FMO DATABASE

FMODB ID: 6YG2Z

Calculation Name: 1LU4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 1LU4

Chain ID: A

ChEMBL ID:

UniProt ID: P9WG65

Base Structure: X-ray

Registration Date: 2023-09-22

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	134
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1159547.7445
FMO2-HF: Nuclear repulsion	1108866.88652
FMO2-HF: Total energy	-50680.857981
FMO2-MP2: Total energy	-50829.360952

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:1001:ALA)

Summations of interaction energy for fragment #1(A:1001: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.
-24.906	-27.063	30.277	-14.273	-13.848	-0.006

Interaction energy analysis for fragmet #1(A:1001:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.028 / q_NPA : 0.003

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	1003	GLU	-1	-0.851	-0.906	3.723	-2.724	-1.092	-0.013	-0.639	-0.979	0.006
4	A	1004	ARG	1	0.874	0.894	1.695	-21.866	-29.591	20.721	-7.047	-5.949	0.027
5	A	1005	LEU	0	0.002	0.009	3.155	0.987	1.751	0.021	-0.233	-0.552	-0.001
6	A	1006	GLN	0	-0.063	-0.027	5.046	0.468	0.528	-0.001	-0.004	-0.055	0.000
7	A	1007	PHE	0	-0.056	-0.030	6.723	0.304	0.304	0.000	0.000	0.000	0.000
8	A	1008	THR	0	0.030	0.012	10.208	-0.015	-0.015	0.000	0.000	0.000	0.000
9	A	1009	ALA	0	0.001	0.003	13.219	0.069	0.069	0.000	0.000	0.000	0.000
10	A	1010	THR	0	0.013	0.005	15.161	-0.035	-0.035	0.000	0.000	0.000	0.000
11	A	1011	THR	0	0.012	0.006	17.408	0.045	0.045	0.000	0.000	0.000	0.000
12	A	1012	LEU	0	0.010	-0.002	19.097	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	1013	SER	0	-0.019	-0.013	21.758	0.004	0.004	0.000	0.000	0.000	0.000
14	A	1014	GLY	0	-0.002	0.008	22.617	-0.008	-0.008	0.000	0.000	0.000	0.000
15	A	1015	ALA	0	-0.030	0.002	21.042	-0.015	-0.015	0.000	0.000	0.000	0.000
16	A	1016	PRO	0	0.019	0.008	18.961	0.014	0.014	0.000	0.000	0.000	0.000
17	A	1017	PHE	0	0.035	0.002	10.945	0.011	0.011	0.000	0.000	0.000	0.000
18	A	1018	ASP	-1	-0.828	-0.919	12.354	-0.711	-0.711	0.000	0.000	0.000	0.000
19	A	1019	GLY	0	0.026	0.024	9.001	0.035	0.035	0.000	0.000	0.000	0.000
20	A	1020	ALA	0	0.035	0.014	8.571	-0.247	-0.247	0.000	0.000	0.000	0.000
21	A	1021	SER	0	-0.075	-0.048	9.845	-0.049	-0.049	0.000	0.000	0.000	0.000
22	A	1022	LEU	0	-0.023	-0.021	7.746	0.137	0.137	0.000	0.000	0.000	0.000
23	A	1023	GLN	0	-0.020	-0.008	6.261	-0.431	-0.431	0.000	0.000	0.000	0.000
24	A	1024	GLY	0	0.008	0.009	7.417	0.289	0.289	0.000	0.000	0.000	0.000
25	A	1025	LYS	1	0.856	0.932	8.782	0.663	0.663	0.000	0.000	0.000	0.000
26	A	1026	PRO	0	-0.014	0.004	8.674	-0.038	-0.038	0.000	0.000	0.000	0.000
27	A	1027	ALA	0	0.023	-0.001	7.889	-0.057	-0.057	0.000	0.000	0.000	0.000
