FMO DATABASE

FMODB ID: LJYJ9

Calculation Name: 2QSR-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

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:

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	161
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1690892.125371
FMO2-HF: Nuclear repulsion	1626037.997101
FMO2-HF: Total energy	-64854.128271
FMO2-MP2: Total energy	-65048.266272

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: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.
-0.052	2.996	0.003	-1.605	-1.447	0.005

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 : 0.082 / q_NPA : 0.036

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	0.740	0.818	3.655	-0.006	2.825	0.004	-1.580	-1.255	0.005
4	A	1008	THR	0	0.013	0.002	4.349	-0.078	0.139	-0.001	-0.025	-0.192	0.000
5	A	1009	LYS	1	0.847	0.928	6.252	0.190	0.190	0.000	0.000	0.000	0.000
6	A	1010	GLY	0	0.055	0.022	8.218	-0.376	-0.376	0.000	0.000	0.000	0.000
7	A	1011	ASN	0	-0.071	-0.048	10.207	0.120	0.120	0.000	0.000	0.000	0.000
8	A	1012	ALA	0	0.027	0.036	13.708	-0.018	-0.018	0.000	0.000	0.000	0.000
9	A	1013	GLU	-1	-0.906	-0.958	16.082	-0.107	-0.107	0.000	0.000	0.000	0.000
10	A	1014	LEU	0	0.023	-0.010	19.227	0.012	0.012	0.000	0.000	0.000	0.000
11	A	1015	ILE	0	-0.002	0.009	22.274	0.007	0.007	0.000	0.000	0.000	0.000
12	A	1016	LEU	0	0.028	-0.002	23.539	0.004	0.004	0.000	0.000	0.000	0.000
13	A	1017	GLN	0	-0.068	-0.036	27.296	0.009	0.009	0.000	0.000	0.000	0.000
14	A	1018	ILE	0	0.023	0.023	28.886	0.004	0.004	0.000	0.000	0.000	0.000
15	A	1019	ASP	-1	-0.913	-0.947	31.177	-0.014	-0.014	0.000	0.000	0.000	0.000
16	A	1020	ALA	0	-0.006	-0.020	29.793	0.005	0.005	0.000	0.000	0.000	0.000
17	A	1021	TYR	0	-0.037	-0.030	31.077	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	1022	LEU	0	0.052	0.020	31.337	0.004	0.004	0.000	0.000	0.000	0.000
19	A	1023	PRO	0	-0.003	-0.002	34.945	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	1024	ASP	-1	-0.853	-0.923	38.743	-0.006	-0.006	0.000	0.000	0.000	0.000
21	A	1025	THR	0	-0.048	-0.037	41.191	0.000	0.000	0.000	0.000	0.000	0.000
22	A	1026	TYR	0	-0.027	-0.015	35.402	0.000	0.000	0.000	0.000	0.000	0.000
23	A	1027	ILE	0	0.033	0.018	34.536	0.001	0.001	0.000	0.000	0.000	0.000
24	A	1028	SER	0	0.020	0.016	38.684	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	1029	ASP	-1	-0.829	-0.905	39.105	-0.004	-0.004	0.000	0.000	0.000	0.000
26	A	1030	GLN	0	0.070	0.028	37.186	0.001	0.001	0.000	0.000	0.000	0.000
27	A	1031	ARG	1	0.849	0.908	35.052	-0.001	-0.001	0.000	0.000	0.000	0.000
