FMO DATABASE

FMODB ID: R8188

Calculation Name: 3FKC-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 3FKC

Chain ID: A

ChEMBL ID:

UniProt ID: Q86T24

Base Structure: X-ray

Registration Date: 2023-09-20

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	113
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-862244.767788
FMO2-HF: Nuclear repulsion	818664.154626
FMO2-HF: Total energy	-43580.613162
FMO2-MP2: Total energy	-43710.914885

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:4:ARG)

Summations of interaction energy for fragment #1(A:4:ARG)

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.
5.012	6.782	-0.013	-0.8	-0.957	0.001

Interaction energy analysis for fragmet #1(A:4:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 1.005 / q_NPA : 0.990

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	6	LEU	0	0.042	0.028	3.839	3.393	5.163	-0.013	-0.800	-0.957	0.001
4	A	7	ILE	0	0.006	0.004	6.232	-0.536	-0.536	0.000	0.000	0.000	0.000
5	A	8	SER	0	-0.016	-0.008	9.587	1.183	1.183	0.000	0.000	0.000	0.000
6	A	9	ALA	0	0.017	0.006	12.940	-0.284	-0.284	0.000	0.000	0.000	0.000
7	A	10	THR	0	-0.022	-0.016	16.404	0.228	0.228	0.000	0.000	0.000	0.000
8	A	11	ASP	-1	-0.831	-0.917	19.873	-11.837	-11.837	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.012	-0.025	22.866	0.329	0.329	0.000	0.000	0.000	0.000
10	A	13	GLN	0	0.019	0.015	25.959	0.679	0.679	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.020	0.009	25.197	0.446	0.446	0.000	0.000	0.000	0.000
12	A	15	SER	0	-0.004	-0.010	27.296	0.369	0.369	0.000	0.000	0.000	0.000
13	A	16	GLY	0	0.048	0.017	29.264	0.306	0.306	0.000	0.000	0.000	0.000
14	A	17	SER	0	0.028	0.023	30.253	0.416	0.416	0.000	0.000	0.000	0.000
15	A	18	LEU	0	-0.017	-0.010	28.866	0.263	0.263	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.020	0.005	31.742	0.245	0.245	0.000	0.000	0.000	0.000
17	A	20	ASN	0	-0.022	-0.008	34.809	0.390	0.390	0.000	0.000	0.000	0.000
18	A	21	SER	0	0.032	0.019	34.037	0.226	0.226	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.036	-0.017	33.322	0.196	0.196	0.000	0.000	0.000	0.000
20	A	23	ASN	0	0.039	0.007	36.971	0.321	0.321	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.897	-0.942	38.897	-7.432	-7.432	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.050	-0.036	35.090	0.243	0.243	0.000	0.000	0.000	0.000
23	A	26	ARG	1	0.886	0.945	40.599	6.990	6.990	0.000	0.000	0.000	0.000
24	A	27	GLY	0	-0.032	-0.005	42.899	0.162	0.162	0.000	0.000	0.000	0.000
25	A	28	HIS	0	-0.006	0.005	42.693	0.261	0.261	0.000	0.000	0.000	0.000
26	A	29	GLY	0	-0.030	-0.021	44.983	0.108	0.108	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.012	-0.014	40.577	-0.002	-0.002	0.000	0.000	0.000	0.000
28	A	31	PHE	0	-0.017	-0.022	37.022	-0.130	-0.130	0.000	0.000	0.000	0.000
29	A	32	CYS	0	-0.101	-0.004	40.313	-0.035	-0.035	0.000	0.000	0.000	0.000
30	A	33	ASP	-1	-0.792	-0.896	40.250	-7.064	-7.064	0.000	0.000	0.000	0.000
31	A	34	VAL	0	-0.039	-0.023	43.411	0.075	0.075	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.058	-0.029	45.873	-0.010	-0.010	0.000	0.000	0.000	0.000