28	A	1028	VAL	0	0.001	0.000	9.015	0.257	0.257	0.000	0.000	0.000	0.000
29	A	1029	LEU	0	-0.028	0.009	5.835	-0.190	-0.190	0.000	0.000	0.000	0.000
30	A	1030	TRP	0	-0.022	-0.022	9.738	0.128	0.128	0.000	0.000	0.000	0.000
31	A	1031	PHE	0	-0.013	-0.002	7.883	-0.136	-0.136	0.000	0.000	0.000	0.000
32	A	1032	TRP	0	-0.011	-0.025	13.737	-0.027	-0.027	0.000	0.000	0.000	0.000
33	A	1033	THR	0	0.070	0.008	17.519	-0.019	-0.019	0.000	0.000	0.000	0.000
34	A	1034	PRO	0	0.020	0.010	20.689	0.001	0.001	0.000	0.000	0.000	0.000
35	A	1035	TRP	0	-0.010	-0.002	22.745	-0.004	-0.004	0.000	0.000	0.000	0.000
36	A	1036	CYS	0	-0.037	0.019	21.473	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	1037	PRO	0	0.033	0.016	24.487	0.001	0.001	0.000	0.000	0.000	0.000
38	A	1038	PHE	0	0.069	0.021	22.382	-0.008	-0.008	0.000	0.000	0.000	0.000
39	A	1039	CYS	0	0.010	0.022	19.108	0.015	0.015	0.000	0.000	0.000	0.000
40	A	1040	ASN	0	-0.016	-0.010	21.755	-0.032	-0.032	0.000	0.000	0.000	0.000
41	A	1041	ALA	0	-0.029	-0.003	25.046	-0.015	-0.015	0.000	0.000	0.000	0.000
42	A	1042	GLU	-1	-0.756	-0.892	18.765	0.544	0.544	0.000	0.000	0.000	0.000
43	A	1043	ALA	0	-0.008	0.013	21.518	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	1044	PRO	0	0.006	-0.015	22.567	-0.012	-0.012	0.000	0.000	0.000	0.000
45	A	1045	SER	0	0.018	0.015	21.981	-0.028	-0.028	0.000	0.000	0.000	0.000
46	A	1046	LEU	0	0.001	-0.004	16.091	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	1047	SER	0	-0.072	-0.035	20.005	-0.023	-0.023	0.000	0.000	0.000	0.000
48	A	1048	GLN	0	-0.019	-0.012	22.620	-0.028	-0.028	0.000	0.000	0.000	0.000
49	A	1049	VAL	0	0.016	0.002	18.381	-0.018	-0.018	0.000	0.000	0.000	0.000
50	A	1050	ALA	0	0.016	0.011	18.449	-0.016	-0.016	0.000	0.000	0.000	0.000
51	A	1051	ALA	0	-0.038	-0.015	19.395	-0.032	-0.032	0.000	0.000	0.000	0.000
52	A	1052	ALA	0	-0.027	-0.010	22.593	-0.024	-0.024	0.000	0.000	0.000	0.000
53	A	1053	ASN	0	-0.080	-0.045	17.893	-0.017	-0.017	0.000	0.000	0.000	0.000
54	A	1054	PRO	0	0.064	0.028	18.016	0.002	0.002	0.000	0.000	0.000	0.000
55	A	1055	ALA	0	-0.047	-0.014	17.541	-0.024	-0.024	0.000	0.000	0.000	0.000
56	A	1056	VAL	0	-0.033	-0.009	12.424	-0.038	-0.038	0.000	0.000	0.000	0.000
57	A	1057	THR	0	-0.043	-0.022	12.054	-0.023	-0.023	0.000	0.000	0.000	0.000
58	A	1058	PHE	0	0.034	0.023	12.051	0.074	0.074	0.000	0.000	0.000	0.000
59	A	1059	VAL	0	-0.022	-0.021	10.910	-0.094	-0.094	0.000	0.000	0.000	0.000
60	A	1060	GLY	0	0.010	0.018	12.200	0.147	0.147	0.000	0.000	0.000	0.000
61	A	1061	ILE	0	-0.024	-0.016	9.540	-0.099	-0.099	0.000	0.000	0.000	0.000
62	A	1062	ALA	0	0.038	0.019	13.993	0.077	0.077	0.000	0.000	0.000	0.000
