FMO DATABASE

FMODB ID: Q833Y

Calculation Name: 2QSR-A-Xray311

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: 2021-09-06

Reference: C. Watanabe, S. Koyama, K. Kamisaka, D. Takaya, T. Honma et. al., Interaction energy analysis of Apo structure dataset on FMODB, To be pubulished.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 1.20200116

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	163
LigandCharge
Software	ABINIT-MP - Open Ver.1 Rev. 15 / 20190524

Total energy (hartree)

FMO2-HF: Electronic energy	-1697088.919514
FMO2-HF: Nuclear repulsion	1632066.287749
FMO2-HF: Total energy	-65022.631765
FMO2-MP2: Total energy	-65217.514085

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:1004:ACE )

Summations of interaction energy for fragment #1(A:1004:ACE )

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.
-0.426	0.572	-0.001	-0.448	-0.55	0

Interaction energy analysis for fragmet #1(A:1004:ACE )

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.001 / q_NPA : -0.012

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].
3	A	1006	LEU	0	0.006	0.027	3.840	1.035	1.793	-0.006	-0.359	-0.393
4	A	1007	ARG	1	0.832	0.908	4.372	-0.602	-0.449	0.000	-0.025	-0.129
5	A	1008	THR	0	-0.007	-0.002	5.113	-0.392	-0.458	0.000	-0.005	0.071
6	A	1009	LYS	1	0.925	0.980	7.771	0.114	0.114	0.000	0.000	0.000
7	A	1010	GLY	0	0.005	-0.012	8.259	0.067	0.067	0.000	0.000	0.000
8	A	1011	ASN	0	-0.056	-0.023	9.181	-0.091	-0.091	0.000	0.000	0.000
9	A	1012	ALA	0	0.029	0.023	12.815	0.027	0.027	0.000	0.000	0.000
10	A	1013	GLU	-1	-0.917	-0.965	15.003	0.118	0.118	0.000	0.000	0.000
11	A	1014	LEU	0	-0.011	-0.017	18.233	0.005	0.005	0.000	0.000	0.000
12	A	1015	ILE	0	0.002	0.010	21.130	-0.011	-0.011	0.000	0.000	0.000
13	A	1016	LEU	0	0.031	-0.007	22.639	0.002	0.002	0.000	0.000	0.000
14	A	1017	GLN	0	-0.056	-0.030	26.365	-0.005	-0.005	0.000	0.000	0.000
15	A	1018	ILE	0	0.015	0.035	28.075	-0.002	-0.002	0.000	0.000	0.000
16	A	1019	ASP	-1	-0.927	-0.957	29.997	0.031	0.031	0.000	0.000	0.000
17	A	1020	ALA	0	-0.009	-0.017	28.915	-0.004	-0.004	0.000	0.000	0.000
18	A	1021	TYR	0	-0.048	-0.041	30.436	0.001	0.001	0.000	0.000	0.000
19	A	1022	LEU	0	0.025	0.009	31.142	-0.002	-0.002	0.000	0.000	0.000
20	A	1023	PRO	0	-0.001	-0.006	34.245	0.001	0.001	0.000	0.000	0.000
21	A	1024	ASP	-1	-0.879	-0.948	37.928	0.003	0.003	0.000	0.000	0.000
22	A	1025	THR	0	-0.066	-0.043	40.568	-0.001	-0.001	0.000	0.000	0.000
