FMO DATABASE

FMODB ID: ZVN8N

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:

Apendix: None

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	134
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1158783.150666
FMO2-HF: Nuclear repulsion	1108099.981148
FMO2-HF: Total energy	-50683.169517
FMO2-MP2: Total energy	-50831.449298

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.
-24.043	-23.387	19.639	-10.07	-10.222	0.01

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 : -0.004 / q_NPA : -0.005

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	-0.845	-0.890	3.903	0.269	1.339	-0.002	-0.425	-0.643	0.000
4	A	1004	ARG	1	0.856	0.914	1.942	-20.627	-25.205	15.372	-5.835	-4.958	0.029
5	A	1005	LEU	0	0.014	0.009	4.941	0.482	0.482	0.000	0.000	0.000	0.000
6	A	1006	GLN	0	-0.056	-0.029	7.263	-0.296	-0.296	0.000	0.000	0.000	0.000
7	A	1007	PHE	0	-0.060	-0.032	8.969	0.007	0.007	0.000	0.000	0.000	0.000
8	A	1008	THR	0	0.025	0.014	12.293	-0.007	-0.007	0.000	0.000	0.000	0.000
9	A	1009	ALA	0	0.005	0.000	15.394	0.057	0.057	0.000	0.000	0.000	0.000
10	A	1010	THR	0	0.000	0.004	17.395	-0.055	-0.055	0.000	0.000	0.000	0.000
11	A	1011	THR	0	-0.006	-0.011	19.787	0.038	0.038	0.000	0.000	0.000	0.000
12	A	1012	LEU	0	0.001	-0.013	21.244	-0.026	-0.026	0.000	0.000	0.000	0.000
13	A	1013	SER	0	0.000	0.004	23.752	-0.017	-0.017	0.000	0.000	0.000	0.000
14	A	1014	GLY	0	-0.012	0.005	24.932	-0.022	-0.022	0.000	0.000	0.000	0.000
15	A	1015	ALA	0	0.008	0.012	23.725	-0.011	-0.011	0.000	0.000	0.000	0.000
16	A	1016	PRO	0	0.010	0.006	21.405	0.034	0.034	0.000	0.000	0.000	0.000
17	A	1017	PHE	0	0.024	-0.006	13.099	-0.014	-0.014	0.000	0.000	0.000	0.000
18	A	1018	ASP	-1	-0.793	-0.907	14.321	0.118	0.118	0.000	0.000	0.000	0.000
19	A	1019	GLY	0	0.014	0.030	11.041	0.005	0.005	0.000	0.000	0.000	0.000
20	A	1020	ALA	0	0.038	0.014	10.150	-0.023	-0.023	0.000	0.000	0.000	0.000
21	A	1021	SER	0	-0.073	-0.046	11.267	-0.117	-0.117	0.000	0.000	0.000	0.000
22	A	1022	LEU	0	-0.033	-0.023	9.076	-0.016	-0.016	0.000	0.000	0.000	0.000
23	A	1023	GLN	0	-0.020	-0.009	7.181	-0.247	-0.247	0.000	0.000	0.000	0.000
24	A	1024	GLY	0	0.007	0.006	8.496	0.119	0.119	0.000	0.000	0.000	0.000
25	A	1025	LYS	1	0.852	0.928	9.699	0.003	0.003	0.000	0.000	0.000	0.000
26	A	1026	PRO	0	0.003	0.019	9.378	0.013	0.013	0.000	0.000	0.000	0.000
27	A	1027	ALA	0	0.019	-0.004	8.527	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	1028	VAL	0	-0.002	-0.004	9.613	0.095	0.095	0.000	0.000	0.000	0.000
29	A	1029	LEU	0	-0.012	0.019	7.307	-0.123	-0.123	0.000	0.000	0.000	0.000
30	A	1030	TRP	0	-0.022	-0.023	10.697	0.012	0.012	0.000	0.000	0.000	0.000
