FMO DATABASE

FMODB ID: J3N39

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	OptH
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	-1689476.023427
FMO2-HF: Nuclear repulsion	1624624.276251
FMO2-HF: Total energy	-64851.747176
FMO2-MP2: Total energy	-65046.108211

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.
-1.903	2.661	-0.015	-2.009	-2.539	0.009

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 : 0.075 / q_NPA : 0.035

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	0.828	0.904	2.998	-0.994	3.058	-0.020	-1.828	-2.204	0.010
4	A	1008	THR	0	-0.010	-0.004	3.852	-0.649	-0.137	0.005	-0.181	-0.335	-0.001
5	A	1009	LYS	1	0.923	0.979	6.189	0.337	0.337	0.000	0.000	0.000	0.000
6	A	1010	GLY	0	0.009	-0.010	8.084	-0.320	-0.320	0.000	0.000	0.000	0.000
7	A	1011	ASN	0	-0.054	-0.023	9.607	0.115	0.115	0.000	0.000	0.000	0.000
8	A	1012	ALA	0	0.023	0.021	13.244	-0.006	-0.006	0.000	0.000	0.000	0.000
9	A	1013	GLU	-1	-0.911	-0.963	15.826	-0.143	-0.143	0.000	0.000	0.000	0.000
10	A	1014	LEU	0	-0.013	-0.018	19.122	0.016	0.016	0.000	0.000	0.000	0.000
11	A	1015	ILE	0	0.001	0.011	22.002	0.003	0.003	0.000	0.000	0.000	0.000
12	A	1016	LEU	0	0.032	-0.007	23.620	0.006	0.006	0.000	0.000	0.000	0.000
13	A	1017	GLN	0	-0.057	-0.030	27.345	0.010	0.010	0.000	0.000	0.000	0.000
14	A	1018	ILE	0	0.015	0.035	28.822	0.004	0.004	0.000	0.000	0.000	0.000
15	A	1019	ASP	-1	-0.925	-0.956	30.636	-0.032	-0.032	0.000	0.000	0.000	0.000
16	A	1020	ALA	0	-0.008	-0.017	29.286	0.005	0.005	0.000	0.000	0.000	0.000
17	A	1021	TYR	0	-0.048	-0.040	30.707	-0.006	-0.006	0.000	0.000	0.000	0.000
18	A	1022	LEU	0	0.023	0.008	30.931	0.005	0.005	0.000	0.000	0.000	0.000
19	A	1023	PRO	0	0.000	-0.005	34.152	-0.003	-0.003	0.000	0.000	0.000	0.000
20	A	1024	ASP	-1	-0.881	-0.949	37.891	-0.019	-0.019	0.000	0.000	0.000	0.000
21	A	1025	THR	0	-0.066	-0.043	40.403	0.001	0.001	0.000	0.000	0.000	0.000
22	A	1026	TYR	0	-0.043	-0.013	35.036	0.000	0.000	0.000	0.000	0.000	0.000
23	A	1027	ILE	0	0.011	0.007	34.541	0.001	0.001	0.000	0.000	0.000	0.000
24	A	1028	SER	0	0.025	0.013	38.544	-0.003	-0.003	0.000	0.000	0.000	0.000
25	A	1029	ASP	-1	-0.913	-0.963	39.138	-0.018	-0.018	0.000	0.000	0.000	0.000
26	A	1030	GLN	0	0.073	0.021	36.762	0.000	0.000	0.000	0.000	0.000	0.000
27	A	1031	ARG	1	0.955	0.953	34.570	0.011	0.011	0.000	0.000	0.000	0.000
28	A	1032	HIS	0	0.061	0.055	33.431	-0.003	-0.003	0.000	0.000	0.000	0.000
29	A	1033	LYS	1	0.932	1.001	32.564	0.022	0.022	0.000	0.000	0.000	0.000
