FMO DATABASE

FMODB ID: 3QLQL

Calculation Name: 2QSR-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2QSR

Chain ID: A

ChEMBL ID:

UniProt ID: Q8DRQ1

Base Structure: X-ray

Registration Date: 2023-06-19

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	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	161
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1688975.539246
FMO2-HF: Nuclear repulsion	1624122.157141
FMO2-HF: Total energy	-64853.382105
FMO2-MP2: Total energy	-65047.643991

3D Structure Molmil

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:1005:SER)

Summations of interaction energy for fragment #1(A:1005:SER)

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.
-1.233	3.436	-0.006	-2.059	-2.605	0.01

Interaction energy analysis for fragmet #1(A:1005:SER)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.084 / q_NPA : 0.038

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	1007	ARG	1	0.805	0.848	2.996	-0.782	3.388	-0.011	-1.883	-2.277	0.011
4	A	1008	THR	0	-0.005	-0.006	3.856	-0.448	0.051	0.005	-0.176	-0.328	-0.001
5	A	1009	LYS	1	0.889	0.966	6.177	0.367	0.367	0.000	0.000	0.000	0.000
6	A	1010	GLY	0	-0.011	-0.009	8.067	-0.343	-0.343	0.000	0.000	0.000	0.000
7	A	1011	ASN	0	-0.060	-0.031	9.596	0.119	0.119	0.000	0.000	0.000	0.000
8	A	1012	ALA	0	0.014	0.026	13.226	-0.009	-0.009	0.000	0.000	0.000	0.000
9	A	1013	GLU	-1	-0.911	-0.966	15.816	-0.147	-0.147	0.000	0.000	0.000	0.000
10	A	1014	LEU	0	-0.006	-0.015	19.106	0.016	0.016	0.000	0.000	0.000	0.000
11	A	1015	ILE	0	0.000	0.009	21.993	0.003	0.003	0.000	0.000	0.000	0.000
12	A	1016	LEU	0	0.049	0.002	23.498	0.006	0.006	0.000	0.000	0.000	0.000
13	A	1017	GLN	0	-0.057	-0.033	27.343	0.010	0.010	0.000	0.000	0.000	0.000
14	A	1018	ILE	0	0.020	0.032	28.589	0.004	0.004	0.000	0.000	0.000	0.000
15	A	1019	ASP	-1	-0.926	-0.956	30.631	-0.029	-0.029	0.000	0.000	0.000	0.000
16	A	1020	ALA	0	-0.010	-0.020	29.321	0.005	0.005	0.000	0.000	0.000	0.000
17	A	1021	TYR	0	-0.038	-0.030	30.697	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	1022	LEU	0	0.049	0.024	30.856	0.005	0.005	0.000	0.000	0.000	0.000
19	A	1023	PRO	0	0.001	-0.002	34.140	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	1024	ASP	-1	-0.869	-0.924	37.879	-0.018	-0.018	0.000	0.000	0.000	0.000
21	A	1025	THR	0	-0.060	-0.036	40.387	0.001	0.001	0.000	0.000	0.000	0.000
22	A	1026	TYR	0	-0.028	-0.014	35.110	0.000	0.000	0.000	0.000	0.000	0.000
23	A	1027	ILE	0	0.012	0.015	34.372	0.001	0.001	0.000	0.000	0.000	0.000
24	A	1028	SER	0	0.046	0.020	38.532	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	1029	ASP	-1	-0.845	-0.922	39.016	-0.015	-0.015	0.000	0.000	0.000	0.000