31	A	1031	PHE	0	-0.014	-0.006	8.790	-0.072	-0.072	0.000	0.000	0.000	0.000
32	A	1032	TRP	0	-0.005	-0.014	14.591	-0.104	-0.104	0.000	0.000	0.000	0.000
33	A	1033	THR	0	0.069	0.005	18.414	0.001	0.001	0.000	0.000	0.000	0.000
34	A	1034	PRO	0	-0.003	0.008	21.741	-0.014	-0.014	0.000	0.000	0.000	0.000
35	A	1035	TRP	0	-0.012	-0.011	22.808	-0.015	-0.015	0.000	0.000	0.000	0.000
36	A	1036	CYS	0	-0.040	0.014	21.335	-0.027	-0.027	0.000	0.000	0.000	0.000
37	A	1037	PRO	0	0.021	0.015	24.653	0.005	0.005	0.000	0.000	0.000	0.000
38	A	1038	PHE	0	0.044	0.013	22.111	-0.005	-0.005	0.000	0.000	0.000	0.000
39	A	1039	CYS	0	0.025	0.024	19.392	0.012	0.012	0.000	0.000	0.000	0.000
40	A	1040	ASN	0	-0.027	-0.012	22.065	-0.020	-0.020	0.000	0.000	0.000	0.000
41	A	1041	ALA	0	0.001	0.011	25.112	-0.014	-0.014	0.000	0.000	0.000	0.000
42	A	1042	GLU	-1	-0.771	-0.890	18.664	0.495	0.495	0.000	0.000	0.000	0.000
43	A	1043	ALA	0	-0.002	0.010	22.191	0.000	0.000	0.000	0.000	0.000	0.000
44	A	1044	PRO	0	0.016	-0.004	23.180	-0.002	-0.002	0.000	0.000	0.000	0.000
45	A	1045	SER	0	0.021	0.008	22.382	-0.023	-0.023	0.000	0.000	0.000	0.000
46	A	1046	LEU	0	0.005	0.001	16.668	-0.002	-0.002	0.000	0.000	0.000	0.000
47	A	1047	SER	0	-0.052	-0.025	20.527	-0.012	-0.012	0.000	0.000	0.000	0.000
48	A	1048	GLN	0	-0.022	-0.013	23.228	-0.026	-0.026	0.000	0.000	0.000	0.000
49	A	1049	VAL	0	0.011	0.005	18.595	-0.018	-0.018	0.000	0.000	0.000	0.000
50	A	1050	ALA	0	0.021	0.014	19.058	-0.009	-0.009	0.000	0.000	0.000	0.000
51	A	1051	ALA	0	-0.034	-0.019	19.992	-0.023	-0.023	0.000	0.000	0.000	0.000
52	A	1052	ALA	0	-0.028	-0.009	22.629	-0.022	-0.022	0.000	0.000	0.000	0.000
53	A	1053	ASN	0	-0.083	-0.043	18.043	-0.038	-0.038	0.000	0.000	0.000	0.000
54	A	1054	PRO	0	0.053	0.017	18.329	0.022	0.022	0.000	0.000	0.000	0.000
55	A	1055	ALA	0	-0.049	-0.018	18.168	-0.005	-0.005	0.000	0.000	0.000	0.000
56	A	1056	VAL	0	-0.019	0.001	12.796	-0.020	-0.020	0.000	0.000	0.000	0.000
57	A	1057	THR	0	-0.044	-0.031	12.439	-0.007	-0.007	0.000	0.000	0.000	0.000
58	A	1058	PHE	0	0.017	0.015	12.474	0.142	0.142	0.000	0.000	0.000	0.000
59	A	1059	VAL	0	-0.021	-0.020	12.374	-0.082	-0.082	0.000	0.000	0.000	0.000
60	A	1060	GLY	0	-0.004	0.011	13.669	0.141	0.141	0.000	0.000	0.000	0.000
61	A	1061	ILE	0	-0.036	-0.023	11.334	-0.048	-0.048	0.000	0.000	0.000	0.000
62	A	1062	ALA	0	0.035	0.018	15.575	0.022	0.022	0.000	0.000	0.000	0.000
63	A	1063	THR	0	0.022	-0.006	18.005	-0.031	-0.031	0.000	0.000	0.000	0.000
64	A	1064	ARG	1	0.940	0.962	20.185	-0.384	-0.384	0.000	0.000	0.000	0.000
65	A	1065	ALA	0	0.002	0.007	23.242	-0.020	-0.020	0.000	0.000	0.000	0.000
