FMO DATABASE

FMODB ID: G5GN1

Calculation Name: 3FQ4-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3FQ4

Chain ID: A

ChEMBL ID:

UniProt ID: P16144

Base Structure: X-ray

Registration Date: 2023-09-23

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

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	109
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-866815.63231
FMO2-HF: Nuclear repulsion	823924.365134
FMO2-HF: Total energy	-42891.267176
FMO2-MP2: Total energy	-43019.168895

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:988:MET)

Summations of interaction energy for fragment #1(A:988:MET)

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.
-4.173	-1.556	6.506	-2.414	-6.711	-0.001

Interaction energy analysis for fragmet #1(A:988:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.033 / q_NPA : -0.026

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	990	ASP	-1	-0.789	-0.885	3.707	-0.411	1.613	-0.014	-0.955	-1.056	0.001
4	A	991	VAL	0	-0.051	-0.016	2.684	-0.370	0.211	0.493	-0.212	-0.862	-0.001
5	A	992	VAL	0	0.015	-0.005	5.273	-0.007	0.029	-0.001	-0.002	-0.033	0.000
6	A	993	SER	0	-0.013	0.000	8.674	-0.071	-0.071	0.000	0.000	0.000	0.000
7	A	994	PHE	0	0.008	0.000	11.041	0.076	0.076	0.000	0.000	0.000	0.000
8	A	995	GLU	-1	-0.955	-0.975	13.851	-0.384	-0.384	0.000	0.000	0.000	0.000
9	A	996	GLN	0	-0.004	-0.005	15.643	-0.032	-0.032	0.000	0.000	0.000	0.000
10	A	997	PRO	0	0.017	0.009	17.187	0.016	0.016	0.000	0.000	0.000	0.000
11	A	998	GLU	-1	-0.807	-0.886	18.529	-0.178	-0.178	0.000	0.000	0.000	0.000
12	A	999	PHE	0	0.013	0.016	18.777	-0.005	-0.005	0.000	0.000	0.000	0.000
13	A	1000	SER	0	0.007	0.005	24.169	0.009	0.009	0.000	0.000	0.000	0.000
14	A	1001	VAL	0	-0.016	0.002	27.579	0.000	0.000	0.000	0.000	0.000	0.000
15	A	1002	SER	0	-0.024	-0.033	30.264	0.001	0.001	0.000	0.000	0.000	0.000
16	A	1003	ARG	1	0.856	0.902	33.771	0.072	0.072	0.000	0.000	0.000	0.000
17	A	1004	GLY	0	0.040	0.022	35.358	0.004	0.004	0.000	0.000	0.000	0.000
18	A	1005	ASP	-1	-0.851	-0.891	32.632	-0.082	-0.082	0.000	0.000	0.000	0.000
19	A	1006	GLN	0	-0.074	-0.030	34.157	0.006	0.006	0.000	0.000	0.000	0.000
20	A	1007	VAL	0	-0.052	-0.033	28.500	0.004	0.004	0.000	0.000	0.000	0.000
21	A	1008	ALA	0	0.001	0.015	26.356	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	1009	ARG	1	0.888	0.931	25.170	0.076	0.076	0.000	0.000	0.000	0.000
23	A	1010	ILE	0	-0.023	-0.019	19.706	-0.014	-0.014	0.000	0.000	0.000	0.000
24	A	1011	PRO	0	0.040	0.044	18.310	0.017	0.017	0.000	0.000	0.000	0.000
25	A	1012	VAL	0	-0.031	-0.024	13.392	-0.033	-0.033	0.000	0.000	0.000	0.000
26	A	1013	ILE	0	0.046	0.021	11.327	0.033	0.033	0.000	0.000	0.000	0.000
27	A	1014	ARG	1	0.755	0.852	8.727	-0.158	-0.158	0.000	0.000	0.000	0.000
28	A	1015	ARG	1	0.965	0.978	6.658	1.496	1.496	0.000	0.000	0.000	0.000
29	A	1016	VAL	0	-0.032	-0.028	4.796	-0.219	-0.124	-0.001	-0.017	-0.078	0.000
30	A	1017	LEU	0	0.015	0.023	6.874	0.022	0.022	0.000	0.000	0.000	0.000
