FMO DATABASE

FMODB ID: 89M2Y

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:

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	109
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-866963.461298
FMO2-HF: Nuclear repulsion	824072.117626
FMO2-HF: Total energy	-42891.343672
FMO2-MP2: Total energy	-43019.288445

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.
-3.308	-0.748	5.386	-2.086	-5.86	0

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 : -0.025 / q_NPA : -0.024

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	-0.782	-0.873	3.878	0.375	2.107	-0.012	-0.834	-0.886	0.001
4	A	991	VAL	0	-0.027	-0.005	2.494	-0.177	0.298	0.804	-0.269	-1.009	-0.001
5	A	992	VAL	0	0.015	0.002	5.129	-0.165	-0.130	-0.001	-0.003	-0.032	0.000
6	A	993	SER	0	-0.046	-0.021	8.705	-0.031	-0.031	0.000	0.000	0.000	0.000
7	A	994	PHE	0	0.023	0.006	11.031	0.057	0.057	0.000	0.000	0.000	0.000
8	A	995	GLU	-1	-0.924	-0.960	13.808	-0.331	-0.331	0.000	0.000	0.000	0.000
9	A	996	GLN	0	-0.016	-0.010	16.021	-0.032	-0.032	0.000	0.000	0.000	0.000
10	A	997	PRO	0	0.013	0.012	17.329	0.018	0.018	0.000	0.000	0.000	0.000
11	A	998	GLU	-1	-0.787	-0.865	18.594	-0.150	-0.150	0.000	0.000	0.000	0.000
12	A	999	PHE	0	0.034	0.020	18.894	-0.009	-0.009	0.000	0.000	0.000	0.000
13	A	1000	SER	0	-0.025	-0.013	24.289	0.007	0.007	0.000	0.000	0.000	0.000
14	A	1001	VAL	0	-0.021	0.006	28.041	0.000	0.000	0.000	0.000	0.000	0.000
15	A	1002	SER	0	-0.028	-0.055	30.708	0.001	0.001	0.000	0.000	0.000	0.000
16	A	1003	ARG	1	0.784	0.864	33.958	0.056	0.056	0.000	0.000	0.000	0.000
17	A	1004	GLY	0	0.064	0.040	35.861	0.004	0.004	0.000	0.000	0.000	0.000
18	A	1005	ASP	-1	-0.826	-0.867	32.527	-0.070	-0.070	0.000	0.000	0.000	0.000
19	A	1006	GLN	0	-0.063	-0.040	33.731	0.006	0.006	0.000	0.000	0.000	0.000
20	A	1007	VAL	0	-0.086	-0.049	28.512	0.006	0.006	0.000	0.000	0.000	0.000
21	A	1008	ALA	0	0.016	0.022	26.350	-0.006	-0.006	0.000	0.000	0.000	0.000
22	A	1009	ARG	1	0.830	0.900	25.335	0.057	0.057	0.000	0.000	0.000	0.000
23	A	1010	ILE	0	-0.025	-0.009	19.729	-0.014	-0.014	0.000	0.000	0.000	0.000
24	A	1011	PRO	0	0.038	0.036	18.531	0.020	0.020	0.000	0.000	0.000	0.000
25	A	1012	VAL	0	-0.033	-0.027	13.697	-0.022	-0.022	0.000	0.000	0.000	0.000
26	A	1013	ILE	0	0.026	0.010	11.583	0.024	0.024	0.000	0.000	0.000	0.000
27	A	1014	ARG	1	0.751	0.846	8.710	-0.181	-0.181	0.000	0.000	0.000	0.000
28	A	1015	ARG	1	0.966	0.977	6.766	1.319	1.319	0.000	0.000	0.000	0.000
29	A	1016	VAL	0	-0.014	-0.015	4.816	-0.131	-0.131	0.000	0.000	0.000	0.000
30	A	1017	LEU	0	0.002	0.018	6.589	-0.041	-0.041	0.000	0.000	0.000	0.000
31	A	1018	ASP	-1	-0.892	-0.936	7.530	1.345	1.345	0.000	0.000	0.000	0.000
32	A	1019	GLY	0	0.023	0.014	9.159	-0.007	-0.007	0.000	0.000	0.000	0.000
33	A	1020	GLY	0	-0.003	0.006	11.903	-0.056	-0.056	0.000	0.000	0.000	0.000