66	A	1066	ASP	-1	-0.789	-0.880	25.350	0.225	0.225	0.000	0.000	0.000	0.000
67	A	1067	VAL	0	0.053	0.001	24.948	0.013	0.013	0.000	0.000	0.000	0.000
68	A	1068	GLY	0	0.050	0.043	26.659	0.003	0.003	0.000	0.000	0.000	0.000
69	A	1069	ALA	0	0.005	0.006	27.842	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	1070	MET	0	-0.064	-0.023	22.066	0.013	0.013	0.000	0.000	0.000	0.000
71	A	1071	GLN	0	0.009	-0.011	25.243	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	1072	SER	0	-0.026	-0.010	27.225	-0.012	-0.012	0.000	0.000	0.000	0.000
73	A	1073	PHE	0	-0.035	-0.019	21.927	-0.013	-0.013	0.000	0.000	0.000	0.000
74	A	1074	VAL	0	0.010	-0.006	22.759	0.000	0.000	0.000	0.000	0.000	0.000
75	A	1075	SER	0	-0.034	-0.023	25.421	-0.012	-0.012	0.000	0.000	0.000	0.000
76	A	1076	LYS	1	0.835	0.923	29.065	-0.212	-0.212	0.000	0.000	0.000	0.000
77	A	1077	TYR	0	-0.024	-0.041	25.855	-0.021	-0.021	0.000	0.000	0.000	0.000
78	A	1078	ASN	0	0.028	0.019	26.340	0.010	0.010	0.000	0.000	0.000	0.000
79	A	1079	LEU	0	-0.003	0.026	20.997	0.004	0.004	0.000	0.000	0.000	0.000
80	A	1080	ASN	0	-0.041	-0.016	22.569	0.009	0.009	0.000	0.000	0.000	0.000
81	A	1081	PHE	0	0.001	-0.010	17.317	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	1082	THR	0	0.013	0.019	16.518	-0.021	-0.021	0.000	0.000	0.000	0.000
83	A	1083	ASN	0	0.029	0.007	17.345	0.110	0.110	0.000	0.000	0.000	0.000
84	A	1084	LEU	0	-0.011	-0.006	14.157	-0.063	-0.063	0.000	0.000	0.000	0.000
85	A	1085	ASN	0	0.044	0.009	18.206	0.044	0.044	0.000	0.000	0.000	0.000
86	A	1086	ASP	-1	-0.783	-0.880	15.179	0.684	0.684	0.000	0.000	0.000	0.000
87	A	1087	ALA	0	-0.021	-0.004	18.054	0.009	0.009	0.000	0.000	0.000	0.000
88	A	1088	ASP	-1	-0.908	-0.954	19.821	0.282	0.282	0.000	0.000	0.000	0.000
89	A	1089	GLY	0	-0.042	-0.013	16.868	-0.006	-0.006	0.000	0.000	0.000	0.000
90	A	1090	VAL	0	0.020	0.007	14.283	0.072	0.072	0.000	0.000	0.000	0.000
91	A	1091	ILE	0	-0.012	-0.016	10.881	0.095	0.095	0.000	0.000	0.000	0.000
92	A	1092	TRP	0	-0.029	-0.032	10.575	0.317	0.317	0.000	0.000	0.000	0.000
93	A	1093	ALA	0	-0.028	-0.016	11.343	0.138	0.138	0.000	0.000	0.000	0.000
94	A	1094	ARG	1	0.820	0.927	7.889	-0.644	-0.644	0.000	0.000	0.000	0.000
95	A	1095	TYR	0	-0.020	-0.035	4.526	-0.594	-0.490	-0.001	-0.034	-0.069	0.000
96	A	1096	ASN	0	-0.074	-0.022	7.618	-0.043	-0.043	0.000	0.000	0.000	0.000
97	A	1097	VAL	0	0.015	-0.017	12.410	-0.025	-0.025	0.000	0.000	0.000	0.000
98	A	1098	PRO	0	-0.052	0.005	13.002	-0.043	-0.043	0.000	0.000	0.000	0.000
99	A	1099	TRP	0	-0.016	-0.026	15.964	-0.072	-0.072	0.000	0.000	0.000	0.000
100	A	1100	GLN	0	-0.009	0.015	15.944	0.090	0.090	0.000	0.000	0.000	0.000