31	A	1018	ASP	-1	-0.873	-0.928	7.474	1.468	1.468	0.000	0.000	0.000	0.000
32	A	1019	GLY	0	0.008	0.012	9.339	0.021	0.021	0.000	0.000	0.000	0.000
33	A	1020	GLY	0	0.003	0.007	11.851	-0.046	-0.046	0.000	0.000	0.000	0.000
34	A	1021	LYS	1	0.885	0.964	12.905	-0.467	-0.467	0.000	0.000	0.000	0.000
35	A	1022	SER	0	0.006	-0.005	9.828	0.092	0.092	0.000	0.000	0.000	0.000
36	A	1023	GLN	0	-0.015	-0.006	11.582	-0.064	-0.064	0.000	0.000	0.000	0.000
37	A	1024	VAL	0	0.015	0.022	10.284	0.110	0.110	0.000	0.000	0.000	0.000
38	A	1025	SER	0	0.033	0.022	13.061	-0.012	-0.012	0.000	0.000	0.000	0.000
39	A	1026	TYR	0	-0.011	-0.018	15.432	-0.040	-0.040	0.000	0.000	0.000	0.000
40	A	1027	ARG	1	0.945	0.959	17.968	0.080	0.080	0.000	0.000	0.000	0.000
41	A	1028	THR	0	0.051	0.035	20.978	-0.021	-0.021	0.000	0.000	0.000	0.000
42	A	1029	GLN	0	-0.031	-0.006	23.062	0.013	0.013	0.000	0.000	0.000	0.000
43	A	1030	ASP	-1	-0.753	-0.847	24.981	-0.078	-0.078	0.000	0.000	0.000	0.000
44	A	1031	GLY	0	-0.006	-0.002	27.172	-0.010	-0.010	0.000	0.000	0.000	0.000
45	A	1032	THR	0	0.000	-0.002	28.605	0.007	0.007	0.000	0.000	0.000	0.000
46	A	1033	ALA	0	-0.051	-0.021	30.141	0.008	0.008	0.000	0.000	0.000	0.000
47	A	1034	GLN	0	0.038	0.002	30.729	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	1035	GLY	0	0.077	0.028	31.611	0.002	0.002	0.000	0.000	0.000	0.000
49	A	1036	ASN	0	-0.072	-0.048	32.322	0.003	0.003	0.000	0.000	0.000	0.000
50	A	1037	ARG	1	0.807	0.914	35.185	0.067	0.067	0.000	0.000	0.000	0.000
51	A	1038	ASP	-1	-0.739	-0.865	33.323	-0.072	-0.072	0.000	0.000	0.000	0.000
52	A	1039	TYR	0	-0.031	-0.038	27.434	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	1040	ILE	0	0.018	0.015	30.598	0.004	0.004	0.000	0.000	0.000	0.000
54	A	1041	PRO	0	-0.030	-0.010	27.984	-0.004	-0.004	0.000	0.000	0.000	0.000
55	A	1042	VAL	0	-0.006	-0.003	24.148	0.008	0.008	0.000	0.000	0.000	0.000
56	A	1043	GLU	-1	-0.956	-0.983	22.495	0.023	0.023	0.000	0.000	0.000	0.000
57	A	1044	GLY	0	0.073	0.044	21.060	0.005	0.005	0.000	0.000	0.000	0.000
58	A	1045	GLU	-1	-0.887	-0.940	17.829	0.196	0.196	0.000	0.000	0.000	0.000
59	A	1046	LEU	0	-0.021	0.004	15.070	-0.017	-0.017	0.000	0.000	0.000	0.000
60	A	1047	LEU	0	-0.011	-0.014	15.032	0.044	0.044	0.000	0.000	0.000	0.000
61	A	1048	PHE	0	-0.018	-0.016	13.006	-0.034	-0.034	0.000	0.000	0.000	0.000
62	A	1049	GLN	0	0.064	0.018	14.876	0.088	0.088	0.000	0.000	0.000	0.000
63	A	1050	PRO	0	0.024	0.010	15.226	-0.028	-0.028	0.000	0.000	0.000	0.000
64	A	1051	GLY	0	0.014	0.012	15.022	-0.021	-0.021	0.000	0.000	0.000	0.000
65	A	1052	GLU	-1	-0.809	-0.879	15.771	0.003	0.003	0.000	0.000	0.000	0.000
66	A	1053	ALA	0	0.048	0.012	13.581	-0.001	-0.001	0.000	0.000	0.000	0.000
67	A	1054	TRP	0	-0.022	-0.011	14.165	-0.070	-0.070	0.000	0.000	0.000	0.000
68	A	1055	LYS	1	0.810	0.900	16.148	0.008	0.008	0.000	0.000	0.000	0.000
69	A	1056	GLU	-1	-0.790	-0.888	18.405	-0.114	-0.114	0.000	0.000	0.000	0.000
70	A	1057	LEU	0	-0.041	-0.012	18.465	0.022	0.022	0.000	0.000	0.000	0.000