23	A	1026	TYR	0	-0.045	-0.014	35.371	-0.001	-0.001	0.000	0.000	0.000
24	A	1027	ILE	0	0.010	0.006	34.918	-0.002	-0.002	0.000	0.000	0.000
25	A	1028	SER	0	0.027	0.013	38.928	0.001	0.001	0.000	0.000	0.000
26	A	1029	ASP	-1	-0.913	-0.963	39.792	-0.009	-0.009	0.000	0.000	0.000
27	A	1030	GLN	0	0.075	0.021	37.248	-0.001	-0.001	0.000	0.000	0.000
28	A	1031	ARG	1	0.955	0.953	35.282	0.014	0.014	0.000	0.000	0.000
29	A	1032	HIS	0	0.060	0.055	34.186	-0.001	-0.001	0.000	0.000	0.000
30	A	1033	LYS	1	0.930	1.000	33.213	-0.003	-0.003	0.000	0.000	0.000
31	A	1034	ILE	0	-0.037	-0.008	30.551	0.000	0.000	0.000	0.000	0.000
32	A	1035	GLU	-1	-0.882	-0.920	29.577	-0.028	-0.028	0.000	0.000	0.000
33	A	1036	ILE	0	0.047	0.008	28.801	-0.003	-0.003	0.000	0.000	0.000
34	A	1037	TYR	0	0.044	0.021	27.997	0.000	0.000	0.000	0.000	0.000
35	A	1038	LYS	1	0.890	0.948	24.321	0.031	0.031	0.000	0.000	0.000
36	A	1039	LYS	1	0.902	0.928	24.188	0.040	0.040	0.000	0.000	0.000
37	A	1040	ILE	0	0.050	0.034	24.372	-0.006	-0.006	0.000	0.000	0.000
38	A	1041	ARG	1	0.851	0.929	21.138	-0.018	-0.018	0.000	0.000	0.000
39	A	1042	GLN	0	-0.028	-0.002	19.885	-0.005	-0.005	0.000	0.000	0.000
40	A	1043	ILE	0	-0.057	-0.020	20.291	-0.017	-0.017	0.000	0.000	0.000
41	A	1044	ASP	-1	-0.915	-0.962	15.137	-0.175	-0.175	0.000	0.000	0.000
42	A	1045	ASN	0	-0.032	-0.037	16.950	0.000	0.000	0.000	0.000	0.000
43	A	1046	ARG	1	0.988	0.992	19.396	0.048	0.048	0.000	0.000	0.000
44	A	1047	VAL	0	0.073	0.041	22.803	0.007	0.007	0.000	0.000	0.000
45	A	1048	ASN	0	0.000	0.022	20.619	0.002	0.002	0.000	0.000	0.000
46	A	1049	TYR	0	0.000	-0.030	23.826	0.005	0.005	0.000	0.000	0.000
47	A	1050	GLU	-1	-0.897	-0.947	25.597	-0.045	-0.045	0.000	0.000	0.000
48	A	1051	GLU	-1	-0.909	-0.957	26.899	-0.068	-0.068	0.000	0.000	0.000
49	A	1052	LEU	0	-0.073	-0.035	26.424	0.004	0.004	0.000	0.000	0.000
50	A	1053	GLN	0	-0.025	-0.016	29.405	0.002	0.002	0.000	0.000	0.000
51	A	1054	GLU	-1	-0.894	-0.938	31.855	-0.032	-0.032	0.000	0.000	0.000
52	A	1055	GLU	-1	-0.859	-0.942	31.255	-0.036	-0.036	0.000	0.000	0.000
53	A	1056	LEU	0	-0.084	-0.054	31.501	0.003	0.003	0.000	0.000	0.000
54	A	1057	ILE	0	0.050	0.019	34.993	0.002	0.002	0.000	0.000	0.000
55	A	1058	ASP	-1	-0.959	-0.959	36.972	-0.027	-0.027	0.000	0.000	0.000
56	A	1059	ARG	1	0.759	0.858	33.568	0.028	0.028	0.000	0.000	0.000
57	A	1060	PHE	0	-0.135	-0.078	35.742	0.002	0.002	0.000	0.000	0.000
58	A	1061	GLY	0	-0.004	0.019	39.857	0.002	0.002	0.000	0.000	0.000