101	A	1101	PRO	0	0.013	-0.004	17.221	-0.072	-0.072	0.000	0.000	0.000	0.000
102	A	1102	ALA	0	-0.001	-0.005	12.149	-0.011	-0.011	0.000	0.000	0.000	0.000
103	A	1103	PHE	0	0.015	0.005	11.311	-0.001	-0.001	0.000	0.000	0.000	0.000
104	A	1104	VAL	0	-0.034	-0.021	4.675	0.106	0.185	-0.001	-0.009	-0.069	0.000
105	A	1105	PHE	0	0.015	0.017	7.812	-0.046	-0.046	0.000	0.000	0.000	0.000
106	A	1106	TYR	0	0.043	0.019	2.097	0.923	1.200	3.390	-1.689	-1.978	0.000
107	A	1107	ARG	1	0.889	0.935	6.209	0.159	0.159	0.000	0.000	0.000	0.000
108	A	1108	ALA	0	0.006	0.010	7.028	-0.175	-0.175	0.000	0.000	0.000	0.000
109	A	1109	ASP	-1	-0.835	-0.888	7.986	-0.828	-0.828	0.000	0.000	0.000	0.000
110	A	1110	GLY	0	0.053	0.043	4.648	-0.253	-0.192	-0.001	-0.011	-0.048	0.000
111	A	1111	THR	0	-0.066	-0.060	2.768	-3.567	-1.396	0.594	-1.374	-1.391	-0.014
112	A	1112	SER	0	-0.007	-0.018	2.673	0.590	2.006	0.289	-0.689	-1.015	-0.005
113	A	1113	THR	0	-0.046	-0.014	4.979	-0.541	-0.485	-0.001	-0.004	-0.051	0.000
114	A	1114	PHE	0	0.007	-0.004	6.739	0.369	0.369	0.000	0.000	0.000	0.000
115	A	1115	VAL	0	-0.004	0.000	8.427	-0.290	-0.290	0.000	0.000	0.000	0.000
116	A	1116	ASN	0	0.005	-0.013	12.136	0.030	0.030	0.000	0.000	0.000	0.000
117	A	1117	ASN	0	0.036	0.032	14.198	-0.080	-0.080	0.000	0.000	0.000	0.000
118	A	1118	PRO	0	-0.012	0.015	17.899	-0.004	-0.004	0.000	0.000	0.000	0.000
119	A	1119	THR	0	-0.053	-0.044	20.791	-0.034	-0.034	0.000	0.000	0.000	0.000
120	A	1120	ALA	0	-0.010	-0.017	21.919	-0.028	-0.028	0.000	0.000	0.000	0.000
121	A	1121	ALA	0	-0.017	0.004	21.003	0.032	0.032	0.000	0.000	0.000	0.000
122	A	1122	MET	0	-0.041	0.002	14.684	-0.022	-0.022	0.000	0.000	0.000	0.000
123	A	1123	SER	0	-0.002	0.006	20.161	-0.020	-0.020	0.000	0.000	0.000	0.000
124	A	1124	GLN	0	0.026	-0.008	21.339	0.012	0.012	0.000	0.000	0.000	0.000
125	A	1125	ASP	-1	-0.876	-0.935	22.146	0.178	0.178	0.000	0.000	0.000	0.000
126	A	1126	GLU	-1	-0.820	-0.897	18.042	0.333	0.333	0.000	0.000	0.000	0.000
127	A	1127	LEU	0	-0.007	-0.010	16.381	0.020	0.020	0.000	0.000	0.000	0.000
128	A	1128	SER	0	0.006	-0.002	17.410	0.021	0.021	0.000	0.000	0.000	0.000
129	A	1129	GLY	0	0.016	0.012	18.822	-0.014	-0.014	0.000	0.000	0.000	0.000
130	A	1130	ARG	1	0.791	0.868	13.811	-0.423	-0.423	0.000	0.000	0.000	0.000
131	A	1131	VAL	0	0.005	0.005	13.839	0.025	0.025	0.000	0.000	0.000	0.000
132	A	1132	ALA	0	0.010	0.013	15.034	-0.034	-0.034	0.000	0.000	0.000	0.000
133	A	1133	ALA	0	-0.043	-0.015	14.305	-0.043	-0.043	0.000	0.000	0.000	0.000
134	A	1134	LEU	0	-0.125	-0.057	9.787	-0.132	-0.132	0.000	0.000	0.000	0.000

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