30	A	1034	ILE	0	-0.041	-0.010	29.932	-0.003	-0.003	0.000	0.000	0.000	0.000
31	A	1035	GLU	-1	-0.882	-0.920	28.961	-0.009	-0.009	0.000	0.000	0.000	0.000
32	A	1036	ILE	0	0.043	0.007	28.068	-0.002	-0.002	0.000	0.000	0.000	0.000
33	A	1037	TYR	0	0.053	0.024	27.640	0.000	0.000	0.000	0.000	0.000	0.000
34	A	1038	LYS	1	0.886	0.946	23.497	0.056	0.056	0.000	0.000	0.000	0.000
35	A	1039	LYS	1	0.898	0.927	23.558	-0.019	-0.019	0.000	0.000	0.000	0.000
36	A	1040	ILE	0	0.051	0.035	23.683	0.004	0.004	0.000	0.000	0.000	0.000
37	A	1041	ARG	1	0.855	0.930	20.758	0.098	0.098	0.000	0.000	0.000	0.000
38	A	1042	GLN	0	-0.027	-0.002	19.395	-0.024	-0.024	0.000	0.000	0.000	0.000
39	A	1043	ILE	0	-0.061	-0.021	19.274	0.017	0.017	0.000	0.000	0.000	0.000
40	A	1044	ASP	-1	-0.909	-0.960	14.117	0.086	0.086	0.000	0.000	0.000	0.000
41	A	1045	ASN	0	-0.032	-0.037	16.237	0.015	0.015	0.000	0.000	0.000	0.000
42	A	1046	ARG	1	0.985	0.993	18.496	-0.093	-0.093	0.000	0.000	0.000	0.000
43	A	1047	VAL	0	0.074	0.041	21.552	-0.010	-0.010	0.000	0.000	0.000	0.000
44	A	1048	ASN	0	0.000	0.022	19.080	0.004	0.004	0.000	0.000	0.000	0.000
45	A	1049	TYR	0	0.002	-0.029	22.953	-0.006	-0.006	0.000	0.000	0.000	0.000
46	A	1050	GLU	-1	-0.899	-0.948	24.895	0.073	0.073	0.000	0.000	0.000	0.000
47	A	1051	GLU	-1	-0.908	-0.956	25.101	0.070	0.070	0.000	0.000	0.000	0.000
48	A	1052	LEU	0	-0.072	-0.034	25.628	-0.008	-0.008	0.000	0.000	0.000	0.000
49	A	1053	GLN	0	-0.023	-0.015	28.433	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	1054	GLU	-1	-0.899	-0.940	31.016	0.039	0.039	0.000	0.000	0.000	0.000
51	A	1055	GLU	-1	-0.860	-0.942	29.883	0.015	0.015	0.000	0.000	0.000	0.000
52	A	1056	LEU	0	-0.082	-0.053	31.078	-0.005	-0.005	0.000	0.000	0.000	0.000
53	A	1057	ILE	0	0.051	0.020	34.250	-0.003	-0.003	0.000	0.000	0.000	0.000
54	A	1058	ASP	-1	-0.960	-0.961	35.692	0.023	0.023	0.000	0.000	0.000	0.000
55	A	1059	ARG	1	0.759	0.858	32.335	-0.010	-0.010	0.000	0.000	0.000	0.000
56	A	1060	PHE	0	-0.135	-0.076	34.900	-0.004	-0.004	0.000	0.000	0.000	0.000
57	A	1061	GLY	0	-0.005	0.020	39.198	-0.002	-0.002	0.000	0.000	0.000	0.000
58	A	1062	GLU	-1	-0.883	-0.952	38.509	0.019	0.019	0.000	0.000	0.000	0.000
59	A	1063	TYR	0	-0.021	-0.002	32.811	-0.003	-0.003	0.000	0.000	0.000	0.000
60	A	1064	PRO	0	-0.013	-0.005	37.094	0.001	0.001	0.000	0.000	0.000	0.000
61	A	1065	ASP	-1	-0.815	-0.925	35.769	0.005	0.005	0.000	0.000	0.000	0.000
62	A	1066	VAL	0	-0.039	-0.017	33.902	0.000	0.000	0.000	0.000	0.000	0.000