26	A	1030	GLN	0	0.064	0.022	36.430	0.000	0.000	0.000	0.000	0.000	0.000
27	A	1031	ARG	1	0.858	0.905	34.536	0.010	0.010	0.000	0.000	0.000	0.000
28	A	1032	HIS	0	0.067	0.047	33.408	-0.002	-0.002	0.000	0.000	0.000	0.000
29	A	1033	LYS	1	0.860	0.940	32.545	0.018	0.018	0.000	0.000	0.000	0.000
30	A	1034	ILE	0	-0.037	-0.016	29.954	-0.002	-0.002	0.000	0.000	0.000	0.000
31	A	1035	GLU	-1	-0.852	-0.897	28.938	-0.002	-0.002	0.000	0.000	0.000	0.000
32	A	1036	ILE	0	0.054	0.019	28.059	-0.001	-0.001	0.000	0.000	0.000	0.000
33	A	1037	TYR	0	0.037	0.009	27.619	0.001	0.001	0.000	0.000	0.000	0.000
34	A	1038	LYS	1	0.893	0.950	23.540	0.055	0.055	0.000	0.000	0.000	0.000
35	A	1039	LYS	1	0.812	0.859	23.542	-0.020	-0.020	0.000	0.000	0.000	0.000
36	A	1040	ILE	0	0.045	0.031	23.672	0.006	0.006	0.000	0.000	0.000	0.000
37	A	1041	ARG	1	0.872	0.940	20.745	0.097	0.097	0.000	0.000	0.000	0.000
38	A	1042	GLN	0	-0.075	-0.038	19.288	-0.028	-0.028	0.000	0.000	0.000	0.000
39	A	1043	ILE	0	-0.034	-0.001	19.264	0.019	0.019	0.000	0.000	0.000	0.000
40	A	1044	ASP	-1	-0.825	-0.907	13.900	0.155	0.155	0.000	0.000	0.000	0.000
41	A	1045	ASN	0	-0.018	-0.024	16.222	0.020	0.020	0.000	0.000	0.000	0.000
42	A	1046	ARG	1	0.943	0.971	18.484	-0.118	-0.118	0.000	0.000	0.000	0.000
43	A	1047	VAL	0	0.054	0.031	21.275	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	1048	ASN	0	0.008	0.016	19.148	0.002	0.002	0.000	0.000	0.000	0.000
45	A	1049	TYR	0	0.011	-0.044	22.927	-0.008	-0.008	0.000	0.000	0.000	0.000
46	A	1050	GLU	-1	-0.856	-0.919	24.882	0.089	0.089	0.000	0.000	0.000	0.000
47	A	1051	GLU	-1	-0.919	-0.961	24.877	0.085	0.085	0.000	0.000	0.000	0.000
48	A	1052	LEU	0	-0.059	-0.030	25.813	-0.009	-0.009	0.000	0.000	0.000	0.000
49	A	1053	GLN	0	-0.029	-0.017	28.423	-0.003	-0.003	0.000	0.000	0.000	0.000
50	A	1054	GLU	-1	-0.907	-0.948	31.012	0.047	0.047	0.000	0.000	0.000	0.000
51	A	1055	GLU	-1	-0.819	-0.878	29.848	0.018	0.018	0.000	0.000	0.000	0.000
52	A	1056	LEU	0	-0.072	-0.046	30.936	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	1057	ILE	0	0.050	0.015	34.239	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	1058	ASP	-1	-0.952	-0.953	35.719	0.027	0.027	0.000	0.000	0.000	0.000
55	A	1059	ARG	1	0.768	0.851	32.317	-0.013	-0.013	0.000	0.000	0.000	0.000
56	A	1060	PHE	0	-0.124	-0.080	34.784	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	1061	GLY	0	0.000	0.025	39.186	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	1062	GLU	-1	-0.900	-0.949	38.529	0.025	0.025	0.000	0.000	0.000	0.000