59	A	1062	GLU	-1	-0.882	-0.952	38.757	-0.012	-0.012	0.000	0.000	0.000
60	A	1063	TYR	0	-0.022	-0.001	32.908	0.001	0.001	0.000	0.000	0.000
61	A	1064	PRO	0	-0.014	-0.007	37.175	0.001	0.001	0.000	0.000	0.000
62	A	1065	ASP	-1	-0.814	-0.924	35.544	0.005	0.005	0.000	0.000	0.000
63	A	1066	VAL	0	-0.039	-0.017	33.631	0.001	0.001	0.000	0.000	0.000
64	A	1067	VAL	0	-0.015	-0.008	32.105	0.001	0.001	0.000	0.000	0.000
65	A	1068	ALA	0	0.035	0.021	30.908	-0.001	-0.001	0.000	0.000	0.000
66	A	1069	TYR	0	0.022	0.004	29.424	-0.001	-0.001	0.000	0.000	0.000
67	A	1070	LEU	0	-0.057	-0.009	26.622	0.002	0.002	0.000	0.000	0.000
68	A	1071	LEU	0	-0.014	-0.009	26.100	0.000	0.000	0.000	0.000	0.000
69	A	1072	GLU	-1	-0.854	-0.912	25.177	-0.007	-0.007	0.000	0.000	0.000
70	A	1073	ILE	0	-0.030	-0.028	22.606	0.001	0.001	0.000	0.000	0.000
71	A	1074	GLY	0	0.002	0.010	21.719	0.005	0.005	0.000	0.000	0.000
72	A	1075	LEU	0	0.039	0.028	20.321	-0.005	-0.005	0.000	0.000	0.000
73	A	1076	VAL	0	0.033	0.043	19.633	-0.003	-0.003	0.000	0.000	0.000
74	A	1077	LYS	1	0.787	0.866	15.604	-0.054	-0.054	0.000	0.000	0.000
75	A	1078	SER	0	-0.076	-0.057	15.915	0.005	0.005	0.000	0.000	0.000
76	A	1079	TYR	0	0.051	0.015	14.488	-0.019	-0.019	0.000	0.000	0.000
77	A	1080	LEU	0	0.007	-0.001	13.749	0.014	0.014	0.000	0.000	0.000
78	A	1081	ASP	-1	-0.805	-0.881	12.041	0.111	0.111	0.000	0.000	0.000
79	A	1082	LYS	1	0.930	0.977	9.935	0.198	0.198	0.000	0.000	0.000
80	A	1083	VAL	0	-0.031	-0.001	9.145	-0.029	-0.029	0.000	0.000	0.000
81	A	1084	PHE	0	-0.103	-0.057	4.973	0.223	0.223	0.000	0.000	0.000
82	A	1085	VAL	0	0.023	0.009	9.212	0.093	0.093	0.000	0.000	0.000
83	A	1086	GLN	0	-0.033	-0.024	12.228	0.065	0.065	0.000	0.000	0.000
84	A	1087	ARG	1	0.885	0.941	13.529	-0.197	-0.197	0.000	0.000	0.000
85	A	1088	VAL	0	0.011	0.019	17.271	0.004	0.004	0.000	0.000	0.000
86	A	1089	GLU	-1	-0.909	-0.956	20.124	0.107	0.107	0.000	0.000	0.000
87	A	1090	ARG	1	0.927	0.963	23.469	-0.050	-0.050	0.000	0.000	0.000
88	A	1091	LYS	1	0.939	0.969	26.864	-0.077	-0.077	0.000	0.000	0.000
89	A	1092	ASP	-1	-0.905	-0.957	29.392	0.063	0.063	0.000	0.000	0.000
90	A	1093	ASN	0	-0.025	-0.026	32.175	0.001	0.001	0.000	0.000	0.000
91	A	1094	LYS	1	0.952	0.988	27.943	-0.071	-0.071	0.000	0.000	0.000
92	A	1095	ILE	0	0.032	0.027	23.448	0.004	0.004	0.000	0.000	0.000
93	A	1096	THR	0	-0.037	-0.020	22.105	0.003	0.003	0.000	0.000	0.000