63	A	1067	VAL	0	-0.013	-0.008	32.150	-0.004	-0.004	0.000	0.000	0.000	0.000
64	A	1068	ALA	0	0.032	0.019	30.929	0.000	0.000	0.000	0.000	0.000	0.000
65	A	1069	TYR	0	0.020	0.004	29.750	0.003	0.003	0.000	0.000	0.000	0.000
66	A	1070	LEU	0	-0.058	-0.009	26.653	-0.004	-0.004	0.000	0.000	0.000	0.000
67	A	1071	LEU	0	-0.010	-0.009	26.186	-0.005	-0.005	0.000	0.000	0.000	0.000
68	A	1072	GLU	-1	-0.854	-0.911	25.200	0.029	0.029	0.000	0.000	0.000	0.000
69	A	1073	ILE	0	-0.030	-0.028	22.999	0.001	0.001	0.000	0.000	0.000	0.000
70	A	1074	GLY	0	0.000	0.009	21.811	-0.007	-0.007	0.000	0.000	0.000	0.000
71	A	1075	LEU	0	0.045	0.031	20.350	-0.003	-0.003	0.000	0.000	0.000	0.000
72	A	1076	VAL	0	0.029	0.041	19.758	0.004	0.004	0.000	0.000	0.000	0.000
73	A	1077	LYS	1	0.783	0.864	15.888	0.172	0.172	0.000	0.000	0.000	0.000
74	A	1078	SER	0	-0.077	-0.058	15.890	-0.009	-0.009	0.000	0.000	0.000	0.000
75	A	1079	TYR	0	0.054	0.016	14.572	0.003	0.003	0.000	0.000	0.000	0.000
76	A	1080	LEU	0	0.006	-0.001	14.282	0.005	0.005	0.000	0.000	0.000	0.000
77	A	1081	ASP	-1	-0.806	-0.882	12.209	-0.202	-0.202	0.000	0.000	0.000	0.000
78	A	1082	LYS	1	0.933	0.978	10.076	-0.272	-0.272	0.000	0.000	0.000	0.000
79	A	1083	VAL	0	-0.035	-0.003	9.653	0.086	0.086	0.000	0.000	0.000	0.000
80	A	1084	PHE	0	-0.097	-0.055	5.110	-0.007	-0.007	0.000	0.000	0.000	0.000
81	A	1085	VAL	0	0.020	0.008	10.413	0.004	0.004	0.000	0.000	0.000	0.000
82	A	1086	GLN	0	-0.035	-0.025	13.410	-0.089	-0.089	0.000	0.000	0.000	0.000
83	A	1087	ARG	1	0.889	0.941	14.886	0.104	0.104	0.000	0.000	0.000	0.000
84	A	1088	VAL	0	0.010	0.019	18.595	0.020	0.020	0.000	0.000	0.000	0.000
85	A	1089	GLU	-1	-0.910	-0.957	21.404	-0.082	-0.082	0.000	0.000	0.000	0.000
86	A	1090	ARG	1	0.925	0.963	24.798	0.025	0.025	0.000	0.000	0.000	0.000
87	A	1091	LYS	1	0.941	0.970	28.194	0.038	0.038	0.000	0.000	0.000	0.000
88	A	1092	ASP	-1	-0.904	-0.956	30.842	-0.026	-0.026	0.000	0.000	0.000	0.000
89	A	1093	ASN	0	-0.025	-0.026	33.576	0.001	0.001	0.000	0.000	0.000	0.000
90	A	1094	LYS	1	0.953	0.987	29.628	0.011	0.011	0.000	0.000	0.000	0.000
91	A	1095	ILE	0	0.032	0.027	24.852	-0.007	-0.007	0.000	0.000	0.000	0.000
92	A	1096	THR	0	-0.039	-0.021	23.787	0.010	0.010	0.000	0.000	0.000	0.000
93	A	1097	ILE	0	-0.002	0.017	18.539	-0.013	-0.013	0.000	0.000	0.000	0.000
94	A	1098	GLN	0	0.004	0.003	18.433	0.000	0.000	0.000	0.000	0.000	0.000
95	A	1099	PHE	0	0.051	0.026	13.397	-0.021	-0.021	0.000	0.000	0.000	0.000
96	A	1100	GLU	-1	-0.809	-0.904	9.296	-0.718	-0.718	0.000	0.000	0.000	0.000