59	A	1063	TYR	0	-0.004	0.002	33.006	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	1064	PRO	0	-0.014	-0.009	37.228	0.001	0.001	0.000	0.000	0.000	0.000
61	A	1065	ASP	-1	-0.837	-0.931	35.805	0.009	0.009	0.000	0.000	0.000	0.000
62	A	1066	VAL	0	-0.031	-0.013	33.907	0.000	0.000	0.000	0.000	0.000	0.000
63	A	1067	VAL	0	-0.008	-0.008	32.292	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	1068	ALA	0	0.030	0.026	30.932	0.001	0.001	0.000	0.000	0.000	0.000
65	A	1069	TYR	0	0.023	-0.003	29.755	0.004	0.004	0.000	0.000	0.000	0.000
66	A	1070	LEU	0	-0.061	-0.010	26.493	-0.003	-0.003	0.000	0.000	0.000	0.000
67	A	1071	LEU	0	0.003	-0.001	26.186	-0.004	-0.004	0.000	0.000	0.000	0.000
68	A	1072	GLU	-1	-0.839	-0.895	25.208	0.045	0.045	0.000	0.000	0.000	0.000
69	A	1073	ILE	0	-0.026	-0.028	23.322	0.003	0.003	0.000	0.000	0.000	0.000
70	A	1074	GLY	0	0.004	0.012	21.812	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	1075	LEU	0	0.033	0.024	20.357	-0.001	-0.001	0.000	0.000	0.000	0.000
72	A	1076	VAL	0	0.018	0.015	19.775	0.007	0.007	0.000	0.000	0.000	0.000
73	A	1077	LYS	1	0.760	0.865	15.869	0.163	0.163	0.000	0.000	0.000	0.000
74	A	1078	SER	0	-0.064	-0.032	15.880	-0.004	-0.004	0.000	0.000	0.000	0.000
75	A	1079	TYR	0	0.000	-0.032	14.590	0.016	0.016	0.000	0.000	0.000	0.000
76	A	1080	LEU	0	0.015	-0.004	14.308	0.010	0.010	0.000	0.000	0.000	0.000
77	A	1081	ASP	-1	-0.794	-0.875	12.160	-0.185	-0.185	0.000	0.000	0.000	0.000
78	A	1082	LYS	1	0.819	0.900	10.084	-0.299	-0.299	0.000	0.000	0.000	0.000
79	A	1083	VAL	0	-0.017	0.007	9.689	0.103	0.103	0.000	0.000	0.000	0.000
80	A	1084	PHE	0	-0.081	-0.048	5.256	-0.052	-0.052	0.000	0.000	0.000	0.000
81	A	1085	VAL	0	0.011	0.003	10.426	-0.006	-0.006	0.000	0.000	0.000	0.000
82	A	1086	GLN	0	-0.056	-0.037	13.407	-0.088	-0.088	0.000	0.000	0.000	0.000
83	A	1087	ARG	1	0.758	0.854	14.877	0.094	0.094	0.000	0.000	0.000	0.000
84	A	1088	VAL	0	0.025	0.026	18.588	0.021	0.021	0.000	0.000	0.000	0.000
85	A	1089	GLU	-1	-0.818	-0.895	21.404	-0.084	-0.084	0.000	0.000	0.000	0.000
86	A	1090	ARG	1	0.868	0.946	24.795	0.020	0.020	0.000	0.000	0.000	0.000
87	A	1091	LYS	1	0.874	0.910	28.195	0.033	0.033	0.000	0.000	0.000	0.000
88	A	1092	ASP	-1	-0.841	-0.907	30.839	-0.027	-0.027	0.000	0.000	0.000	0.000
89	A	1093	ASN	0	-0.025	-0.022	33.496	0.002	0.002	0.000	0.000	0.000	0.000
90	A	1094	LYS	1	0.912	0.950	30.183	0.009	0.009	0.000	0.000	0.000	0.000
91	A	1095	ILE	0	0.026	0.026	24.819	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	1096	THR	0	-0.005	-0.003	24.020	0.013	0.013	0.000	0.000	0.000	0.000
93	A	1097	ILE	0	-0.022	0.007	18.346	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	1098	GLN	0	0.002	0.000	18.449	-0.004	-0.004	0.000	0.000	0.000	0.000
