FMO DATABASE

FMODB ID: QV8VY

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

Total energy (hartree)

FMO2-HF: Electronic energy	-862267.477066
FMO2-HF: Nuclear repulsion	818686.603981
FMO2-HF: Total energy	-43580.873085
FMO2-MP2: Total energy	-43711.182067

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.
4.567	6.309	-0.016	-0.794	-0.933	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 : 1.003 / q_NPA : 0.987

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	0.044	0.029	3.839	3.007	4.749	-0.016	-0.794	-0.933	0.001
4	A	7	ILE	0	0.004	-0.002	6.234	-0.436	-0.436	0.000	0.000	0.000	0.000
5	A	8	SER	0	-0.017	-0.006	9.590	1.123	1.123	0.000	0.000	0.000	0.000
6	A	9	ALA	0	0.010	0.002	12.943	-0.267	-0.267	0.000	0.000	0.000	0.000
7	A	10	THR	0	-0.005	-0.007	16.406	0.102	0.102	0.000	0.000	0.000	0.000
8	A	11	ASP	-1	-0.829	-0.913	19.875	-11.667	-11.667	0.000	0.000	0.000	0.000
9	A	12	ILE	0	-0.023	-0.028	22.868	0.318	0.318	0.000	0.000	0.000	0.000
10	A	13	GLN	0	0.020	0.015	25.961	0.635	0.635	0.000	0.000	0.000	0.000
11	A	14	TYR	0	-0.019	0.005	25.175	0.429	0.429	0.000	0.000	0.000	0.000
12	A	15	SER	0	0.003	-0.003	27.297	0.348	0.348	0.000	0.000	0.000	0.000
13	A	16	GLY	0	0.041	0.011	29.266	0.311	0.311	0.000	0.000	0.000	0.000
14	A	17	SER	0	0.069	0.036	30.350	0.327	0.327	0.000	0.000	0.000	0.000
15	A	18	LEU	0	-0.056	-0.013	28.728	0.281	0.281	0.000	0.000	0.000	0.000
16	A	19	LEU	0	-0.010	0.004	31.743	0.241	0.241	0.000	0.000	0.000	0.000
17	A	20	ASN	0	-0.029	-0.013	34.810	0.358	0.358	0.000	0.000	0.000	0.000
18	A	21	SER	0	0.014	-0.005	33.914	0.191	0.191	0.000	0.000	0.000	0.000
19	A	22	LEU	0	-0.038	-0.016	33.342	0.194	0.194	0.000	0.000	0.000	0.000
20	A	23	ASN	0	0.024	0.009	36.972	0.323	0.323	0.000	0.000	0.000	0.000
21	A	24	GLU	-1	-0.877	-0.931	38.763	-7.413	-7.413	0.000	0.000	0.000	0.000
22	A	25	GLN	0	-0.053	-0.037	34.992	0.226	0.226	0.000	0.000	0.000	0.000
23	A	26	ARG	1	0.877	0.931	40.600	6.954	6.954	0.000	0.000	0.000	0.000
24	A	27	GLY	0	-0.033	-0.004	42.900	0.157	0.157	0.000	0.000	0.000	0.000
25	A	28	HIS	0	-0.007	0.002	42.744	0.246	0.246	0.000	0.000	0.000	0.000
26	A	29	GLY	0	-0.022	-0.015	44.997	0.106	0.106	0.000	0.000	0.000	0.000
27	A	30	LEU	0	-0.016	-0.011	40.529	-0.004	-0.004	0.000	0.000	0.000	0.000
28	A	31	PHE	0	-0.002	-0.017	37.135	-0.131	-0.131	0.000	0.000	0.000	0.000
29	A	32	CYS	0	-0.082	0.008	40.313	-0.038	-0.038	0.000	0.000	0.000	0.000
30	A	33	ASP	-1	-0.749	-0.860	41.121	-6.965	-6.965	0.000	0.000	0.000	0.000
31	A	34	VAL	0	-0.023	-0.007	43.412	0.067	0.067	0.000	0.000	0.000	0.000
32	A	35	THR	0	-0.053	-0.023	45.873	-0.013	-0.013	0.000	0.000	0.000	0.000
33	A	36	VAL	0	-0.002	-0.007	47.236	0.034	0.034	0.000	0.000	0.000	0.000
34	A	37	ILE	0	-0.025	-0.017	50.130	0.007	0.007	0.000	0.000	0.000	0.000
35	A	38	VAL	0	0.029	0.012	52.080	-0.033	-0.033	0.000	0.000	0.000	0.000