28	A	1032	HIS	0	0.065	0.032	33.833	-0.001	-0.001	0.000	0.000	0.000	0.000
29	A	1033	LYS	1	0.819	0.912	33.260	0.008	0.008	0.000	0.000	0.000	0.000
30	A	1034	ILE	0	-0.041	-0.017	30.333	-0.001	-0.001	0.000	0.000	0.000	0.000
31	A	1035	GLU	-1	-0.852	-0.890	29.402	0.017	0.017	0.000	0.000	0.000	0.000
32	A	1036	ILE	0	0.079	0.038	28.555	0.002	0.002	0.000	0.000	0.000	0.000
33	A	1037	TYR	0	0.015	0.003	28.065	0.002	0.002	0.000	0.000	0.000	0.000
34	A	1038	LYS	1	0.880	0.944	24.079	0.023	0.023	0.000	0.000	0.000	0.000
35	A	1039	LYS	1	0.806	0.872	23.998	-0.035	-0.035	0.000	0.000	0.000	0.000
36	A	1040	ILE	0	0.060	0.028	24.025	0.008	0.008	0.000	0.000	0.000	0.000
37	A	1041	ARG	1	0.895	0.947	21.440	0.059	0.059	0.000	0.000	0.000	0.000
38	A	1042	GLN	0	-0.080	-0.031	19.315	-0.021	-0.021	0.000	0.000	0.000	0.000
39	A	1043	ILE	0	0.007	0.015	19.948	0.023	0.023	0.000	0.000	0.000	0.000
40	A	1044	ASP	-1	-0.847	-0.910	14.036	0.257	0.257	0.000	0.000	0.000	0.000
41	A	1045	ASN	0	-0.036	-0.033	16.137	0.023	0.023	0.000	0.000	0.000	0.000
42	A	1046	ARG	1	0.897	0.941	18.544	-0.143	-0.143	0.000	0.000	0.000	0.000
43	A	1047	VAL	0	0.035	0.026	21.065	-0.014	-0.014	0.000	0.000	0.000	0.000
44	A	1048	ASN	0	0.015	0.009	19.213	0.001	0.001	0.000	0.000	0.000	0.000
45	A	1049	TYR	0	-0.059	-0.064	23.092	-0.014	-0.014	0.000	0.000	0.000	0.000
46	A	1050	GLU	-1	-0.848	-0.920	25.121	0.105	0.105	0.000	0.000	0.000	0.000
47	A	1051	GLU	-1	-0.924	-0.968	24.770	0.107	0.107	0.000	0.000	0.000	0.000
48	A	1052	LEU	0	-0.034	-0.020	26.317	-0.010	-0.010	0.000	0.000	0.000	0.000
49	A	1053	GLN	0	-0.019	-0.018	28.684	-0.004	-0.004	0.000	0.000	0.000	0.000
50	A	1054	GLU	-1	-0.895	-0.936	31.185	0.055	0.055	0.000	0.000	0.000	0.000
51	A	1055	GLU	-1	-0.821	-0.883	30.178	0.035	0.035	0.000	0.000	0.000	0.000
52	A	1056	LEU	0	-0.073	-0.049	31.029	-0.006	-0.006	0.000	0.000	0.000	0.000
53	A	1057	ILE	0	0.029	0.009	34.297	-0.004	-0.004	0.000	0.000	0.000	0.000
54	A	1058	ASP	-1	-0.972	-0.973	36.197	0.035	0.035	0.000	0.000	0.000	0.000
55	A	1059	ARG	1	0.764	0.844	32.361	-0.028	-0.028	0.000	0.000	0.000	0.000
56	A	1060	PHE	0	-0.092	-0.057	34.822	-0.005	-0.005	0.000	0.000	0.000	0.000
57	A	1061	GLY	0	0.016	0.036	39.228	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	1062	GLU	-1	-0.919	-0.958	38.403	0.036	0.036	0.000	0.000	0.000	0.000
59	A	1063	TYR	0	-0.010	0.003	33.378	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	1064	PRO	0	-0.015	-0.007	37.409	0.000	0.000	0.000	0.000	0.000	0.000