95	A	1099	PHE	0	0.067	0.029	13.443	-0.022	-0.022	0.000	0.000	0.000	0.000
96	A	1100	GLU	-1	-0.741	-0.836	8.605	-0.851	-0.851	0.000	0.000	0.000	0.000
97	A	1101	LYS	1	0.971	0.972	11.892	0.258	0.258	0.000	0.000	0.000	0.000
98	A	1102	VAL	0	0.008	0.009	5.617	0.093	0.093	0.000	0.000	0.000	0.000
99	A	1103	THR	0	0.030	0.022	8.915	0.226	0.226	0.000	0.000	0.000	0.000
100	A	1104	GLN	0	-0.020	-0.006	10.901	0.029	0.029	0.000	0.000	0.000	0.000
101	A	1105	ARG	1	0.865	0.930	7.822	-0.857	-0.857	0.000	0.000	0.000	0.000
102	A	1106	LEU	0	-0.017	0.003	7.182	0.072	0.072	0.000	0.000	0.000	0.000
103	A	1107	PHE	0	-0.020	-0.011	11.110	-0.021	-0.021	0.000	0.000	0.000	0.000
104	A	1108	LEU	0	0.006	0.014	14.594	-0.028	-0.028	0.000	0.000	0.000	0.000
105	A	1109	ALA	0	0.064	0.019	18.003	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	1110	GLN	0	0.001	-0.012	20.955	-0.021	-0.021	0.000	0.000	0.000	0.000
107	A	1111	ASP	-1	-0.816	-0.912	16.752	0.287	0.287	0.000	0.000	0.000	0.000
108	A	1112	TYR	0	0.063	0.022	15.244	0.001	0.001	0.000	0.000	0.000	0.000
109	A	1113	PHE	0	0.014	0.010	20.336	-0.010	-0.010	0.000	0.000	0.000	0.000
110	A	1114	LYS	1	0.952	0.986	22.422	-0.143	-0.143	0.000	0.000	0.000	0.000
111	A	1115	ALA	0	0.054	0.040	20.367	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	1116	LEU	0	0.005	-0.007	22.492	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	1117	SER	0	-0.114	-0.075	25.030	-0.008	-0.008	0.000	0.000	0.000	0.000
114	A	1118	VAL	0	-0.051	-0.016	25.070	-0.003	-0.003	0.000	0.000	0.000	0.000
115	A	1119	THR	0	-0.056	-0.002	25.227	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	1120	ASN	0	-0.003	-0.018	28.169	-0.001	-0.001	0.000	0.000	0.000	0.000
117	A	1121	LEU	0	-0.055	-0.015	27.756	-0.006	-0.006	0.000	0.000	0.000	0.000
118	A	1122	LYS	1	0.888	0.946	29.997	-0.014	-0.014	0.000	0.000	0.000	0.000
119	A	1123	ALA	0	-0.008	-0.020	26.429	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	1124	GLY	0	-0.004	0.003	27.299	0.003	0.003	0.000	0.000	0.000	0.000
121	A	1125	ILE	0	-0.026	-0.010	22.344	-0.001	-0.001	0.000	0.000	0.000	0.000
122	A	1126	ALA	0	-0.019	-0.003	24.377	-0.001	-0.001	0.000	0.000	0.000	0.000
123	A	1127	GLU	-1	-0.852	-0.942	22.453	0.029	0.029	0.000	0.000	0.000	0.000
124	A	1128	ASN	0	-0.080	-0.042	23.023	-0.010	-0.010	0.000	0.000	0.000	0.000
125	A	1129	LYS	1	0.935	0.954	22.280	0.082	0.082	0.000	0.000	0.000	0.000
126	A	1130	GLY	0	-0.035	-0.016	21.367	-0.011	-0.011	0.000	0.000	0.000	0.000
127	A	1131	LEU	0	-0.001	0.004	15.389	0.012	0.012	0.000	0.000	0.000	0.000