34	A	1021	LYS	1	0.893	0.971	13.352	-0.495	-0.495	0.000	0.000	0.000	0.000
35	A	1022	SER	0	-0.008	-0.019	9.999	0.149	0.149	0.000	0.000	0.000	0.000
36	A	1023	GLN	0	-0.009	0.005	11.692	-0.073	-0.073	0.000	0.000	0.000	0.000
37	A	1024	VAL	0	0.044	0.031	10.637	0.139	0.139	0.000	0.000	0.000	0.000
38	A	1025	SER	0	0.000	0.010	13.314	-0.033	-0.033	0.000	0.000	0.000	0.000
39	A	1026	TYR	0	-0.040	-0.030	15.871	-0.021	-0.021	0.000	0.000	0.000	0.000
40	A	1027	ARG	1	0.927	0.948	18.155	0.030	0.030	0.000	0.000	0.000	0.000
41	A	1028	THR	0	0.055	0.035	21.070	-0.017	-0.017	0.000	0.000	0.000	0.000
42	A	1029	GLN	0	-0.048	-0.020	23.271	0.016	0.016	0.000	0.000	0.000	0.000
43	A	1030	ASP	-1	-0.730	-0.842	25.294	-0.053	-0.053	0.000	0.000	0.000	0.000
44	A	1031	GLY	0	0.008	-0.004	27.346	-0.009	-0.009	0.000	0.000	0.000	0.000
45	A	1032	THR	0	-0.001	0.011	29.209	0.005	0.005	0.000	0.000	0.000	0.000
46	A	1033	ALA	0	-0.035	-0.014	30.521	0.006	0.006	0.000	0.000	0.000	0.000
47	A	1034	GLN	0	0.006	-0.012	30.954	-0.003	-0.003	0.000	0.000	0.000	0.000
48	A	1035	GLY	0	0.087	0.026	32.008	0.001	0.001	0.000	0.000	0.000	0.000
49	A	1036	ASN	0	-0.080	-0.049	32.645	0.003	0.003	0.000	0.000	0.000	0.000
50	A	1037	ARG	1	0.811	0.910	35.308	0.050	0.050	0.000	0.000	0.000	0.000
51	A	1038	ASP	-1	-0.770	-0.868	33.530	-0.056	-0.056	0.000	0.000	0.000	0.000
52	A	1039	TYR	0	-0.026	-0.032	27.783	-0.004	-0.004	0.000	0.000	0.000	0.000
53	A	1040	ILE	0	0.030	0.017	30.553	0.003	0.003	0.000	0.000	0.000	0.000
54	A	1041	PRO	0	-0.048	-0.019	28.261	-0.002	-0.002	0.000	0.000	0.000	0.000
55	A	1042	VAL	0	-0.007	0.004	24.437	0.006	0.006	0.000	0.000	0.000	0.000
56	A	1043	GLU	-1	-0.903	-0.964	22.627	0.061	0.061	0.000	0.000	0.000	0.000
57	A	1044	GLY	0	0.088	0.070	21.929	-0.003	-0.003	0.000	0.000	0.000	0.000
58	A	1045	GLU	-1	-0.835	-0.920	17.926	0.259	0.259	0.000	0.000	0.000	0.000
59	A	1046	LEU	0	-0.012	0.009	15.200	-0.013	-0.013	0.000	0.000	0.000	0.000
60	A	1047	LEU	0	-0.039	-0.025	15.072	0.045	0.045	0.000	0.000	0.000	0.000
61	A	1048	PHE	0	0.006	-0.001	13.141	-0.040	-0.040	0.000	0.000	0.000	0.000
62	A	1049	GLN	0	0.055	0.011	15.209	0.092	0.092	0.000	0.000	0.000	0.000
63	A	1050	PRO	0	0.003	-0.004	15.557	-0.023	-0.023	0.000	0.000	0.000	0.000
64	A	1051	GLY	0	0.029	0.023	15.137	-0.025	-0.025	0.000	0.000	0.000	0.000
65	A	1052	GLU	-1	-0.809	-0.878	15.878	0.039	0.039	0.000	0.000	0.000	0.000
66	A	1053	ALA	0	0.048	0.017	13.330	0.012	0.012	0.000	0.000	0.000	0.000
67	A	1054	TRP	0	-0.042	-0.011	13.809	-0.060	-0.060	0.000	0.000	0.000	0.000
68	A	1055	LYS	1	0.821	0.903	16.069	-0.041	-0.041	0.000	0.000	0.000	0.000
69	A	1056	GLU	-1	-0.779	-0.879	18.502	-0.083	-0.083	0.000	0.000	0.000	0.000
70	A	1057	LEU	0	-0.044	-0.010	18.856	0.021	0.021	0.000	0.000	0.000	0.000
71	A	1058	GLN	0	0.012	-0.007	22.366	-0.011	-0.011	0.000	0.000	0.000	0.000