61	A	1065	ASP	-1	-0.844	-0.937	36.161	0.020	0.020	0.000	0.000	0.000	0.000
62	A	1066	VAL	0	-0.038	-0.015	34.300	0.001	0.001	0.000	0.000	0.000	0.000
63	A	1067	VAL	0	-0.004	-0.002	32.508	-0.003	-0.003	0.000	0.000	0.000	0.000
64	A	1068	ALA	0	0.014	0.020	31.196	0.002	0.002	0.000	0.000	0.000	0.000
65	A	1069	TYR	0	0.031	-0.005	30.165	0.005	0.005	0.000	0.000	0.000	0.000
66	A	1070	LEU	0	-0.032	-0.005	26.897	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	1071	LEU	0	-0.003	0.004	26.532	-0.001	-0.001	0.000	0.000	0.000	0.000
68	A	1072	GLU	-1	-0.819	-0.886	25.394	0.068	0.068	0.000	0.000	0.000	0.000
69	A	1073	ILE	0	-0.025	-0.025	23.971	0.004	0.004	0.000	0.000	0.000	0.000
70	A	1074	GLY	0	0.007	0.009	22.132	-0.006	-0.006	0.000	0.000	0.000	0.000
71	A	1075	LEU	0	0.017	0.023	20.682	0.006	0.006	0.000	0.000	0.000	0.000
72	A	1076	VAL	0	0.011	0.014	20.252	0.014	0.014	0.000	0.000	0.000	0.000
73	A	1077	LYS	1	0.782	0.880	16.449	0.104	0.104	0.000	0.000	0.000	0.000
74	A	1078	SER	0	-0.076	-0.039	16.518	0.001	0.001	0.000	0.000	0.000	0.000
75	A	1079	TYR	0	0.000	-0.031	15.141	0.033	0.033	0.000	0.000	0.000	0.000
76	A	1080	LEU	0	0.022	-0.001	14.925	0.018	0.018	0.000	0.000	0.000	0.000
77	A	1081	ASP	-1	-0.784	-0.866	12.829	-0.114	-0.114	0.000	0.000	0.000	0.000
78	A	1082	LYS	1	0.821	0.898	10.650	-0.365	-0.365	0.000	0.000	0.000	0.000
79	A	1083	VAL	0	0.002	0.016	10.557	0.117	0.117	0.000	0.000	0.000	0.000
80	A	1084	PHE	0	-0.052	-0.029	5.795	-0.042	-0.042	0.000	0.000	0.000	0.000
81	A	1085	VAL	0	0.018	0.012	10.664	-0.029	-0.029	0.000	0.000	0.000	0.000
82	A	1086	GLN	0	-0.054	-0.033	13.617	-0.088	-0.088	0.000	0.000	0.000	0.000
83	A	1087	ARG	1	0.737	0.832	14.842	0.077	0.077	0.000	0.000	0.000	0.000
84	A	1088	VAL	0	0.022	0.018	18.622	0.018	0.018	0.000	0.000	0.000	0.000
85	A	1089	GLU	-1	-0.841	-0.894	21.552	-0.068	-0.068	0.000	0.000	0.000	0.000
86	A	1090	ARG	1	0.827	0.922	25.064	0.009	0.009	0.000	0.000	0.000	0.000
87	A	1091	LYS	1	0.881	0.912	28.619	0.022	0.022	0.000	0.000	0.000	0.000
88	A	1092	ASP	-1	-0.818	-0.889	31.328	-0.016	-0.016	0.000	0.000	0.000	0.000
89	A	1093	ASN	0	-0.021	-0.017	34.001	0.002	0.002	0.000	0.000	0.000	0.000
90	A	1094	LYS	1	0.875	0.937	30.017	0.001	0.001	0.000	0.000	0.000	0.000
91	A	1095	ILE	0	0.025	0.013	25.081	-0.005	-0.005	0.000	0.000	0.000	0.000
92	A	1096	THR	0	-0.021	-0.002	24.038	0.010	0.010	0.000	0.000	0.000	0.000
93	A	1097	ILE	0	0.031	0.023	18.349	-0.010	-0.010	0.000	0.000	0.000	0.000
94	A	1098	GLN	0	0.006	0.007	18.487	-0.001	-0.001	0.000	0.000	0.000	0.000
95	A	1099	PHE	0	0.066	0.022	13.470	-0.019	-0.019	0.000	0.000	0.000	0.000
