000	0.000	0.000
129	A	413	VAL	0	-0.017	0.003	20.951	-0.023	-0.023	0.000	0.000	0.000	0.000
130	A	414	ARG	1	0.826	0.905	23.034	-0.137	-0.137	0.000	0.000	0.000	0.000
131	A	415	VAL	0	-0.008	-0.001	24.844	-0.013	-0.013	0.000	0.000	0.000	0.000
132	A	416	ASP	-1	-0.809	-0.891	27.085	0.135	0.135	0.000	0.000	0.000	0.000
133	A	417	PHE	0	0.057	-0.001	26.357	-0.008	-0.008	0.000	0.000	0.000	0.000
134	A	418	ASN	0	-0.007	-0.013	29.111	-0.003	-0.003	0.000	0.000	0.000	0.000
135	A	419	THR	0	0.013	0.015	32.813	-0.004	-0.004	0.000	0.000	0.000	0.000
136	A	420	MET	0	-0.067	0.009	26.453	-0.001	-0.001	0.000	0.000	0.000	0.000
137	A	421	SER	0	0.046	-0.011	31.779	-0.005	-0.005	0.000	0.000	0.000	0.000
138	A	422	SER	0	0.021	-0.031	29.734	0.004	0.004	0.000	0.000	0.000	0.000
139	A	423	THR	0	0.003	-0.008	29.355	0.002	0.002	0.000	0.000	0.000	0.000
140	A	424	ASP	-1	-0.827	-0.863	30.362	0.079	0.079	0.000	0.000	0.000	0.000
141	A	425	LEU	0	0.003	0.005	23.340	0.009	0.009	0.000	0.000	0.000	0.000
142	A	426	LEU	0	0.015	0.005	25.503	0.008	0.008	0.000	0.000	0.000	0.000
143	A	427	ASN	0	-0.021	-0.023	26.256	0.000	0.000	0.000	0.000	0.000	0.000
144	A	428	ALA	0	-0.016	-0.005	24.585	0.004	0.004	0.000	0.000	0.000	0.000
145	A	429	LEU	0	0.019	0.006	20.478	0.012	0.012	0.000	0.000	0.000	0.000
146	A	430	LYS	1	0.948	0.975	22.144	-0.051	-0.051	0.000	0.000	0.000	0.000
147	A	431	ARG	1	0.903	0.953	24.109	-0.126	-0.126	0.000	0.000	0.000	0.000
148	A	432	VAL	0	0.001	-0.008	18.486	0.001	0.001	0.000	0.000	0.000	0.000
149	A	433	ILE	0	-0.049	-0.016	18.190	0.013	0.013	0.000	0.000	0.000	0.000
150	A	434	ASN	0	-0.068	-0.041	20.074	-0.014	-0.014	0.000	0.000	0.000	0.000
151	A	435	ASP	-1	-0.866	-0.883	23.027	0.112	0.112	0.000	0.000	0.000	0.000
152	A	436	PRO	0	0.032	-0.007	21.253	0.017	0.017	0.000	0.000	0.000	0.000
153	A	437	SER	0	0.002	-0.014	21.017	0.023	0.023	0.000	0.000	0.000	0.000
154	A	438	TYR	0	0.024	0.023	19.796	0.018	0.018	0.000	0.000	0.000	0.000
155	A	439	LYS	1	0.923	0.945	11.843	-0.315	-0.315	0.000	0.000	0.000	0.000
156	A	440	GLU	-1	-0.919	-0.963	16.869	0.185	0.185	0.000	0.000	0.000	0.000
157	A	441	ASN	0	-0.045	-0.034	19.029	0.012	0.012	0.000	0.000	0.000	0.000
158	A	442	VAL	0	-0.020	-0.003	14.070	0.016	0.016	0.000	0.000	0.000	0.000
159	A	443	MET	0	-0.030	-0.010	12.594	0.077	0.077	0.000	0.000	0.000	0.000
160	A	444	LYS	1	0.839	0.929	15.569	-0.197	-0.197	0.000	0.000	0.000	0.000
161	A	445	LEU	0	-0.077	-0.024	16.356	-0.010	-0.010	0.000	0.000	0.000	0.000
162	A	446	SER	0	-0.043	0.001	11.096	-0.008	-0.008	0.000	0.000	0.000	0.000

Top

Graph

Manual

About

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