36	A	39	GLU	-1	-0.825	-0.911	55.153	-5.186	-5.186	0.000	0.000	0.000	0.000
37	A	40	ASP	-1	-0.903	-0.939	58.920	-5.113	-5.113	0.000	0.000	0.000	0.000
38	A	41	ARG	1	0.901	0.953	53.017	5.576	5.576	0.000	0.000	0.000	0.000
39	A	42	LYS	1	0.950	0.979	53.073	5.310	5.310	0.000	0.000	0.000	0.000
40	A	43	PHE	0	0.009	0.004	48.501	-0.031	-0.031	0.000	0.000	0.000	0.000
41	A	44	ARG	1	0.885	0.959	45.541	6.301	6.301	0.000	0.000	0.000	0.000
42	A	45	ALA	0	0.048	0.013	43.148	-0.058	-0.058	0.000	0.000	0.000	0.000
43	A	46	HIS	0	0.031	0.028	38.459	0.051	0.051	0.000	0.000	0.000	0.000
44	A	47	LYS	1	0.861	0.910	40.016	6.704	6.704	0.000	0.000	0.000	0.000
45	A	48	ASN	0	-0.003	-0.003	33.489	0.116	0.116	0.000	0.000	0.000	0.000
46	A	49	ILE	0	0.029	0.018	34.566	-0.148	-0.148	0.000	0.000	0.000	0.000
47	A	50	LEU	0	0.017	0.021	37.134	-0.038	-0.038	0.000	0.000	0.000	0.000
48	A	51	SER	0	0.006	-0.006	37.607	-0.018	-0.018	0.000	0.000	0.000	0.000
49	A	52	ALA	0	-0.010	0.007	34.230	-0.043	-0.043	0.000	0.000	0.000	0.000
50	A	53	SER	0	-0.035	-0.037	36.052	-0.021	-0.021	0.000	0.000	0.000	0.000
51	A	54	SER	0	-0.052	-0.035	38.380	0.119	0.119	0.000	0.000	0.000	0.000
52	A	55	THR	0	0.037	0.005	40.361	-0.042	-0.042	0.000	0.000	0.000	0.000
53	A	56	TYR	0	0.003	0.021	42.134	0.023	0.023	0.000	0.000	0.000	0.000
54	A	57	PHE	0	0.047	-0.006	42.691	0.067	0.067	0.000	0.000	0.000	0.000
55	A	58	HIS	0	-0.072	-0.016	36.225	-0.011	-0.011	0.000	0.000	0.000	0.000
56	A	59	GLN	0	-0.015	-0.012	40.946	0.056	0.056	0.000	0.000	0.000	0.000
57	A	60	LEU	0	-0.019	0.007	43.745	0.056	0.056	0.000	0.000	0.000	0.000
58	A	61	PHE	0	-0.010	-0.025	41.580	0.075	0.075	0.000	0.000	0.000	0.000
59	A	62	SER	0	-0.045	-0.017	41.543	-0.082	-0.082	0.000	0.000	0.000	0.000
60	A	63	VAL	0	-0.030	-0.005	42.508	0.028	0.028	0.000	0.000	0.000	0.000
61	A	64	ALA	0	-0.007	-0.004	45.191	-0.048	-0.048	0.000	0.000	0.000	0.000
62	A	65	GLY	0	0.056	0.015	46.137	0.115	0.115	0.000	0.000	0.000	0.000
63	A	66	GLN	0	-0.042	-0.028	46.186	-0.024	-0.024	0.000	0.000	0.000	0.000
64	A	67	VAL	0	-0.011	-0.006	48.112	-0.019	-0.019	0.000	0.000	0.000	0.000
65	A	68	VAL	0	-0.017	0.001	47.949	0.020	0.020	0.000	0.000	0.000	0.000
66	A	69	GLU	-1	-0.896	-0.951	51.015	-5.359	-5.359	0.000	0.000	0.000	0.000
67	A	70	LEU	0	-0.044	-0.014	49.418	-0.054	-0.054	0.000	0.000	0.000	0.000
68	A	71	SER	0	0.042	0.014	53.757	0.067	0.067	0.000	0.000	0.000	0.000
69	A	72	PHE	0	-0.056	-0.043	55.510	-0.073	-0.073	0.000	0.000	0.000	0.000
70	A	73	ILE	0	0.000	0.011	51.317	-0.047	-0.047	0.000	0.000	0.000	0.000
71	A	74	ARG	1	0.816	0.867	55.512	5.306	5.306	0.000	0.000	0.000	0.000
72	A	75	ALA	0	0.028	0.002	54.737	-0.135	-0.135	0.000	0.000	0.000	0.000
73	A	76	GLU	-1	-0.875	-0.941	53.550	-5.482	-5.482	0.000	0.000	0.000	0.000
74	A	77	ILE	0	0.022	0.025	52.153	-0.119	-0.119	0.000	0.000	0.000	0.000
75	A	78	PHE	0	0.037	0.001	47.289	-0.174	-0.174	0.000	0.000	0.000	0.000