33	A	36	VAL	0	-0.008	-0.009	47.258	0.036	0.036	0.000	0.000	0.000	0.000
34	A	37	ILE	0	-0.030	-0.018	50.129	0.003	0.003	0.000	0.000	0.000	0.000
35	A	38	VAL	0	0.034	0.015	52.035	-0.034	-0.034	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.827	-0.911	55.152	-5.204	-5.204	0.000	0.000	0.000	0.000
37	A	40	ASP	-1	-0.888	-0.934	58.919	-5.122	-5.122	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.884	0.946	53.151	5.609	5.609	0.000	0.000	0.000	0.000
39	A	42	LYS	1	0.961	0.979	52.935	5.343	5.343	0.000	0.000	0.000	0.000
40	A	43	PHE	0	-0.008	0.001	48.448	-0.036	-0.036	0.000	0.000	0.000	0.000
41	A	44	ARG	1	0.909	0.966	45.757	6.289	6.289	0.000	0.000	0.000	0.000
42	A	45	ALA	0	0.037	0.007	43.043	-0.054	-0.054	0.000	0.000	0.000	0.000
43	A	46	HIS	0	0.069	0.069	38.413	0.042	0.042	0.000	0.000	0.000	0.000
44	A	47	LYS	1	0.876	0.930	39.994	6.653	6.653	0.000	0.000	0.000	0.000
45	A	48	ASN	0	0.002	-0.002	33.429	0.100	0.100	0.000	0.000	0.000	0.000
46	A	49	ILE	0	0.031	0.022	34.616	-0.147	-0.147	0.000	0.000	0.000	0.000
47	A	50	LEU	0	0.007	0.004	37.133	-0.035	-0.035	0.000	0.000	0.000	0.000
48	A	51	SER	0	0.005	-0.008	37.578	-0.015	-0.015	0.000	0.000	0.000	0.000
49	A	52	ALA	0	-0.011	0.008	34.249	-0.042	-0.042	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.036	-0.030	36.051	-0.022	-0.022	0.000	0.000	0.000	0.000
51	A	54	SER	0	-0.051	-0.031	38.379	0.122	0.122	0.000	0.000	0.000	0.000
52	A	55	THR	0	0.025	-0.001	40.406	-0.034	-0.034	0.000	0.000	0.000	0.000
53	A	56	TYR	0	0.016	0.027	42.133	0.025	0.025	0.000	0.000	0.000	0.000
54	A	57	PHE	0	0.039	-0.008	42.613	0.069	0.069	0.000	0.000	0.000	0.000
55	A	58	HIS	0	-0.067	-0.011	36.504	0.024	0.024	0.000	0.000	0.000	0.000
56	A	59	GLN	0	-0.019	-0.012	40.945	0.084	0.084	0.000	0.000	0.000	0.000
57	A	60	LEU	0	-0.014	0.007	43.744	0.057	0.057	0.000	0.000	0.000	0.000
58	A	61	PHE	0	-0.022	-0.031	41.445	0.076	0.076	0.000	0.000	0.000	0.000
59	A	62	SER	0	-0.043	-0.017	41.550	-0.082	-0.082	0.000	0.000	0.000	0.000
60	A	63	VAL	0	-0.014	0.007	42.508	0.029	0.029	0.000	0.000	0.000	0.000
61	A	64	ALA	0	-0.017	-0.009	45.190	-0.054	-0.054	0.000	0.000	0.000	0.000
62	A	65	GLY	0	0.059	0.015	46.137	0.108	0.108	0.000	0.000	0.000	0.000
63	A	66	GLN	0	-0.013	-0.009	46.091	-0.030	-0.030	0.000	0.000	0.000	0.000
64	A	67	VAL	0	0.002	0.004	48.112	-0.021	-0.021	0.000	0.000	0.000	0.000
65	A	68	VAL	0	-0.026	-0.002	48.091	0.021	0.021	0.000	0.000	0.000	0.000
66	A	69	GLU	-1	-0.879	-0.948	51.015	-5.390	-5.390	0.000	0.000	0.000	0.000
67	A	70	LEU	0	-0.061	-0.020	49.473	-0.059	-0.059	0.000	0.000	0.000	0.000
68	A	71	SER	0	0.054	0.024	53.756	0.066	0.066	0.000	0.000	0.000	0.000
69	A	72	PHE	0	-0.061	-0.046	55.509	-0.073	-0.073	0.000	0.000	0.000	0.000
70	A	73	ILE	0	-0.002	0.006	51.241	-0.046	-0.046	0.000	0.000	0.000	0.000
71	A	74	ARG	1	0.818	0.882	55.511	5.340	5.340	0.000	0.000	0.000	0.000
72	A	75	ALA	0	0.033	0.000	54.735	-0.136	-0.136	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.902	-0.959	53.549	-5.531	-5.531	0.000	0.000	0.000	0.000