97	A	1101	LYS	1	0.977	0.972	11.952	0.255	0.255	0.000	0.000	0.000	0.000
98	A	1102	VAL	0	0.005	0.008	5.881	0.076	0.076	0.000	0.000	0.000	0.000
99	A	1103	THR	0	0.018	0.016	8.904	0.229	0.229	0.000	0.000	0.000	0.000
100	A	1104	GLN	0	0.008	0.007	10.872	0.031	0.031	0.000	0.000	0.000	0.000
101	A	1105	ARG	1	0.859	0.927	7.769	-0.924	-0.924	0.000	0.000	0.000	0.000
102	A	1106	LEU	0	-0.041	-0.017	6.945	0.089	0.089	0.000	0.000	0.000	0.000
103	A	1107	PHE	0	-0.039	-0.018	11.056	-0.023	-0.023	0.000	0.000	0.000	0.000
104	A	1108	LEU	0	-0.009	0.001	14.545	-0.023	-0.023	0.000	0.000	0.000	0.000
105	A	1109	ALA	0	0.075	0.022	17.956	-0.008	-0.008	0.000	0.000	0.000	0.000
106	A	1110	GLN	0	-0.001	-0.013	20.913	-0.022	-0.022	0.000	0.000	0.000	0.000
107	A	1111	ASP	-1	-0.825	-0.908	16.856	0.256	0.256	0.000	0.000	0.000	0.000
108	A	1112	TYR	0	0.051	0.013	14.687	-0.006	-0.006	0.000	0.000	0.000	0.000
109	A	1113	PHE	0	0.001	0.001	20.293	-0.009	-0.009	0.000	0.000	0.000	0.000
110	A	1114	LYS	1	0.953	0.975	22.233	-0.128	-0.128	0.000	0.000	0.000	0.000
111	A	1115	ALA	0	0.049	0.033	20.313	-0.007	-0.007	0.000	0.000	0.000	0.000
112	A	1116	LEU	0	0.002	-0.012	22.445	-0.010	-0.010	0.000	0.000	0.000	0.000
113	A	1117	SER	0	-0.117	-0.061	24.990	-0.007	-0.007	0.000	0.000	0.000	0.000
114	A	1118	VAL	0	-0.038	-0.004	24.630	-0.002	-0.002	0.000	0.000	0.000	0.000
115	A	1119	THR	0	-0.023	0.019	25.186	-0.004	-0.004	0.000	0.000	0.000	0.000
116	A	1120	ASN	0	0.055	0.006	28.129	0.001	0.001	0.000	0.000	0.000	0.000
117	A	1121	LEU	0	-0.074	-0.014	27.549	-0.005	-0.005	0.000	0.000	0.000	0.000
118	A	1122	LYS	1	0.952	0.985	29.963	-0.010	-0.010	0.000	0.000	0.000	0.000
119	A	1123	ALA	0	-0.001	-0.014	26.415	-0.006	-0.006	0.000	0.000	0.000	0.000
120	A	1124	GLY	0	-0.016	-0.006	27.271	0.003	0.003	0.000	0.000	0.000	0.000
121	A	1125	ILE	0	-0.011	-0.002	22.533	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	1126	ALA	0	-0.034	-0.007	24.361	0.000	0.000	0.000	0.000	0.000	0.000
123	A	1127	GLU	-1	-0.860	-0.941	22.779	0.024	0.024	0.000	0.000	0.000	0.000
124	A	1128	ASN	0	-0.049	-0.016	23.014	-0.010	-0.010	0.000	0.000	0.000	0.000
125	A	1129	LYS	1	0.923	0.952	22.162	0.082	0.082	0.000	0.000	0.000	0.000
126	A	1130	GLY	0	-0.033	-0.014	21.370	-0.010	-0.010	0.000	0.000	0.000	0.000
127	A	1131	LEU	0	0.007	0.006	15.415	0.011	0.011	0.000	0.000	0.000	0.000
128	A	1132	MET	0	0.001	0.016	17.398	0.007	0.007	0.000	0.000	0.000	0.000
129	A	1133	GLU	-1	-0.899	-0.960	19.029	-0.057	-0.057	0.000	0.000	0.000	0.000