94	A	1097	ILE	0	-0.008	0.015	16.934	0.006	0.006	0.000	0.000	0.000
95	A	1098	GLN	0	0.008	0.004	16.609	0.001	0.001	0.000	0.000	0.000
96	A	1099	PHE	0	0.052	0.026	11.587	-0.005	-0.005	0.000	0.000	0.000
97	A	1100	GLU	-1	-0.809	-0.904	7.892	0.838	0.838	0.000	0.000	0.000
98	A	1101	LYS	1	0.978	0.973	9.919	-0.617	-0.617	0.000	0.000	0.000
99	A	1102	VAL	0	0.000	0.005	3.873	-0.009	0.141	0.005	-0.055	-0.101
100	A	1103	THR	0	0.021	0.017	6.527	-0.084	-0.084	0.000	0.000	0.000
101	A	1104	GLN	0	0.009	0.009	8.508	-0.124	-0.124	0.000	0.000	0.000
102	A	1105	ARG	1	0.860	0.927	5.108	-0.506	-0.506	0.000	0.000	0.000
103	A	1106	LEU	0	-0.044	-0.018	4.678	-0.179	-0.176	0.000	-0.004	0.002
104	A	1107	PHE	0	-0.039	-0.018	8.415	-0.096	-0.096	0.000	0.000	0.000
105	A	1108	LEU	0	-0.005	0.000	11.922	0.037	0.037	0.000	0.000	0.000
106	A	1109	ALA	0	0.073	0.022	15.134	-0.008	-0.008	0.000	0.000	0.000
107	A	1110	GLN	0	-0.002	-0.013	18.211	0.001	0.001	0.000	0.000	0.000
108	A	1111	ASP	-1	-0.822	-0.906	14.356	0.075	0.075	0.000	0.000	0.000
109	A	1112	TYR	0	0.048	0.012	12.578	-0.010	-0.010	0.000	0.000	0.000
110	A	1113	PHE	0	0.002	0.002	18.194	-0.015	-0.015	0.000	0.000	0.000
111	A	1114	LYS	1	0.955	0.976	20.322	-0.025	-0.025	0.000	0.000	0.000
112	A	1115	ALA	0	0.047	0.033	18.720	-0.008	-0.008	0.000	0.000	0.000
113	A	1116	LEU	0	0.000	-0.013	20.834	-0.005	-0.005	0.000	0.000	0.000
114	A	1117	SER	0	-0.117	-0.060	23.362	-0.008	-0.008	0.000	0.000	0.000
115	A	1118	VAL	0	-0.035	-0.003	23.312	-0.005	-0.005	0.000	0.000	0.000
116	A	1119	THR	0	-0.021	0.018	24.058	-0.003	-0.003	0.000	0.000	0.000
117	A	1120	ASN	0	0.052	0.005	26.963	0.001	0.001	0.000	0.000	0.000
118	A	1121	LEU	0	-0.078	-0.015	26.373	0.001	0.001	0.000	0.000	0.000
119	A	1122	LYS	1	0.955	0.987	28.535	-0.052	-0.052	0.000	0.000	0.000
120	A	1123	ALA	0	-0.002	-0.014	24.728	0.003	0.003	0.000	0.000	0.000
121	A	1124	GLY	0	-0.015	-0.006	25.448	-0.006	-0.006	0.000	0.000	0.000
122	A	1125	ILE	0	-0.013	-0.003	20.140	0.005	0.005	0.000	0.000	0.000
123	A	1126	ALA	0	-0.032	-0.007	22.211	-0.011	-0.011	0.000	0.000	0.000
124	A	1127	GLU	-1	-0.861	-0.941	20.144	0.210	0.210	0.000	0.000	0.000
125	A	1128	ASN	0	-0.048	-0.016	20.846	-0.013	-0.013	0.000	0.000	0.000
126	A	1129	LYS	1	0.924	0.952	20.112	-0.170	-0.170	0.000	0.000	0.000
127	A	1130	GLY	0	-0.034	-0.014	19.224	0.028	0.028	0.000	0.000	0.000
128	A	1131	LEU	0	0.006	0.005	13.158	0.024	0.024	0.000	0.000	0.000
129	A	1132	MET	0	0.003	0.017	14.788	-0.041	-0.041	0.000	0.000	0.000