74	A	77	ILE	0	0.026	0.031	52.190	-0.120	-0.120	0.000	0.000	0.000	0.000
75	A	78	PHE	0	0.035	0.003	47.121	-0.173	-0.173	0.000	0.000	0.000	0.000
76	A	79	ALA	0	-0.040	-0.021	48.793	-0.148	-0.148	0.000	0.000	0.000	0.000
77	A	80	GLU	-1	-0.901	-0.954	48.119	-6.418	-6.418	0.000	0.000	0.000	0.000
78	A	81	ILE	0	-0.022	-0.003	45.392	-0.185	-0.185	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.005	-0.011	43.822	-0.210	-0.210	0.000	0.000	0.000	0.000
80	A	83	ASN	0	0.007	0.003	43.226	-0.223	-0.223	0.000	0.000	0.000	0.000
81	A	84	TYR	0	0.004	0.034	39.101	-0.197	-0.197	0.000	0.000	0.000	0.000
82	A	85	ILE	0	-0.047	-0.019	39.413	-0.230	-0.230	0.000	0.000	0.000	0.000
83	A	86	TYR	0	-0.036	-0.060	38.573	-0.167	-0.167	0.000	0.000	0.000	0.000
84	A	87	SER	0	-0.009	-0.044	38.523	-0.063	-0.063	0.000	0.000	0.000	0.000
85	A	88	SER	0	-0.093	-0.041	36.483	-0.213	-0.213	0.000	0.000	0.000	0.000
86	A	89	LYS	1	0.941	0.965	38.614	7.819	7.819	0.000	0.000	0.000	0.000
87	A	90	ILE	0	0.046	0.035	41.928	0.076	0.076	0.000	0.000	0.000	0.000
88	A	91	VAL	0	-0.014	-0.021	44.891	-0.047	-0.047	0.000	0.000	0.000	0.000
89	A	92	ARG	1	0.909	0.947	47.487	6.128	6.128	0.000	0.000	0.000	0.000
90	A	93	VAL	0	0.086	0.054	49.833	0.088	0.088	0.000	0.000	0.000	0.000
91	A	94	ARG	1	0.867	0.931	52.448	5.348	5.348	0.000	0.000	0.000	0.000
92	A	95	SER	0	0.031	0.003	55.569	-0.041	-0.041	0.000	0.000	0.000	0.000
93	A	96	ASP	-1	-0.821	-0.908	56.591	-5.328	-5.328	0.000	0.000	0.000	0.000
94	A	97	LEU	0	0.015	0.014	55.522	0.039	0.039	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.018	-0.001	50.551	-0.079	-0.079	0.000	0.000	0.000	0.000
96	A	99	ASP	-1	-0.838	-0.921	53.266	-5.700	-5.700	0.000	0.000	0.000	0.000
97	A	100	GLU	-1	-0.799	-0.888	54.698	-5.449	-5.449	0.000	0.000	0.000	0.000
98	A	101	LEU	0	-0.008	-0.002	48.646	-0.070	-0.070	0.000	0.000	0.000	0.000
99	A	102	ILE	0	-0.003	0.008	49.923	-0.119	-0.119	0.000	0.000	0.000	0.000
100	A	103	LYS	1	0.961	0.993	50.395	5.662	5.662	0.000	0.000	0.000	0.000
101	A	104	SER	0	0.034	-0.011	50.893	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	105	GLY	0	0.006	0.004	47.092	-0.085	-0.085	0.000	0.000	0.000	0.000
103	A	106	GLN	0	-0.037	-0.033	46.865	-0.030	-0.030	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.063	-0.018	48.651	-0.038	-0.038	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.037	0.019	46.019	-0.038	-0.038	0.000	0.000	0.000	0.000
106	A	109	GLY	0	0.064	0.063	44.554	-0.152	-0.152	0.000	0.000	0.000	0.000
107	A	110	VAL	0	-0.033	-0.012	41.695	-0.245	-0.245	0.000	0.000	0.000	0.000
108	A	111	LYS	1	0.880	0.917	38.606	7.786	7.786	0.000	0.000	0.000	0.000
109	A	112	PHE	0	0.022	0.013	40.260	0.070	0.070	0.000	0.000	0.000	0.000
110	A	113	ILE	0	0.039	0.023	42.237	0.075	0.075	0.000	0.000	0.000	0.000
111	A	114	ALA	0	-0.035	-0.021	45.444	0.138	0.138	0.000	0.000	0.000	0.000
112	A	115	ALA	0	-0.044	-0.010	44.238	0.108	0.108	0.000	0.000	0.000	0.000
113	A	116	LEU	0	-0.025	0.004	45.678	0.018	0.018	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:4:ARG)