71	A	1058	GLN	0	-0.015	-0.017	22.026	-0.007	-0.007	0.000	0.000	0.000	0.000
72	A	1059	VAL	0	-0.019	0.011	24.388	0.010	0.010	0.000	0.000	0.000	0.000
73	A	1060	LYS	1	0.983	0.985	27.128	0.023	0.023	0.000	0.000	0.000	0.000
74	A	1061	LEU	0	-0.028	-0.010	29.563	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	1062	LEU	0	-0.010	0.000	32.848	0.006	0.006	0.000	0.000	0.000	0.000
76	A	1063	GLU	-1	-0.881	-0.951	36.279	-0.058	-0.058	0.000	0.000	0.000	0.000
77	A	1064	LEU	0	-0.046	-0.018	38.295	0.003	0.003	0.000	0.000	0.000	0.000
78	A	1074	ARG	1	0.983	0.994	40.245	0.061	0.061	0.000	0.000	0.000	0.000
79	A	1075	GLN	0	-0.093	-0.050	37.701	-0.004	-0.004	0.000	0.000	0.000	0.000
80	A	1076	VAL	0	0.016	0.001	32.526	-0.003	-0.003	0.000	0.000	0.000	0.000
81	A	1077	ARG	1	0.790	0.895	32.792	0.073	0.073	0.000	0.000	0.000	0.000
82	A	1078	ARG	1	0.872	0.919	26.623	0.169	0.169	0.000	0.000	0.000	0.000
83	A	1079	PHE	0	-0.008	0.016	25.027	0.006	0.006	0.000	0.000	0.000	0.000
84	A	1080	HIS	0	0.013	0.015	21.610	-0.026	-0.026	0.000	0.000	0.000	0.000
85	A	1081	VAL	0	0.002	0.000	19.300	0.024	0.024	0.000	0.000	0.000	0.000
86	A	1082	GLN	0	-0.003	0.002	16.927	-0.020	-0.020	0.000	0.000	0.000	0.000
87	A	1083	LEU	0	0.016	0.018	11.983	0.040	0.040	0.000	0.000	0.000	0.000
88	A	1084	SER	0	-0.026	-0.023	13.051	-0.017	-0.017	0.000	0.000	0.000	0.000
89	A	1085	ASN	0	-0.011	-0.011	13.267	0.076	0.076	0.000	0.000	0.000	0.000
90	A	1086	PRO	0	0.023	0.019	8.463	-0.036	-0.036	0.000	0.000	0.000	0.000
91	A	1087	LYS	1	0.878	0.922	10.533	-0.204	-0.204	0.000	0.000	0.000	0.000
92	A	1088	PHE	0	-0.015	-0.042	10.797	-0.009	-0.009	0.000	0.000	0.000	0.000
93	A	1089	GLY	0	0.071	0.047	8.028	-0.057	-0.057	0.000	0.000	0.000	0.000
94	A	1090	ALA	0	-0.020	0.009	6.114	0.586	0.586	0.000	0.000	0.000	0.000
95	A	1091	HIS	1	0.858	0.914	2.953	-5.298	-5.450	6.030	-1.221	-4.658	-0.001
96	A	1092	LEU	0	0.014	0.025	4.881	-0.629	-0.596	-0.001	-0.007	-0.024	0.000
97	A	1093	GLY	0	-0.001	-0.012	5.711	-0.407	-0.407	0.000	0.000	0.000	0.000
98	A	1094	GLN	0	-0.068	-0.013	7.222	0.340	0.340	0.000	0.000	0.000	0.000
99	A	1095	PRO	0	0.019	0.013	10.239	-0.054	-0.054	0.000	0.000	0.000	0.000
100	A	1096	HIS	0	0.100	0.027	9.654	0.065	0.065	0.000	0.000	0.000	0.000
101	A	1097	SER	0	-0.031	-0.024	12.550	0.088	0.088	0.000	0.000	0.000	0.000
102	A	1098	THR	0	-0.032	-0.024	16.199	-0.032	-0.032	0.000	0.000	0.000	0.000
103	A	1099	THR	0	0.002	-0.008	19.126	0.023	0.023	0.000	0.000	0.000	0.000
104	A	1100	ILE	0	-0.005	0.004	22.411	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	1101	ILE	0	-0.048	-0.035	25.482	0.013	0.013	0.000	0.000	0.000	0.000
106	A	1102	ILE	0	0.005	0.008	28.613	0.002	0.002	0.000	0.000	0.000	0.000
107	A	1103	ARG	1	0.920	0.935	29.678	0.137	0.137	0.000	0.000	0.000	0.000
108	A	1104	ASP	-1	-0.794	-0.906	34.570	-0.070	-0.070	0.000	0.000	0.000	0.000
109	A	1105	PRO	0	0.004	0.011	37.867	-0.004	-0.004	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:988:MET)