130	A	1134	LEU	0	-0.003	0.003	19.852	0.013	0.013	0.000	0.000	0.000	0.000
131	A	1135	VAL	0	0.008	-0.003	23.040	-0.012	-0.012	0.000	0.000	0.000	0.000
132	A	1136	PHE	0	0.011	-0.004	23.250	0.007	0.007	0.000	0.000	0.000	0.000
133	A	1137	ASP	-1	-0.960	-0.996	28.374	-0.003	-0.003	0.000	0.000	0.000	0.000
134	A	1138	VAL	0	-0.005	-0.001	29.795	0.004	0.004	0.000	0.000	0.000	0.000
135	A	1139	GLN	0	0.001	-0.009	32.790	-0.002	-0.002	0.000	0.000	0.000	0.000
136	A	1140	ASN	0	-0.085	-0.045	36.550	0.001	0.001	0.000	0.000	0.000	0.000
137	A	1141	LYS	1	0.891	0.966	33.258	-0.015	-0.015	0.000	0.000	0.000	0.000
138	A	1142	LYS	1	0.964	0.976	35.233	-0.014	-0.014	0.000	0.000	0.000	0.000
139	A	1143	ASP	-1	-0.786	-0.907	32.038	-0.007	-0.007	0.000	0.000	0.000	0.000
140	A	1144	TYR	0	0.036	0.002	30.921	0.000	0.000	0.000	0.000	0.000	0.000
141	A	1145	GLU	-1	-0.838	-0.907	30.938	0.019	0.019	0.000	0.000	0.000	0.000
142	A	1146	ILE	0	-0.040	-0.020	27.522	0.003	0.003	0.000	0.000	0.000	0.000
143	A	1147	LEU	0	-0.021	-0.018	25.888	0.001	0.001	0.000	0.000	0.000	0.000
144	A	1148	GLU	-1	-0.890	-0.933	26.048	0.044	0.044	0.000	0.000	0.000	0.000
145	A	1149	GLY	0	0.000	-0.005	26.564	0.007	0.007	0.000	0.000	0.000	0.000
146	A	1150	LEU	0	-0.034	-0.020	22.431	0.006	0.006	0.000	0.000	0.000	0.000
147	A	1151	LEU	0	0.007	0.008	21.941	0.006	0.006	0.000	0.000	0.000	0.000
148	A	1152	ILE	0	0.024	0.019	21.929	0.012	0.012	0.000	0.000	0.000	0.000
149	A	1153	PHE	0	-0.035	-0.033	18.373	0.015	0.015	0.000	0.000	0.000	0.000
150	A	1154	GLY	0	0.002	-0.014	18.219	0.015	0.015	0.000	0.000	0.000	0.000
151	A	1155	GLU	-1	-0.951	-0.975	17.659	0.124	0.124	0.000	0.000	0.000	0.000
152	A	1156	SER	0	0.010	0.007	19.142	0.031	0.031	0.000	0.000	0.000	0.000
153	A	1157	LEU	0	-0.033	-0.028	15.221	0.023	0.023	0.000	0.000	0.000	0.000
154	A	1158	LEU	0	-0.049	-0.043	12.543	0.040	0.040	0.000	0.000	0.000	0.000
155	A	1159	GLU	-1	-0.906	-0.939	14.756	0.248	0.248	0.000	0.000	0.000	0.000
156	A	1160	ILE	0	-0.025	-0.001	16.069	0.036	0.036	0.000	0.000	0.000	0.000
157	A	1161	LYS	1	0.883	0.943	7.051	-0.706	-0.706	0.000	0.000	0.000	0.000
158	A	1162	GLU	-1	-0.929	-0.967	12.445	0.555	0.555	0.000	0.000	0.000	0.000
159	A	1163	SER	0	-0.096	-0.046	13.441	0.012	0.012	0.000	0.000	0.000	0.000
160	A	1164	LYS	1	0.820	0.930	12.521	-0.449	-0.449	0.000	0.000	0.000	0.000
161	A	1165	GLU	-1	-0.980	-0.976	10.473	0.583	0.583	0.000	0.000	0.000	0.000

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