63	A	1063	THR	0	0.007	-0.023	16.862	-0.036	-0.036	0.000	0.000	0.000	0.000
64	A	1064	ARG	1	0.951	0.972	18.790	-0.312	-0.312	0.000	0.000	0.000	0.000
65	A	1065	ALA	0	0.007	0.002	22.060	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	1066	ASP	-1	-0.804	-0.887	23.810	0.122	0.122	0.000	0.000	0.000	0.000
67	A	1067	VAL	0	0.073	0.015	23.509	0.010	0.010	0.000	0.000	0.000	0.000
68	A	1068	GLY	0	0.051	0.035	25.279	0.002	0.002	0.000	0.000	0.000	0.000
69	A	1069	ALA	0	-0.001	0.006	26.613	0.003	0.003	0.000	0.000	0.000	0.000
70	A	1070	MET	0	-0.083	-0.031	20.096	0.010	0.010	0.000	0.000	0.000	0.000
71	A	1071	GLN	0	0.010	-0.012	23.887	0.008	0.008	0.000	0.000	0.000	0.000
72	A	1072	SER	0	-0.019	-0.002	25.672	-0.005	-0.005	0.000	0.000	0.000	0.000
73	A	1073	PHE	0	-0.042	-0.017	20.922	-0.002	-0.002	0.000	0.000	0.000	0.000
74	A	1074	VAL	0	0.023	0.008	21.369	0.004	0.004	0.000	0.000	0.000	0.000
75	A	1075	SER	0	-0.035	-0.026	24.077	-0.010	-0.010	0.000	0.000	0.000	0.000
76	A	1076	LYS	1	0.836	0.923	27.666	-0.170	-0.170	0.000	0.000	0.000	0.000
77	A	1077	TYR	0	-0.025	-0.039	24.652	-0.008	-0.008	0.000	0.000	0.000	0.000
78	A	1078	ASN	0	0.004	0.013	25.529	0.002	0.002	0.000	0.000	0.000	0.000
79	A	1079	LEU	0	-0.013	0.009	20.043	0.005	0.005	0.000	0.000	0.000	0.000
80	A	1080	ASN	0	-0.011	0.007	21.857	-0.015	-0.015	0.000	0.000	0.000	0.000
81	A	1081	PHE	0	0.011	-0.011	16.306	-0.003	-0.003	0.000	0.000	0.000	0.000
82	A	1082	THR	0	-0.001	0.012	15.292	0.009	0.009	0.000	0.000	0.000	0.000
83	A	1083	ASN	0	0.032	0.011	16.001	0.094	0.094	0.000	0.000	0.000	0.000
84	A	1084	LEU	0	0.007	-0.007	12.086	-0.053	-0.053	0.000	0.000	0.000	0.000
85	A	1085	ASN	0	0.050	0.011	16.256	0.074	0.074	0.000	0.000	0.000	0.000
86	A	1086	ASP	-1	-0.808	-0.896	13.976	0.279	0.279	0.000	0.000	0.000	0.000
87	A	1087	ALA	0	-0.019	0.003	16.551	0.040	0.040	0.000	0.000	0.000	0.000
88	A	1088	ASP	-1	-0.903	-0.949	18.711	0.104	0.104	0.000	0.000	0.000	0.000
89	A	1089	GLY	0	-0.061	-0.029	15.864	0.015	0.015	0.000	0.000	0.000	0.000
90	A	1090	VAL	0	0.014	0.001	13.015	0.066	0.066	0.000	0.000	0.000	0.000
91	A	1091	ILE	0	-0.013	-0.013	8.994	0.040	0.040	0.000	0.000	0.000	0.000
92	A	1092	TRP	0	-0.027	-0.040	9.754	0.314	0.314	0.000	0.000	0.000	0.000
93	A	1093	ALA	0	-0.040	0.013	11.227	0.177	0.177	0.000	0.000	0.000	0.000
94	A	1094	ARG	1	0.858	0.929	6.634	0.871	0.871	0.000	0.000	0.000	0.000
95	A	1095	TYR	0	-0.052	-0.043	3.222	-0.501	-0.016	0.015	-0.211	-0.290	0.000
96	A	1096	ASN	0	-0.046	-0.050	7.766	-0.013	-0.013	0.000	0.000	0.000	0.000
97	A	1097	VAL	0	0.055	0.045	11.986	0.025	0.025	0.000	0.000	0.000	0.000
98	A	1098	PRO	0	0.298	0.339	13.119	-0.179	-0.179	0.000	0.000	0.000	0.000
99	A	1099	TRP	0	-0.307	-0.299	15.952	-0.033	-0.033	0.000	0.000	0.000	0.000