96	A	1100	GLU	-1	-0.744	-0.833	8.338	-0.870	-0.870	0.000	0.000	0.000	0.000
97	A	1101	LYS	1	0.957	0.973	11.419	0.237	0.237	0.000	0.000	0.000	0.000
98	A	1102	VAL	0	0.002	0.008	5.202	0.108	0.108	0.000	0.000	0.000	0.000
99	A	1103	THR	0	0.033	0.012	8.182	0.268	0.268	0.000	0.000	0.000	0.000
100	A	1104	GLN	0	-0.015	-0.007	10.734	0.029	0.029	0.000	0.000	0.000	0.000
101	A	1105	ARG	1	0.865	0.929	7.873	-0.866	-0.866	0.000	0.000	0.000	0.000
102	A	1106	LEU	0	-0.017	0.005	7.089	0.144	0.144	0.000	0.000	0.000	0.000
103	A	1107	PHE	0	0.002	0.014	10.910	-0.011	-0.011	0.000	0.000	0.000	0.000
104	A	1108	LEU	0	0.001	0.001	14.520	-0.023	-0.023	0.000	0.000	0.000	0.000
105	A	1109	ALA	0	0.066	0.021	17.860	-0.007	-0.007	0.000	0.000	0.000	0.000
106	A	1110	GLN	0	0.009	-0.010	20.162	-0.026	-0.026	0.000	0.000	0.000	0.000
107	A	1111	ASP	-1	-0.824	-0.900	16.946	0.287	0.287	0.000	0.000	0.000	0.000
108	A	1112	TYR	0	0.066	0.020	14.990	0.004	0.004	0.000	0.000	0.000	0.000
109	A	1113	PHE	0	0.016	0.008	20.235	-0.011	-0.011	0.000	0.000	0.000	0.000
110	A	1114	LYS	1	0.940	0.981	22.593	-0.160	-0.160	0.000	0.000	0.000	0.000
111	A	1115	ALA	0	0.041	0.025	20.478	-0.006	-0.006	0.000	0.000	0.000	0.000
112	A	1116	LEU	0	-0.023	-0.014	22.581	-0.011	-0.011	0.000	0.000	0.000	0.000
113	A	1117	SER	0	-0.075	-0.053	25.179	-0.009	-0.009	0.000	0.000	0.000	0.000
114	A	1118	VAL	0	-0.068	-0.028	24.998	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	1119	THR	0	-0.016	0.010	25.621	-0.003	-0.003	0.000	0.000	0.000	0.000
116	A	1120	ASN	0	-0.028	-0.033	28.745	-0.004	-0.004	0.000	0.000	0.000	0.000
117	A	1121	LEU	0	-0.049	-0.016	28.584	-0.007	-0.007	0.000	0.000	0.000	0.000
118	A	1122	LYS	1	0.883	0.939	29.548	-0.022	-0.022	0.000	0.000	0.000	0.000
119	A	1123	ALA	0	0.006	-0.012	26.807	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	1124	GLY	0	-0.014	-0.002	27.423	0.003	0.003	0.000	0.000	0.000	0.000
121	A	1125	ILE	0	-0.016	-0.004	22.074	0.000	0.000	0.000	0.000	0.000	0.000
122	A	1126	ALA	0	-0.007	-0.004	24.132	-0.002	-0.002	0.000	0.000	0.000	0.000
123	A	1127	GLU	-1	-0.840	-0.929	21.690	0.031	0.031	0.000	0.000	0.000	0.000
124	A	1128	ASN	0	-0.059	-0.040	22.667	-0.012	-0.012	0.000	0.000	0.000	0.000
125	A	1129	LYS	1	0.902	0.940	22.022	0.074	0.074	0.000	0.000	0.000	0.000
126	A	1130	GLY	0	-0.015	0.002	21.797	-0.010	-0.010	0.000	0.000	0.000	0.000
127	A	1131	LEU	0	-0.045	-0.024	15.092	0.005	0.005	0.000	0.000	0.000	0.000
128	A	1132	MET	0	0.004	0.017	16.923	0.003	0.003	0.000	0.000	0.000	0.000