130	A	1133	GLU	-1	-0.899	-0.960	17.001	0.214	0.214	0.000	0.000	0.000
131	A	1134	LEU	0	-0.003	0.003	18.148	-0.019	-0.019	0.000	0.000	0.000
132	A	1135	VAL	0	0.010	-0.002	21.277	-0.001	-0.001	0.000	0.000	0.000
133	A	1136	PHE	0	0.011	-0.005	21.776	-0.008	-0.008	0.000	0.000	0.000
134	A	1137	ASP	-1	-0.962	-0.996	26.822	0.053	0.053	0.000	0.000	0.000
135	A	1138	VAL	0	-0.003	-0.001	28.523	-0.003	-0.003	0.000	0.000	0.000
136	A	1139	GLN	0	-0.002	-0.011	31.423	-0.006	-0.006	0.000	0.000	0.000
137	A	1140	ASN	0	-0.083	-0.044	35.165	-0.001	-0.001	0.000	0.000	0.000
138	A	1141	LYS	1	0.890	0.966	32.014	-0.035	-0.035	0.000	0.000	0.000
139	A	1142	LYS	1	0.964	0.975	34.158	-0.016	-0.016	0.000	0.000	0.000
140	A	1143	ASP	-1	-0.785	-0.907	31.267	0.032	0.032	0.000	0.000	0.000
141	A	1144	TYR	0	0.036	0.002	30.116	0.002	0.002	0.000	0.000	0.000
142	A	1145	GLU	-1	-0.836	-0.906	30.225	0.023	0.023	0.000	0.000	0.000
143	A	1146	ILE	0	-0.041	-0.021	26.526	0.003	0.003	0.000	0.000	0.000
144	A	1147	LEU	0	-0.023	-0.018	25.207	0.005	0.005	0.000	0.000	0.000
145	A	1148	GLU	-1	-0.887	-0.932	25.351	0.009	0.009	0.000	0.000	0.000
146	A	1149	GLY	0	-0.001	-0.005	25.792	-0.001	-0.001	0.000	0.000	0.000
147	A	1150	LEU	0	-0.044	-0.024	21.327	0.005	0.005	0.000	0.000	0.000
148	A	1151	LEU	0	0.018	0.011	21.087	0.003	0.003	0.000	0.000	0.000
149	A	1152	ILE	0	0.024	0.019	21.287	-0.002	-0.002	0.000	0.000	0.000
150	A	1153	PHE	0	-0.037	-0.033	17.080	0.002	0.002	0.000	0.000	0.000
151	A	1154	GLY	0	0.003	-0.014	17.316	0.006	0.006	0.000	0.000	0.000
152	A	1155	GLU	-1	-0.951	-0.975	16.938	-0.031	-0.031	0.000	0.000	0.000
153	A	1156	SER	0	0.009	0.007	18.519	-0.012	-0.012	0.000	0.000	0.000
154	A	1157	LEU	0	-0.043	-0.031	13.790	-0.002	-0.002	0.000	0.000	0.000
155	A	1158	LEU	0	-0.038	-0.039	12.450	-0.003	-0.003	0.000	0.000	0.000
156	A	1159	GLU	-1	-0.906	-0.939	14.071	-0.090	-0.090	0.000	0.000	0.000
157	A	1160	ILE	0	-0.027	-0.002	14.147	-0.017	-0.017	0.000	0.000	0.000
158	A	1161	LYS	1	0.884	0.943	6.908	0.428	0.428	0.000	0.000	0.000
159	A	1162	GLU	-1	-0.929	-0.966	11.618	-0.313	-0.313	0.000	0.000	0.000
160	A	1163	SER	0	-0.096	-0.045	13.305	-0.015	-0.015	0.000	0.000	0.000
161	A	1164	LYS	1	0.814	0.928	11.099	0.026	0.026	0.000	0.000	0.000
162	A	1165	GLU	-1	-0.909	-0.959	11.302	-0.312	-0.312	0.000	0.000	0.000
163	A	1166	NME	0	-0.069	-0.018	10.284	0.030	0.030	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1004:ACE )