100	A	1100	GLN	0	-0.179	-0.087	16.122	0.081	0.081	0.000	0.000	0.000	0.000
101	A	1101	PRO	0	0.026	-0.014	16.955	-0.066	-0.066	0.000	0.000	0.000	0.000
102	A	1102	ALA	0	0.015	0.006	12.444	0.044	0.044	0.000	0.000	0.000	0.000
103	A	1103	PHE	0	0.005	0.000	11.723	-0.055	-0.055	0.000	0.000	0.000	0.000
104	A	1104	VAL	0	-0.036	-0.016	4.876	0.310	0.310	0.000	0.000	0.000	0.000
105	A	1105	PHE	0	0.021	0.012	8.237	-0.381	-0.381	0.000	0.000	0.000	0.000
106	A	1106	TYR	0	0.031	0.009	1.941	1.522	0.846	8.489	-4.262	-3.552	-0.020
107	A	1107	ARG	1	0.942	0.960	6.409	-0.218	-0.218	0.000	0.000	0.000	0.000
108	A	1108	ALA	0	-0.006	0.001	6.726	-0.238	-0.238	0.000	0.000	0.000	0.000
109	A	1109	ASP	-1	-0.827	-0.895	7.637	-0.622	-0.622	0.000	0.000	0.000	0.000
110	A	1110	GLY	0	0.057	0.043	4.130	-0.313	-0.256	-0.001	-0.025	-0.032	0.000
111	A	1111	THR	0	-0.070	-0.048	2.681	-3.188	-0.901	0.987	-1.425	-1.850	-0.015
112	A	1112	SER	0	-0.020	-0.026	3.058	0.936	1.859	0.060	-0.422	-0.560	-0.003
113	A	1113	THR	0	-0.031	-0.008	4.753	-0.320	-0.284	-0.001	-0.005	-0.029	0.000
114	A	1114	PHE	0	0.041	0.009	7.578	0.147	0.147	0.000	0.000	0.000	0.000
115	A	1115	VAL	0	-0.006	0.013	9.281	-0.304	-0.304	0.000	0.000	0.000	0.000
116	A	1116	ASN	0	-0.016	-0.020	13.027	-0.059	-0.059	0.000	0.000	0.000	0.000
117	A	1117	ASN	0	0.040	0.028	14.929	-0.068	-0.068	0.000	0.000	0.000	0.000
118	A	1118	PRO	0	0.031	0.037	18.453	-0.027	-0.027	0.000	0.000	0.000	0.000
119	A	1119	THR	0	-0.065	-0.051	21.392	-0.054	-0.054	0.000	0.000	0.000	0.000
120	A	1120	ALA	0	-0.024	-0.023	22.628	-0.043	-0.043	0.000	0.000	0.000	0.000
121	A	1121	ALA	0	-0.020	0.004	21.891	0.039	0.039	0.000	0.000	0.000	0.000
122	A	1122	MET	0	-0.041	-0.002	15.261	-0.023	-0.023	0.000	0.000	0.000	0.000
123	A	1123	SER	0	0.014	0.008	20.877	-0.032	-0.032	0.000	0.000	0.000	0.000
124	A	1124	GLN	0	0.042	0.003	21.662	0.015	0.015	0.000	0.000	0.000	0.000
125	A	1125	ASP	-1	-0.887	-0.937	22.275	0.227	0.227	0.000	0.000	0.000	0.000
126	A	1126	GLU	-1	-0.847	-0.909	18.113	0.538	0.538	0.000	0.000	0.000	0.000
127	A	1127	LEU	0	0.013	-0.006	16.360	0.036	0.036	0.000	0.000	0.000	0.000
128	A	1128	SER	0	0.001	-0.008	17.677	0.014	0.014	0.000	0.000	0.000	0.000
129	A	1129	GLY	0	0.010	0.016	19.080	-0.017	-0.017	0.000	0.000	0.000	0.000
130	A	1130	ARG	1	0.804	0.875	13.594	-0.701	-0.701	0.000	0.000	0.000	0.000
131	A	1131	VAL	0	-0.006	-0.007	14.303	0.025	0.025	0.000	0.000	0.000	0.000
132	A	1132	ALA	0	0.019	0.017	15.223	-0.043	-0.043	0.000	0.000	0.000	0.000
133	A	1133	ALA	0	-0.060	-0.022	14.485	-0.047	-0.047	0.000	0.000	0.000	0.000
134	A	1134	LEU	0	-0.121	-0.049	9.888	-0.098	-0.098	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1001:ALA)