129	A	1133	GLU	-1	-0.855	-0.894	18.822	-0.051	-0.051	0.000	0.000	0.000	0.000
130	A	1134	LEU	0	-0.020	-0.008	19.838	0.012	0.012	0.000	0.000	0.000	0.000
131	A	1135	VAL	0	-0.024	-0.010	22.782	-0.010	-0.010	0.000	0.000	0.000	0.000
132	A	1136	PHE	0	0.057	0.015	23.166	0.006	0.006	0.000	0.000	0.000	0.000
133	A	1137	ASP	-1	-0.852	-0.911	28.457	0.007	0.007	0.000	0.000	0.000	0.000
134	A	1138	VAL	0	0.016	0.004	30.185	0.004	0.004	0.000	0.000	0.000	0.000
135	A	1139	GLN	0	-0.041	-0.038	33.239	-0.003	-0.003	0.000	0.000	0.000	0.000
136	A	1140	ASN	0	-0.057	-0.031	36.974	0.001	0.001	0.000	0.000	0.000	0.000
137	A	1141	LYS	1	0.816	0.926	33.142	-0.029	-0.029	0.000	0.000	0.000	0.000
138	A	1142	LYS	1	0.915	0.931	35.597	-0.030	-0.030	0.000	0.000	0.000	0.000
139	A	1143	ASP	-1	-0.775	-0.895	32.542	0.011	0.011	0.000	0.000	0.000	0.000
140	A	1144	TYR	0	0.092	0.042	31.391	0.000	0.000	0.000	0.000	0.000	0.000
141	A	1145	GLU	-1	-0.771	-0.852	31.453	0.035	0.035	0.000	0.000	0.000	0.000
142	A	1146	ILE	0	-0.036	-0.014	28.174	0.004	0.004	0.000	0.000	0.000	0.000
143	A	1147	LEU	0	-0.022	-0.008	27.055	0.002	0.002	0.000	0.000	0.000	0.000
144	A	1148	GLU	-1	-0.857	-0.909	26.614	0.065	0.065	0.000	0.000	0.000	0.000
145	A	1149	GLY	0	0.013	0.000	27.067	0.009	0.009	0.000	0.000	0.000	0.000
146	A	1150	LEU	0	-0.019	-0.025	22.842	0.007	0.007	0.000	0.000	0.000	0.000
147	A	1151	LEU	0	-0.012	0.011	22.266	0.009	0.009	0.000	0.000	0.000	0.000
148	A	1152	ILE	0	0.018	0.016	22.429	0.016	0.016	0.000	0.000	0.000	0.000
149	A	1153	PHE	0	-0.017	-0.012	18.902	0.016	0.016	0.000	0.000	0.000	0.000
150	A	1154	GLY	0	0.005	-0.002	18.695	0.017	0.017	0.000	0.000	0.000	0.000
151	A	1155	GLU	-1	-0.832	-0.899	18.045	0.170	0.170	0.000	0.000	0.000	0.000
152	A	1156	SER	0	-0.026	-0.014	19.099	0.024	0.024	0.000	0.000	0.000	0.000
153	A	1157	LEU	0	-0.030	-0.031	15.735	0.023	0.023	0.000	0.000	0.000	0.000
154	A	1158	LEU	0	-0.043	-0.020	12.778	0.048	0.048	0.000	0.000	0.000	0.000
155	A	1159	GLU	-1	-0.854	-0.918	14.866	0.279	0.279	0.000	0.000	0.000	0.000
156	A	1160	ILE	0	-0.058	-0.029	16.432	0.037	0.037	0.000	0.000	0.000	0.000
157	A	1161	LYS	1	0.759	0.876	8.190	-0.828	-0.828	0.000	0.000	0.000	0.000
158	A	1162	GLU	-1	-0.773	-0.884	11.137	0.865	0.865	0.000	0.000	0.000	0.000
159	A	1163	SER	0	-0.097	-0.041	13.319	-0.011	-0.011	0.000	0.000	0.000	0.000
160	A	1164	LYS	1	0.751	0.872	12.257	-0.519	-0.519	0.000	0.000	0.000	0.000
161	A	1165	GLU	-1	-0.966	-0.965	10.908	0.631	0.631	0.000	0.000	0.000	0.000

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