72	A	1059	VAL	0	-0.001	0.014	24.361	0.009	0.009	0.000	0.000	0.000	0.000
73	A	1060	LYS	1	0.985	0.987	27.128	0.009	0.009	0.000	0.000	0.000	0.000
74	A	1061	LEU	0	-0.021	-0.004	30.027	-0.001	-0.001	0.000	0.000	0.000	0.000
75	A	1062	LEU	0	-0.027	-0.003	32.889	0.006	0.006	0.000	0.000	0.000	0.000
76	A	1063	GLU	-1	-0.828	-0.923	36.376	-0.047	-0.047	0.000	0.000	0.000	0.000
77	A	1064	LEU	0	-0.046	-0.010	38.810	0.003	0.003	0.000	0.000	0.000	0.000
78	A	1074	ARG	1	0.990	0.997	40.645	0.051	0.051	0.000	0.000	0.000	0.000
79	A	1075	GLN	0	-0.069	-0.036	37.634	-0.003	-0.003	0.000	0.000	0.000	0.000
80	A	1076	VAL	0	0.013	-0.001	32.728	-0.002	-0.002	0.000	0.000	0.000	0.000
81	A	1077	ARG	1	0.802	0.889	32.959	0.059	0.059	0.000	0.000	0.000	0.000
82	A	1078	ARG	1	0.849	0.899	26.637	0.146	0.146	0.000	0.000	0.000	0.000
83	A	1079	PHE	0	0.004	0.022	25.487	0.005	0.005	0.000	0.000	0.000	0.000
84	A	1080	HIS	0	0.013	0.017	21.865	-0.023	-0.023	0.000	0.000	0.000	0.000
85	A	1081	VAL	0	0.015	0.005	19.618	0.022	0.022	0.000	0.000	0.000	0.000
86	A	1082	GLN	0	-0.012	0.002	17.145	-0.014	-0.014	0.000	0.000	0.000	0.000
87	A	1083	LEU	0	0.014	0.021	12.215	0.036	0.036	0.000	0.000	0.000	0.000
88	A	1084	SER	0	-0.041	-0.033	13.218	-0.022	-0.022	0.000	0.000	0.000	0.000
89	A	1085	ASN	0	-0.003	-0.020	13.379	0.087	0.087	0.000	0.000	0.000	0.000
90	A	1086	PRO	0	0.025	0.019	8.702	-0.043	-0.043	0.000	0.000	0.000	0.000
91	A	1087	LYS	1	0.838	0.892	10.915	-0.262	-0.262	0.000	0.000	0.000	0.000
92	A	1088	PHE	0	-0.010	-0.040	11.259	-0.002	-0.002	0.000	0.000	0.000	0.000
93	A	1089	GLY	0	0.077	0.050	8.400	-0.087	-0.087	0.000	0.000	0.000	0.000
94	A	1090	ALA	0	-0.017	0.005	6.611	0.567	0.567	0.000	0.000	0.000	0.000
95	A	1091	HIS	1	0.850	0.912	3.323	-4.895	-4.598	4.596	-0.974	-3.919	0.000
96	A	1092	LEU	0	0.007	0.021	5.312	-0.728	-0.707	-0.001	-0.006	-0.014	0.000
97	A	1093	GLY	0	0.002	-0.009	5.653	-0.229	-0.229	0.000	0.000	0.000	0.000
98	A	1094	GLN	0	-0.035	-0.021	7.280	0.206	0.206	0.000	0.000	0.000	0.000
99	A	1095	PRO	0	0.034	0.031	10.250	-0.071	-0.071	0.000	0.000	0.000	0.000
100	A	1096	HIS	0	0.051	0.023	10.409	0.042	0.042	0.000	0.000	0.000	0.000
101	A	1097	SER	0	-0.046	-0.040	12.446	0.080	0.080	0.000	0.000	0.000	0.000
102	A	1098	THR	0	-0.016	-0.014	16.217	-0.034	-0.034	0.000	0.000	0.000	0.000
103	A	1099	THR	0	-0.014	-0.017	19.206	0.022	0.022	0.000	0.000	0.000	0.000
104	A	1100	ILE	0	-0.018	-0.009	22.399	-0.008	-0.008	0.000	0.000	0.000	0.000
105	A	1101	ILE	0	-0.028	-0.027	25.700	0.012	0.012	0.000	0.000	0.000	0.000
106	A	1102	ILE	0	0.013	0.021	28.911	0.002	0.002	0.000	0.000	0.000	0.000
107	A	1103	ARG	1	0.928	0.945	29.953	0.115	0.115	0.000	0.000	0.000	0.000
108	A	1104	ASP	-1	-0.806	-0.908	35.058	-0.056	-0.056	0.000	0.000	0.000	0.000
109	A	1105	PRO	0	-0.015	0.003	38.500	-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)