76	A	79	ALA	0	-0.035	-0.019	48.794	-0.146	-0.146	0.000	0.000	0.000	0.000
77	A	80	GLU	-1	-0.854	-0.922	48.120	-6.410	-6.410	0.000	0.000	0.000	0.000
78	A	81	ILE	0	-0.037	-0.007	45.426	-0.186	-0.186	0.000	0.000	0.000	0.000
79	A	82	LEU	0	-0.023	-0.012	44.353	-0.209	-0.209	0.000	0.000	0.000	0.000
80	A	83	ASN	0	-0.001	-0.009	43.228	-0.231	-0.231	0.000	0.000	0.000	0.000
81	A	84	TYR	0	0.009	0.034	39.050	-0.193	-0.193	0.000	0.000	0.000	0.000
82	A	85	ILE	0	-0.048	-0.019	39.445	-0.228	-0.228	0.000	0.000	0.000	0.000
83	A	86	TYR	0	-0.028	-0.044	38.575	-0.177	-0.177	0.000	0.000	0.000	0.000
84	A	87	SER	0	-0.014	-0.041	38.515	-0.068	-0.068	0.000	0.000	0.000	0.000
85	A	88	SER	0	-0.092	-0.039	36.455	-0.234	-0.234	0.000	0.000	0.000	0.000
86	A	89	LYS	1	0.944	0.961	38.616	7.813	7.813	0.000	0.000	0.000	0.000
87	A	90	ILE	0	0.049	0.037	41.930	0.076	0.076	0.000	0.000	0.000	0.000
88	A	91	VAL	0	-0.011	-0.017	44.910	-0.043	-0.043	0.000	0.000	0.000	0.000
89	A	92	ARG	1	0.918	0.954	47.489	6.065	6.065	0.000	0.000	0.000	0.000
90	A	93	VAL	0	0.076	0.049	50.224	0.092	0.092	0.000	0.000	0.000	0.000
91	A	94	ARG	1	0.861	0.921	52.450	5.331	5.331	0.000	0.000	0.000	0.000
92	A	95	SER	0	0.056	0.017	55.567	-0.048	-0.048	0.000	0.000	0.000	0.000
93	A	96	ASP	-1	-0.853	-0.915	56.593	-5.330	-5.330	0.000	0.000	0.000	0.000
94	A	97	LEU	0	0.004	0.008	55.532	0.042	0.042	0.000	0.000	0.000	0.000
95	A	98	LEU	0	-0.014	0.000	50.633	-0.077	-0.077	0.000	0.000	0.000	0.000
96	A	99	ASP	-1	-0.843	-0.920	53.267	-5.671	-5.671	0.000	0.000	0.000	0.000
97	A	100	GLU	-1	-0.803	-0.886	54.700	-5.409	-5.409	0.000	0.000	0.000	0.000
98	A	101	LEU	0	-0.003	0.002	48.659	-0.070	-0.070	0.000	0.000	0.000	0.000
99	A	102	ILE	0	-0.004	0.008	49.924	-0.120	-0.120	0.000	0.000	0.000	0.000
100	A	103	LYS	1	0.936	0.980	50.396	5.686	5.686	0.000	0.000	0.000	0.000
101	A	104	SER	0	0.043	-0.011	50.851	-0.003	-0.003	0.000	0.000	0.000	0.000
102	A	105	GLY	0	0.010	0.008	47.095	-0.084	-0.084	0.000	0.000	0.000	0.000
103	A	106	GLN	0	-0.036	-0.034	46.866	-0.036	-0.036	0.000	0.000	0.000	0.000
104	A	107	LEU	0	-0.058	-0.016	48.652	-0.046	-0.046	0.000	0.000	0.000	0.000
105	A	108	LEU	0	0.042	0.021	46.118	-0.042	-0.042	0.000	0.000	0.000	0.000
106	A	109	GLY	0	0.064	0.062	44.551	-0.151	-0.151	0.000	0.000	0.000	0.000
107	A	110	VAL	0	-0.036	-0.014	41.769	-0.244	-0.244	0.000	0.000	0.000	0.000
108	A	111	LYS	1	0.866	0.909	38.615	7.751	7.751	0.000	0.000	0.000	0.000
109	A	112	PHE	0	0.030	0.017	40.241	0.072	0.072	0.000	0.000	0.000	0.000
110	A	113	ILE	0	0.041	0.020	42.238	0.077	0.077	0.000	0.000	0.000	0.000
111	A	114	ALA	0	-0.034	-0.017	45.446	0.138	0.138	0.000	0.000	0.000	0.000
112	A	115	ALA	0	-0.036	-0.008	44.225	0.113	0.113	0.000	0.000	0.000	0.000
113	A	116	LEU	0	-0.046	-0.005	45.442	0.084	0.084	0.000	0.000	0.000	0.000

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