128	A	1132	MET	0	0.010	0.023	17.192	0.008	0.008	0.000	0.000	0.000	0.000
129	A	1133	GLU	-1	-0.872	-0.919	19.045	-0.060	-0.060	0.000	0.000	0.000	0.000
130	A	1134	LEU	0	-0.007	0.001	19.976	0.013	0.013	0.000	0.000	0.000	0.000
131	A	1135	VAL	0	0.017	0.007	23.062	-0.012	-0.012	0.000	0.000	0.000	0.000
132	A	1136	PHE	0	0.026	-0.002	23.128	0.007	0.007	0.000	0.000	0.000	0.000
133	A	1137	ASP	-1	-0.851	-0.905	28.395	0.000	0.000	0.000	0.000	0.000	0.000
134	A	1138	VAL	0	0.001	-0.009	29.661	0.004	0.004	0.000	0.000	0.000	0.000
135	A	1139	GLN	0	-0.023	-0.027	32.807	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	1140	ASN	0	-0.074	-0.042	36.566	0.001	0.001	0.000	0.000	0.000	0.000
137	A	1141	LYS	1	0.802	0.912	32.930	-0.020	-0.020	0.000	0.000	0.000	0.000
138	A	1142	LYS	1	0.978	0.986	35.247	-0.020	-0.020	0.000	0.000	0.000	0.000
139	A	1143	ASP	-1	-0.779	-0.898	31.998	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	1144	TYR	0	0.048	0.011	30.937	0.000	0.000	0.000	0.000	0.000	0.000
141	A	1145	GLU	-1	-0.777	-0.867	30.960	0.026	0.026	0.000	0.000	0.000	0.000
142	A	1146	ILE	0	-0.023	-0.010	27.690	0.004	0.004	0.000	0.000	0.000	0.000
143	A	1147	LEU	0	-0.017	-0.017	26.557	0.002	0.002	0.000	0.000	0.000	0.000
144	A	1148	GLU	-1	-0.869	-0.915	26.072	0.054	0.054	0.000	0.000	0.000	0.000
145	A	1149	GLY	0	0.019	0.007	26.596	0.008	0.008	0.000	0.000	0.000	0.000
146	A	1150	LEU	0	-0.031	-0.017	22.396	0.008	0.008	0.000	0.000	0.000	0.000
147	A	1151	LEU	0	-0.001	0.010	21.970	0.008	0.008	0.000	0.000	0.000	0.000
148	A	1152	ILE	0	0.020	0.012	21.963	0.014	0.014	0.000	0.000	0.000	0.000
149	A	1153	PHE	0	-0.025	-0.025	18.462	0.017	0.017	0.000	0.000	0.000	0.000
150	A	1154	GLY	0	0.008	-0.010	18.253	0.017	0.017	0.000	0.000	0.000	0.000
151	A	1155	GLU	-1	-0.889	-0.924	17.700	0.151	0.151	0.000	0.000	0.000	0.000
152	A	1156	SER	0	-0.006	0.002	19.190	0.025	0.025	0.000	0.000	0.000	0.000
153	A	1157	LEU	0	-0.018	-0.022	15.177	0.023	0.023	0.000	0.000	0.000	0.000
154	A	1158	LEU	0	-0.026	-0.032	12.524	0.049	0.049	0.000	0.000	0.000	0.000
155	A	1159	GLU	-1	-0.928	-0.944	14.734	0.283	0.283	0.000	0.000	0.000	0.000
156	A	1160	ILE	0	-0.037	-0.015	15.974	0.036	0.036	0.000	0.000	0.000	0.000
157	A	1161	LYS	1	0.827	0.910	8.320	-0.731	-0.731	0.000	0.000	0.000	0.000
158	A	1162	GLU	-1	-0.856	-0.928	11.658	0.744	0.744	0.000	0.000	0.000	0.000
159	A	1163	SER	0	-0.094	-0.040	13.428	0.007	0.007	0.000	0.000	0.000	0.000
160	A	1164	LYS	1	0.758	0.889	12.489	-0.504	-0.504	0.000	0.000	0.000	0.000
161	A	1165	GLU	-1	-0.968	-0.973	10.493	0.623	0.623	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1005:SER)